TGM1_HUMAN
ID TGM1_HUMAN Reviewed; 817 AA.
AC P22735; B4DWR7; Q197M4;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 4.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase K;
DE EC=2.3.2.13;
DE AltName: Full=Epidermal TGase;
DE AltName: Full=Transglutaminase K;
DE Short=TG(K);
DE Short=TGK;
DE Short=TGase K;
DE AltName: Full=Transglutaminase-1;
DE Short=TGase-1;
GN Name=TGM1; Synonyms=KTG;
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] (ISOFORM 1).
RX PubMed=1979171; DOI=10.1073/pnas.87.23.9333;
RA Phillips M.A., Stewart B.E., Qin Q., Chakravarty R., Floyd E.E.,
RA Jetten A.M., Rice R.H.;
RT "Primary structure of keratinocyte transglutaminase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9333-9337(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Keratinocyte;
RX PubMed=1673840; DOI=10.1016/0006-291x(91)91651-r;
RA Yamanishi K., Liew F.M., Konishi K., Yasuno H., Doi H., Hirano J.,
RA Fukushima S.;
RT "Molecular cloning of human epidermal transglutaminase cDNA from
RT keratinocytes in culture.";
RL Biochem. Biophys. Res. Commun. 175:906-913(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1670769; DOI=10.1016/s0021-9258(18)52469-8;
RA Kim H.C., Idler W.W., Kim I.-G., Han J.H., Chung S.-I., Steinert P.M.;
RT "The complete amino acid sequence of the human transglutaminase K enzyme
RT deduced from the nucleic acid sequences of cDNA clones.";
RL J. Biol. Chem. 266:536-539(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=1346394; DOI=10.1016/s0021-9258(18)45875-9;
RA Phillips M.A., Stewart B.E., Rice R.H.;
RT "Genomic structure of keratinocyte transglutaminase. Recruitment of new
RT exon for modified function.";
RL J. Biol. Chem. 267:2282-2286(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1348508; DOI=10.1016/s0021-9258(18)42573-2;
RA Kim I.-G., McBride O.W., Wang M., Kim S.-Y., Idler W.W., Steinert P.M.;
RT "Structure and organization of the human transglutaminase 1 gene.";
RL J. Biol. Chem. 267:7710-7717(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=1381356; DOI=10.1016/s0021-9258(19)37122-4;
RA Yamanishi K., Inazawa J., Liew F., Nonomura K., Ariyama T., Yasuno H.,
RA Abe T., Doi H., Hirano J., Fukushima S.;
RT "Structure of the gene for human transglutaminase 1.";
RL J. Biol. Chem. 267:17858-17863(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=1350092; DOI=10.1073/pnas.89.10.4476;
RA Polakowska R.R., Eickbush T., Falciano V., Razvi F., Goldsmith L.A.;
RT "Organization and evolution of the human epidermal keratinocyte
RT transglutaminase I gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4476-4480(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Esophagus;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-42; ILE-372; MET-518;
RP CYS-607; LEU-755 AND VAL-802.
RG NIEHS SNPs program;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [11]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-551 (ISOFORM 1).
RX PubMed=1704039; DOI=10.1111/1523-1747.ep12464554;
RA Polakowska R., Herting E., Goldsmith L.A.;
RT "Isolation of cDNA for human epidermal type I transglutaminase.";
RL J. Invest. Dermatol. 96:285-288(1991).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 375-817 (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=1351505; DOI=10.1111/1523-1747.ep12611394;
RA Schroeder W., Thacher S., Stewart-Galetka S., Annarella M., Chema D.,
RA Sicliano M., Davies P., Tang H.Y., Sowa B., Duvic M.;
RT "Type I keratinocyte transglutaminase: expression in human skin and
RT psoriasis.";
RL J. Invest. Dermatol. 99:27-34(1992).
RN [15]
RP PHOSPHORYLATION AT SER-24; SER-82; SER-85 AND SER-92.
RX PubMed=8973564; DOI=10.1042/bj3200547;
RA Rice R.H., Mehrpouyan M., Quin Q., Phillips M.A., Lee Y.M.;
RT "Identification of phosphorylation sites in keratinocyte
RT transglutaminase.";
RL Biochem. J. 320:547-550(1996).
RN [16]
RP SUBCELLULAR LOCATION, INTERACTION WITH PLAAT4, AND PALMITOYLATION.
