TTHY_MOUSE
ID TTHY_MOUSE Reviewed; 147 AA.
AC P07309;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Transthyretin;
DE AltName: Full=Prealbumin;
DE Flags: Precursor;
GN Name=Ttr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND THYROID HORMONE-BINDING SITES LYS-35 AND
RP GLU-74.
RC TISSUE=Liver;
RX PubMed=3005251; DOI=10.1093/oxfordjournals.jbchem.a135442;
RA Wakasugi S., Maeda S., Shimada K., Nakashima H., Migita S.;
RT "Structural comparisons between mouse and human prealbumin.";
RL J. Biochem. 98:1707-1714(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3020014; DOI=10.1093/oxfordjournals.jbchem.a121705;
RA Wakasugi S., Maeda S., Shimada K.;
RT "Structure and expression of the mouse prealbumin gene.";
RL J. Biochem. 100:49-58(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J; TISSUE=Choroid plexus;
RA Kita H., Kawamoto S., Okubo K., Matsubara K.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 21-147, INCREASED STABILITY OF
RP THE MOUSE PROTEIN, AND SUBUNIT.
RX PubMed=18006495; DOI=10.1074/jbc.m708028200;
RA Reixach N., Foss T.R., Santelli E., Pascual J., Kelly J.W., Buxbaum J.N.;
RT "Human-murine transthyretin heterotetramers are kinetically stable and non-
RT amyloidogenic. A lesson in the generation of transgenic models of diseases
RT involving oligomeric proteins.";
RL J. Biol. Chem. 283:2098-2107(2008).
CC -!- FUNCTION: Thyroid hormone-binding protein. Probably transports
CC thyroxine from the bloodstream to the brain.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Detected in plasma (at protein level). Detected in
CC liver.
CC -!- MISCELLANEOUS: The mouse protein shows increased stability and much
CC reduced propensity to form amyloid fibrils, compared to the human
CC protein.
CC -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X03351; CAA27057.1; -; mRNA.
DR EMBL; D00073; BAA00050.1; -; Genomic_DNA.
DR EMBL; D89076; BAA13757.1; -; mRNA.
DR EMBL; AK018701; BAB31352.1; -; mRNA.
DR EMBL; BC024702; AAH24702.1; -; mRNA.
DR CCDS; CCDS29085.1; -.
DR PIR; A24132; VBMS.
DR RefSeq; NP_038725.1; NM_013697.5.
DR PDB; 2QPF; X-ray; 2.05 A; A/B/C/D/E/F/G/H=21-147.
DR PDBsum; 2QPF; -.
DR AlphaFoldDB; P07309; -.
DR SMR; P07309; -.
DR BioGRID; 204369; 20.
DR DIP; DIP-29726N; -.
DR IntAct; P07309; 3.
DR MINT; P07309; -.
DR STRING; 10090.ENSMUSP00000074783; -.
DR GlyGen; P07309; 1 site.
DR iPTMnet; P07309; -.
DR PhosphoSitePlus; P07309; -.
DR UCD-2DPAGE; P07309; -.
DR CPTAC; non-CPTAC-3625; -.
DR CPTAC; non-CPTAC-5622; -.
DR jPOST; P07309; -.
DR PaxDb; P07309; -.
DR PeptideAtlas; P07309; -.
DR PRIDE; P07309; -.
DR ProteomicsDB; 298011; -.
DR ABCD; P07309; 2 sequenced antibodies.
DR Antibodypedia; 650; 1323 antibodies from 45 providers.
DR DNASU; 22139; -.
DR Ensembl; ENSMUST00000075312; ENSMUSP00000074783; ENSMUSG00000061808.
DR GeneID; 22139; -.
DR KEGG; mmu:22139; -.
DR UCSC; uc008eet.2; mouse.
DR CTD; 7276; -.
DR MGI; MGI:98865; Ttr.
DR VEuPathDB; HostDB:ENSMUSG00000061808; -.
DR eggNOG; KOG3006; Eukaryota.
DR GeneTree; ENSGT00940000153229; -.
DR HOGENOM; CLU_115536_2_0_1; -.
DR InParanoid; P07309; -.
DR OMA; TWEPFAT; -.
DR OrthoDB; 1453185at2759; -.
DR PhylomeDB; P07309; -.
DR TreeFam; TF300210; -.
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 22139; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ttr; mouse.
DR EvolutionaryTrace; P07309; -.
DR PRO; PR:P07309; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P07309; protein.
DR Bgee; ENSMUSG00000061808; Expressed in choroid plexus epithelium and 217 other tissues.
DR ExpressionAtlas; P07309; baseline and differential.
DR Genevisible; P07309; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042562; F:hormone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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; Gamma-carboxyglutamic acid; Glycoprotein; Hormone;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Thyroid hormone;
KW Transport.
FT SIGNAL 1..20
FT CHAIN 21..147
FT /note="Transthyretin"
FT /id="PRO_0000035760"
FT BINDING 35
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250"
FT BINDING 135..139
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250"
FT MOD_RES 62
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P02766"
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:17330941"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2QPF"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:2QPF"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:2QPF"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:2QPF"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2QPF"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2QPF"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2QPF"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:2QPF"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2QPF"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:2QPF"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:2QPF"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:2QPF"
SQ SEQUENCE 147 AA; 15776 MW; 9803CCC3024BA911 CRC64;
MASLRLFLLC LAGLVFVSEA GPAGAGESKC PLMVKVLDAV RGSPAVDVAV KVFKKTSEGS
WEPFASGKTA ESGELHGLTT DEKFVEGVYR VELDTKSYWK TLGISPFHEF ADVVFTANDS
GHRHYTIAAL LSPYSYSTTA VVSNPQN
