TTHY_HUMAN
ID TTHY_HUMAN Reviewed; 147 AA.
AC P02766; Q549C7; Q6IB96; Q9UBZ6; Q9UCM9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 257.
DE RecName: Full=Transthyretin;
DE AltName: Full=ATTR;
DE AltName: Full=Prealbumin;
DE AltName: Full=TBPA;
DE Flags: Precursor;
GN Name=TTR; Synonyms=PALB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=6093805; DOI=10.1016/0006-291x(84)91590-0;
RA Mita S., Maeda S., Shimada K., Araki S.;
RT "Cloning and sequence analysis of cDNA for human prealbumin.";
RL Biochem. Biophys. Res. Commun. 124:558-564(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2990465; DOI=10.1016/0006-291x(85)91956-4;
RA Wallace M.R., Naylor S.L., Kluve-Beckerman B., Long G.L., McDonald L.,
RA Shows T.B., Benson M.D.;
RT "Localization of the human prealbumin gene to chromosome 18.";
RL Biochem. Biophys. Res. Commun. 129:753-758(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=4054629; DOI=10.1016/0378-1119(85)90272-0;
RA Sasaki H., Yoshioka N., Takagi Y., Sakaki Y.;
RT "Structure of the chromosomal gene for human serum prealbumin.";
RL Gene 37:191-197(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2995367; DOI=10.1016/s0021-9258(17)39013-0;
RA Tsuzuki T., Mita S., Maeda S., Araki S., Shimada K.;
RT "Structure of the human prealbumin gene.";
RL J. Biol. Chem. 260:12224-12227(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT AMYL-TTR MET-50.
RX PubMed=3818577; DOI=10.1093/oxfordjournals.jbchem.a121826;
RA Mita S., Maeda S., Shimada K., Araki S.;
RT "Analyses of prealbumin mRNAs in individuals with familial amyloidotic
RT polyneuropathy.";
RL J. Biochem. 100:1215-1222(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT AMYL-TTR MET-50.
RC TISSUE=Liver;
RX PubMed=3022108;
RA Maeda S., Mita S., Araki S., Shimada K.;
RT "Structure and expression of the mutant prealbumin gene associated with
RT familial amyloidotic polyneuropathy.";
RL Mol. Biol. Med. 3:329-338(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-28.
RC TISSUE=Liver;
RX PubMed=2015890; DOI=10.1016/0014-5793(91)80387-i;
RA Christmanson L., Betsholtz C., Gustavsson A., Johansson B., Sletten K.,
RA Westermark P.;
RT "The transthyretin cDNA sequence is normal in transthyretin-derived senile
RT systemic amyloidosis.";
RL FEBS Lett. 281:177-180(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1666289;
RA Gu J.R., Jiang H.Q., He L.P., Li D.Z., Zhou X.M., Dai W.L., Qian L.F.,
RA Chen Y.Q., Schweinfest C., Papas T.;
RT "Transthyretin (prealbumin) gene in human primary hepatic cancer.";
RL Sci. China, Ser. B, Chem. Life Sci. Earth Sci. 34:1312-1318(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Retina;
RX PubMed=10328977; DOI=10.1006/exer.1998.0646;
RA Getz R.K., Kennedy B.G., Mangini N.J.;
RT "Transthyretin localization in cultured and native human retinal pigment
RT epithelium.";
RL Exp. Eye Res. 68:629-636(1999).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Corpus callosum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [15]
RP PROTEIN SEQUENCE OF 21-147.
RX PubMed=4607556; DOI=10.1016/s0021-9258(19)42128-5;
RA Kanda Y., Goodman D.S., Canfield R.E., Morgan F.J.;
RT "The amino acid sequence of human plasma prealbumin.";
RL J. Biol. Chem. 249:6796-6805(1974).
RN [16]
RP PRELIMINARY PROTEIN SEQUENCE OF 21-147, AND VARIANT SER-26.
RX PubMed=6300852; DOI=10.1073/pnas.80.2.539;
RA Pras M., Prelli F., Franklin E.C., Frangione B.;
RT "Primary structure of an amyloid prealbumin variant in familial
RT polyneuropathy of Jewish origin.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:539-542(1983).
RN [17]
RP PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR MET-50.
RX PubMed=6651852; DOI=10.1016/s0006-291x(83)80224-1;
RA Tawara S., Nakazato M., Kangawa K., Matsuo H., Araki S.;
RT "Identification of amyloid prealbumin variant in familial amyloidotic
RT polyneuropathy (Japanese type).";
RL Biochem. Biophys. Res. Commun. 116:880-888(1983).
RN [18]
RP PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR MET-50.
RX PubMed=6583672; DOI=10.1073/pnas.81.3.694;
RA Dwulet F.E., Benson M.D.;
RT "Primary structure of an amyloid prealbumin and its plasma precursor in a
RT heredofamilial polyneuropathy of Swedish origin.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:694-698(1984).
RN [19]
RP PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR ILE-142.
RX PubMed=3135807; DOI=10.1016/0006-291x(88)90188-x;
RA Cornwell G.G. III, Sletten K., Johansson B., Westermark P.;
RT "Evidence that the amyloid fibril protein in senile systemic amyloidosis is
RT derived from normal prealbumin.";
RL Biochem. Biophys. Res. Commun. 154:648-653(1988).
RN [20]
RP PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR MET-50.
RX PubMed=1517749; DOI=10.1016/0022-510x(92)90048-p;
RA Kametani F., Ikeda S., Yanagisawa N., Ishi T., Hanyu N.;
RT "Characterization of a transthyretin-related amyloid fibril protein from
RT cerebral amyloid angiopathy in type I familial amyloid polyneuropathy.";
RL J. Neurol. Sci. 108:178-183(1992).
RN [21]
RP PROTEIN SEQUENCE OF 21-41.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [22]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, AND VARIANT AMYL-TTR LEU-53.
RX PubMed=1932142; DOI=10.1016/0925-4439(91)90033-6;
RA Harding J., Skare J., Skinner M.;
RT "A second transthyretin mutation at position 33 (Leu/Phe) associated with
RT familial amyloidotic polyneuropathy.";
RL Biochim. Biophys. Acta 1097:183-186(1991).
RN [23]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, VARIANT AMYL-TTR GLY-62, AND
RP VARIANT ASN-110.
RX PubMed=7923855; DOI=10.1111/j.1399-0004.1994.tb04030.x;
RA Skare J.C., Jones L.A., Myles N., Kane K., Milunsky A., Cohen A.S.,
RA Skinner M.;
RT "Two transthyretin mutations (Glu42Gly, His90Asn) in an Italian family with
RT amyloidosis.";
RL Clin. Genet. 45:281-284(1994).
RN [24]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-147.
RX PubMed=4044580; DOI=10.1016/s0021-9258(17)39100-7;
RA Soprano D.R., Herbert J., Soprano K.J., Schon E.A., Goodman D.S.;
RT "Demonstration of transthyretin mRNA in the brain and other extrahepatic
RT tissues in the rat.";
RL J. Biol. Chem. 260:11793-11798(1985).
RN [25]
RP PROTEIN SEQUENCE OF 42-68; 101-123 AND 125-146, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [26]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-129, AND VARIANT DTTRH THR-129.
RX PubMed=1979335; DOI=10.1172/jci114938;
RA Moses A.C., Rosen H.N., Moller D.E., Tsuzaki S., Haddow J.E., Lawlor J.,
RA Liepnieks J.J., Nichols W.C., Benson M.D.;
RT "A point mutation in transthyretin increases affinity for thyroxine and
RT produces euthyroid hyperthyroxinemia.";
RL J. Clin. Invest. 86:2025-2033(1990).
RN [27]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=7474944;
RA Gustavsson A., Jahr H., Tobiassen R., Jacobson D.R., Sletten K.,
RA Westermark P.;
RT "Amyloid fibril composition and transthyretin gene structure in senile
RT systemic amyloidosis.";
RL Lab. Invest. 73:703-708(1995).
RN [28]
RP BINDING SITES FOR THYROID HORMONES.
RX PubMed=201845; DOI=10.1038/268115a0;
RA Blake C.C.F., Oatley S.J.;
RT "Protein-DNA and protein-hormone interactions in prealbumin: a model of the
RT thyroid hormone nuclear receptor?";
RL Nature 268:115-120(1977).
RN [29]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=3714052; DOI=10.1212/wnl.36.7.900;
RA Herbert J., Wilcox J.N., Pham K.T., Fremeau R.T. Jr., Zeviani M., Dwork A.,
RA Soprano D.R., Makover A., Goodman D.S., Zimmerman E.A., Roberts J.L.,
RA Schon E.A.;
RT "Transthyretin: a choroid plexus-specific transport protein in human brain.
RT The 1986 S. Weir Mitchell award.";
RL Neurology 36:900-911(1986).
RN [30]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [31]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [32]
RP GAMMA-CARBOXYGLUTAMATION AT GLU-62, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=18221012; DOI=10.2174/092986608783330297;
RA Rueggeberg S., Horn P., Li X., Vajkoczy P., Franz T.;
RT "Detection of a gamma-carboxy-glutamate as novel post-translational
RT modification of human transthyretin.";
RL Protein Pept. Lett. 15:43-46(2008).
RN [33]
RP GLYCOSYLATION AT ASN-118, AND CHARACTERIZATION OF VARIANT AMYL-TTR GLY-38.
RX PubMed=19167329; DOI=10.1016/j.cell.2008.11.047;
RA Ruiz-Canada C., Kelleher D.J., Gilmore R.;
RT "Cotranslational and posttranslational N-glycosylation of polypeptides by
RT distinct mammalian OST isoforms.";
RL Cell 136:272-283(2009).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=4216640; DOI=10.1016/0022-2836(74)90291-5;
RA Blake C.C.F., Geisow M.J., Swan I.D.A., Rerat C., Rerat B.;
RT "Structure of human plasma prealbumin at 2.5-A resolution. A preliminary
RT report on the polypeptide chain conformation, quaternary structure and
RT thyroxine binding.";
RL J. Mol. Biol. 88:1-12(1974).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=671542; DOI=10.1016/0022-2836(78)90368-6;
RA Blake C.C.F., Geisow M.J., Oatley S.J., Rerat B., Rerat C.;
RT "Structure of prealbumin: secondary, tertiary and quaternary interactions
RT determined by Fourier refinement at 1.8 A.";
RL J. Mol. Biol. 121:339-356(1978).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF VARIANT AMYL-TTR MET-50.
RX PubMed=8382610; DOI=10.1002/j.1460-2075.1993.tb05707.x;
RA Terry C.J., Damas A.M., Oliveira P., Saraiva M.J.M., Alves I.L.,
RA Costa P.P., Matias P.M., Sakaki Y., Blake C.C.F.;
RT "Structure of Met30 variant of transthyretin and its amyloidogenic
RT implications.";
RL EMBO J. 12:735-741(1993).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF VARIANT AMYL-TTR MET-50.
RX PubMed=8428915; DOI=10.1016/s0021-9258(18)53792-3;
RA Hamilton J.A., Steinrauf L.K., Braden B.C., Liepnieks J., Benson M.D.,
RA Holmgren G., Sandgren O., Steen L.;
RT "The X-ray crystal structure refinements of normal human transthyretin and
RT the amyloidogenic Val-30-->Met variant to 1.7-A resolution.";
RL J. Biol. Chem. 268:2416-2424(1993).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF COMPLEX WITH RBP.
RX PubMed=7754382; DOI=10.1126/science.7754382;
RA Monaco H.L., Rizzi M., Coda A.;
RT "Structure of a complex of two plasma proteins: transthyretin and retinol-
RT binding protein.";
RL Science 268:1039-1041(1995).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANTS.
RX PubMed=9818054; DOI=10.3109/13506129809003843;
RA Schormann N., Murrell J.R., Benson M.D.;
RT "Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin
RT variants: new model for amyloid fibril formation.";
RL Amyloid 5:175-187(1998).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR PRO-75.
RX PubMed=9733771; DOI=10.1074/jbc.273.38.24715;
RA Sebastiao M.P., Saraiva M.J., Damas A.M.;
RT "The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant
RT reveals a possible pathway for transthyretin polymerization into amyloid
RT fibrils.";
RL J. Biol. Chem. 273:24715-24722(1998).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9789022; DOI=10.1073/pnas.95.22.12956;
RA Peterson S.A., Klabunde T., Lashuel H.A., Purkey H., Sacchettini J.C.,
RA Kelly J.W.;
RT "Inhibiting transthyretin conformational changes that lead to amyloid
RT fibril formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12956-12960(1998).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH RBP4, AND SUBUNIT.
RX PubMed=10052934; DOI=10.1021/bi982291i;
RA Naylor H.M., Newcomer M.E.;
RT "The structure of human retinol-binding protein (RBP) with its carrier
RT protein transthyretin reveals an interaction with the carboxy terminus of
RT RBP.";
RL Biochemistry 38:2647-2653(1999).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 21-147.
RX PubMed=10986125; DOI=10.1006/jmbi.2000.4078;
RA Hoernberg A., Eneqvist T., Olofsson A., Lundgren E., Sauer-Eriksson A.E.;
RT "A comparative analysis of 23 structures of the amyloidogenic protein
RT transthyretin.";
RL J. Mol. Biol. 302:649-669(2000).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10742177; DOI=10.1038/74082;
RA Klabunde T., Petrassi H.M., Oza V.B., Raman P., Kelly J.W.,
RA Sacchettini J.C.;
RT "Rational design of potent human transthyretin amyloid disease
RT inhibitors.";
RL Nat. Struct. Biol. 7:312-321(2000).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-147, MUTAGENESIS OF PHE-107 AND
RP LEU-130, IDENTIFICATION BY MASS SPECTROMETRY, FORMATION OF AMYLOID FIBERS
RP AT ACIDIC PH, AND SUBUNIT.
RX PubMed=11560492; DOI=10.1021/bi011194d;
RA Jiang X., Smith C.S., Petrassi H.M., Hammarstroem P., White J.T.,
RA Sacchettini J.C., Kelly J.W.;
RT "An engineered transthyretin monomer that is nonamyloidogenic, unless it is
RT partially denatured.";
RL Biochemistry 40:11442-11452(2001).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 30-144 OF VARIANT AMYL-TTR MET-50
RP AND VARIANT CHICAGO MET-139 IN COMPLEX WITH L-THYROXINE, AND SUBUNIT.
RX PubMed=11243784; DOI=10.1006/jmbi.2000.4415;
RA Sebastiao M.P., Lamzin V., Saraiva M.J., Damas A.M.;
RT "Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis
RT at atomic resolution.";
RL J. Mol. Biol. 306:733-744(2001).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR
RP CYS-134.
RX PubMed=12403615; DOI=10.1021/bi025800w;
RA Eneqvist T., Olofsson A., Ando Y., Miyakawa T., Katsuragi S., Jass J.,
RA Lundgren E., Sauer-Eriksson A.E.;
RT "Disulfide-bond formation in the transthyretin mutant Y114C prevents
RT amyloid fibril formation in vivo and in vitro.";
RL Biochemistry 41:13143-13151(2002).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-147IN COMPLEX WITH
RP AMYLOIDOGENESIS INHIBITORS.
RX PubMed=12820260; DOI=10.1002/anie.200351179;
RA Razavi H., Palaninathan S.K., Powers E.T., Wiseman R.L., Purkey H.E.,
RA Mohamedmohaideen N.N., Deechongkit S., Chiang K.P., Dendle M.T.A.,
RA Sacchettini J.C., Kelly J.W.;
RT "Benzoxazoles as transthyretin amyloid fibril inhibitors: synthesis,
RT evaluation, and mechanism of action.";
RL Angew. Chem. Int. Ed. 42:2758-2761(2003).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 21-147 IN COMPLEX WITH
RP AMYLOIDOGENESIS INHIBITORS, AND FIBRIL FORMATION.
RX PubMed=14583036; DOI=10.1021/ja030294z;
RA Green N.S., Palaninathan S.K., Sacchettini J.C., Kelly J.W.;
RT "Synthesis and characterization of potent bivalent amyloidosis inhibitors
RT that bind prior to transthyretin tetramerization.";
RL J. Am. Chem. Soc. 125:13404-13414(2003).
RN [51]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-147 IN COMPLEX WITH DIFLUNISAL
RP ANALOGS, AND INHIBITION OF AMYLOID FORMATION.
RX PubMed=14711308; DOI=10.1021/jm030347n;
RA Adamski-Werner S.L., Palaninathan S.K., Sacchettini J.C., Kelly J.W.;
RT "Diflunisal analogues stabilize the native state of transthyretin. Potent
RT inhibition of amyloidogenesis.";
RL J. Med. Chem. 47:355-374(2004).
RN [52]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR PHE-98
RP AND VARIANT HIS-124, AND SUBUNIT.
RX PubMed=15735344; DOI=10.1107/s0907444904034316;
RA Neto-Silva R.M., Macedo-Ribeiro S., Pereira P.J.B., Coll M., Saraiva M.J.,
RA Damas A.M.;
RT "X-ray crystallographic studies of two transthyretin variants: further
RT insights into amyloidogenesis.";
RL Acta Crystallogr. D 61:333-339(2005).
RN [53]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147 IN COMPLEXES WITH CHLORIDE
RP AND IODIDE IONS.
RX PubMed=15981995; DOI=10.1021/bi050249z;
RA Hoernberg A., Hultdin U.W., Olofsson A., Sauer-Eriksson A.E.;
RT "The effect of iodide and chloride on transthyretin structure and
RT stability.";
RL Biochemistry 44:9290-9299(2005).
RN [54]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR
RP CYS-134.