RX PubMed=17762858; DOI=10.1038/sj.jid.5701035;
RA Jans R., Sturniolo M.T., Eckert R.L.;
RT "Localization of the TIG3 transglutaminase interaction domain and
RT demonstration that the amino-terminal region is required for TIG3 function
RT as a keratinocyte differentiation regulator.";
RL J. Invest. Dermatol. 128:517-529(2008).
RN [17]
RP REVIEW ON VARIANTS.
RX PubMed=19241467; DOI=10.1002/humu.20952;
RA Herman M.L., Farasat S., Steinbach P.J., Wei M.H., Toure O., Fleckman P.,
RA Blake P., Bale S.J., Toro J.R.;
RT "Transglutaminase-1 gene mutations in autosomal recessive congenital
RT ichthyosis: summary of mutations (including 23 novel) and modeling of
RT TGase-1.";
RL Hum. Mutat. 30:537-547(2009).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 693-787.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the human transglutaminase 1 beta-barrel domain.";
RL Submitted (JAN-2011) to the PDB data bank.
RN [19]
RP VARIANTS ARCI1 TYR-42 AND GLN-323, AND INVOLVEMENT IN ARC11.
RX PubMed=7824952; DOI=10.1126/science.7824952;
RA Huber M., Rettler I., Bernasconi K., Frenk E., Lavrijsen S.P.M., Ponec M.,
RA Bon A., Lautenschlager S., Schorderet D.F., Hohl D.;
RT "Mutations of keratinocyte transglutaminase in lamellar ichthyosis.";
RL Science 267:525-528(1995).
RN [20]
RP VARIANTS ARCI1 HIS-142 AND HIS-143.
RX PubMed=7773290; DOI=10.1038/ng0395-279;
RA Russell L.J., Digiovanna J.J., Rogers G.R., Steinert P.M., Hashem N.,
RA Compton J.G., Bale S.J.;
RT "Mutations in the gene for transglutaminase 1 in autosomal recessive
RT lamellar ichthyosis.";
RL Nat. Genet. 9:279-283(1995).
RN [21]
RP VARIANTS ARCI1 HIS-142; CYS-143; SER-218; LEU-379 AND LEU-396.
RX PubMed=9326318; DOI=10.1086/515498;
RA Laiho E., Ignatius J., Mikkola H., Yee V.C., Teller D.C., Niemi K.-M.,
RA Saarialho-Kere U., Kere J., Palotie A.;
RT "Transglutaminase 1 mutations in autosomal recessive congenital ichthyosis:
RT private and recurrent mutations in an isolated population.";
RL Am. J. Hum. Genet. 61:529-538(1997).
RN [22]
RP VARIANT ARCI1 HIS-389.
RX PubMed=11251583; DOI=10.1046/j.1365-2133.2001.04037.x;
RA Akiyama M., Takizawa Y., Kokaji T., Shimizu H.;
RT "Novel mutations of TGM1 in a child with congenital ichthyosiform
RT erythroderma.";
RL Br. J. Dermatol. 144:401-407(2001).
RN [23]
RP VARIANTS ARCI1 VAL-102; THR-289 AND TRP-307.
RX PubMed=11511296; DOI=10.1046/j.0022-202x.2001.01429.x;
RA Yang J.M., Ahn K.S., Cho M.O., Yoneda K., Lee C.H., Lee J.H., Lee E.S.,
RA Candi E., Melino G., Ahvazi B., Steinert P.M.;
RT "Novel mutations of the transglutaminase 1 gene in lamellar ichthyosis.";
RL J. Invest. Dermatol. 117:214-218(2001).
RN [24]
RP VARIANT ARCI1 GLY-307.
RX PubMed=19890349; DOI=10.1038/jid.2009.346;
RA Vahlquist A., Bygum A., Gaanemo A., Virtanen M., Hellstroem-Pigg M.,
RA Strauss G., Brandrup F., Fischer J.;
RT "Genotypic and clinical spectrum of self-improving collodion ichthyosis:
RT ALOX12B, ALOXE3, and TGM1 mutations in Scandinavian patients.";
RL J. Invest. Dermatol. 130:438-443(2010).
RN [25]
RP VARIANTS ARCI1 CYS-143 AND PHE-212, CHARACTERIZATION OF VARIANTS ARCI1
RP CYS-143 AND PHE-212, AND FUNCTION.
