GenomeNet

Database: UniProt/SWISS-PROT
Entry: TGM1_HUMAN
LinkDB: TGM1_HUMAN
Original site: 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   22-NOV-2017, entry version 186.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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;
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
RT   enzyme 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;
RA   Phillips M.A., Stewart B.E., Rice R.H.;
RT   "Genomic structure of keratinocyte transglutaminase. Recruitment of
RT   new exon for modified function.";
RL   J. Biol. Chem. 267:2282-2286(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1348508;
RA   Kim I.-G., McBride O.W., Wang M., Kim S.-Y., Idler W.W.,
RA   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;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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;
RP   MET-518; 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.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   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.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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   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.,
RA   Fleckman P., 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   [17]
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
RT   domain.";
RL   Submitted (JAN-2011) to the PDB data bank.
RN   [18]
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.,
RA   Ponec M., Bon A., Lautenschlager S., Schorderet D.F., Hohl D.;
RT   "Mutations of keratinocyte transglutaminase in lamellar ichthyosis.";
RL   Science 267:525-528(1995).
RN   [19]
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   [20]
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
RT   ichthyosis: private and recurrent mutations in an isolated
RT   population.";
RL   Am. J. Hum. Genet. 61:529-538(1997).
RN   [21]
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   [22]
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.,
RA   Lee E.S., Candi E., Melino G., Ahvazi B., Steinert P.M.;
RT   "Novel mutations of the transglutaminase 1 gene in lamellar
RT   ichthyosis.";
RL   J. Invest. Dermatol. 117:214-218(2001).
RN   [23]
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
RT   ichthyosis: ALOX12B, ALOXE3, and TGM1 mutations in Scandinavian
RT   patients.";
RL   J. Invest. Dermatol. 130:438-443(2010).
RN   [24]
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
RT   transglutaminase 1 gene mutation associated with autosomal recessive
RT   congenital ichthyosis.";
RL   Int. J. Dermatol. 55:201-207(2016).
CC   -!- FUNCTION: Catalyzes the cross-linking of proteins and the
CC       conjugation of polyamines to proteins. Responsible for cross-
CC       linking epidermal proteins during formation of the stratum
CC       corneum. Involved in cell proliferation (PubMed:26220141).
CC       {ECO:0000269|PubMed:26220141}.
CC   -!- CATALYTIC ACTIVITY: A protein-L-glutamine + a protein-L-lysine = a
CC       protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3).
CC       {ECO:0000255|PROSITE-ProRule:PRU10024}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC       Note=Binds 1 Ca(2+) ion per subunit.;
CC   -!- INTERACTION:
CC       B2R4U6:-; NbExp=4; IntAct=EBI-2562368, EBI-10175477;
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
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         Note=No experimental confirmation available.;
CC   -!- PTM: The membrane anchorage region possesses a cluster of five
CC       cysteines within which fatty acid(s) may become thioester-linked.
CC       It is subject to phorbol ester-stimulated phosphorylation and is
CC       hypersensitive to proteolysis, which releases the enzyme in a
CC       soluble form. {ECO:0000269|PubMed:8973564}.
CC   -!- DISEASE: Ichthyosis, congenital, autosomal recessive 1 (ARCI1)
CC       [MIM:242300]: A form of autosomal recessive congenital ichthyosis,
CC       a disorder of keratinization with abnormal differentiation and
CC       desquamation of the epidermis, resulting in abnormal skin scaling
CC       over the whole body. The main skin phenotypes are lamellar
CC       ichthyosis (LI) and non-bullous congenital ichthyosiform
CC       erythroderma (NCIE), although phenotypic overlap within the same
CC       patient or among patients from the same family can occur. Lamellar
CC       ichthyosis is a condition often associated with an embedment in a
CC       collodion-like membrane at birth; skin scales later develop,
CC       covering the entire body surface. Non-bullous congenital
CC       ichthyosiform erythroderma characterized by fine whitish scaling
CC       on an erythrodermal background; larger brownish scales are present
CC       on the buttocks, neck and legs. {ECO:0000269|PubMed:11251583,
CC       ECO:0000269|PubMed:11511296, ECO:0000269|PubMed:19890349,
CC       ECO:0000269|PubMed:26220141, ECO:0000269|PubMed:7773290,
CC       ECO:0000269|PubMed:7824952, ECO:0000269|PubMed:9326318}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA61166.1; Type=Frameshift; Positions=16; Evidence={ECO:0000305};
CC       Sequence=M86360; Type=Frameshift; Positions=16, 421, 651; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/tgm1/";
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   UniGene; Hs.508950; -.