RX PubMed=16185074; DOI=10.1021/bi050795s;
RA Karlsson A., Olofsson A., Eneqvist T., Sauer-Eriksson A.E.;
RT "Cys114-linked dimers of transthyretin are compatible with amyloid
RT formation.";
RL Biochemistry 44:13063-13070(2005).
RN [55]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 21-147 IN COMPLEX WITH THYROID
RP HORMONE ANALOG, AND SUBUNIT.
RX PubMed=15826192; DOI=10.1021/ja042929f;
RA Wiseman R.L., Johnson S.M., Kelker M.S., Foss T., Wilson I.A., Kelly J.W.;
RT "Kinetic stabilization of an oligomeric protein by a single ligand binding
RT event.";
RL J. Am. Chem. Soc. 127:5540-5551(2005).
RN [56]
RP X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) OF 31-147, AND SUBUNIT.
RX PubMed=15769474; DOI=10.1016/j.jmb.2005.01.050;
RA Foss T.R., Kelker M.S., Wiseman R.L., Wilson I.A., Kelly J.W.;
RT "Kinetic stabilization of the native state by protein engineering:
RT implications for inhibition of transthyretin amyloidogenesis.";
RL J. Mol. Biol. 347:841-854(2005).
RN [57]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF WILD-TYPE AND VARIANTS
RP AMYL-TTR PRO-75 AND PHE-98.
RX PubMed=16627944; DOI=10.1107/s0907444906006962;
RA Morais-de-Sa E., Neto-Silva R.M., Pereira P.J.B., Saraiva M.J., Damas A.M.;
RT "The binding of 2,4-dinitrophenol to wild-type and amyloidogenic
RT transthyretin.";
RL Acta Crystallogr. D 62:512-519(2006).
RN [58]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 21-147.
RX PubMed=17175208; DOI=10.1016/j.bbapap.2006.10.015;
RA Gales L., Saraiva M.J., Damas A.M.;
RT "Structural basis for the protective role of sulfite against transthyretin
RT amyloid formation.";
RL Biochim. Biophys. Acta 1774:59-64(2007).
RN [59]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147.
RX PubMed=17196219; DOI=10.1016/j.jmb.2006.11.076;
RA Pasquato N., Berni R., Folli C., Alfieri B., Cendron L., Zanotti G.;
RT "Acidic pH-induced conformational changes in amyloidogenic mutant
RT transthyretin.";
RL J. Mol. Biol. 366:711-719(2007).
RN [60]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 IN COMPLEX WITH
RP 3,5-DIIODOSALICYLIC ACID, AND THYROXINE BINDING.
RX PubMed=18155178; DOI=10.1016/j.bbapap.2007.11.014;
RA Gales L., Almeida M.R., Arsequell G., Valencia G., Saraiva M.J.,
RA Damas A.M.;
RT "Iodination of salicylic acid improves its binding to transthyretin.";
RL Biochim. Biophys. Acta 1784:512-517(2008).
RN [61]
RP X-RAY CRYSTALLOGRAPHY (3.38 ANGSTROMS) OF 21-147 IN COMPLEX WITH RBP4.
RX PubMed=19021760; DOI=10.1111/j.1742-4658.2008.06705.x;
RA Zanotti G., Folli C., Cendron L., Alfieri B., Nishida S.K., Gliubich F.,
RA Pasquato N., Negro A., Berni R.;
RT "Structural and mutational analyses of protein-protein interactions between
RT transthyretin and retinol-binding protein.";
RL FEBS J. 275:5841-5854(2008).
RN [62]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 21-147 IN COMPLEX WITH
RP 2-ARYLBENZOXAZOLE-BASED TRANSTHYRETIN AMYLOIDOGENESIS INHIBITORS.
RX PubMed=18095641; DOI=10.1021/jm0708735;
RA Johnson S.M., Connelly S., Wilson I.A., Kelly J.W.;
RT "Biochemical and structural evaluation of highly selective 2-
RT arylbenzoxazole-based transthyretin amyloidogenesis inhibitors.";
RL J. Med. Chem. 51:260-270(2008).
RN [63]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 21-147 IN COMPLEX WITH BISARYL
RP AMYLOIDOGENESIS INHIBITORS.
RX PubMed=18811132; DOI=10.1021/jm800435s;
RA Johnson S.M., Connelly S., Wilson I.A., Kelly J.W.;
RT "Toward optimization of the linker substructure common to transthyretin
RT amyloidogenesis inhibitors using biochemical and structural studies.";
RL J. Med. Chem. 51:6348-6358(2008).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 21-147 AT PH 3.5 AND 4.5.
RX PubMed=18662699; DOI=10.1016/j.jmb.2008.07.029;
RA Palaninathan S.K., Mohamedmohaideen N.N., Snee W.C., Kelly J.W.,
RA Sacchettini J.C.;
RT "Structural insight into pH-induced conformational changes within the
RT native human transthyretin tetramer.";
RL J. Mol. Biol. 382:1157-1167(2008).
RN [65]
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 21-147.
RG Mycobacterium tuberculosis structural genomics consortium (TB);
RT "Crystal structure of the F87M/L110M mutant of human transthyretin at pH
RT 4.6 soaked.";
RL Submitted (JUL-2008) to the PDB data bank.
RN [66]
RP REVIEW ON VARIANTS.
RX PubMed=7599630; DOI=10.1002/humu.1380050302;
RA Saraiva M.J.M.;
RT "Transthyretin mutations in health and disease.";
RL Hum. Mutat. 5:191-196(1995).
RN [67]
RP VARIANT AMYL-TTR ILE-53.
RX PubMed=6487335; DOI=10.1016/s0006-291x(84)80222-3;
RA Nakazato M., Kangawa K., Minamino N., Tawara S., Matsuo H., Araki S.;
RT "Revised analysis of amino acid replacement in a prealbumin variant (SKO-
RT III) associated with familial amyloidotic polyneuropathy of Jewish
RT origin.";
RL Biochem. Biophys. Res. Commun. 123:921-928(1984).
RN [68]
RP VARIANT AMYL-TTR SER-104.
RX PubMed=3722385; DOI=10.1172/jci112573;
RA Wallace M.R., Dwulet F.E., Conneally P.M., Benson M.D.;
RT "Biochemical and molecular genetic characterization of a new variant
RT prealbumin associated with hereditary amyloidosis.";
RL J. Clin. Invest. 78:6-12(1986).
RN [69]
RP VARIANT VAL-136.
RX PubMed=3675594; DOI=10.1016/0006-291x(87)91135-1;
RA Strahler J.R., Rosenblum B.B., Hanash S.M.;
RT "Identification and characterization of a human transthyretin variant.";
RL Biochem. Biophys. Res. Commun. 148:471-477(1987).
RN [70]
RP VARIANT AMYL-TTR TYR-97.
RX PubMed=2891727; DOI=10.1172/jci113293;
RA Wallace M.R., Dwulet F.E., Williams E.C., Conneally P.M., Benson M.D.;
RT "Identification of a new hereditary amyloidosis prealbumin variant, Tyr-77,
RT and detection of the gene by DNA analysis.";
RL J. Clin. Invest. 81:189-193(1988).
RN [71]
RP VARIANT AMYL-TTR CYS-134.
RX PubMed=2161654; DOI=10.1016/0006-291x(90)91445-x;
RA Ueno S., Uemichi T., Yorifuji S., Tarui S.;
RT "A novel variant of transthyretin (Tyr114 to Cys) deduced from the
RT nucleotide sequences of gene fragments from familial amyloidotic
RT polyneuropathy in Japanese sibling cases.";
RL Biochem. Biophys. Res. Commun. 169:143-147(1990).
RN [72]
RP VARIANTS AMYL-TTR GLY-62 AND ARG-70.
RX PubMed=2363717; DOI=10.1016/0006-291x(90)92011-n;
RA Ueno S., Uemichi T., Takahashi N., Soga F., Yorifuji S., Tarui S.;
RT "Two novel variants of transthyretin identified in Japanese cases with
RT familial amyloidotic polyneuropathy: transthyretin (Glu42 to Gly) and
RT transthyretin (Ser50 to Arg).";
RL Biochem. Biophys. Res. Commun. 169:1117-1121(1990).
RN [73]
RP VARIANT CHICAGO MET-139.
RX PubMed=1877623; DOI=10.1002/ajmg.1320390415;
RA Harrison H.H., Gordon E.D., Nichols W.C., Benson M.D.;
RT "Biochemical and clinical characterization of prealbuminCHICAGO: an
RT apparently benign variant of serum prealbumin (transthyretin) discovered
RT with high-resolution two-dimensional electrophoresis.";
RL Am. J. Med. Genet. 39:442-452(1991).
RN [74]
RP VARIANT AMYL-TTR ARG-78.
RX PubMed=1656975; DOI=10.1016/s0006-291x(05)81304-x;
RA Saeki Y., Ueno S., Yorifuji S., Sugiyama Y., Ide Y., Matsuzawa Y.;
RT "New mutant gene (transthyretin Arg 58) in cases with hereditary
RT polyneuropathy detected by non-isotope method of single-strand conformation
RT polymorphism analysis.";
RL Biochem. Biophys. Res. Commun. 180:380-385(1991).
RN [75]
RP VARIANT ASN-110.
RX PubMed=1997217; DOI=10.1111/j.1399-0004.1991.tb02979.x;
RA Skare J.C., Milunsky J.M., Milunsky A., Skare I.B., Cohen A.S., Skinner M.;
RT "A new transthyretin variant from a patient with familial amyloidotic
RT polyneuropathy has asparagine substituted for histidine at position 90.";
RL Clin. Genet. 39:6-12(1991).
RN [76]
RP VARIANTS AMYL-TTR LEU-53 AND LEU-84.
RX PubMed=2046936; DOI=10.1212/wnl.41.6.893;
RA Li S., Minnerath S., Li K., Dyck P.J., Sommer S.S.;
RT "Two-tiered DNA-based diagnosis of transthyretin amyloidosis reveals two
RT novel point mutations.";
RL Neurology 41:893-898(1991).
RN [77]
RP VARIANT AMYL-TTR THR-65.
RX PubMed=1570831;
RA Saraiva M.J.M., Almeida M.R., Sherman W., Gawinowicz M., Costa P.,
RA Costa P.P., Goodman D.S.;
RT "A new transthyretin mutation associated with amyloid cardiomyopathy.";
RL Am. J. Hum. Genet. 50:1027-1030(1992).
RN [78]
RP VARIANT AMYL-TTR ARG-67.
RX PubMed=1734866; DOI=10.1016/0006-291x(92)91763-g;
RA Murakami T., Maeda S., Yi S., Ikegawa S., Kawashima E., Onodera S.,
RA Shimada K., Araki S.;
RT "A novel transthyretin mutation associated with familial amyloidotic
RT polyneuropathy.";
RL Biochem. Biophys. Res. Commun. 182:520-526(1992).
RN [79]
RP VARIANT AMYL-TTR LEU-50.
RX PubMed=1520326; DOI=10.1016/s0006-291x(05)81506-2;
RA Murakami T., Atsumi T., Maeda S., Tanase S., Ishikawa K., Mita S.,
RA Kumamoto T., Araki S., Ando M.;
RT "A novel transthyretin mutation at position 30 (Leu for Val) associated
RT with familial amyloidotic polyneuropathy.";
RL Biochem. Biophys. Res. Commun. 187:397-403(1992).
RN [80]
RP VARIANT AMYL-TTR ILE-70.
RX PubMed=1520336; DOI=10.1016/s0006-291x(05)81516-5;
RA Nishi H., Kimura A., Harada H., Hayashi Y., Nakamura M., Sasazuki T.;
RT "Novel variant transthyretin gene (Ser50 to Ile) in familial cardiac
RT amyloidosis.";
RL Biochem. Biophys. Res. Commun. 187:460-466(1992).
RN [81]
RP VARIANT AMYL-TTR ALA-50.
RX PubMed=1544214; DOI=10.1111/j.1399-0004.1992.tb03635.x;
RA Jones L.A., Skare J.C., Cohen A.S., Harding J.A., Milunsky A., Skinner M.;
RT "Familial amyloidotic polyneuropathy: a new transthyretin position 30
RT mutation (alanine for valine) in a family of German descent.";
RL Clin. Genet. 41:70-73(1992).
RN [82]
RP VARIANT AMYL-TTR PRO-75.
RX PubMed=1351039; DOI=10.1007/bf00220559;
RA Jacobson D.R., McFarlin D.E., Kane I., Buxbaum J.N.;
RT "Transthyretin Pro55, a variant associated with early-onset, aggressive,
RT diffuse amyloidosis with cardiac and neurologic involvement.";
RL Hum. Genet. 89:353-356(1992).
RN [83]
RP VARIANTS AMYL-TTR ALA-69 AND GLN-109.
RX PubMed=1301926; DOI=10.1002/humu.1380010306;
RA Almeida M.R., Ferlini A., Forabosco A., Gawinowicz M.A., Costa P.P.,
RA Salvi F., Plasmati R., Tassinari C.A., Altland K., Saraiva M.J.;
RT "Two transthyretin variants (TTR Ala-49 and TTR Gln-89) in two Sicilian
RT kindreds with hereditary amyloidosis.";
RL Hum. Mutat. 1:211-215(1992).
RN [84]
RP VARIANT AMYL-TTR ARG-30.
RX PubMed=1362222; DOI=10.1136/jmg.29.12.888;
RA Uemichi T., Murrel J.R., Zeldenrust S., Benson M.D.;
RT "A new mutant transthyretin (Arg 10) associated with familial amyloid
RT polyneuropathy.";
RL J. Med. Genet. 29:888-891(1992).
RN [85]
RP VARIANT AMYL-TTR ASN-90.
RX PubMed=1436517; DOI=10.1212/wnl.42.11.2094;
RA Izumoto S., Younger D., Hays A.P., Martone R.L., Smith R.T., Herbert J.;
RT "Familial amyloidotic polyneuropathy presenting with carpal tunnel syndrome
RT and a new transthyretin mutation, asparagine 70.";
RL Neurology 42:2094-2102(1992).
RN [86]
RP VARIANT AMYL-TTR LYS-81.
RX PubMed=8352764; DOI=10.1006/bbrc.1993.1933;
RA Shiomi K., Nakazato M., Matsukura S., Ohnishi A., Hatanaka H., Tsuji S.,
RA Murai Y., Kojima M., Kangawa K., Matsuo H.;
RT "A basic transthyretin variant (Glu61-->Lys) causes familial amyloidotic
RT polyneuropathy: protein and DNA sequencing and PCR-induced mutation
RT restriction analysis.";
RL Biochem. Biophys. Res. Commun. 194:1090-1096(1993).
RN [87]
RP VARIANT AMYL-TTR LEU-88.
RX PubMed=8038017; DOI=10.1136/hrt.70.2.111;
RA Hesse A., Altland K., Linke R.P., Almeida M.R., Saraiva M.J.M.,
RA Steinmetz A., Maisch B.;
RT "Cardiac amyloidosis: a review and report of a new transthyretin
RT (prealbumin) variant.";
RL Br. Heart J. 70:111-115(1993).
RN [88]
RP VARIANT AMYL-TTR ALA-91.
RX PubMed=8257997; DOI=10.1002/humu.1380020516;
RA Almeida M.R., Lopez-Andreu F., Munar-Ques M., Costa P.P., Saraiva M.J.;
RT "Transthyretin Ala-71: a new transthyretin variant in a Spanish family with
RT familial amyloidotic polyneuropathy.";
RL Hum. Mutat. 2:420-421(1993).
RN [89]
RP VARIANT AMYL-TTR ALA-91.
RX PubMed=8095302; DOI=10.1136/jmg.30.2.120;
RA Benson M.D. II, Turpin J.C., Lucotte G., Zeldenrust S., Lechevalier B.,
RA Benson M.D.;
RT "A transthyretin variant (alanine 71) associated with familial amyloidotic
RT polyneuropathy in a French family.";
RL J. Med. Genet. 30:120-122(1993).
RN [90]
RP VARIANT AMYL-TTR ALA-67.
RA Ferlini A., Salvi F., Patrosso C., Fini S., Vezzoni P., Forbasco A.;
RT "Gly47Ala: a new transthyretin gene mutation in hereditary amyloidosis TTR-
RT related.";
RL J. Rheumatol. 20:187-187(1993).
RN [91]
RP VARIANT SER-26, AND VARIANT AMYL-TTR ILE-53.
RX PubMed=8019560; DOI=10.1002/humu.1380030313;
RA Jacobson D.R., Buxbaum J.N.;
RT "A double-variant transthyretin allele (Ser 6, Ile 33) in the Israeli
RT patient 'SKO' with familial amyloidotic polyneuropathy.";
RL Hum. Mutat. 3:254-260(1994).
RN [92]
RP VARIANT AMYL-TTR VAL-127.
RX PubMed=8081397; DOI=10.1002/humu.1380030414;
RA Jacobson D., Gertz M.A., Buxbaum J.N.;
RT "Transthyretin VAL107, a new variant associated with familial cardiac and
RT neuropathic amyloidosis.";
RL Hum. Mutat. 3:399-401(1994).
RN [93]
RP VARIANT SER-104, AND RBP BINDING STUDIES.
RX PubMed=8089102; DOI=10.1016/s0021-9258(17)31527-2;
RA Berni R., Malpeli G., Folli C., Murrell J.R., Liepnieks J.J., Benson M.D.;
RT "The Ile-84-->Ser amino acid substitution in transthyretin interferes with
RT the interaction with plasma retinol-binding protein.";
RL J. Biol. Chem. 269:23395-23398(1994).
RN [94]
RP VARIANT AMYL-TTR VAL-127.