RX PubMed=26220141; DOI=10.1111/ijd.12806;
RA Zhang S.Q., Li C.X., Gao X.Q., Qiu W.Y., Chen Q., Li X.M., Zhou X.,
RA Tian X., Tang Z.P., Zhao T., Zhang F., Zhang X.B.;
RT "Identification and functional characterization of a novel transglutaminase
RT 1 gene mutation associated with autosomal recessive congenital
RT ichthyosis.";
RL Int. J. Dermatol. 55:201-207(2016).
CC -!- FUNCTION: Catalyzes the cross-linking of proteins and the conjugation
CC of polyamines to proteins. Responsible for cross-linking epidermal
CC proteins during formation of the stratum corneum. Involved in cell
CC proliferation (PubMed:26220141). {ECO:0000269|PubMed:26220141}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10024};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- SUBUNIT: Interacts with PLAAT4. {ECO:0000269|PubMed:17762858}.
CC -!- INTERACTION:
CC P22735; P28330: ACADL; NbExp=3; IntAct=EBI-2562368, EBI-12059321;
CC P22735; P05187: ALPP; NbExp=3; IntAct=EBI-2562368, EBI-1211484;
CC P22735; Q9BXJ1-2: C1QTNF1; NbExp=6; IntAct=EBI-2562368, EBI-11536642;
CC P22735; P55212: CASP6; NbExp=3; IntAct=EBI-2562368, EBI-718729;
CC P22735; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-2562368, EBI-741032;
CC P22735; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-2562368, EBI-713677;
CC P22735; Q92608: DOCK2; NbExp=3; IntAct=EBI-2562368, EBI-448771;
CC P22735; P09211: GSTP1; NbExp=3; IntAct=EBI-2562368, EBI-353467;
CC P22735; P13284: IFI30; NbExp=3; IntAct=EBI-2562368, EBI-2868897;
CC P22735; Q969P0: IGSF8; NbExp=3; IntAct=EBI-2562368, EBI-8293590;
CC P22735; P16144-2: ITGB4; NbExp=3; IntAct=EBI-2562368, EBI-11051601;
CC P22735; Q15040: JOSD1; NbExp=3; IntAct=EBI-2562368, EBI-2510602;
CC P22735; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-2562368, EBI-739863;
CC P22735; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-2562368, EBI-3958099;
CC P22735; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2562368, EBI-21591415;
CC P22735; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-2562368, EBI-10245913;
CC P22735; Q5T753: LCE1E; NbExp=3; IntAct=EBI-2562368, EBI-11955335;
CC P22735; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-2562368, EBI-9394625;
CC P22735; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-2562368, EBI-10246358;
CC P22735; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-2562368, EBI-2858213;
CC P22735; Q92692-2: NECTIN2; NbExp=3; IntAct=EBI-2562368, EBI-6979889;
CC P22735; Q9Y5Y2: NUBP2; NbExp=3; IntAct=EBI-2562368, EBI-1048886;
CC P22735; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-2562368, EBI-5280197;
CC P22735; Q14162: SCARF1; NbExp=3; IntAct=EBI-2562368, EBI-12056025;
CC P22735; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2562368, EBI-2623095;
CC P22735; Q9BR01: SULT4A1; NbExp=3; IntAct=EBI-2562368, EBI-6690555;
CC P22735; B2RWP4: TACC2; NbExp=3; IntAct=EBI-2562368, EBI-14211313;
CC P22735; P22735: TGM1; NbExp=3; IntAct=EBI-2562368, EBI-2562368;
CC P22735; Q8WVR3: TRAPPC14; NbExp=3; IntAct=EBI-2562368, EBI-719893;
CC P22735; Q6EMK4: VASN; NbExp=3; IntAct=EBI-2562368, EBI-10249550;
CC P22735; Q8IW00: VSTM4; NbExp=3; IntAct=EBI-2562368, EBI-4311759;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17762858}; Lipid-
CC anchor {ECO:0000305|PubMed:17762858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P22735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P22735-2; Sequence=VSP_056840;
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:17762858}.
CC -!- PTM: The membrane anchorage region possesses a cluster of five
CC cysteines within which fatty acid(s) may become thioester-linked. It is
CC subject to phorbol ester-stimulated phosphorylation and is
CC hypersensitive to proteolysis, which releases the enzyme in a soluble
CC form. {ECO:0000269|PubMed:8973564}.
CC -!- PTM: Tyrosine-phosphorylated. {ECO:0000250|UniProtKB:Q9JLF6}.