DR   PDB; 2XZZ; X-ray; 2.30 A; A=693-787.
DR   PDBsum; 2XZZ; -.
DR   ProteinModelPortal; P22735; -.
DR   SMR; P22735; -.
DR   BioGrid; 112909; 43.
DR   IntAct; P22735; 34.
DR   STRING; 9606.ENSP00000206765; -.
DR   BindingDB; P22735; -.
DR   ChEMBL; CHEMBL2810; -.
DR   DrugBank; DB00130; L-Glutamine.
DR   iPTMnet; P22735; -.
DR   PhosphoSitePlus; P22735; -.
DR   SwissPalm; P22735; -.
DR   BioMuta; TGM1; -.
DR   DMDM; 57015359; -.
DR   EPD; P22735; -.
DR   MaxQB; P22735; -.
DR   PaxDb; P22735; -.
DR   PeptideAtlas; P22735; -.
DR   PRIDE; P22735; -.
DR   DNASU; 7051; -.
DR   Ensembl; ENST00000206765; ENSP00000206765; ENSG00000092295. [P22735-1]
DR   Ensembl; ENST00000544573; ENSP00000439446; ENSG00000092295. [P22735-2]
DR   GeneID; 7051; -.
DR   KEGG; hsa:7051; -.
DR   UCSC; uc001wod.3; human. [P22735-1]
DR   CTD; 7051; -.
DR   DisGeNET; 7051; -.
DR   EuPathDB; HostDB:ENSG00000092295.11; -.
DR   GeneCards; TGM1; -.
DR   GeneReviews; TGM1; -.
DR   HGNC; HGNC:11777; TGM1.
DR   HPA; CAB015159; -.
DR   HPA; HPA040171; -.
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-healing collodion baby.
DR   PharmGKB; PA36490; -.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   GeneTree; ENSGT00760000119108; -.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; P22735; -.
DR   KO; K05619; -.
DR   OMA; DDDWGPE; -.
DR   OrthoDB; EOG091G030K; -.
DR   PhylomeDB; P22735; -.
DR   TreeFam; TF324278; -.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   SIGNOR; P22735; -.
DR   GeneWiki; Keratinocyte_transglutaminase; -.
DR   GenomeRNAi; 7051; -.
DR   PRO; PR:P22735; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000092295; -.
DR   CleanEx; HS_TGM1; -.
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; IDA:UniProtKB.
DR   GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0006464; P:cellular protein modification process; NAS:UniProtKB.
DR   GO; GO:0070268; P:cornification; TAS:Reactome.
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   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; 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; SSF81296; SSF81296; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Alternative splicing; Calcium;
KW   Complete proteome; Disease mutation; Ichthyosis; Keratinization;
KW   Lipoprotein; Membrane; Metal-binding; Phosphoprotein; Polymorphism;
KW   Reference proteome; Transferase.
FT   CHAIN         1    817       Protein-glutamine gamma-
FT                                glutamyltransferase K.
FT                                /FTId=PRO_0000213701.
FT   REGION        1    100       Membrane anchorage region.
FT   ACT_SITE    377    377       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    436    436       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    459    459       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       499    499       Calcium. {ECO:0000250}.
FT   METAL       501    501       Calcium. {ECO:0000250}.
FT   METAL       548    548       Calcium. {ECO:0000250}.
FT   METAL       553    553       Calcium. {ECO:0000250}.
FT   MOD_RES      22     22       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9JLF6}.
FT   MOD_RES      24     24       Phosphoserine.
FT                                {ECO:0000269|PubMed:8973564}.
FT   MOD_RES      68     68       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P23606}.
FT   MOD_RES      82     82       Phosphoserine.
FT                                {ECO:0000269|PubMed:8973564}.
FT   MOD_RES      85     85       Phosphoserine.
FT                                {ECO:0000269|PubMed:8973564}.
FT   MOD_RES      92     92       Phosphoserine.
FT                                {ECO:0000269|PubMed:8973564}.
FT   MOD_RES      95     95       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9JLF6}.
FT   VAR_SEQ       1    442       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056840.