RX PubMed=7914929; DOI=10.1136/jmg.31.5.416;
RA Uemichi T., Gertz M.A., Benson M.D.;
RT "Amyloid polyneuropathy in two German-American families: a new
RT transthyretin variant (Val 107).";
RL J. Med. Genet. 31:416-417(1994).
RN [95]
RP VARIANT AMYL-TTR GLY-117.
RX PubMed=8133316; DOI=10.1016/0022-510x(94)90162-7;
RA Yasuda T., Sobue G., Doyu M., Nakazato M., Shiomi K., Yanagi T.,
RA Mitsuma T.;
RT "Familial amyloidotic polyneuropathy with late-onset and well-preserved
RT autonomic function: a Japanese kindred with novel mutant transthyretin
RT (Ala97 to Gly).";
RL J. Neurol. Sci. 121:97-102(1994).
RN [96]
RP VARIANT AMYL-TTR PRO-75.
RX PubMed=7910950; DOI=10.1002/mus.880170611;
RA Yamamoto K., Hsu S.P., Yoshida K., Ikeda S., Nakazato M., Shiomi K.,
RA Cheng S.Y., Furihata K., Ueno I., Yanagisawa N.;
RT "Familial amyloid polyneuropathy in Taiwan: identification of transthyretin
RT variant (Leu55-->Pro).";
RL Muscle Nerve 17:637-641(1994).
RN [97]
RP VARIANT CTS1 HIS-134.
RX PubMed=8309582; DOI=10.1212/wnl.44.2.315;
RA Murakami T., Tachibana S., Endo Y., Kawai R., Hara M., Tanase S., Ando M.;
RT "Familial carpal tunnel syndrome due to amyloidogenic transthyretin His 114
RT variant.";
RL Neurology 44:315-318(1994).
RN [98]
RP VARIANTS AMYL-TTR MET-50; ASN-55; ALA-69; ARG-70; ALA-80; TYR-97 AND
RP GLN-109.
RX PubMed=7655883; DOI=10.1093/brain/118.4.849;
RA Reilly M.M., Adams D., Booth D.R., Davis M.B., Said G.,
RA Laubriat-Bianchin M., Pepys M.B., Thomas P.K., Harding A.E.;
RT "Transthyretin gene analysis in European patients with suspected familial
RT amyloid polyneuropathy.";
RL Brain 118:849-856(1995).
RN [99]
RP VARIANT AMYL-TTR LYS-79.
RX PubMed=7850982; DOI=10.1161/01.cir.91.4.962;
RA Booth D.R., Tan S.Y., Hawkins P.N., Pepys M.B., Frustaci A.;
RT "A novel variant of transthyretin, 59Thr-->Lys, associated with autosomal
RT dominant cardiac amyloidosis in an Italian family.";
RL Circulation 91:962-967(1995).
RN [100]
RP VARIANT AMYL-TTR GLY-38.
RX PubMed=8579098;
RA Vidal R., Garzuly F., Budka H., Lalowski M., Linke R.P., Brittig F.,
RA Frangione B., Wisniewski T.;
RT "Meningocerebrovascular amyloidosis associated with a novel transthyretin
RT mis-sense mutation at codon 18 (TTRD 18G).";
RL Am. J. Pathol. 148:361-366(1996).
RN [101]
RP VARIANT AMYL-TTR GLY-50.
RX PubMed=9066351; DOI=10.1002/ana.410410305;
RA Petersen R.B., Goren H., Cohen M., Richardson S.L., Tresser N., Lynn A.,
RA Gali M., Estes M., Gambetti P.;
RT "Transthyretin amyloidosis: a new mutation associated with dementia.";
RL Ann. Neurol. 41:307-313(1997).
RN [102]
RP VARIANT AMYL-TTR ILE-40.
RX PubMed=8990019;
RX DOI=10.1002/(sici)1098-1004(1997)9:1<83::aid-humu19>3.0.co;2-l;
RA Jacobson D.R., Pan T., Kyle R.A., Buxbaum J.N.;
RT "Transthyretin ILE20, a new variant associated with late-onset cardiac
RT amyloidosis.";
RL Hum. Mutat. 9:83-85(1997).
RN [103]
RP VARIANT AMYL-TTR THR-54.
RX PubMed=9605286;
RX DOI=10.1002/(sici)1096-8628(19980501)77:2<135::aid-ajmg5>3.0.co;2-r;
RA Patrosso M.C., Salvi F., De Grandis D., Vezzoni P., Jacobson D.R.,
RA Ferlini A.;
RT "Novel transthyretin missense mutation (Thr34) in an Italian family with
RT hereditary amyloidosis.";
RL Am. J. Med. Genet. 77:135-138(1998).
RN [104]
RP VARIANT AMYL-TTR ASP-62.
RX PubMed=10036587; DOI=10.3109/13506129809007302;
RA Dupuy O., Bletry O., Blanc A.S., Droz D., Viemont M., Delpech M.,
RA Grateau G.;
RT "A novel variant of transthyretin (Glu42Asp) associated with sporadic late-
RT onset cardiac amyloidosis.";
RL Amyloid 5:285-287(1998).
RN [105]
RP VARIANTS AMYL-TTR SER-111 AND SER-136.
RX PubMed=10627135;
RX DOI=10.1002/(sici)1098-1004(1998)12:1<71::aid-humu15>3.0.co;2-7;
RA Misrahi A.M., Plante V., Lalu T., Serre I., Adams D., Lacroix D.C.,
RA Said G.;
RT "New transthyretin variants Ser 91 and Ser 116 associated with familial
RT amyloidotic polyneuropathy.";
RL Hum. Mutat. 12:71-71(1998).
RN [106]
RP VARIANT AMYL-TTR VAL-93.
RX PubMed=10694917;
RX DOI=10.1002/(sici)1098-1004(1998)12:2<135::aid-humu9>3.0.co;2-k;
RA Booth D.R., Gillmore J.D., Persey M.R., Booth S.E., Cafferty K.D.,
RA Tennent G.A., Madhoo S., Cochrane S.W., Whitehead T.C., Pasvol G.,
RA Hawkins P.N.;
RT "Transthyretin Ile73Val is associated with familial amyloidotic
RT polyneuropathy in a Bangladeshi family.";
RL Hum. Mutat. 12:135-135(1998).
RN [107]
RP VARIANT SER-121, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10671063;
RA Kishikawa M., Nakanishi T., Miyazaki A., Hatanaka M., Shimizu A.,
RA Tamoto S., Ohsawa N., Hayashi H., Kanai M.;
RT "A new nonamyloid transthyretin variant, G101S, detected by electrospray
RT ionization/mass spectrometry.";
RL Hum. Mutat. 12:363-363(1998).
RN [108]
RP VARIANT SER-64.
RX PubMed=9818883; DOI=10.1212/wnl.51.5.1462;
RA Klein C.J., Nakumura M., Jacobson D.R., Lacy M.Q., Benson M.D.,
RA Petersen R.C.;
RT "Transthyretin amyloidosis (serine 44) with headache, hearing loss, and
RT peripheral neuropathy.";
RL Neurology 51:1462-1464(1998).
RN [109]
RP VARIANT AMYL-TTR ALA-142, VARIANT SER-26, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=10211412; DOI=10.3109/13506129908993288;
RA Theberge R., Connors L., Skare J., Skinner M., Falk R.H., Costello C.E.;
RT "A new amyloidogenic transthyretin variant (Val122Ala) found in a compound
RT heterozygous patient.";
RL Amyloid 6:54-58(1999).
RN [110]
RP VARIANT AMYL-TTR ASN-43, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10439117; DOI=10.3109/13506129909007311;
RA Connors L.H., Theberge R., Skare J., Costello C.E., Falk R.H., Skinner M.;
RT "A new transthyretin variant (Ser23Asn) associated with familial
RT amyloidosis in a Portuguese patient.";
RL Amyloid 6:114-118(1999).
RN [111]
RP VARIANTS AMYL-TTR LEU-50; VAL-53; ALA-58; ARG-70; GLY-117 AND SER-117, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10611950; DOI=10.3109/13506129909007341;
RA Tachibana N., Tokuda T., Yoshida K., Taketomi T., Nakazato M., Li Y.F.,
RA Masuda Y., Ikeda S.;
RT "Usefulness of MALDI/TOF mass spectrometry of immunoprecipitated serum
RT variant transthyretin in the diagnosis of familial amyloid
RT polyneuropathy.";
RL Amyloid 6:282-288(1999).
RN [112]
RP VARIANT HIS-124, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10529370; DOI=10.1006/bbrc.1999.1514;
RA Terazaki H., Ando Y., Misumi S., Nakamura M., Ando E., Matsunaga N.,
RA Shoji S., Okuyama M., Ideta H., Nakagawa K., Ishizaki T., Ando M.,
RA Saraiva M.J.;
RT "A novel compound heterozygote (FAP ATTR Arg104His/ATTR Val30Met) with high
RT serum transthyretin (TTR) and retinol binding protein (RBP) levels.";
RL Biochem. Biophys. Res. Commun. 264:365-370(1999).
RN [113]
RP VARIANT AMYL-TTR PRO-32.
RX PubMed=10071047; DOI=10.1093/brain/122.2.183;
RA Brett M., Persey M.R., Reilly M.M., Revesz T., Booth D.R., Booth S.E.,
RA Hawkins P.N., Pepys M.B., Morgan-Hughes J.A.;
RT "Transthyretin Leu12Pro is associated with systemic, neuropathic and
RT leptomeningeal amyloidosis.";
RL Brain 122:183-190(1999).
RN [114]
RP VARIANT AMYL-TTR ILE-69, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10436378; DOI=10.1159/000022872;
RA Nakamura M., Yamashita T., Ando Y., Hamidi Asl K., Tashima K., Ohlsson P.,
RA Kususe Y., Benson M.D.;
RT "Identification of a new transthyretin variant (Ile49) in familial
RT amyloidotic polyneuropathy using electrospray ionization mass spectrometry
RT and nonisotopic RNase cleavage assay.";
RL Hum. Hered. 49:186-189(1999).
RN [115]
RP VARIANT AMYL-TTR LYS-109.
RX PubMed=10842705; DOI=10.3109/13506120009146824;
RA Nakamura M., Hamidi Asl K., Benson M.D.;
RT "A novel variant of transthyretin (Glu89Lys) associated with familial
RT amyloidotic polyneuropathy.";
RL Amyloid 7:46-50(2000).
RN [116]
RP VARIANT AMYL-TTR SER-65, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10842718; DOI=10.3109/13506120009146252;
RA Janunger T., Anan I., Holmgren G., Lovheim O., Ohlsson P.I., Suhr O.B.,
RA Tashima K.;
RT "Heart failure caused by a novel amyloidogenic mutation of the
RT transthyretin gene: ATTR Ala45Ser.";
RL Amyloid 7:137-140(2000).
RN [117]
RP VARIANT AMYL-TTR MET-48.
RX PubMed=10882995;
RX DOI=10.1002/1097-4598(200007)23:7<1016::aid-mus3>3.0.co;2-w;
RA de Carvalho M., Moreira P., Evangelista T., Ducla-Soares J.L., Bento M.,
RA Fernandes R., Saraiva M.J.;
RT "New transthyretin mutation V28M in a Portuguese kindred with amyloid
RT polyneuropathy.";
RL Muscle Nerve 23:1016-1021(2000).
RN [118]
RP VARIANT AMYL-TTR GLU-73.
RX PubMed=11445644; DOI=10.1212/wnl.57.1.135;
RA Ellie E., Camou F., Vital A., Rummens C., Grateau G., Delpech M.,
RA Valleix S.;
RT "Recurrent subarachnoid hemorrhage associated with a new transthyretin
RT variant (Gly53Glu).";
RL Neurology 57:135-137(2001).
RN [119]
RP VARIANT AMYL-TTR GLN-75.
RX PubMed=12557757; DOI=10.3109/13506120209114105;
RA Yazaki M., Varga J., Dyck P.J., Benson M.D.;
RT "A new transthyretin variant Leu55Gln in a patient with systemic
RT amyloidosis.";
RL Amyloid 9:268-271(2002).
RN [120]
RP VARIANTS SER-26 AND MET-139, VARIANTS AMYL-TTR ALA-58; LEU-61; SER-64 AND
RP LEU-84, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11866053; DOI=10.1021/ac010780+;
RA Lim A., Prokaeva T., McComb M.E., O'Connor P.B., Theberge R., Connors L.H.,
RA Skinner M., Costello C.E.;
RT "Characterization of transthyretin variants in familial transthyretin
RT amyloidosis by mass spectrometric peptide mapping and DNA sequence
RT analysis.";
RL Anal. Chem. 74:741-751(2002).
RN [121]
RP VARIANTS AMYL-TTR MET-50; LEU-53; VAL-53; VAL-58; GLU-67; ALA-80; SER-140
RP AND ILE-142.
RX PubMed=12050338; DOI=10.1056/nejmoa013354;
RA Lachmann H.J., Booth D.R., Booth S.E., Bybee A., Gilbertson J.A.,
RA Gillmore J.D., Pepys M.B., Hawkins P.N.;
RT "Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis.";
RL N. Engl. J. Med. 346:1786-1791(2002).
RN [122]
RP VARIANT AMYL-TTR HIS-89.
RX PubMed=12771253; DOI=10.1212/01.wnl.0000065901.18353.ab;
RA Blevins G., Macaulay R., Harder S., Fladeland D., Yamashita T., Yazaki M.,
RA Hamidi Asl K., Benson M.D., Donat J.R.;
RT "Oculoleptomeningeal amyloidosis in a large kindred with a new
RT transthyretin variant Tyr69His.";
RL Neurology 60:1625-1630(2003).
RN [123]
RP VARIANT CYS-53, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12876326; DOI=10.1110/ps.0349703;
RA Lim A., Prokaeva T., McComb M.E., Connors L.H., Skinner M., Costello C.E.;
RT "Identification of S-sulfonation and S-thiolation of a novel transthyretin
RT Phe33Cys variant from a patient diagnosed with familial transthyretin
RT amyloidosis.";
RL Protein Sci. 12:1775-1785(2003).
RN [124]
RP VARIANT AMYL-TTR LYS-74.
RX PubMed=15214015; DOI=10.1002/ajmg.a.30007;
RA Busse A., Sanchez M.A., Monterroso V., Alvarado M.V., Leon P.;
RT "A severe form of amyloidotic polyneuropathy in a Costa Rican family with a
RT rare transthyretin mutation (Glu54Lys).";
RL Am. J. Med. Genet. A 128:190-194(2004).
RN [125]
RP VARIANT AMYL-TTR VAL-53.
RX PubMed=15478468; DOI=10.1080/13506120410001727767;
RA Frigerio R., Fabrizi G.M., Ferrarini M., Cavallaro T., Brighina L.,
RA Santoro P., Agostoni E., Cavaletti G., Rizzuto N., Ferrarese C.;
RT "An unusual transthyretin gene missense mutation (TTR Phe33Val) linked to
RT familial amyloidotic polyneuropathy.";
RL Amyloid 11:121-124(2004).
RN [126]
RP VARIANTS SER-26; CYS-53 AND ALA-114, VARIANTS AMYL-TTR GLU-67; HIS-78;
RP ALA-80 AND TYR-97, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15217993; DOI=10.1373/clinchem.2004.033266;
RA Bergen H.R. III, Zeldenrust S.R., Butz M.L., Snow D.S., Dyck P.J.,
RA Dyck P.J.B., Klein C.J., O'Brien J.F., Thibodeau S.N., Muddiman D.C.;
RT "Identification of transthyretin variants by sequential proteomic and
RT genomic analysis.";
RL Clin. Chem. 50:1544-1552(2004).
RN [127]
RP VARIANT AMYL-TTR GLY-81.
RX PubMed=17453626; DOI=10.1080/13506120601116625;
RA Rosenzweig M., Skinner M., Prokaeva T., Theberge R., Costello C.,
RA Drachman B.M., Connors L.H.;
RT "A new transthyretin variant (Glu61Gly) associated with cardiomyopathy.";
RL Amyloid 14:65-71(2007).
RN [128]
RP VARIANT AMYL-TTR SER-144.
RX PubMed=17577687; DOI=10.1080/13506120701259895;
RA Bergstroem J., Patrosso M.C., Colussi G., Salvadore M., Penco S., Lando G.,
RA Marocchi A., Ueda A., Nakamura M., Ando Y.;
RT "A novel type of familial transthyretin amyloidosis, ATTR Asn124Ser, with
RT co-localization of kappa light chains.";
RL Amyloid 14:141-145(2007).
RN [129]
RP VARIANTS AMYL-TTR PRO-32; ILE-40; SER-44; ALA-50; MET-50; LEU-53; VAL-53;
RP PRO-56; THR-65; ALA-67; ALA-69; ILE-69; ALA-80; LEU-84; LEU-88; ALA-91;
RP TYR-97; PHE-98; SER-104; ASN-104; THR-104; ALA-114; GLY-117; ASN-126;
RP MET-127; VAL-127; MET-131 AND ILE-142, VARIANTS ILE-33; SER-121 AND
RP THR-129, AND VARIANT CHICAGO MET-139.
RX PubMed=17503405; DOI=10.1002/elps.200600840;
RA Altland K., Benson M.D., Costello C.E., Ferlini A., Hazenberg B.P.C.,
RA Hund E., Kristen A.V., Linke R.P., Merlini G., Salvi F., Saraiva M.J.,
RA Singer R., Skinner M., Winter P.;
RT "Genetic microheterogeneity of human transthyretin detected by IEF.";
RL Electrophoresis 28:2053-2064(2007).
RN [130]
RP VARIANT AMYL-TTR VAL-58.