CC -!- DISEASE: Ichthyosis, congenital, autosomal recessive 1 (ARCI1)
CC [MIM:242300]: A form of autosomal recessive congenital ichthyosis, a
CC disorder of keratinization with abnormal differentiation and
CC desquamation of the epidermis, resulting in abnormal skin scaling over
CC the whole body. The main skin phenotypes are lamellar ichthyosis (LI)
CC and non-bullous congenital ichthyosiform erythroderma (NCIE), although
CC phenotypic overlap within the same patient or among patients from the
CC same family can occur. Lamellar ichthyosis is a condition often
CC associated with an embedment in a collodion-like membrane at birth;
CC skin scales later develop, covering the entire body surface. Non-
CC bullous congenital ichthyosiform erythroderma characterized by fine
CC whitish scaling on an erythrodermal background; larger brownish scales
CC are present on the buttocks, neck and legs.
CC {ECO:0000269|PubMed:11251583, ECO:0000269|PubMed:11511296,
CC ECO:0000269|PubMed:19890349, ECO:0000269|PubMed:26220141,
CC ECO:0000269|PubMed:7773290, ECO:0000269|PubMed:7824952,
CC ECO:0000269|PubMed:9326318}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61166.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=M86360; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tgm1/";
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DR EMBL; M55183; AAA59474.1; -; mRNA.
DR EMBL; D90287; BAA14329.1; -; mRNA.
DR EMBL; M62925; AAA61166.1; ALT_FRAME; mRNA.
DR EMBL; M83230; AAA61156.1; -; Genomic_DNA.
DR EMBL; M83227; AAA61156.1; JOINED; Genomic_DNA.
DR EMBL; M83228; AAA61156.1; JOINED; Genomic_DNA.
DR EMBL; M83229; AAA61156.1; JOINED; Genomic_DNA.
DR EMBL; M86360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D10353; BAA34203.1; -; Genomic_DNA.
DR EMBL; M98447; AAA96667.1; -; Genomic_DNA.
DR EMBL; AK301652; BAG63129.1; -; mRNA.
DR EMBL; AK315843; BAF98734.1; -; mRNA.
DR EMBL; DQ640500; ABF70204.1; -; Genomic_DNA.
DR EMBL; AL096870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66047.1; -; Genomic_DNA.
DR EMBL; BC034699; AAH34699.1; -; mRNA.
DR EMBL; X57974; CAA41040.1; -; mRNA.
DR CCDS; CCDS9622.1; -. [P22735-1]
DR PIR; A43401; TGHUM1.
DR RefSeq; NP_000350.1; NM_000359.2. [P22735-1]
DR PDB; 2XZZ; X-ray; 2.30 A; A=693-787.
DR PDBsum; 2XZZ; -.
DR AlphaFoldDB; P22735; -.
DR SMR; P22735; -.
DR BioGRID; 112909; 250.
DR IntAct; P22735; 66.
DR MINT; P22735; -.
DR STRING; 9606.ENSP00000206765; -.
DR BindingDB; P22735; -.
DR ChEMBL; CHEMBL2810; -.
DR DrugBank; DB00130; L-Glutamine.
DR CarbonylDB; P22735; -.
DR GlyGen; P22735; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P22735; -.
DR PhosphoSitePlus; P22735; -.
DR SwissPalm; P22735; -.
DR BioMuta; TGM1; -.
DR DMDM; 57015359; -.
DR EPD; P22735; -.
DR jPOST; P22735; -.
DR MassIVE; P22735; -.
DR MaxQB; P22735; -.
DR PaxDb; P22735; -.
DR PeptideAtlas; P22735; -.
DR PRIDE; P22735; -.
DR ProteomicsDB; 5372; -.
DR ProteomicsDB; 54031; -. [P22735-1]
DR Antibodypedia; 4193; 290 antibodies from 33 providers.
DR DNASU; 7051; -.
DR Ensembl; ENST00000206765.11; ENSP00000206765.6; ENSG00000092295.12. [P22735-1]
DR Ensembl; ENST00000544573.5; ENSP00000439446.1; ENSG00000092295.12. [P22735-2]
DR Ensembl; ENST00000642845.2; ENSP00000493587.1; ENSG00000285348.2. [P22735-1]
DR Ensembl; ENST00000646057.1; ENSP00000496483.1; ENSG00000285348.2. [P22735-2]
DR GeneID; 7051; -.