FT   VARIANT      42     42       S -> Y (in ARCI1; skin phenotype
FT                                consistent with lamellar ichthyosis;
FT                                dbSNP:rs41295338).
FT                                {ECO:0000269|PubMed:7824952,
FT                                ECO:0000269|Ref.9}.
FT                                /FTId=VAR_015220.
FT   VARIANT      53     53       C -> S (in ARCI1).
FT                                /FTId=VAR_058638.
FT   VARIANT      94     94       G -> D (in ARCI1; dbSNP:rs121918729).
FT                                /FTId=VAR_058639.
FT   VARIANT     102    102       D -> V (in ARCI1; skin phenotype
FT                                consistent with lamellar ichthyosis;
FT                                dbSNP:rs398122901).
FT                                {ECO:0000269|PubMed:11511296}.
FT                                /FTId=VAR_020918.
FT   VARIANT     126    126       R -> C (in ARCI1; dbSNP:rs397514524).
FT                                /FTId=VAR_058640.
FT   VARIANT     126    126       R -> H (in ARCI1; dbSNP:rs200491579).
FT                                /FTId=VAR_058641.
FT   VARIANT     132    132       D -> N (in dbSNP:rs2229462).
FT                                /FTId=VAR_029268.
FT   VARIANT     134    134       Y -> C (in ARCI1; dbSNP:rs147916609).
FT                                /FTId=VAR_058642.
FT   VARIANT     142    142       R -> C (in ARCI1; dbSNP:rs121918716).
FT                                /FTId=VAR_058643.
FT   VARIANT     142    142       R -> H (in ARCI1; skin phenotype
FT                                consistent with lamellar ichthyosis;
FT                                dbSNP:rs121918718).
FT                                {ECO:0000269|PubMed:7773290,
FT                                ECO:0000269|PubMed:9326318}.
FT                                /FTId=VAR_007476.
FT   VARIANT     142    142       R -> P (in ARCI1).
FT                                /FTId=VAR_058644.
FT   VARIANT     143    143       R -> C (in ARCI1; compound heterozygote
FT                                with F-212; inhibits cell proliferation;
FT                                dbSNP:rs531650682).
FT                                {ECO:0000269|PubMed:26220141,
FT                                ECO:0000269|PubMed:9326318}.
FT                                /FTId=VAR_007477.
FT   VARIANT     143    143       R -> H (in ARCI1; skin phenotype
FT                                consistent with lamellar ichthyosis;
FT                                dbSNP:rs121918719).
FT                                {ECO:0000269|PubMed:7773290}.
FT                                /FTId=VAR_007478.
FT   VARIANT     144    144       G -> E (in ARCI1).
FT                                /FTId=VAR_058645.
FT   VARIANT     144    144       G -> R (in ARCI1; dbSNP:rs778635368).
FT                                /FTId=VAR_058646.
FT   VARIANT     160    160       S -> C (in ARCI1; dbSNP:rs121918728).
FT                                /FTId=VAR_058647.
FT   VARIANT     205    205       L -> Q (in ARCI1; dbSNP:rs878853259).
FT                                /FTId=VAR_058648.
FT   VARIANT     209    209       V -> F (in ARCI1).
FT                                /FTId=VAR_058649.
FT   VARIANT     212    212       S -> F (in ARCI1; compound heterozygote
FT                                with C-143; inhibits cell proliferation).
FT                                {ECO:0000269|PubMed:26220141}.
FT                                /FTId=VAR_075227.
FT   VARIANT     218    218       G -> S (in ARCI1; skin phenotype
FT                                consistent with lamellar ichthyosis;
FT                                dbSNP:rs121918732).
FT                                {ECO:0000269|PubMed:9326318}.
FT                                /FTId=VAR_007479.
FT   VARIANT     225    225       R -> H (in ARCI1; dbSNP:rs549195122).
FT                                /FTId=VAR_058650.
FT   VARIANT     225    225       R -> P (in ARCI1).
FT                                /FTId=VAR_058651.
FT   VARIANT     243    243       I -> S (in ARCI1).
FT                                /FTId=VAR_058652.
FT   VARIANT     249    249       P -> L (in ARCI1).
FT                                /FTId=VAR_058653.
FT   VARIANT     264    264       R -> Q (in ARCI1; dbSNP:rs781006633).