RX PubMed=17635579; DOI=10.1111/j.1365-2362.2007.01836.x;
RA Augustin S., Llige D., Andreu A., Gonzalez A., Genesca J.;
RT "Familial amyloidosis in a large Spanish kindred resulting from a D38V
RT mutation in the transthyretin gene.";
RL Eur. J. Clin. Invest. 37:673-678(2007).
RN [131]
RP VARIANT AMYL-TTR ARG-70.
RX PubMed=23317988; DOI=10.1016/j.jaad.2012.07.026;
RA Dekmezian M.S., Tschen J.A., Cho-Vega J.H.;
RT "Delayed diagnosis of transthyretin amyloidosis with a novel mutation
RT (c.210T>A) in the transthyretin gene.";
RL J. Am. Acad. Dermatol. 68:E49-E51(2013).
CC -!- FUNCTION: Thyroid hormone-binding protein. Probably transports
CC thyroxine from the bloodstream to the brain.
CC {ECO:0000269|PubMed:3714052}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. In the homotetramer, subunits
CC assemble around a central channel that can accommodate two ligand
CC molecules. Interacts with RBP4. {ECO:0000269|PubMed:10052934,
CC ECO:0000269|PubMed:11243784, ECO:0000269|PubMed:11560492,
CC ECO:0000269|PubMed:12820260, ECO:0000269|PubMed:14583036,
CC ECO:0000269|PubMed:14711308, ECO:0000269|PubMed:15735344,
CC ECO:0000269|PubMed:15769474, ECO:0000269|PubMed:15826192,
CC ECO:0000269|PubMed:18095641, ECO:0000269|PubMed:18155178,
CC ECO:0000269|PubMed:18811132, ECO:0000269|PubMed:19021760}.
CC -!- INTERACTION:
CC P02766; Q15109: AGER; NbExp=2; IntAct=EBI-711909, EBI-1646426;
CC P02766; P05067: APP; NbExp=3; IntAct=EBI-711909, EBI-77613;
CC P02766; PRO_0000000092 [P05067]: APP; NbExp=2; IntAct=EBI-711909, EBI-821758;
CC P02766; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-711909, EBI-2875816;
CC P02766; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-711909, EBI-14199987;
CC P02766; P18848: ATF4; NbExp=3; IntAct=EBI-711909, EBI-492498;
CC P02766; Q9Y2D1: ATF5; NbExp=3; IntAct=EBI-711909, EBI-492509;
CC P02766; P15313: ATP6V1B1; NbExp=3; IntAct=EBI-711909, EBI-2891281;
CC P02766; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-711909, EBI-741210;
CC P02766; Q8N163: CCAR2; NbExp=3; IntAct=EBI-711909, EBI-355410;
CC P02766; Q01850: CDR2; NbExp=3; IntAct=EBI-711909, EBI-1181367;
CC P02766; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-711909, EBI-11953200;
CC P02766; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-711909, EBI-744045;
CC P02766; Q9Y240: CLEC11A; NbExp=3; IntAct=EBI-711909, EBI-3957044;
CC P02766; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-711909, EBI-25836090;
CC P02766; Q96MW5: COG8; NbExp=3; IntAct=EBI-711909, EBI-720875;
CC P02766; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-711909, EBI-350590;
CC P02766; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-711909, EBI-10213520;
CC P02766; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-711909, EBI-25835236;
CC P02766; Q9UHY8: FEZ2; NbExp=3; IntAct=EBI-711909, EBI-396453;
CC P02766; Q7Z602: GPR141; NbExp=3; IntAct=EBI-711909, EBI-21649723;
CC P02766; P68431: H3C12; NbExp=3; IntAct=EBI-711909, EBI-79722;
CC P02766; Q86U28: ISCA2; NbExp=3; IntAct=EBI-711909, EBI-10258659;
CC P02766; Q96SI1-2: KCTD15; NbExp=3; IntAct=EBI-711909, EBI-12382297;
CC P02766; Q06136: KDSR; NbExp=3; IntAct=EBI-711909, EBI-3909166;
CC P02766; Q12756: KIF1A; NbExp=3; IntAct=EBI-711909, EBI-2679809;
CC P02766; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-711909, EBI-714379;
CC P02766; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-711909, EBI-8487781;
CC P02766; P41218: MNDA; NbExp=3; IntAct=EBI-711909, EBI-2829677;
CC P02766; P25713: MT3; NbExp=3; IntAct=EBI-711909, EBI-8084264;
CC P02766; Q16718: NDUFA5; NbExp=3; IntAct=EBI-711909, EBI-746417;
CC P02766; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-711909, EBI-10172876;
CC P02766; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-711909, EBI-1059321;
CC P02766; Q96FW1: OTUB1; NbExp=4; IntAct=EBI-711909, EBI-1058491;
CC P02766; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-711909, EBI-25830200;
CC P02766; O75781-2: PALM; NbExp=3; IntAct=EBI-711909, EBI-16399860;
CC P02766; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-711909, EBI-2513978;
CC P02766; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-711909, EBI-9090282;
CC P02766; P11908: PRPS2; NbExp=3; IntAct=EBI-711909, EBI-4290895;
CC P02766; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-711909, EBI-25830870;
CC P02766; P02753: RBP4; NbExp=4; IntAct=EBI-711909, EBI-2116134;
CC P02766; Q96D59: RNF183; NbExp=3; IntAct=EBI-711909, EBI-743938;
CC P02766; Q9C004: SPRY4; NbExp=3; IntAct=EBI-711909, EBI-354861;
CC P02766; Q8IXS7: SRGAP3; NbExp=3; IntAct=EBI-711909, EBI-18616594;
CC P02766; Q8NBJ7: SUMF2; NbExp=3; IntAct=EBI-711909, EBI-723091;
CC P02766; Q8WUA7-2: TBC1D22A; NbExp=3; IntAct=EBI-711909, EBI-21575846;
CC P02766; Q13569: TDG; NbExp=3; IntAct=EBI-711909, EBI-348333;
CC P02766; P21980-2: TGM2; NbExp=3; IntAct=EBI-711909, EBI-25842075;
CC P02766; A0AVI4-2: TMEM129; NbExp=3; IntAct=EBI-711909, EBI-25871541;
CC P02766; P02766: TTR; NbExp=11; IntAct=EBI-711909, EBI-711909;
CC P02766; Q969T4: UBE2E3; NbExp=3; IntAct=EBI-711909, EBI-348496;
CC P02766; O95164: UBL3; NbExp=3; IntAct=EBI-711909, EBI-12876508;
CC P02766; Q8IWV7: UBR1; NbExp=3; IntAct=EBI-711909, EBI-711736;
CC P02766; P45880: VDAC2; NbExp=3; IntAct=EBI-711909, EBI-354022;
CC P02766; P58304: VSX2; NbExp=3; IntAct=EBI-711909, EBI-6427899;
CC P02766; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-711909, EBI-7705033;
CC P02766; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-711909, EBI-1538838;
CC P02766; Q86V28; NbExp=3; IntAct=EBI-711909, EBI-10259496;
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm.
CC -!- TISSUE SPECIFICITY: Detected in serum and cerebrospinal fluid (at
CC protein level). Highly expressed in choroid plexus epithelial cells.
CC Detected in retina pigment epithelium and liver.
CC {ECO:0000269|PubMed:10328977, ECO:0000269|PubMed:3714052}.
CC -!- DOMAIN: Each monomer has two 4-stranded beta sheets and the shape of a
CC prolate ellipsoid. Antiparallel beta-sheet interactions link monomers
CC into dimers. A short loop from each monomer forms the main dimer-dimer
CC interaction. These two pairs of loops separate the opposed, convex
CC beta-sheets of the dimers to form an internal channel.
CC -!- PTM: Not glycosylated under normal conditions. Following unfolding,
CC caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118
CC site is exposed and glycosylated by STT3B-containing OST complex,
CC leading to its degradation by the ER-associated degradation (ERAD)
CC pathway. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:19167329}.
CC -!- DISEASE: Amyloidosis, transthyretin-related (AMYL-TTR) [MIM:105210]: A
CC hereditary generalized amyloidosis due to transthyretin amyloid
CC deposition. Protein fibrils can form in different tissues leading to
CC amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel
CC syndrome, systemic senile amyloidosis. The disease includes
CC leptomeningeal amyloidosis that is characterized by primary involvement
CC of the central nervous system. Neuropathologic examination shows
CC amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and
CC subpial deposits. Some patients also develop vitreous amyloid
CC deposition that leads to visual impairment (oculoleptomeningeal
CC amyloidosis). Clinical features include seizures, stroke-like episodes,
CC dementia, psychomotor deterioration, variable amyloid deposition in the
CC vitreous humor. {ECO:0000269|PubMed:10036587,
CC ECO:0000269|PubMed:10071047, ECO:0000269|PubMed:10211412,
CC ECO:0000269|PubMed:10436378, ECO:0000269|PubMed:10439117,
CC ECO:0000269|PubMed:10611950, ECO:0000269|PubMed:10627135,
CC ECO:0000269|PubMed:10694917, ECO:0000269|PubMed:10842705,
CC ECO:0000269|PubMed:10842718, ECO:0000269|PubMed:10882995,
CC ECO:0000269|PubMed:11243784, ECO:0000269|PubMed:11445644,
CC ECO:0000269|PubMed:11866053, ECO:0000269|PubMed:12050338,
CC ECO:0000269|PubMed:12403615, ECO:0000269|PubMed:12557757,
CC ECO:0000269|PubMed:12771253, ECO:0000269|PubMed:1301926,
CC ECO:0000269|PubMed:1351039, ECO:0000269|PubMed:1362222,
CC ECO:0000269|PubMed:1436517, ECO:0000269|PubMed:1517749,
CC ECO:0000269|PubMed:1520326, ECO:0000269|PubMed:1520336,
CC ECO:0000269|PubMed:15214015, ECO:0000269|PubMed:15217993,
CC ECO:0000269|PubMed:1544214, ECO:0000269|PubMed:15478468,
CC ECO:0000269|PubMed:1570831, ECO:0000269|PubMed:15735344,
CC ECO:0000269|PubMed:16185074, ECO:0000269|PubMed:1656975,
CC ECO:0000269|PubMed:16627944, ECO:0000269|PubMed:1734866,
CC ECO:0000269|PubMed:17453626, ECO:0000269|PubMed:17503405,
CC ECO:0000269|PubMed:17577687, ECO:0000269|PubMed:17635579,
CC ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:1932142,
CC ECO:0000269|PubMed:2046936, ECO:0000269|PubMed:2161654,
CC ECO:0000269|PubMed:23317988, ECO:0000269|PubMed:2363717,
CC ECO:0000269|PubMed:2891727, ECO:0000269|PubMed:3022108,
CC ECO:0000269|PubMed:3135807, ECO:0000269|PubMed:3722385,
CC ECO:0000269|PubMed:3818577, ECO:0000269|PubMed:6487335,
CC ECO:0000269|PubMed:6583672, ECO:0000269|PubMed:6651852,
CC ECO:0000269|PubMed:7655883, ECO:0000269|PubMed:7850982,
CC ECO:0000269|PubMed:7910950, ECO:0000269|PubMed:7914929,
CC ECO:0000269|PubMed:7923855, ECO:0000269|PubMed:8019560,
CC ECO:0000269|PubMed:8038017, ECO:0000269|PubMed:8081397,
CC ECO:0000269|PubMed:8095302, ECO:0000269|PubMed:8133316,
CC ECO:0000269|PubMed:8257997, ECO:0000269|PubMed:8352764,
CC ECO:0000269|PubMed:8382610, ECO:0000269|PubMed:8428915,
CC ECO:0000269|PubMed:8579098, ECO:0000269|PubMed:8990019,
CC ECO:0000269|PubMed:9066351, ECO:0000269|PubMed:9605286,
CC ECO:0000269|PubMed:9733771, ECO:0000269|Ref.90}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Hyperthyroxinemia, dystransthyretinemic (DTTRH) [MIM:145680]:
CC A condition characterized by elevation of total and free thyroxine in
CC healthy, euthyroid persons without detectable binding protein
CC abnormalities. {ECO:0000269|PubMed:1979335}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Carpal tunnel syndrome 1 (CTS1) [MIM:115430]: A condition
CC characterized by entrapment of the median nerve within the carpal
CC tunnel. Symptoms include burning pain and paresthesias involving the
CC ventral surface of the hand and fingers which may radiate proximally.
CC Impairment of sensation in the distribution of the median nerve and
CC thenar muscle atrophy may occur. This condition may be associated with
CC repetitive occupational trauma, wrist injuries, amyloid neuropathies,
CC rheumatoid arthritis. {ECO:0000269|PubMed:8309582}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Tetramer dissociation and partial unfolding leads to the
CC formation of aggregates and amyloid fibrils. Small molecules that
CC occupy at least one of the thyroid hormone binding sites stabilize the
CC tetramer, and thereby stabilize the native state and protect against
CC misfolding and the formation of amyloid fibrils.
CC -!- MISCELLANEOUS: Two binding sites for thyroxine are located in the
CC channel. Less than 1% of plasma prealbumin molecules are normally
CC involved in thyroxine transport. L-thyroxine binds to the transthyretin
CC by an order of magnitude stronger than does the triiodo-L-thyronine.
CC Thyroxine-binding globulin is the major carrier protein for thyroid
CC hormones in man.
CC -!- MISCELLANEOUS: About 40% of plasma transthyretin circulates in a tight
CC protein-protein complex with the plasma retinol-binding protein (RBP).
CC The formation of the complex with RBP stabilizes the binding of retinol
CC to RBP and decreases the glomerular filtration and renal catabolism of
CC the relatively small RBP molecule. There is evidence for 2 binding
CC sites for RBP, one possibly being a region that includes Ile-104,
CC located on the outer surface of the transthyretin molecule.
CC -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Transthyretin entry;
CC URL="https://en.wikipedia.org/wiki/Transthyretin";
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DR EMBL; K02091; AAA60011.1; -; mRNA.
DR EMBL; M10605; AAA60012.1; -; mRNA.
DR EMBL; M11518; AAA98771.1; -; Genomic_DNA.
DR EMBL; M11844; AAA60013.1; -; Genomic_DNA.
DR EMBL; X59498; CAA42087.1; -; mRNA.
DR EMBL; D00096; BAA00059.1; -; mRNA.
DR EMBL; M15517; AAA60018.1; -; Genomic_DNA.
DR EMBL; M15515; AAA60018.1; JOINED; Genomic_DNA.
DR EMBL; M15516; AAA60018.1; JOINED; Genomic_DNA.
DR EMBL; U19780; AAA73473.1; -; mRNA.
DR EMBL; AF162690; AAD45014.1; -; mRNA.
DR EMBL; AK312051; BAG34987.1; -; mRNA.
DR EMBL; BT007189; AAP35853.1; -; mRNA.
DR EMBL; CR456908; CAG33189.1; -; mRNA.
DR EMBL; CH471088; EAX01264.1; -; Genomic_DNA.
DR EMBL; BC005310; AAH05310.1; -; mRNA.
DR EMBL; BC020791; AAH20791.1; -; mRNA.
DR EMBL; S63185; AAD14937.2; -; Genomic_DNA.
DR EMBL; S72385; AAD14098.1; -; Genomic_DNA.
DR EMBL; M11714; AAA61181.1; -; mRNA.
DR EMBL; M63285; AAA36784.1; -; Genomic_DNA.
DR CCDS; CCDS11899.1; -.
DR PIR; A91532; VBHU.
DR RefSeq; NP_000362.1; NM_000371.3.
DR PDB; 1BM7; X-ray; 2.00 A; A/B=21-147.
DR PDB; 1BMZ; X-ray; 2.00 A; A/B=21-147.
DR PDB; 1BZ8; X-ray; 2.00 A; A/B=21-147.
DR PDB; 1BZD; X-ray; 1.90 A; A/B=21-147.
DR PDB; 1BZE; X-ray; 1.80 A; A/B=21-147.
DR PDB; 1DVQ; X-ray; 2.00 A; A/B=21-144.
DR PDB; 1DVS; X-ray; 2.00 A; A/B=21-144.
DR PDB; 1DVT; X-ray; 1.90 A; A/B=21-144.
DR PDB; 1DVU; X-ray; 1.90 A; A/B=21-144.
DR PDB; 1DVX; X-ray; 2.00 A; A/B=21-144.
DR PDB; 1DVY; X-ray; 1.90 A; A/B=21-144.
DR PDB; 1DVZ; X-ray; 1.90 A; A/B=21-144.
DR PDB; 1E3F; X-ray; 1.90 A; A/B=21-147.
DR PDB; 1E4H; X-ray; 1.80 A; A/B=21-147.
DR PDB; 1E5A; X-ray; 1.80 A; A/B=21-147.
DR PDB; 1ETA; X-ray; 1.70 A; 1/2=21-147.
DR PDB; 1ETB; X-ray; 1.70 A; 1/2=21-147.
DR PDB; 1F41; X-ray; 1.30 A; A/B=21-147.
DR PDB; 1F86; X-ray; 1.10 A; A/B=30-144.
DR PDB; 1FH2; X-ray; 1.80 A; A/B=21-147.
DR PDB; 1FHN; X-ray; 1.75 A; A/B=21-147.
DR PDB; 1G1O; X-ray; 2.30 A; A/B/C/D=21-147.
DR PDB; 1GKO; X-ray; 2.10 A; A/B/C/D=21-147.
DR PDB; 1ICT; X-ray; 3.00 A; A/B/C/D/E/F/G/H=21-147.
DR PDB; 1III; X-ray; 2.00 A; A/B=21-147.