DR KEGG; hsa:7051; -.
DR MANE-Select; ENST00000206765.11; ENSP00000206765.6; NM_000359.3; NP_000350.1.
DR UCSC; uc001wod.3; human. [P22735-1]
DR CTD; 7051; -.
DR DisGeNET; 7051; -.
DR GeneCards; TGM1; -.
DR GeneReviews; TGM1; -.
DR HGNC; HGNC:11777; TGM1.
DR HPA; ENSG00000092295; Tissue enriched (esophagus).
DR MalaCards; TGM1; -.
DR MIM; 190195; gene.
DR MIM; 242300; phenotype.
DR neXtProt; NX_P22735; -.
DR OpenTargets; ENSG00000092295; -.
DR Orphanet; 281127; Acral self-healing collodion baby.
DR Orphanet; 100976; Bathing suit ichthyosis.
DR Orphanet; 79394; Congenital non-bullous ichthyosiform erythroderma.
DR Orphanet; 313; Lamellar ichthyosis.
DR Orphanet; 281122; Self-improving collodion baby.
DR PharmGKB; PA36490; -.
DR VEuPathDB; HostDB:ENSG00000092295; -.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR GeneTree; ENSGT01050000244939; -.
DR HOGENOM; CLU_013435_0_2_1; -.
DR InParanoid; P22735; -.
DR OMA; WSGNYSD; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; P22735; -.
DR TreeFam; TF324278; -.
DR BRENDA; 2.3.2.13; 2681.
DR PathwayCommons; P22735; -.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; P22735; -.
DR SIGNOR; P22735; -.
DR BioGRID-ORCS; 7051; 10 hits in 1068 CRISPR screens.
DR ChiTaRS; TGM1; human.
DR GeneWiki; Keratinocyte_transglutaminase; -.
DR GenomeRNAi; 7051; -.
DR Pharos; P22735; Tchem.
DR PRO; PR:P22735; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P22735; protein.
DR Bgee; ENSG00000092295; Expressed in lower esophagus mucosa and 95 other tissues.
DR ExpressionAtlas; P22735; baseline and differential.
DR Genevisible; P22735; HS.
DR GO; GO:0001533; C:cornified envelope; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043163; P:cell envelope organization; TAS:UniProtKB.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
DR GO; GO:0018149; P:peptide cross-linking; IDA:CAFA.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IMP:UniProtKB.
DR GO; GO:0036211; P:protein modification process; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.90.260.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR InterPro; IPR023608; Transglutaminase_animal.
DR InterPro; IPR013808; Transglutaminase_AS.
DR InterPro; IPR008958; Transglutaminase_C.
DR InterPro; IPR036238; Transglutaminase_C_sf.
DR InterPro; IPR001102; Transglutaminase_N.
DR Pfam; PF00927; Transglut_C; 2.
DR Pfam; PF01841; Transglut_core; 1.
DR Pfam; PF00868; Transglut_N; 1.
DR PIRSF; PIRSF000459; TGM_EBP42; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF49309; SSF49309; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Calcium;
KW Disease variant; Ichthyosis; Keratinization; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..817
FT /note="Protein-glutamine gamma-glutamyltransferase K"
FT /id="PRO_0000213701"
FT REGION 1..100
FT /note="Membrane anchorage region"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 436
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 501
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 548