FT                                /FTId=VAR_058654.
FT   VARIANT     264    264       R -> W (in ARCI1; dbSNP:rs201868387).
FT                                /FTId=VAR_058655.
FT   VARIANT     272    272       S -> P (in ARCI1; dbSNP:rs764040146).
FT                                /FTId=VAR_058656.
FT   VARIANT     276    276       Y -> N (in ARCI1; dbSNP:rs397514523).
FT                                /FTId=VAR_058657.
FT   VARIANT     278    278       G -> R (in ARCI1; dbSNP:rs121918725).
FT                                /FTId=VAR_058658.
FT   VARIANT     285    285       E -> K (in ARCI1; dbSNP:rs749721551).
FT                                /FTId=VAR_058659.
FT   VARIANT     286    286       R -> Q (in ARCI1; dbSNP:rs121918727).
FT                                /FTId=VAR_058660.
FT   VARIANT     289    289       N -> T (in ARCI1; skin phenotype
FT                                consistent with lamellar ichthyosis;
FT                                dbSNP:rs121918730).
FT                                {ECO:0000269|PubMed:11511296}.
FT                                /FTId=VAR_020919.
FT   VARIANT     293    293       F -> V (in ARCI1).
FT                                /FTId=VAR_058661.
FT   VARIANT     304    304       I -> F (in ARCI1; dbSNP:rs753798494).
FT                                /FTId=VAR_058662.
FT   VARIANT     307    307       R -> G (in ARCI1; dbSNP:rs121918731).
FT                                {ECO:0000269|PubMed:19890349}.
FT                                /FTId=VAR_058663.
FT   VARIANT     307    307       R -> W (in ARCI1; skin phenotype
FT                                consistent with lamellar ichthyosis;
FT                                dbSNP:rs121918731).
FT                                {ECO:0000269|PubMed:11511296}.
FT                                /FTId=VAR_020920.
FT   VARIANT     315    315       R -> C (in ARCI1; dbSNP:rs397514525).
FT                                /FTId=VAR_058664.
FT   VARIANT     315    315       R -> H (in ARCI1; dbSNP:rs143473912).
FT                                /FTId=VAR_058665.
FT   VARIANT     315    315       R -> L (in ARCI1; dbSNP:rs143473912).
FT                                /FTId=VAR_058666.
FT   VARIANT     323    323       R -> Q (in ARCI1; skin phenotype
FT                                consistent with lamellar ichthyosis;
FT                                dbSNP:rs121918717).
FT                                {ECO:0000269|PubMed:7824952}.
FT                                /FTId=VAR_015221.
FT   VARIANT     323    323       R -> W (in ARCI1; dbSNP:rs771820315).
FT                                /FTId=VAR_058667.
FT   VARIANT     330    330       N -> H (in ARCI1).
FT                                /FTId=VAR_058668.
FT   VARIANT     331    331       S -> P (in ARCI1).
FT                                /FTId=VAR_058669.
FT   VARIANT     342    342       W -> R (in ARCI1).
FT                                /FTId=VAR_058670.
FT   VARIANT     358    358       S -> R (in ARCI1; dbSNP:rs779287673).
FT                                /FTId=VAR_058671.
FT   VARIANT     359    359       V -> M (in ARCI1; dbSNP:rs202037016).
FT                                /FTId=VAR_058672.
FT   VARIANT     365    365       Y -> D (in ARCI1).
FT                                /FTId=VAR_058673.
FT   VARIANT     366    366       L -> P (in ARCI1).
FT                                /FTId=VAR_058674.
FT   VARIANT     372    372       V -> I (in dbSNP:rs41293794).
FT                                {ECO:0000269|Ref.9}.
FT                                /FTId=VAR_055374.
FT   VARIANT     379    379       V -> L (in ARCI1; dbSNP:rs121918720).
FT                                {ECO:0000269|PubMed:9326318}.
FT                                /FTId=VAR_007480.
FT   VARIANT     382    382       G -> R (in ARCI1).
FT                                /FTId=VAR_058675.
FT   VARIANT     383    383       V -> M (in ARCI1; dbSNP:rs121918722).
FT                                /FTId=VAR_058676.
FT   VARIANT     389    389       R -> H (in ARCI1; skin phenotype
FT                                consistent with non-bullous congenital
FT                                ichthyosiform erythroderma;
FT                                dbSNP:rs121918723).