DR PDB; 1IIK; X-ray; 2.00 A; A/B=21-147.
DR PDB; 1IJN; X-ray; 1.70 A; A/B=21-147.
DR PDB; 1QAB; X-ray; 3.20 A; A/B/C/D=21-147.
DR PDB; 1QWH; X-ray; 1.36 A; A/B=31-147.
DR PDB; 1RLB; X-ray; 3.10 A; A/B/C/D=21-147.
DR PDB; 1SOK; X-ray; 1.60 A; A/B=21-147.
DR PDB; 1SOQ; X-ray; 2.10 A; A/B/C/D=21-147.
DR PDB; 1THA; X-ray; 2.00 A; A/B=21-147.
DR PDB; 1THC; X-ray; 2.30 A; A/B=21-147.
DR PDB; 1TLM; X-ray; 1.90 A; A/B=21-147.
DR PDB; 1TSH; X-ray; 1.70 A; A/B=21-147.
DR PDB; 1TT6; X-ray; 1.80 A; A/B=21-147.
DR PDB; 1TTA; X-ray; 1.70 A; A/B=21-147.
DR PDB; 1TTB; X-ray; 1.70 A; A/B=21-147.
DR PDB; 1TTC; X-ray; 1.70 A; A/B=21-147.
DR PDB; 1TTR; X-ray; 1.90 A; A/B=21-147.
DR PDB; 1TYR; X-ray; 1.80 A; A/B=21-147.
DR PDB; 1TZ8; X-ray; 1.85 A; A/B/C/D=21-147.
DR PDB; 1U21; X-ray; 1.69 A; A/B=21-147.
DR PDB; 1X7S; X-ray; 1.55 A; A/B=21-147.
DR PDB; 1X7T; X-ray; 1.60 A; A/B=21-147.
DR PDB; 1Y1D; X-ray; 1.70 A; A/B=21-147.
DR PDB; 1Z7J; X-ray; 2.20 A; A/B=21-147.
DR PDB; 1ZCR; X-ray; 1.80 A; A/B=21-147.
DR PDB; 1ZD6; X-ray; 1.90 A; A/B=21-147.
DR PDB; 2B14; X-ray; 2.00 A; A/B=21-147.
DR PDB; 2B15; X-ray; 1.70 A; A/B=21-147.
DR PDB; 2B16; X-ray; 1.75 A; A/B=21-147.
DR PDB; 2B77; X-ray; 1.70 A; A/B=21-147.
DR PDB; 2B9A; X-ray; 1.54 A; A/B=21-147.
DR PDB; 2F7I; X-ray; 1.60 A; A/B=21-147.
DR PDB; 2F8I; X-ray; 1.54 A; A/B=21-147.
DR PDB; 2FBR; X-ray; 1.46 A; A/B=21-147.
DR PDB; 2FLM; X-ray; 1.65 A; A/B=21-147.
DR PDB; 2G3X; X-ray; 1.58 A; A/B=21-147.
DR PDB; 2G3Z; X-ray; 1.90 A; A/B=21-147.
DR PDB; 2G4E; X-ray; 2.17 A; A/B=21-147.
DR PDB; 2G4G; X-ray; 1.85 A; A/B=21-147.
DR PDB; 2G5U; X-ray; 1.80 A; A/B=21-147.
DR PDB; 2G9K; X-ray; 1.85 A; A/B=21-147.
DR PDB; 2GAB; X-ray; 1.85 A; A/B=21-147.
DR PDB; 2H4E; X-ray; 1.45 A; A/B=21-147.
DR PDB; 2M5N; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=125-135.
DR PDB; 2NBO; NMR; -; A=21-147.
DR PDB; 2NBP; NMR; -; A=21-147.
DR PDB; 2NOY; X-ray; 1.80 A; A/B=21-147.
DR PDB; 2PAB; X-ray; 1.80 A; A/B=21-147.
DR PDB; 2QEL; X-ray; 2.29 A; A/B/C/D=21-147.
DR PDB; 2QGB; X-ray; 1.40 A; A/B=21-147.
DR PDB; 2QGC; X-ray; 1.30 A; A/B=21-147.
DR PDB; 2QGD; X-ray; 1.50 A; A/B=21-147.
DR PDB; 2QGE; X-ray; 1.45 A; A/B=21-147.
DR PDB; 2ROX; X-ray; 2.00 A; A/B=21-147.
DR PDB; 2ROY; X-ray; 2.20 A; A/B=21-147.
DR PDB; 2TRH; X-ray; 1.90 A; A/B=21-147.
DR PDB; 2TRY; X-ray; 2.00 A; A/B=21-147.
DR PDB; 2WQA; X-ray; 2.85 A; A/B/C/D=21-147.
DR PDB; 3A4D; X-ray; 2.00 A; A/B=21-147.
DR PDB; 3A4E; X-ray; 1.70 A; A/B=21-147.
DR PDB; 3A4F; X-ray; 1.99 A; A/B=21-147.
DR PDB; 3B56; X-ray; 1.55 A; A/B=21-147.
DR PDB; 3BSZ; X-ray; 3.38 A; A/B/C/D=21-147.
DR PDB; 3BT0; X-ray; 1.59 A; A/B=21-147.
DR PDB; 3CBR; X-ray; 1.70 A; A/B=21-147.
DR PDB; 3CFM; X-ray; 1.60 A; A/B=30-147.
DR PDB; 3CFN; X-ray; 1.87 A; A/B=30-147.
DR PDB; 3CFQ; X-ray; 2.09 A; A/B=30-147.
DR PDB; 3CFT; X-ray; 1.87 A; A/B=30-147.
DR PDB; 3CN0; X-ray; 1.52 A; A/B=21-147.
DR PDB; 3CN1; X-ray; 1.52 A; A/B=21-147.
DR PDB; 3CN2; X-ray; 1.52 A; A/B=21-147.
DR PDB; 3CN3; X-ray; 1.80 A; A/B=21-147.
DR PDB; 3CN4; X-ray; 1.40 A; A/B=21-147.
DR PDB; 3CXF; X-ray; 2.30 A; A/B=21-147.
DR PDB; 3D2T; X-ray; 1.85 A; A/B=21-147.
DR PDB; 3D7P; X-ray; 1.72 A; A/B=21-147.
DR PDB; 3DGD; X-ray; 1.38 A; A/B/C/D=21-147.
DR PDB; 3DID; X-ray; 1.78 A; A/B/C/D=21-147.
DR PDB; 3DJR; X-ray; 2.02 A; A/B=21-147.
DR PDB; 3DJS; X-ray; 1.80 A; A/B=21-147.
DR PDB; 3DJT; X-ray; 2.30 A; A/B=21-147.
DR PDB; 3DJZ; X-ray; 1.82 A; A/B=21-147.
DR PDB; 3DK0; X-ray; 1.87 A; A/B=21-147.
DR PDB; 3DK2; X-ray; 2.35 A; A/B=21-147.
DR PDB; 3DO4; X-ray; 2.40 A; A/B/C/D/E/F/G/H=21-147.
DR PDB; 3ESN; X-ray; 1.35 A; A/B=21-147.
DR PDB; 3ESO; X-ray; 1.31 A; A/B=21-147.
DR PDB; 3ESP; X-ray; 1.31 A; A/B=21-147.
DR PDB; 3FC8; X-ray; 1.85 A; A/B=21-144.
DR PDB; 3FCB; X-ray; 1.80 A; A/B=21-144.
DR PDB; 3GLZ; X-ray; 1.78 A; A/B=21-147.
DR PDB; 3GPS; X-ray; 1.78 A; A/B/C/D=21-147.
DR PDB; 3GRB; X-ray; 1.75 A; A/B/C/D=21-147.
DR PDB; 3GRG; X-ray; 1.90 A; A/B/C/D=21-147.
DR PDB; 3GS0; X-ray; 1.85 A; A/B=21-147.
DR PDB; 3GS4; X-ray; 1.78 A; A/B=21-147.
DR PDB; 3GS7; X-ray; 1.80 A; A/B=21-147.
DR PDB; 3HJ0; X-ray; 1.34 A; A/B=21-147.
DR PDB; 3I9A; X-ray; 1.65 A; A/B=21-147.
DR PDB; 3I9I; X-ray; 1.80 A; A/B=30-145.
DR PDB; 3I9P; X-ray; 1.90 A; A/B=30-145.
DR PDB; 3IMR; X-ray; 1.70 A; A/B=21-147.
DR PDB; 3IMS; X-ray; 1.40 A; A/B=21-147.
DR PDB; 3IMT; X-ray; 1.40 A; A/B=21-147.
DR PDB; 3IMU; X-ray; 1.40 A; A/B=21-147.
DR PDB; 3IMV; X-ray; 1.47 A; A/B=21-147.
DR PDB; 3IMW; X-ray; 1.31 A; A/B=21-147.
DR PDB; 3IPB; X-ray; 1.90 A; A/B=21-147.
DR PDB; 3IPE; X-ray; 1.40 A; A/B=21-147.
DR PDB; 3KGS; X-ray; 1.80 A; A/B=21-147.
DR PDB; 3KGT; X-ray; 1.95 A; A/B=21-147.
DR PDB; 3KGU; X-ray; 1.85 A; A/B=21-147.
DR PDB; 3M1O; X-ray; 1.20 A; A/B=21-147.
DR PDB; 3NEE; X-ray; 1.55 A; A/B=30-145.
DR PDB; 3NEO; X-ray; 2.00 A; A/B=30-145.
DR PDB; 3NES; X-ray; 1.75 A; A/B=30-145.
DR PDB; 3NEX; X-ray; 1.70 A; A/B=30-145.
DR PDB; 3NG5; X-ray; 1.70 A; A/B=21-147.
DR PDB; 3OZK; X-ray; 1.90 A; A/B=21-147.
DR PDB; 3OZL; X-ray; 1.90 A; A/B=21-147.
DR PDB; 3P3R; X-ray; 1.25 A; A/B=21-147.
DR PDB; 3P3S; X-ray; 1.60 A; A/B=21-147.
DR PDB; 3P3T; X-ray; 1.45 A; A/B=21-147.
DR PDB; 3P3U; X-ray; 1.50 A; A/B=21-147.
DR PDB; 3SSG; X-ray; 2.00 A; A=21-147.
DR PDB; 3TCT; X-ray; 1.30 A; A/B=21-147.
DR PDB; 3TFB; X-ray; 2.03 A; A/B=30-145.
DR PDB; 3U2I; X-ray; 1.70 A; A/B=32-147.
DR PDB; 3U2J; Neutron; 2.00 A; A/B=32-147.
DR PDB; 3W3B; X-ray; 1.90 A; A/B=21-147.
DR PDB; 4ABQ; X-ray; 1.70 A; A/B=21-144.
DR PDB; 4ABU; X-ray; 1.86 A; A/B=21-144.
DR PDB; 4ABV; X-ray; 1.80 A; A/B=21-144.
DR PDB; 4ABW; X-ray; 1.70 A; A/B=21-144.
DR PDB; 4AC2; X-ray; 1.81 A; A/B=21-144.
DR PDB; 4AC4; X-ray; 1.80 A; A/B=21-147.
DR PDB; 4ACT; X-ray; 1.80 A; A/B=21-147.
DR PDB; 4ANK; X-ray; 1.70 A; A/B=1-147.
DR PDB; 4D7B; X-ray; 1.15 A; A/B=21-147.
DR PDB; 4DER; X-ray; 1.90 A; A/B=30-145.
DR PDB; 4DES; X-ray; 1.75 A; A/B=30-145.
DR PDB; 4DET; X-ray; 2.05 A; A/B=30-145.
DR PDB; 4DEU; X-ray; 1.60 A; A/B=30-145.
DR PDB; 4DEW; X-ray; 1.90 A; A/B=1-147.
DR PDB; 4FI6; X-ray; 1.46 A; A/B=21-147.
DR PDB; 4FI7; X-ray; 1.40 A; A/B=21-147.
DR PDB; 4FI8; X-ray; 1.22 A; A/B=21-147.
DR PDB; 4HIQ; X-ray; 1.18 A; A/B=21-147.
DR PDB; 4HIS; X-ray; 1.20 A; A/B=21-147.
DR PDB; 4HJS; X-ray; 1.22 A; A/B=30-145.
DR PDB; 4HJT; X-ray; 1.45 A; A/B=21-147.
DR PDB; 4HJU; X-ray; 1.35 A; A/B=21-147.
DR PDB; 4I85; X-ray; 1.67 A; A/B=21-147.
DR PDB; 4I87; X-ray; 1.69 A; A/B=21-147.
DR PDB; 4I89; X-ray; 1.69 A; A/B=21-147.
DR PDB; 4IIZ; X-ray; 2.10 A; A/B=21-147.
DR PDB; 4IK6; X-ray; 2.00 A; A/B=21-147.
DR PDB; 4IK7; X-ray; 2.10 A; A/B=21-147.
DR PDB; 4IKI; X-ray; 2.00 A; A/B=21-147.
DR PDB; 4IKJ; X-ray; 2.10 A; A/B=21-147.
DR PDB; 4IKK; X-ray; 1.90 A; A/B=21-147.
DR PDB; 4IKL; X-ray; 1.90 A; A/B=21-147.
DR PDB; 4KY2; X-ray; 1.13 A; A/B=21-147.
DR PDB; 4L1S; X-ray; 1.50 A; A/B=21-147.
DR PDB; 4L1T; X-ray; 1.16 A; A/B=21-147.
DR PDB; 4MAS; X-ray; 1.22 A; A/B=21-147.
DR PDB; 4MRB; X-ray; 1.27 A; A/B=21-147.
DR PDB; 4MRC; X-ray; 1.54 A; A/B=22-147.
DR PDB; 4N85; X-ray; 1.60 A; A/B=1-147.
DR PDB; 4N86; X-ray; 2.00 A; A/B=1-147.
DR PDB; 4N87; X-ray; 1.79 A; A/B=1-147.
DR PDB; 4PM1; X-ray; 1.23 A; A/B=21-147.
DR PDB; 4PME; X-ray; 1.26 A; A/B=29-146.
DR PDB; 4PMF; X-ray; 1.35 A; A/B=29-145.
DR PDB; 4PVL; X-ray; 1.85 A; A/B=21-147.
DR PDB; 4PVM; Other; 2.00 A; A/B=21-147.
DR PDB; 4PVN; Other; 2.30 A; A/B=21-147.
DR PDB; 4PWE; X-ray; 1.40 A; A/B=1-147.
DR PDB; 4PWF; X-ray; 1.60 A; A/B=1-147.
DR PDB; 4PWG; X-ray; 1.80 A; A/B=1-147.
DR PDB; 4PWH; X-ray; 1.80 A; A/B=1-147.
DR PDB; 4PWI; X-ray; 1.49 A; A/B=1-147.
DR PDB; 4PWJ; X-ray; 1.55 A; A/B=1-147.
DR PDB; 4PWK; X-ray; 1.59 A; A/B=1-147.
DR PDB; 4QRF; X-ray; 1.80 A; A/B=1-147.
DR PDB; 4QXV; X-ray; 1.12 A; A/B=21-147.
DR PDB; 4QYA; X-ray; 1.70 A; A/B=21-147.
DR PDB; 4TKW; X-ray; 1.80 A; A/B=29-147.
DR PDB; 4TL4; X-ray; 1.75 A; A/B=29-147.
DR PDB; 4TL5; X-ray; 1.44 A; A/B=29-147.
DR PDB; 4TLK; X-ray; 1.44 A; A/B=29-147.
DR PDB; 4TLS; X-ray; 1.35 A; A/B=29-147.
DR PDB; 4TLT; X-ray; 1.70 A; A/B=29-147.
DR PDB; 4TLU; X-ray; 1.75 A; A/B=29-147.
DR PDB; 4TM9; X-ray; 1.70 A; A/B=29-147.
DR PDB; 4TNE; X-ray; 1.55 A; A/B=29-147.
DR PDB; 4TNF; X-ray; 1.60 A; A/B=29-147.
DR PDB; 4TNG; X-ray; 1.60 A; A/B=29-147.
DR PDB; 4TQ8; X-ray; 1.52 A; A/B=21-147.
DR PDB; 4TQH; X-ray; 1.51 A; A/B=21-147.
DR PDB; 4TQI; X-ray; 1.25 A; A/B=21-147.
DR PDB; 4TQP; X-ray; 1.58 A; A/B=21-147.
DR PDB; 4WNJ; X-ray; 1.40 A; A/B=21-147.
DR PDB; 4WNS; X-ray; 1.40 A; A/B=21-147.
DR PDB; 4WO0; X-ray; 1.34 A; A/B=21-147.
DR PDB; 4Y9B; X-ray; 1.40 A; A/B=1-147.
DR PDB; 4Y9C; X-ray; 1.49 A; A/B=1-147.
DR PDB; 4Y9E; X-ray; 1.49 A; A/B=1-147.
DR PDB; 4Y9F; X-ray; 1.50 A; A/B=1-147.
DR PDB; 4Y9G; X-ray; 1.89 A; A/B=1-147.
DR PDB; 4YDM; X-ray; 1.25 A; A/B=21-147.
DR PDB; 4YDN; X-ray; 1.35 A; A/B=21-147.
DR PDB; 5A6I; X-ray; 1.86 A; A=21-147.
DR PDB; 5AKS; X-ray; 1.25 A; A/B=21-147.
DR PDB; 5AKT; X-ray; 1.35 A; A/B=21-147.
DR PDB; 5AKV; X-ray; 1.52 A; A/B=21-147.
DR PDB; 5AL0; X-ray; 1.39 A; A/B=21-147.