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLF6"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8973564"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23606"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8973564"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8973564"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8973564"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLF6"
FT VAR_SEQ 1..442
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056840"
FT VARIANT 42
FT /note="S -> Y (in ARCI1; skin phenotype consistent with
FT lamellar ichthyosis; dbSNP:rs41295338)"
FT /evidence="ECO:0000269|PubMed:7824952, ECO:0000269|Ref.9"
FT /id="VAR_015220"
FT VARIANT 53
FT /note="C -> S (in ARCI1)"
FT /id="VAR_058638"
FT VARIANT 94
FT /note="G -> D (in ARCI1; dbSNP:rs121918729)"
FT /id="VAR_058639"
FT VARIANT 102
FT /note="D -> V (in ARCI1; skin phenotype consistent with
FT lamellar ichthyosis; dbSNP:rs398122901)"
FT /evidence="ECO:0000269|PubMed:11511296"
FT /id="VAR_020918"
FT VARIANT 126
FT /note="R -> C (in ARCI1; dbSNP:rs397514524)"
FT /id="VAR_058640"
FT VARIANT 126
FT /note="R -> H (in ARCI1; dbSNP:rs200491579)"
FT /id="VAR_058641"
FT VARIANT 132
FT /note="D -> N (in dbSNP:rs2229462)"
FT /id="VAR_029268"
FT VARIANT 134
FT /note="Y -> C (in ARCI1; dbSNP:rs147916609)"
FT /id="VAR_058642"
FT VARIANT 142
FT /note="R -> C (in ARCI1; dbSNP:rs121918716)"
FT /id="VAR_058643"
FT VARIANT 142
FT /note="R -> H (in ARCI1; skin phenotype consistent with
FT lamellar ichthyosis; dbSNP:rs121918718)"
FT /evidence="ECO:0000269|PubMed:7773290,
FT ECO:0000269|PubMed:9326318"
FT /id="VAR_007476"
FT VARIANT 142
FT /note="R -> P (in ARCI1)"
FT /id="VAR_058644"
FT VARIANT 143
FT /note="R -> C (in ARCI1; inhibits cell proliferation;
FT dbSNP:rs531650682)"
FT /evidence="ECO:0000269|PubMed:26220141,
FT ECO:0000269|PubMed:9326318"
FT /id="VAR_007477"
FT VARIANT 143
FT /note="R -> H (in ARCI1; skin phenotype consistent with
FT lamellar ichthyosis; dbSNP:rs121918719)"
FT /evidence="ECO:0000269|PubMed:7773290"
FT /id="VAR_007478"
FT VARIANT 144
FT /note="G -> E (in ARCI1; dbSNP:rs1465243895)"
FT /id="VAR_058645"
FT VARIANT 144
FT /note="G -> R (in ARCI1; dbSNP:rs778635368)"
FT /id="VAR_058646"
FT VARIANT 160
FT /note="S -> C (in ARCI1; dbSNP:rs121918728)"
FT /id="VAR_058647"
FT VARIANT 205
FT /note="L -> Q (in ARCI1; dbSNP:rs878853259)"
FT /id="VAR_058648"
FT VARIANT 209
FT /note="V -> F (in ARCI1)"
FT /id="VAR_058649"
FT VARIANT 212
FT /note="S -> F (in ARCI1; inhibits cell proliferation;
FT dbSNP:rs1555306304)"
FT /evidence="ECO:0000269|PubMed:26220141"
FT /id="VAR_075227"
FT VARIANT 218
FT /note="G -> S (in ARCI1; skin phenotype consistent with
FT lamellar ichthyosis; dbSNP:rs121918732)"
FT /evidence="ECO:0000269|PubMed:9326318"
FT /id="VAR_007479"
FT VARIANT 225
FT /note="R -> H (in ARCI1; dbSNP:rs549195122)"
FT /id="VAR_058650"
FT VARIANT 225
FT /note="R -> P (in ARCI1; dbSNP:rs549195122)"
FT /id="VAR_058651"
FT VARIANT 243
FT /note="I -> S (in ARCI1)"
FT /id="VAR_058652"
FT VARIANT 249
FT /note="P -> L (in ARCI1)"
FT /id="VAR_058653"
FT VARIANT 264
FT /note="R -> Q (in ARCI1; dbSNP:rs781006633)"
FT /id="VAR_058654"
FT VARIANT 264
FT /note="R -> W (in ARCI1; dbSNP:rs201868387)"
FT /id="VAR_058655"
FT VARIANT 272
FT /note="S -> P (in ARCI1; dbSNP:rs764040146)"