FT                                {ECO:0000269|PubMed:11251583}.
FT                                /FTId=VAR_015222.
FT   VARIANT     389    389       R -> P (in ARCI1; dbSNP:rs121918723).
FT                                /FTId=VAR_058677.
FT   VARIANT     392    392       G -> D (in ARCI1; dbSNP:rs121918726).
FT                                /FTId=VAR_058678.
FT   VARIANT     396    396       R -> H (in ARCI1; dbSNP:rs121918721).
FT                                /FTId=VAR_058679.
FT   VARIANT     396    396       R -> L (in ARCI1; skin phenotype
FT                                consistent with non-bullous congenital
FT                                ichthyosiform erythroderma;
FT                                dbSNP:rs121918721).
FT                                {ECO:0000269|PubMed:9326318}.
FT                                /FTId=VAR_007481.
FT   VARIANT     396    396       R -> S (in ARCI1).
FT                                /FTId=VAR_058680.
FT   VARIANT     401    401       F -> V (in ARCI1).
FT                                /FTId=VAR_058681.
FT   VARIANT     430    430       D -> V (in ARCI1).
FT                                /FTId=VAR_058682.
FT   VARIANT     473    473       G -> S (in ARCI1).
FT                                /FTId=VAR_058683.
FT   VARIANT     490    490       D -> G (in ARCI1; dbSNP:rs121918724).
FT                                /FTId=VAR_058684.
FT   VARIANT     518    518       V -> M (in dbSNP:rs35312232).
FT                                {ECO:0000269|Ref.9}.
FT                                /FTId=VAR_052550.
FT   VARIANT     520    520       E -> G (in ARCI1; dbSNP:rs142404759).
FT                                /FTId=VAR_058685.
FT   VARIANT     544    544       Y -> C (in ARCI1).
FT                                /FTId=VAR_058686.
FT   VARIANT     607    607       R -> C (in dbSNP:rs2229464).
FT                                {ECO:0000269|Ref.9}.
FT                                /FTId=VAR_052551.
FT   VARIANT     687    687       R -> C (in ARCI1; dbSNP:rs147516124).
FT                                /FTId=VAR_058687.
FT   VARIANT     687    687       R -> H (in ARCI1).
FT                                /FTId=VAR_058688.
FT   VARIANT     755    755       S -> L (in dbSNP:rs35926651).
FT                                {ECO:0000269|Ref.9}.
FT                                /FTId=VAR_052552.
FT   VARIANT     764    764       R -> C (in ARCI1; dbSNP:rs201853046).
FT                                /FTId=VAR_058689.
FT   VARIANT     802    802       D -> V (in dbSNP:rs2228337).
FT                                {ECO:0000269|Ref.9}.
FT                                /FTId=VAR_024660.
FT   CONFLICT    119    120       Missing (in Ref. 5; M86360).
FT                                {ECO:0000305}.
FT   CONFLICT    301    301       C -> A (in Ref. 4; AAA61156).
FT                                {ECO:0000305}.
FT   CONFLICT    508    508       Q -> H (in Ref. 5; M86360).
FT                                {ECO:0000305}.
FT   CONFLICT    551    551       D -> E (in Ref. 5; M86360).
FT                                {ECO:0000305}.
FT   CONFLICT    554    554       R -> A (in Ref. 3; AAA61166).
FT                                {ECO:0000305}.
FT   CONFLICT    669    669       V -> I (in Ref. 3; AAA61166).
FT                                {ECO:0000305}.
FT   STRAND      693    699       {ECO:0000244|PDB:2XZZ}.
FT   STRAND      703    705       {ECO:0000244|PDB:2XZZ}.
FT   STRAND      707    714       {ECO:0000244|PDB:2XZZ}.
FT   STRAND      717    719       {ECO:0000244|PDB:2XZZ}.
FT   STRAND      723    730       {ECO:0000244|PDB:2XZZ}.
FT   TURN        731    733       {ECO:0000244|PDB:2XZZ}.
FT   STRAND      734    741       {ECO:0000244|PDB:2XZZ}.
FT   STRAND      749    756       {ECO:0000244|PDB:2XZZ}.
FT   STRAND      767    771       {ECO:0000244|PDB:2XZZ}.
FT   HELIX       773    776       {ECO:0000244|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
//
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