DR PDB; 5AL8; X-ray; 1.50 A; A/B=21-147.
DR PDB; 5AYT; X-ray; 1.40 A; A/B=1-147.
DR PDB; 5BOJ; X-ray; 1.75 A; A/B=21-147.
DR PDB; 5CLX; X-ray; 1.28 A; A/B=21-147.
DR PDB; 5CLY; X-ray; 1.23 A; A/B=21-147.
DR PDB; 5CLZ; X-ray; 1.22 A; A/B=21-147.
DR PDB; 5CM1; X-ray; 1.22 A; A/B=21-147.
DR PDB; 5CN3; X-ray; 1.30 A; A/B=21-147.
DR PDB; 5CNH; X-ray; 1.42 A; A/B=21-147.
DR PDB; 5CR1; X-ray; 1.54 A; A/B=30-145.
DR PDB; 5DEJ; X-ray; 1.37 A; A/B=30-145.
DR PDB; 5DWP; X-ray; 1.20 A; A/B=30-145.
DR PDB; 5E23; X-ray; 1.41 A; A/B=21-147.
DR PDB; 5E4A; X-ray; 1.33 A; A/B=10-146.
DR PDB; 5E4O; X-ray; 1.50 A; A/B=30-146.
DR PDB; 5EN3; X-ray; 1.25 A; A/B=21-147.
DR PDB; 5EZP; X-ray; 2.50 A; A/B/C/D/E/F/G/H=26-147.
DR PDB; 5FO2; X-ray; 1.45 A; A/B=21-147.
DR PDB; 5FW6; X-ray; 1.30 A; A/B=21-147.
DR PDB; 5FW7; X-ray; 1.20 A; A/B=21-147.
DR PDB; 5FW8; X-ray; 1.60 A; A/B=21-147.
DR PDB; 5H0V; X-ray; 1.58 A; A/B/C/D=31-147.
DR PDB; 5H0W; X-ray; 1.90 A; A=31-147.
DR PDB; 5H0X; X-ray; 1.57 A; A/B=31-147.
DR PDB; 5H0Y; X-ray; 1.80 A; A=31-147.
DR PDB; 5H0Z; X-ray; 1.74 A; A=31-147.
DR PDB; 5HJG; X-ray; 1.40 A; A/B=21-147.
DR PDB; 5IHH; X-ray; 1.35 A; A/B=21-147.
DR PDB; 5JID; X-ray; 1.20 A; A/B=21-147.
DR PDB; 5JIM; X-ray; 1.26 A; A/B=21-147.
DR PDB; 5JIQ; X-ray; 1.45 A; A/B=21-147.
DR PDB; 5K1J; X-ray; 1.69 A; A/B=30-145.
DR PDB; 5K1N; X-ray; 1.81 A; A/B=30-147.
DR PDB; 5L4F; X-ray; 1.48 A; A/B=21-147.
DR PDB; 5L4I; X-ray; 1.45 A; A/B=21-147.
DR PDB; 5L4J; X-ray; 1.62 A; A/B=21-147.
DR PDB; 5L4M; X-ray; 1.58 A; A/B=21-147.
DR PDB; 5LLL; X-ray; 1.42 A; A/B=21-147.
DR PDB; 5LLV; X-ray; 1.70 A; A/B/C/D=21-147.
DR PDB; 5N5Q; X-ray; 2.53 A; A/B=30-145.
DR PDB; 5N62; X-ray; 1.80 A; A/B=30-146.
DR PDB; 5N7C; X-ray; 2.45 A; A/B=30-145.
DR PDB; 5NFE; Other; 1.85 A; A/B=21-147.
DR PDB; 5NFW; Other; 1.80 A; A/B=21-147.
DR PDB; 5OQ0; X-ray; 1.94 A; A=21-147.
DR PDB; 5TTR; X-ray; 2.70 A; A/B/C/D/E/F/G/H=21-147.
DR PDB; 5TZL; X-ray; 1.40 A; A/B=21-147.
DR PDB; 5U48; X-ray; 1.50 A; A/B=21-147.
DR PDB; 5U49; X-ray; 2.22 A; A=21-147.
DR PDB; 5U4A; X-ray; 1.90 A; A/B=21-147.
DR PDB; 5U4B; X-ray; 1.45 A; A/B=21-147.
DR PDB; 5U4C; X-ray; 1.70 A; A/B=21-147.
DR PDB; 5U4D; X-ray; 1.55 A; A/B=21-147.
DR PDB; 5U4E; X-ray; 1.45 A; A/B=21-147.
DR PDB; 5U4F; X-ray; 1.50 A; A/B=21-147.
DR PDB; 5U4G; X-ray; 1.80 A; A/B=21-147.
DR PDB; 6D0W; X-ray; 1.70 A; A/B=21-147.
DR PDB; 6E6Z; X-ray; 1.75 A; A/B=30-144.
DR PDB; 6E70; X-ray; 1.99 A; A/B=30-144.
DR PDB; 6E71; X-ray; 1.50 A; A/B=30-144.
DR PDB; 6E72; X-ray; 1.45 A; A/B=30-144.
DR PDB; 6E73; X-ray; 1.80 A; A/B=30-144.
DR PDB; 6E74; X-ray; 1.60 A; A/B=30-144.
DR PDB; 6E75; X-ray; 1.50 A; A/B=30-144.
DR PDB; 6E76; X-ray; 1.60 A; A/B=30-144.
DR PDB; 6E77; X-ray; 1.60 A; A/B=30-144.
DR PDB; 6E78; X-ray; 1.50 A; A/B=30-144.
DR PDB; 6EOY; X-ray; 1.38 A; A/B=30-144.
DR PDB; 6EP1; X-ray; 1.30 A; A/B=30-144.
DR PDB; 6FFT; Other; 2.00 A; A/B=21-147.
DR PDB; 6FWD; X-ray; 1.58 A; A/B=21-147.
DR PDB; 6FXU; X-ray; 1.36 A; A/B=21-147.
DR PDB; 6FZL; X-ray; 1.45 A; A/B=21-147.
DR PDB; 6GR7; X-ray; 1.40 A; A/B=21-147.
DR PDB; 6GRP; X-ray; 1.60 A; A/B=21-147.
DR PDB; 6IMX; X-ray; 1.60 A; A/B=1-147.
DR PDB; 6IMY; X-ray; 1.50 A; A/B=1-147.
DR PDB; 6KGB; X-ray; 1.30 A; A/B=1-146.
DR PDB; 6R66; X-ray; 1.30 A; A/B=1-147.
DR PDB; 6R67; X-ray; 1.30 A; A/B=1-147.
DR PDB; 6R68; X-ray; 1.45 A; A/B=1-147.
DR PDB; 6R6I; X-ray; 1.47 A; A/B=1-147.
DR PDB; 6SDZ; EM; 2.97 A; A/B/C/D/E/F/G/H/I/J/K=21-147.
DR PDB; 6SUG; X-ray; 1.21 A; A/B=1-147.
DR PDB; 6SUH; X-ray; 1.26 A; A/B=1-147.
DR PDB; 6TI9; X-ray; 1.45 A; A/B=21-147.
DR PDB; 6TJN; X-ray; 1.70 A; A/B=21-147.
DR PDB; 6TXV; X-ray; 1.60 A; A/B=30-145.
DR PDB; 6TXW; X-ray; 1.15 A; A/B=30-145.
DR PDB; 6U0Q; X-ray; 1.75 A; A/B=21-147.
DR PDB; 6XTK; X-ray; 1.70 A; A/B=30-145.
DR PDB; 7ACU; X-ray; 1.54 A; A/B=30-144.
DR PDB; 7DT3; X-ray; 1.20 A; A/B=1-147.
DR PDB; 7DT5; X-ray; 1.25 A; A/B=1-147.
DR PDB; 7DT6; X-ray; 1.30 A; A/B=1-147.
DR PDB; 7DT8; X-ray; 1.25 A; A/B=1-147.
DR PDB; 7EJQ; X-ray; 1.15 A; A/B=1-146.
DR PDB; 7EJR; X-ray; 1.45 A; A/B=1-146.
DR PDB; 7ERH; X-ray; 1.55 A; A/B=1-147.
DR PDB; 7ERI; X-ray; 1.81 A; A/B=1-147.
DR PDB; 7ERJ; X-ray; 1.89 A; A/B=1-147.
DR PDB; 7ERK; X-ray; 1.70 A; A/B=1-147.
DR PDB; 7OB4; EM; 3.22 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=21-147.
DR PDBsum; 1BM7; -.
DR PDBsum; 1BMZ; -.
DR PDBsum; 1BZ8; -.
DR PDBsum; 1BZD; -.
DR PDBsum; 1BZE; -.
DR PDBsum; 1DVQ; -.
DR PDBsum; 1DVS; -.
DR PDBsum; 1DVT; -.
DR PDBsum; 1DVU; -.
DR PDBsum; 1DVX; -.
DR PDBsum; 1DVY; -.
DR PDBsum; 1DVZ; -.
DR PDBsum; 1E3F; -.
DR PDBsum; 1E4H; -.
DR PDBsum; 1E5A; -.
DR PDBsum; 1ETA; -.
DR PDBsum; 1ETB; -.
DR PDBsum; 1F41; -.
DR PDBsum; 1F86; -.
DR PDBsum; 1FH2; -.
DR PDBsum; 1FHN; -.
DR PDBsum; 1G1O; -.
DR PDBsum; 1GKO; -.
DR PDBsum; 1ICT; -.
DR PDBsum; 1III; -.
DR PDBsum; 1IIK; -.
DR PDBsum; 1IJN; -.
DR PDBsum; 1QAB; -.
DR PDBsum; 1QWH; -.
DR PDBsum; 1RLB; -.
DR PDBsum; 1SOK; -.
DR PDBsum; 1SOQ; -.
DR PDBsum; 1THA; -.
DR PDBsum; 1THC; -.
DR PDBsum; 1TLM; -.
DR PDBsum; 1TSH; -.
DR PDBsum; 1TT6; -.
DR PDBsum; 1TTA; -.
DR PDBsum; 1TTB; -.
DR PDBsum; 1TTC; -.
DR PDBsum; 1TTR; -.
DR PDBsum; 1TYR; -.
DR PDBsum; 1TZ8; -.
DR PDBsum; 1U21; -.
DR PDBsum; 1X7S; -.
DR PDBsum; 1X7T; -.
DR PDBsum; 1Y1D; -.
DR PDBsum; 1Z7J; -.
DR PDBsum; 1ZCR; -.
DR PDBsum; 1ZD6; -.
DR PDBsum; 2B14; -.
DR PDBsum; 2B15; -.
DR PDBsum; 2B16; -.
DR PDBsum; 2B77; -.
DR PDBsum; 2B9A; -.
DR PDBsum; 2F7I; -.
DR PDBsum; 2F8I; -.
DR PDBsum; 2FBR; -.
DR PDBsum; 2FLM; -.
DR PDBsum; 2G3X; -.
DR PDBsum; 2G3Z; -.
DR PDBsum; 2G4E; -.
DR PDBsum; 2G4G; -.
DR PDBsum; 2G5U; -.
DR PDBsum; 2G9K; -.
DR PDBsum; 2GAB; -.
DR PDBsum; 2H4E; -.
DR PDBsum; 2M5N; -.
DR PDBsum; 2NBO; -.
DR PDBsum; 2NBP; -.
DR PDBsum; 2NOY; -.
DR PDBsum; 2PAB; -.
DR PDBsum; 2QEL; -.
DR PDBsum; 2QGB; -.
DR PDBsum; 2QGC; -.
DR PDBsum; 2QGD; -.
DR PDBsum; 2QGE; -.
DR PDBsum; 2ROX; -.
DR PDBsum; 2ROY; -.
DR PDBsum; 2TRH; -.
DR PDBsum; 2TRY; -.
DR PDBsum; 2WQA; -.
DR PDBsum; 3A4D; -.
DR PDBsum; 3A4E; -.
DR PDBsum; 3A4F; -.
DR PDBsum; 3B56; -.
DR PDBsum; 3BSZ; -.
DR PDBsum; 3BT0; -.
DR PDBsum; 3CBR; -.
DR PDBsum; 3CFM; -.
DR PDBsum; 3CFN; -.
DR PDBsum; 3CFQ; -.
DR PDBsum; 3CFT; -.
DR PDBsum; 3CN0; -.
DR PDBsum; 3CN1; -.
DR PDBsum; 3CN2; -.
DR PDBsum; 3CN3; -.
DR PDBsum; 3CN4; -.
DR PDBsum; 3CXF; -.
DR PDBsum; 3D2T; -.
DR PDBsum; 3D7P; -.
DR PDBsum; 3DGD; -.
DR PDBsum; 3DID; -.
DR PDBsum; 3DJR; -.
DR PDBsum; 3DJS; -.
DR PDBsum; 3DJT; -.
DR PDBsum; 3DJZ; -.
DR PDBsum; 3DK0; -.
DR PDBsum; 3DK2; -.
DR PDBsum; 3DO4; -.
DR PDBsum; 3ESN; -.
DR PDBsum; 3ESO; -.
DR PDBsum; 3ESP; -.
DR PDBsum; 3FC8; -.
DR PDBsum; 3FCB; -.
DR PDBsum; 3GLZ; -.
DR PDBsum; 3GPS; -.
DR PDBsum; 3GRB; -.
DR PDBsum; 3GRG; -.
DR PDBsum; 3GS0; -.
DR PDBsum; 3GS4; -.
DR PDBsum; 3GS7; -.
DR PDBsum; 3HJ0; -.
DR PDBsum; 3I9A; -.
DR PDBsum; 3I9I; -.
DR PDBsum; 3I9P; -.
DR PDBsum; 3IMR; -.
DR PDBsum; 3IMS; -.
DR PDBsum; 3IMT; -.
DR PDBsum; 3IMU; -.
DR PDBsum; 3IMV; -.
DR PDBsum; 3IMW; -.
DR PDBsum; 3IPB; -.
DR PDBsum; 3IPE; -.
DR PDBsum; 3KGS; -.
DR PDBsum; 3KGT; -.
DR PDBsum; 3KGU; -.
DR PDBsum; 3M1O; -.
DR PDBsum; 3NEE; -.
DR PDBsum; 3NEO; -.
DR PDBsum; 3NES; -.
DR PDBsum; 3NEX; -.
DR PDBsum; 3NG5; -.
DR PDBsum; 3OZK; -.
DR PDBsum; 3OZL; -.
DR PDBsum; 3P3R; -.
DR PDBsum; 3P3S; -.
DR PDBsum; 3P3T; -.
DR PDBsum; 3P3U; -.
DR PDBsum; 3SSG; -.
DR PDBsum; 3TCT; -.
DR PDBsum; 3TFB; -.
DR PDBsum; 3U2I; -.
DR PDBsum; 3U2J; -.
DR PDBsum; 3W3B; -.
DR PDBsum; 4ABQ; -.
DR PDBsum; 4ABU; -.
DR PDBsum; 4ABV; -.
DR PDBsum; 4ABW; -.
DR PDBsum; 4AC2; -.
DR PDBsum; 4AC4; -.
DR PDBsum; 4ACT; -.
DR PDBsum; 4ANK; -.
DR PDBsum; 4D7B; -.
DR PDBsum; 4DER; -.
DR PDBsum; 4DES; -.
DR PDBsum; 4DET; -.
DR PDBsum; 4DEU; -.
DR PDBsum; 4DEW; -.
DR PDBsum; 4FI6; -.
DR PDBsum; 4FI7; -.
DR PDBsum; 4FI8; -.
DR PDBsum; 4HIQ; -.
DR PDBsum; 4HIS; -.
DR PDBsum; 4HJS; -.
DR PDBsum; 4HJT; -.
DR PDBsum; 4HJU; -.
DR PDBsum; 4I85; -.
DR PDBsum; 4I87; -.
DR PDBsum; 4I89; -.
DR PDBsum; 4IIZ; -.
DR PDBsum; 4IK6; -.
DR PDBsum; 4IK7; -.
DR PDBsum; 4IKI; -.
DR PDBsum; 4IKJ; -.
DR PDBsum; 4IKK; -.
DR PDBsum; 4IKL; -.
DR PDBsum; 4KY2; -.
DR PDBsum; 4L1S; -.
DR PDBsum; 4L1T; -.
DR PDBsum; 4MAS; -.
DR PDBsum; 4MRB; -.
DR PDBsum; 4MRC; -.
DR PDBsum; 4N85; -.
DR PDBsum; 4N86; -.
DR PDBsum; 4N87; -.
DR PDBsum; 4PM1; -.
DR PDBsum; 4PME; -.
DR PDBsum; 4PMF; -.
DR PDBsum; 4PVL; -.
DR PDBsum; 4PVM; -.
DR PDBsum; 4PVN; -.
DR PDBsum; 4PWE; -.
DR PDBsum; 4PWF; -.
DR PDBsum; 4PWG; -.
DR PDBsum; 4PWH; -.
DR PDBsum; 4PWI; -.
DR PDBsum; 4PWJ; -.
DR PDBsum; 4PWK; -.
DR PDBsum; 4QRF; -.
DR PDBsum; 4QXV; -.
DR PDBsum; 4QYA; -.
DR PDBsum; 4TKW; -.
DR PDBsum; 4TL4; -.
DR PDBsum; 4TL5; -.
DR PDBsum; 4TLK; -.
DR PDBsum; 4TLS; -.
DR PDBsum; 4TLT; -.
DR PDBsum; 4TLU; -.
DR PDBsum; 4TM9; -.
DR PDBsum; 4TNE; -.
DR PDBsum; 4TNF; -.
DR PDBsum; 4TNG; -.
DR PDBsum; 4TQ8; -.