FT /id="VAR_058656"
FT VARIANT 276
FT /note="Y -> N (in ARCI1; dbSNP:rs397514523)"
FT /id="VAR_058657"
FT VARIANT 278
FT /note="G -> R (in ARCI1; dbSNP:rs121918725)"
FT /id="VAR_058658"
FT VARIANT 285
FT /note="E -> K (in ARCI1; dbSNP:rs749721551)"
FT /id="VAR_058659"
FT VARIANT 286
FT /note="R -> Q (in ARCI1; dbSNP:rs121918727)"
FT /id="VAR_058660"
FT VARIANT 289
FT /note="N -> T (in ARCI1; skin phenotype consistent with
FT lamellar ichthyosis; dbSNP:rs121918730)"
FT /evidence="ECO:0000269|PubMed:11511296"
FT /id="VAR_020919"
FT VARIANT 293
FT /note="F -> V (in ARCI1)"
FT /id="VAR_058661"
FT VARIANT 304
FT /note="I -> F (in ARCI1; dbSNP:rs753798494)"
FT /id="VAR_058662"
FT VARIANT 307
FT /note="R -> G (in ARCI1; dbSNP:rs121918731)"
FT /evidence="ECO:0000269|PubMed:19890349"
FT /id="VAR_058663"
FT VARIANT 307
FT /note="R -> W (in ARCI1; skin phenotype consistent with
FT lamellar ichthyosis; dbSNP:rs121918731)"
FT /evidence="ECO:0000269|PubMed:11511296"
FT /id="VAR_020920"
FT VARIANT 315
FT /note="R -> C (in ARCI1; dbSNP:rs397514525)"
FT /id="VAR_058664"
FT VARIANT 315
FT /note="R -> H (in ARCI1; dbSNP:rs143473912)"
FT /id="VAR_058665"
FT VARIANT 315
FT /note="R -> L (in ARCI1; dbSNP:rs143473912)"
FT /id="VAR_058666"
FT VARIANT 323
FT /note="R -> Q (in ARCI1; skin phenotype consistent with
FT lamellar ichthyosis; dbSNP:rs121918717)"
FT /evidence="ECO:0000269|PubMed:7824952"
FT /id="VAR_015221"
FT VARIANT 323
FT /note="R -> W (in ARCI1; dbSNP:rs771820315)"
FT /id="VAR_058667"
FT VARIANT 330
FT /note="N -> H (in ARCI1)"
FT /id="VAR_058668"
FT VARIANT 331
FT /note="S -> P (in ARCI1)"
FT /id="VAR_058669"
FT VARIANT 342
FT /note="W -> R (in ARCI1)"
FT /id="VAR_058670"
FT VARIANT 358
FT /note="S -> R (in ARCI1; dbSNP:rs779287673)"
FT /id="VAR_058671"
FT VARIANT 359
FT /note="V -> M (in ARCI1; dbSNP:rs202037016)"
FT /id="VAR_058672"
FT VARIANT 365
FT /note="Y -> D (in ARCI1)"
FT /id="VAR_058673"
FT VARIANT 366
FT /note="L -> P (in ARCI1)"
FT /id="VAR_058674"
FT VARIANT 372
FT /note="V -> I (in dbSNP:rs41293794)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_055374"
FT VARIANT 379
FT /note="V -> L (in ARCI1; dbSNP:rs121918720)"
FT /evidence="ECO:0000269|PubMed:9326318"
FT /id="VAR_007480"
FT VARIANT 382
FT /note="G -> R (in ARCI1)"
FT /id="VAR_058675"
FT VARIANT 383
FT /note="V -> M (in ARCI1; dbSNP:rs121918722)"
FT /id="VAR_058676"
FT VARIANT 389
FT /note="R -> H (in ARCI1; skin phenotype consistent with
FT non-bullous congenital ichthyosiform erythroderma;
FT dbSNP:rs121918723)"
FT /evidence="ECO:0000269|PubMed:11251583"
FT /id="VAR_015222"
FT VARIANT 389
FT /note="R -> P (in ARCI1; dbSNP:rs121918723)"
FT /id="VAR_058677"
FT VARIANT 392
FT /note="G -> D (in ARCI1; dbSNP:rs121918726)"
FT /id="VAR_058678"
FT VARIANT 396
FT /note="R -> H (in ARCI1; dbSNP:rs121918721)"
FT /id="VAR_058679"
FT VARIANT 396
FT /note="R -> L (in ARCI1; skin phenotype consistent with
FT non-bullous congenital ichthyosiform erythroderma;
FT dbSNP:rs121918721)"
FT /evidence="ECO:0000269|PubMed:9326318"
FT /id="VAR_007481"
FT VARIANT 396
FT /note="R -> S (in ARCI1)"
FT /id="VAR_058680"
FT VARIANT 401
FT /note="F -> V (in ARCI1; dbSNP:rs991194429)"
FT /id="VAR_058681"
FT VARIANT 430
FT /note="D -> V (in ARCI1; dbSNP:rs1555306103)"
FT /id="VAR_058682"
FT VARIANT 473
FT /note="G -> S (in ARCI1; dbSNP:rs904122716 and
FT dbSNP:rs1057517838)"
FT /id="VAR_058683"
FT VARIANT 490
FT /note="D -> G (in ARCI1; dbSNP:rs121918724)"
FT /id="VAR_058684"
FT VARIANT 518
FT /note="V -> M (in dbSNP:rs35312232)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_052550"
FT VARIANT 520
FT /note="E -> G (in ARCI1; dbSNP:rs142404759)"
FT /id="VAR_058685"
FT VARIANT 544
FT /note="Y -> C (in ARCI1; dbSNP:rs1044429462)"
FT /id="VAR_058686"
FT VARIANT 607
FT /note="R -> C (in dbSNP:rs2229464)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_052551"
FT VARIANT 687
FT /note="R -> C (in ARCI1; dbSNP:rs147516124)"
FT /id="VAR_058687"
FT VARIANT 687
FT /note="R -> H (in ARCI1)"
FT /id="VAR_058688"
FT VARIANT 755
FT /note="S -> L (in dbSNP:rs35926651)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_052552"
FT VARIANT 764
FT /note="R -> C (in ARCI1; dbSNP:rs201853046)"
FT /id="VAR_058689"
FT VARIANT 802
FT /note="D -> V (in dbSNP:rs2228337)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_024660"
FT CONFLICT 119..120
FT /note="Missing (in Ref. 5; M86360)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="C -> A (in Ref. 4; AAA61156)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="Q -> H (in Ref. 5; M86360)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="D -> E (in Ref. 5; M86360)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="R -> A (in Ref. 3; AAA61166)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="V -> I (in Ref. 3; AAA61166)"
FT /evidence="ECO:0000305"
FT STRAND 693..699
FT /evidence="ECO:0007829|PDB:2XZZ"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:2XZZ"
FT STRAND 707..714
FT /evidence="ECO:0007829|PDB:2XZZ"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:2XZZ"
FT STRAND 723..730
FT /evidence="ECO:0007829|PDB:2XZZ"
FT TURN 731..733
FT /evidence="ECO:0007829|PDB:2XZZ"
FT STRAND 734..741
FT /evidence="ECO:0007829|PDB:2XZZ"
FT STRAND 749..756
FT /evidence="ECO:0007829|PDB:2XZZ"
FT STRAND 767..771
FT /evidence="ECO:0007829|PDB:2XZZ"
FT HELIX 773..776
FT /evidence="ECO:0007829|PDB:2XZZ"
SQ SEQUENCE 817 AA; 89787 MW; 4732F28234F5D5F1 CRC64;
MMDGPRSDVG RWGGNPLQPP TTPSPEPEPE PDGRSRRGGG RSFWARCCGC CSCRNAADDD
WGPEPSDSRG RGSSSGTRRP GSRGSDSRRP VSRGSGVNAA GDGTIREGML VVNGVDLLSS
RSDQNRREHH TDEYEYDELI VRRGQPFHML LLLSRTYESS DRITLELLIG NNPEVGKGTH
VIIPVGKGGS GGWKAQVVKA SGQNLNLRVH TSPNAIIGKF QFTVRTQSDA GEFQLPFDPR
NEIYILFNPW CPEDIVYVDH EDWRQEYVLN ESGRIYYGTE AQIGERTWNY GQFDHGVLDA
CLYILDRRGM PYGGRGDPVN VSRVISAMVN SLDDNGVLIG NWSGDYSRGT NPSAWVGSVE
ILLSYLRTGY SVPYGQCWVF AGVTTTVLRC LGLATRTVTN FNSAHDTDTS LTMDIYFDEN
MKPLEHLNHD SVWNFHVWND CWMKRPDLPS GFDGWQVVDA TPQETSSGIF CCGPCSVESI
KNGLVYMKYD TPFIFAEVNS DKVYWQRQDD GSFKIVYVEE KAIGTLIVTK AISSNMREDI
TYLYKHPEGS DAERKAVETA AAHGSKPNVY ANRGSAEDVA MQVEAQDAVM GQDLMVSVML
INHSSSRRTV KLHLYLSVTF YTGVSGTIFK ETKKEVELAP GASDRVTMPV AYKEYRPHLV
DQGAMLLNVS GHVKESGQVL AKQHTFRLRT PDLSLTLLGA AVVGQECEVQ IVFKNPLPVT
LTNVVFRLEG SGLQRPKILN VGDIGGNETV TLRQSFVPVR PGPRQLIASL DSPQLSQVHG
VIQVDVAPAP GDGGFFSDAG GDSHLGETIP MASRGGA