DR PDBsum; 4TQH; -.
DR PDBsum; 4TQI; -.
DR PDBsum; 4TQP; -.
DR PDBsum; 4WNJ; -.
DR PDBsum; 4WNS; -.
DR PDBsum; 4WO0; -.
DR PDBsum; 4Y9B; -.
DR PDBsum; 4Y9C; -.
DR PDBsum; 4Y9E; -.
DR PDBsum; 4Y9F; -.
DR PDBsum; 4Y9G; -.
DR PDBsum; 4YDM; -.
DR PDBsum; 4YDN; -.
DR PDBsum; 5A6I; -.
DR PDBsum; 5AKS; -.
DR PDBsum; 5AKT; -.
DR PDBsum; 5AKV; -.
DR PDBsum; 5AL0; -.
DR PDBsum; 5AL8; -.
DR PDBsum; 5AYT; -.
DR PDBsum; 5BOJ; -.
DR PDBsum; 5CLX; -.
DR PDBsum; 5CLY; -.
DR PDBsum; 5CLZ; -.
DR PDBsum; 5CM1; -.
DR PDBsum; 5CN3; -.
DR PDBsum; 5CNH; -.
DR PDBsum; 5CR1; -.
DR PDBsum; 5DEJ; -.
DR PDBsum; 5DWP; -.
DR PDBsum; 5E23; -.
DR PDBsum; 5E4A; -.
DR PDBsum; 5E4O; -.
DR PDBsum; 5EN3; -.
DR PDBsum; 5EZP; -.
DR PDBsum; 5FO2; -.
DR PDBsum; 5FW6; -.
DR PDBsum; 5FW7; -.
DR PDBsum; 5FW8; -.
DR PDBsum; 5H0V; -.
DR PDBsum; 5H0W; -.
DR PDBsum; 5H0X; -.
DR PDBsum; 5H0Y; -.
DR PDBsum; 5H0Z; -.
DR PDBsum; 5HJG; -.
DR PDBsum; 5IHH; -.
DR PDBsum; 5JID; -.
DR PDBsum; 5JIM; -.
DR PDBsum; 5JIQ; -.
DR PDBsum; 5K1J; -.
DR PDBsum; 5K1N; -.
DR PDBsum; 5L4F; -.
DR PDBsum; 5L4I; -.
DR PDBsum; 5L4J; -.
DR PDBsum; 5L4M; -.
DR PDBsum; 5LLL; -.
DR PDBsum; 5LLV; -.
DR PDBsum; 5N5Q; -.
DR PDBsum; 5N62; -.
DR PDBsum; 5N7C; -.
DR PDBsum; 5NFE; -.
DR PDBsum; 5NFW; -.
DR PDBsum; 5OQ0; -.
DR PDBsum; 5TTR; -.
DR PDBsum; 5TZL; -.
DR PDBsum; 5U48; -.
DR PDBsum; 5U49; -.
DR PDBsum; 5U4A; -.
DR PDBsum; 5U4B; -.
DR PDBsum; 5U4C; -.
DR PDBsum; 5U4D; -.
DR PDBsum; 5U4E; -.
DR PDBsum; 5U4F; -.
DR PDBsum; 5U4G; -.
DR PDBsum; 6D0W; -.
DR PDBsum; 6E6Z; -.
DR PDBsum; 6E70; -.
DR PDBsum; 6E71; -.
DR PDBsum; 6E72; -.
DR PDBsum; 6E73; -.
DR PDBsum; 6E74; -.
DR PDBsum; 6E75; -.
DR PDBsum; 6E76; -.
DR PDBsum; 6E77; -.
DR PDBsum; 6E78; -.
DR PDBsum; 6EOY; -.
DR PDBsum; 6EP1; -.
DR PDBsum; 6FFT; -.
DR PDBsum; 6FWD; -.
DR PDBsum; 6FXU; -.
DR PDBsum; 6FZL; -.
DR PDBsum; 6GR7; -.
DR PDBsum; 6GRP; -.
DR PDBsum; 6IMX; -.
DR PDBsum; 6IMY; -.
DR PDBsum; 6KGB; -.
DR PDBsum; 6R66; -.
DR PDBsum; 6R67; -.
DR PDBsum; 6R68; -.
DR PDBsum; 6R6I; -.
DR PDBsum; 6SDZ; -.
DR PDBsum; 6SUG; -.
DR PDBsum; 6SUH; -.
DR PDBsum; 6TI9; -.
DR PDBsum; 6TJN; -.
DR PDBsum; 6TXV; -.
DR PDBsum; 6TXW; -.
DR PDBsum; 6U0Q; -.
DR PDBsum; 6XTK; -.
DR PDBsum; 7ACU; -.
DR PDBsum; 7DT3; -.
DR PDBsum; 7DT5; -.
DR PDBsum; 7DT6; -.
DR PDBsum; 7DT8; -.
DR PDBsum; 7EJQ; -.
DR PDBsum; 7EJR; -.
DR PDBsum; 7ERH; -.
DR PDBsum; 7ERI; -.
DR PDBsum; 7ERJ; -.
DR PDBsum; 7ERK; -.
DR PDBsum; 7OB4; -.
DR AlphaFoldDB; P02766; -.
DR BMRB; P02766; -.
DR PCDDB; P02766; -.
DR SMR; P02766; -.
DR BioGRID; 113127; 99.
DR CORUM; P02766; -.
DR DIP; DIP-1083N; -.
DR IntAct; P02766; 102.
DR MINT; P02766; -.
DR STRING; 9606.ENSP00000237014; -.
DR BindingDB; P02766; -.
DR ChEMBL; CHEMBL3194; -.
DR DrugBank; DB07201; (2S)-3-[(9H-fluoren-9-ylideneamino)oxy]-2-methylpropanoic acid.
DR DrugBank; DB07176; 1-Naphthylamine-5-sulfonic acid.
DR DrugBank; DB07047; 2',4'-DICHLORO-4-HYDROXY-1,1'-BIPHENYL-3-CARBOXYLIC ACID.
DR DrugBank; DB06935; 2',6'-DIFLUOROBIPHENYL-4-CARBOXYLIC ACID.
DR DrugBank; DB02417; 2,4,6-Tribromophenol.
DR DrugBank; DB07694; 2,5-dichloro-N-(3,5-dibromo-4-hydroxyphenyl)benzamide.
DR DrugBank; DB08101; 2,6-dibromo-4-[(E)-2-phenylethenyl]phenol.
DR DrugBank; DB08103; 2,6-dibromo-4-phenoxyphenol.
DR DrugBank; DB08100; 2,6-dimethyl-4-[(E)-2-phenylethenyl]phenol.
DR DrugBank; DB06907; 2-(2,6-DICHLOROPHENYL)-1,3-BENZOXAZOLE-6-CARBOXYLIC ACID.
DR DrugBank; DB08207; 2-(3,5-DIMETHYLPHENYL)-1,3-BENZOXAZOLE.
DR DrugBank; DB04756; 2-[(3,5-Dichloro-4-trioxidanylphenyl)amino]benzoic acid.
DR DrugBank; DB04674; 2-HYDROXY-3,5-DIIODOBENZOIC ACID.
DR DrugBank; DB07775; 3',5'-DIBROMO-2',4,4',6'-TETRAHYDROXY AURONE.
DR DrugBank; DB07753; 3',5'-DIFLUOROBIPHENYL-4-CARBOXYLIC ACID.
DR DrugBank; DB03239; 3',5'-Dinitro-N-Acetyl-L-Thyronine.
DR DrugBank; DB03346; 3,3',5,5'-tetrachlorobiphenyl-4,4'-diol.
DR DrugBank; DB08102; 3,5-dibromobiphenyl-4-ol.
DR DrugBank; DB07282; 3-({[(1Z)-(2-methoxyphenyl)methylidene]amino}oxy)propanoic acid.
DR DrugBank; DB07240; 3-[(9H-fluoren-9-ylideneamino)oxy]propanoic acid.
DR DrugBank; DB06885; 3-[({(1E)-[2-(trifluoromethyl)phenyl]methylidene}amino)oxy]propanoic acid.
DR DrugBank; DB08206; 4-(1,3-BENZOXAZOL-2-YL)-2,6-DIBROMOPHENOL.
DR DrugBank; DB08205; 4-(1,3-BENZOXAZOL-2-YL)-2,6-DIMETHYLPHENOL.
DR DrugBank; DB01838; 6,4'-Dihydroxy-3-Methyl-3',5'-Dibromoflavone.
DR DrugBank; DB04474; 8-anilinonaphthalene-1-sulfonic acid.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB03682; Dibenzofuran-4,6-Dicarboxylic Acid.
DR DrugBank; DB00586; Diclofenac.
DR DrugBank; DB00255; Diethylstilbestrol.
DR DrugBank; DB00861; Diflunisal.
DR DrugBank; DB01093; Dimethyl sulfoxide.
DR DrugBank; DB02266; Flufenamic acid.
DR DrugBank; DB05352; Fx-1006A.
DR DrugBank; DB01645; Genistein.
DR DrugBank; DB00451; Levothyroxine.
DR DrugBank; DB00279; Liothyronine.
DR DrugBank; DB01583; Liotrix.
DR DrugBank; DB07962; METHYL N-[(2',4'-DIFLUORO-4-HYDROXY-5-IODOBIPHENYL-3-YL)CARBONYL]-BETA-ALANINATE.
DR DrugBank; DB07693; N-(3,5-dibromo-4-hydroxyphenyl)-2,6-dimethylbenzamide.
DR DrugBank; DB07695; N-(3,5-dibromo-4-hydroxyphenyl)-4-hydroxy-3,5-dimethylbenzamide.
DR DrugBank; DB08104; N-(3,5-dibromo-4-hydroxyphenyl)benzamide.
DR DrugBank; DB02698; N-(M-Trifluoromethylphenyl) Phenoxazine-4,6-Dicarboxylic Acid.
DR DrugBank; DB07963; N-[(2',4'-DIFLUORO-4-HYDROXY-5-IODOBIPHENYL-3-YL)CARBONYL]-BETA-ALANINE.
DR DrugBank; DB05235; NRP409.
DR DrugBank; DB02179; O-Trifluoromethylphenyl Anthranilic Acid.
DR DrugBank; DB03167; Pentabromophenol.
DR DrugBank; DB02709; Resveratrol.
DR DrugBank; DB11644; Tafamidis.
DR DrugBank; DB01751; Tetraiodothyroacetic acid.
DR DrugBank; DB09100; Thyroid, porcine.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR DrugCentral; P02766; -.
DR GuidetoPHARMACOLOGY; 2851; -.
DR CarbonylDB; P02766; -.
DR GlyGen; P02766; 1 site.
DR iPTMnet; P02766; -.
DR PhosphoSitePlus; P02766; -.
DR BioMuta; TTR; -.
DR DMDM; 136464; -.
DR DOSAC-COBS-2DPAGE; P02766; -.
DR REPRODUCTION-2DPAGE; P02766; -.
DR SWISS-2DPAGE; P02766; -.
DR UCD-2DPAGE; P02766; -.
DR CPTAC; non-CPTAC-1165; -.
DR EPD; P02766; -.
DR jPOST; P02766; -.
DR MassIVE; P02766; -.
DR MaxQB; P02766; -.
DR PaxDb; P02766; -.
DR PeptideAtlas; P02766; -.
DR PRIDE; P02766; -.
DR ProteomicsDB; 51586; -.
DR TopDownProteomics; P02766; -.
DR Antibodypedia; 650; 1323 antibodies from 45 providers.
DR CPTC; P02766; 1 antibody.
DR DNASU; 7276; -.
DR Ensembl; ENST00000237014.8; ENSP00000237014.4; ENSG00000118271.12.
DR Ensembl; ENST00000649620.1; ENSP00000497927.1; ENSG00000118271.12.
DR GeneID; 7276; -.
DR KEGG; hsa:7276; -.
DR MANE-Select; ENST00000237014.8; ENSP00000237014.4; NM_000371.4; NP_000362.1.
DR UCSC; uc002kwx.5; human.
DR CTD; 7276; -.
DR DisGeNET; 7276; -.
DR GeneCards; TTR; -.
DR GeneReviews; TTR; -.
DR HGNC; HGNC:12405; TTR.
DR HPA; ENSG00000118271; Tissue enriched (choroid).
DR MalaCards; TTR; -.
DR MIM; 105210; phenotype.
DR MIM; 115430; phenotype.
DR MIM; 145680; phenotype.
DR MIM; 176300; gene.
DR neXtProt; NX_P02766; -.
DR OpenTargets; ENSG00000118271; -.
DR Orphanet; 85451; ATTRV122I amyloidosis.
DR Orphanet; 85447; ATTRV30M amyloidosis.
DR Orphanet; 597939; Euthyroid dysprealbuminemic hyperthyroxinemia.
DR PharmGKB; PA37069; -.
DR VEuPathDB; HostDB:ENSG00000118271; -.
DR eggNOG; KOG3006; Eukaryota.
DR GeneTree; ENSGT00940000153229; -.
DR HOGENOM; CLU_115536_2_0_1; -.
DR InParanoid; P02766; -.
DR OMA; TWEPFAT; -.
DR OrthoDB; 720138at2759; -.
DR PhylomeDB; P02766; -.
DR TreeFam; TF300210; -.
DR PathwayCommons; P02766; -.
DR Reactome; R-HSA-2453864; Retinoid cycle disease events.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; P02766; -.
DR BioGRID-ORCS; 7276; 9 hits in 1069 CRISPR screens.
DR ChiTaRS; TTR; human.
DR EvolutionaryTrace; P02766; -.
DR GeneWiki; Transthyretin; -.
DR GenomeRNAi; 7276; -.
DR Pharos; P02766; Tclin.
DR PRO; PR:P02766; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P02766; protein.
DR Bgee; ENSG00000118271; Expressed in choroid plexus epithelium and 141 other tissues.
DR ExpressionAtlas; P02766; baseline and differential.
DR Genevisible; P02766; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0070324; F:thyroid hormone binding; IBA:GO_Central.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IEA:InterPro.
DR GO; GO:0070327; P:thyroid hormone transport; IEA:InterPro.
DR Gene3D; 2.60.40.180; -; 1.
DR InterPro; IPR023418; Thyroxine_BS.
DR InterPro; IPR030178; Transthyretin.
DR InterPro; IPR000895; Transthyretin/HIU_hydrolase.
DR InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
DR InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
DR InterPro; IPR023419; Transthyretin_CS.
DR PANTHER; PTHR10395; PTHR10395; 1.
DR PANTHER; PTHR10395:SF12; PTHR10395:SF12; 1.
DR Pfam; PF00576; Transthyretin; 1.
DR PRINTS; PR00189; TRNSTHYRETIN.
DR SMART; SM00095; TR_THY; 1.
DR SUPFAM; SSF49472; SSF49472; 1.
DR PROSITE; PS00768; TRANSTHYRETIN_1; 1.
DR PROSITE; PS00769; TRANSTHYRETIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amyloid; Amyloidosis; Cytoplasm; Direct protein sequencing;
KW Disease variant; Gamma-carboxyglutamic acid; Glycoprotein; Hormone;
KW Neuropathy; Phosphoprotein; Reference proteome; Secreted; Signal;
KW Thyroid hormone; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:1517749, ECO:0000269|PubMed:3135807,
FT ECO:0000269|PubMed:4607556, ECO:0000269|PubMed:6583672,
FT ECO:0000269|PubMed:6651852"
FT CHAIN 21..147
FT /note="Transthyretin"
FT /id="PRO_0000035755"
FT BINDING 35
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT BINDING 74
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT BINDING 135..139
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT MOD_RES 62
FT /note="4-carboxyglutamate; in a patient with Moyamoya
FT disease"
FT /evidence="ECO:0000269|PubMed:18221012"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02767"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19167329"
FT VARIANT 26
FT /note="G -> S (in dbSNP:rs1800458)"
FT /evidence="ECO:0000269|PubMed:10211412,
FT ECO:0000269|PubMed:11866053, ECO:0000269|PubMed:15217993,
FT ECO:0000269|PubMed:6300852, ECO:0000269|PubMed:8019560"
FT /id="VAR_007546"
FT VARIANT 30
FT /note="C -> R (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918083)"
FT /evidence="ECO:0000269|PubMed:1362222"
FT /id="VAR_007547"
FT VARIANT 32
FT /note="L -> P (in AMYL-TTR; dbSNP:rs121918094)"
FT /evidence="ECO:0000269|PubMed:10071047,
FT ECO:0000269|PubMed:17503405"
FT /id="VAR_038959"
FT VARIANT 33
FT /note="M -> I"
FT /evidence="ECO:0000269|PubMed:17503405"
FT /id="VAR_038960"
FT VARIANT 38
FT /note="D -> E (in AMYL-TTR; amyloid polyneuropathy)"
FT /id="VAR_007548"
FT VARIANT 38
FT /note="D -> G (in AMYL-TTR; leptomeningeal amyloidosis;
FT leads to unfolding and exposure of N-118 to glycosylation
FT by STT3B and subsequent degradation by the ERAD pathway;
FT dbSNP:rs121918098)"
FT /evidence="ECO:0000269|PubMed:19167329,
FT ECO:0000269|PubMed:8579098"
FT /id="VAR_007549"
FT VARIANT 40
FT /note="V -> I (in AMYL-TTR; late-onset amyloid
FT polyneuropathy with carpal tunnel syndrome;
FT dbSNP:rs121918093)"
FT /evidence="ECO:0000269|PubMed:17503405,
FT ECO:0000269|PubMed:8990019"
FT /id="VAR_007550"
FT VARIANT 43
FT /note="S -> N (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:10439117"
FT /id="VAR_038961"
FT VARIANT 44
FT /note="P -> S (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs11541790)"
FT /evidence="ECO:0000269|PubMed:17503405"
FT /id="VAR_007551"
FT VARIANT 48
FT /note="V -> M (in AMYL-TTR; amyloid polyneuropathy)"
FT /evidence="ECO:0000269|PubMed:10882995"
FT /id="VAR_010658"
FT VARIANT 50
FT /note="V -> A (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs79977247)"
FT /evidence="ECO:0000269|PubMed:1544214,
FT ECO:0000269|PubMed:17503405"
FT /id="VAR_007552"
FT VARIANT 50
FT /note="V -> G (in AMYL-TTR; dbSNP:rs79977247)"
FT /evidence="ECO:0000269|PubMed:9066351"
FT /id="VAR_038962"
FT VARIANT 50
FT /note="V -> L (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs28933979)"
FT /evidence="ECO:0000269|PubMed:10611950,
FT ECO:0000269|PubMed:1520326"
FT /id="VAR_007553"
FT VARIANT 50
FT /note="V -> M (in AMYL-TTR; amyloid polyneuropathy; by far
FT the most frequent mutation; dbSNP:rs28933979)"
FT /evidence="ECO:0000269|PubMed:12050338,
FT ECO:0000269|PubMed:1517749, ECO:0000269|PubMed:17503405,
FT ECO:0000269|PubMed:3022108, ECO:0000269|PubMed:3818577,
FT ECO:0000269|PubMed:6583672, ECO:0000269|PubMed:6651852,
FT ECO:0000269|PubMed:7655883, ECO:0000269|PubMed:8382610,
FT ECO:0000269|PubMed:8428915"
FT /id="VAR_007554"
FT VARIANT 53
FT /note="F -> C (in a patient with amyloidosis)"
FT /evidence="ECO:0000269|PubMed:12876326,
FT ECO:0000269|PubMed:15217993"
FT /id="VAR_038963"
FT VARIANT 53
FT /note="F -> I (in AMYL-TTR; Jewish 'SKO' amyloid
FT polyneuropathy; dbSNP:rs121918068)"
FT /evidence="ECO:0000269|PubMed:6487335,
FT ECO:0000269|PubMed:8019560"
FT /id="VAR_007555"
FT VARIANT 53
FT /note="F -> L (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918068)"
FT /evidence="ECO:0000269|PubMed:12050338,
FT ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:1932142,
FT ECO:0000269|PubMed:2046936"
FT /id="VAR_007556"
FT VARIANT 53
FT /note="F -> V (in AMYL-TTR; amyloid polyneuropathy)"
FT /evidence="ECO:0000269|PubMed:10611950,
FT ECO:0000269|PubMed:12050338, ECO:0000269|PubMed:15478468,
FT ECO:0000269|PubMed:17503405"
FT /id="VAR_038964"
FT VARIANT 54
FT /note="R -> T (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:9605286"
FT /id="VAR_038965"
FT VARIANT 55
FT /note="K -> N (in AMYL-TTR; amyloid polyneuropathy)"
FT /evidence="ECO:0000269|PubMed:7655883"
FT /id="VAR_038966"
FT VARIANT 56
FT /note="A -> P (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918077)"
FT /evidence="ECO:0000269|PubMed:17503405"
FT /id="VAR_007557"
FT VARIANT 58
FT /note="D -> A (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:10611950,
FT ECO:0000269|PubMed:11866053"
FT /id="VAR_038967"
FT VARIANT 58
FT /note="D -> V (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:12050338,
FT ECO:0000269|PubMed:17635579"
FT /id="VAR_038968"
FT VARIANT 61
FT /note="W -> L (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:11866053"
FT /id="VAR_038969"
FT VARIANT 62
FT /note="E -> D (in AMYL-TTR; dbSNP:rs11541796)"
FT /evidence="ECO:0000269|PubMed:10036587"
FT /id="VAR_038970"
FT VARIANT 62
FT /note="E -> G (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs11541796)"
FT /evidence="ECO:0000269|PubMed:2363717,
FT ECO:0000269|PubMed:7923855"
FT /id="VAR_007558"
FT VARIANT 64
FT /note="F -> S (in AMYL-TTR; dbSNP:rs104894665)"
FT /evidence="ECO:0000269|PubMed:11866053,
FT ECO:0000269|PubMed:9818883"
FT /id="VAR_038971"
FT VARIANT 65
FT /note="A -> D (in AMYL-TTR; amyloid cardiomyopathy;
FT dbSNP:rs730881169)"
FT /id="VAR_007559"
FT VARIANT 65
FT /note="A -> S (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:10842718"
FT /id="VAR_038972"
FT VARIANT 65
FT /note="A -> T (in AMYL-TTR; amyloid cardiomyopathy;
FT dbSNP:rs121918078)"
FT /evidence="ECO:0000269|PubMed:1570831,
FT ECO:0000269|PubMed:17503405"
FT /id="VAR_007560"
FT VARIANT 67
FT /note="G -> A (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918090)"
FT /evidence="ECO:0000269|PubMed:17503405, ECO:0000269|Ref.90"
FT /id="VAR_007561"
FT VARIANT 67
FT /note="G -> E (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:12050338,
FT ECO:0000269|PubMed:15217993"
FT /id="VAR_038973"
FT VARIANT 67
FT /note="G -> R (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs387906523)"
FT /evidence="ECO:0000269|PubMed:1734866"
FT /id="VAR_007562"
FT VARIANT 67
FT /note="G -> V (in AMYL-TTR; amyloid polyneuropathy with
FT carpal tunnel syndrome)"
FT /id="VAR_007563"
FT VARIANT 69
FT /note="T -> A (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918081)"
FT /evidence="ECO:0000269|PubMed:1301926,
FT ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:7655883"
FT /id="VAR_007564"
FT VARIANT 69
FT /note="T -> I (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:10436378,
FT ECO:0000269|PubMed:17503405"
FT /id="VAR_038974"
FT VARIANT 70
FT /note="S -> I (in AMYL-TTR; amyloid cardiomyopathy;
FT dbSNP:rs121918080)"
FT /evidence="ECO:0000269|PubMed:1520336"
FT /id="VAR_007565"
FT VARIANT 70
FT /note="S -> R (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs386134269)"
FT /evidence="ECO:0000269|PubMed:10611950,
FT ECO:0000269|PubMed:23317988, ECO:0000269|PubMed:2363717,
FT ECO:0000269|PubMed:7655883"
FT /id="VAR_007566"
FT VARIANT 72
FT /note="S -> P (in AMYL-TTR; amyloid polyneuropathy)"
FT /id="VAR_007567"
FT VARIANT 73
FT /note="G -> E (in AMYL-TTR; dbSNP:rs121918097)"
FT /evidence="ECO:0000269|PubMed:11445644"
FT /id="VAR_038975"
FT VARIANT 74
FT /note="E -> G (in AMYL-TTR; amyloid polyneuropathy)"
FT /id="VAR_007568"
FT VARIANT 74
FT /note="E -> K (in AMYL-TTR; early-onset amyloid
FT polyneuropathy)"
FT /evidence="ECO:0000269|PubMed:15214015"
FT /id="VAR_038976"
FT VARIANT 75
FT /note="L -> P (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918079)"
FT /evidence="ECO:0000269|PubMed:1351039,
FT ECO:0000269|PubMed:16627944, ECO:0000269|PubMed:7910950,
FT ECO:0000269|PubMed:9733771"
FT /id="VAR_007569"
FT VARIANT 75
FT /note="L -> Q (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:12557757"
FT /id="VAR_038977"
FT VARIANT 78
FT /note="L -> H (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918069)"
FT /evidence="ECO:0000269|PubMed:15217993"
FT /id="VAR_007570"
FT VARIANT 78
FT /note="L -> R (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918069)"
FT /evidence="ECO:0000269|PubMed:1656975"
FT /id="VAR_007571"
FT VARIANT 79
FT /note="T -> K (in AMYL-TTR; amyloid cardiomyopathy;
FT dbSNP:rs730881163)"
FT /evidence="ECO:0000269|PubMed:7850982"
FT /id="VAR_007572"
FT VARIANT 80
FT /note="T -> A (in AMYL-TTR; amyloid polyneuropathy and
FT cardiomyopathy; dbSNP:rs121918070)"
FT /evidence="ECO:0000269|PubMed:12050338,
FT ECO:0000269|PubMed:15217993, ECO:0000269|PubMed:17503405,
FT ECO:0000269|PubMed:7655883"
FT /id="VAR_007573"
FT VARIANT 81
FT /note="E -> G (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:17453626"
FT /id="VAR_038978"
FT VARIANT 81
FT /note="E -> K (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918086)"
FT /evidence="ECO:0000269|PubMed:8352764"
FT /id="VAR_007574"
FT VARIANT 84
FT /note="F -> L (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918091)"
FT /evidence="ECO:0000269|PubMed:11866053,
FT ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:2046936"
FT /id="VAR_007575"
FT VARIANT 88
FT /note="I -> L (in AMYL-TTR; amyloid cardiomyopathy;
FT dbSNP:rs121918085)"
FT /evidence="ECO:0000269|PubMed:17503405,
FT ECO:0000269|PubMed:8038017"
FT /id="VAR_007576"
FT VARIANT 89
FT /note="Y -> H (in AMYL-TTR; leptomeningeal amyloidosis;
FT vitreous amyloid in some patients; dbSNP:rs121918100)"
FT /evidence="ECO:0000269|PubMed:12771253"
FT /id="VAR_007577"
FT VARIANT 90
FT /note="K -> N (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs267607160)"
FT /evidence="ECO:0000269|PubMed:1436517"
FT /id="VAR_007578"
FT VARIANT 91
FT /note="V -> A (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918084)"
FT /evidence="ECO:0000269|PubMed:17503405,
FT ECO:0000269|PubMed:8095302, ECO:0000269|PubMed:8257997"
FT /id="VAR_007579"
FT VARIANT 93
FT /note="I -> V (in AMYL-TTR; amyloid polyneuropathy)"
FT /evidence="ECO:0000269|PubMed:10694917"
FT /id="VAR_007580"
FT VARIANT 94
FT /note="D -> H (in dbSNP:rs730881164)"
FT /id="VAR_007581"
FT VARIANT 97
FT /note="S -> Y (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918071)"
FT /evidence="ECO:0000269|PubMed:15217993,
FT ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:2891727,
FT ECO:0000269|PubMed:7655883"
FT /id="VAR_007582"
FT VARIANT 98
FT /note="Y -> F (in AMYL-TTR; dbSNP:rs958191819)"
FT /evidence="ECO:0000269|PubMed:16627944,
FT ECO:0000269|PubMed:17503405"
FT /id="VAR_038979"
FT VARIANT 104
FT /note="I -> N (in AMYL-TTR; vitrous amyloid)"
FT /evidence="ECO:0000269|PubMed:17503405"
FT /id="VAR_007583"
FT VARIANT 104
FT /note="I -> S (in AMYL-TTR; amyloid polyneuropathy; almost
FT no RBP binding; dbSNP:rs121918072)"
FT /evidence="ECO:0000269|PubMed:17503405,
FT ECO:0000269|PubMed:3722385, ECO:0000269|PubMed:8089102"
FT /id="VAR_007584"
FT VARIANT 104
FT /note="I -> T (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:17503405"
FT /id="VAR_038980"
FT VARIANT 109
FT /note="E -> K (in AMYL-TTR; amyloid polyneuropathy)"
FT /evidence="ECO:0000269|PubMed:10842705"
FT /id="VAR_010659"
FT VARIANT 109
FT /note="E -> Q (in AMYL-TTR; amyloid polyneuropathy and
FT cardiomyopathy; dbSNP:rs121918082)"
FT /evidence="ECO:0000269|PubMed:1301926,
FT ECO:0000269|PubMed:7655883"
FT /id="VAR_007585"
FT VARIANT 110
FT /note="H -> N (in dbSNP:rs121918074)"
FT /evidence="ECO:0000269|PubMed:1997217,
FT ECO:0000269|PubMed:7923855"
FT /id="VAR_007586"
FT VARIANT 111
FT /note="A -> S (in AMYL-TTR; amyloid polyneuropathy)"
FT /evidence="ECO:0000269|PubMed:10627135"
FT /id="VAR_007587"
FT VARIANT 114
FT /note="V -> A (in a patient with amyloidosis)"
FT /evidence="ECO:0000269|PubMed:15217993,
FT ECO:0000269|PubMed:17503405"
FT /id="VAR_038981"
FT VARIANT 117
FT /note="A -> G (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918087)"
FT /evidence="ECO:0000269|PubMed:10611950,
FT ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:8133316"
FT /id="VAR_007588"
FT VARIANT 117
FT /note="A -> S (in AMYL-TTR; dbSNP:rs267607161)"
FT /evidence="ECO:0000269|PubMed:10611950"
FT /id="VAR_038982"
FT VARIANT 121
FT /note="G -> S (in dbSNP:rs755337715)"
FT /evidence="ECO:0000269|PubMed:10671063,
FT ECO:0000269|PubMed:17503405"
FT /id="VAR_007589"
FT VARIANT 122
FT /note="P -> R"
FT /id="VAR_007590"
FT VARIANT 124
FT /note="R -> C (in dbSNP:rs745834030)"
FT /id="VAR_007591"
FT VARIANT 124
FT /note="R -> H (in dbSNP:rs121918095)"
FT /evidence="ECO:0000269|PubMed:10529370,
FT ECO:0000269|PubMed:15735344"
FT /id="VAR_038983"
FT VARIANT 126
FT /note="T -> N (in AMYL-TTR; dbSNP:rs1456101911)"
FT /evidence="ECO:0000269|PubMed:17503405"
FT /id="VAR_038984"
FT VARIANT 127
FT /note="I -> M (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:17503405"
FT /id="VAR_038985"
FT VARIANT 127
FT /note="I -> V (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918089)"
FT /evidence="ECO:0000269|PubMed:17503405,
FT ECO:0000269|PubMed:7914929, ECO:0000269|PubMed:8081397"
FT /id="VAR_007592"
FT VARIANT 129
FT /note="A -> T (in DTTRH; increased affinity for thyroxine;
FT dbSNP:rs267607159)"
FT /evidence="ECO:0000269|PubMed:17503405,
FT ECO:0000269|PubMed:1979335"
FT /id="VAR_007593"
FT VARIANT 131
FT /note="L -> M (in AMYL-TTR; dbSNP:rs121918073)"
FT /evidence="ECO:0000269|PubMed:17503405"
FT /id="VAR_007594"
FT VARIANT 134
FT /note="Y -> C (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs121918075)"
FT /evidence="ECO:0000269|PubMed:12403615,
FT ECO:0000269|PubMed:16185074, ECO:0000269|PubMed:2161654"
FT /id="VAR_007595"
FT VARIANT 134
FT /note="Y -> H (in CTS1; amyloid deposit on carpal tunnel;
FT patients show no other abnormalities; dbSNP:rs121918088)"
FT /evidence="ECO:0000269|PubMed:8309582"
FT /id="VAR_007598"
FT VARIANT 136
FT /note="Y -> S (in AMYL-TTR; amyloid polyneuropathy;
FT dbSNP:rs730881167)"
FT /evidence="ECO:0000269|PubMed:10627135"
FT /id="VAR_007596"
FT VARIANT 136
FT /note="Y -> V (requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:3675594"
FT /id="VAR_007597"
FT VARIANT 139
FT /note="T -> M (in Chicago variant; dbSNP:rs28933981)"
FT /evidence="ECO:0000269|PubMed:11866053,
FT ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:1877623"
FT /id="VAR_007599"
FT VARIANT 140
FT /note="A -> S (in AMYL-TTR; dbSNP:rs876658108)"
FT /evidence="ECO:0000269|PubMed:12050338"
FT /id="VAR_038986"
FT VARIANT 142
FT /note="V -> A (in AMYL-TTR)"
FT /evidence="ECO:0000269|PubMed:10211412"
FT /id="VAR_038987"
FT VARIANT 142
FT /note="V -> I (in AMYL-TTR; dbSNP:rs76992529)"
FT /evidence="ECO:0000269|PubMed:12050338,
FT ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:3135807"
FT /id="VAR_007600"
FT VARIANT 144
FT /note="N -> S (in AMYL-TTR; dbSNP:rs144965179)"
FT /evidence="ECO:0000269|PubMed:17577687"
FT /id="VAR_038988"
FT MUTAGEN 107
FT /note="F->M: Loss of tetramerization; when associated with
FT M-130."
FT /evidence="ECO:0000269|PubMed:11560492"
FT MUTAGEN 130
FT /note="L->M: Loss of tetramerization; when associated with
FT M-107."
FT /evidence="ECO:0000269|PubMed:11560492"
FT CONFLICT 41
FT /note="R -> P (in Ref. 3; AAA98771)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="E -> D (in Ref. 12; CAG33189)"
FT /evidence="ECO:0000305"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:1TSH"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1F86"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:1F86"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1F86"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:6E78"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1F86"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1F86"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2QEL"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1F86"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1F86"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:1F86"
FT STRAND 107..118
FT /evidence="ECO:0007829|PDB:1F86"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5JIM"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:1F86"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:1F86"
SQ SEQUENCE 147 AA; 15887 MW; 3A6AEBCBBA56BC44 CRC64;
MASHRLLLLC LAGLVFVSEA GPTGTGESKC PLMVKVLDAV RGSPAINVAV HVFRKAADDT
WEPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK ALGISPFHEH AEVVFTANDS
GPRRYTIAAL LSPYSYSTTA VVTNPKE
