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Protein-glutamine gamma-glutamyltransferase K (EC 2.3.2.13) (Epidermal TGase) (Transglutaminase K) (TG(K)) (TGK) (TGase K) (Transglutaminase-1) (TGase-1)

 TGM1_HUMAN              Reviewed;         817 AA.
P22735; B4DWR7; Q197M4;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 4.
25-OCT-2017, entry version 185.
RecName: Full=Protein-glutamine gamma-glutamyltransferase K;
EC=2.3.2.13;
AltName: Full=Epidermal TGase;
AltName: Full=Transglutaminase K;
Short=TG(K);
Short=TGK;
Short=TGase K;
AltName: Full=Transglutaminase-1;
Short=TGase-1;
Name=TGM1; Synonyms=KTG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1979171; DOI=10.1073/pnas.87.23.9333;
Phillips M.A., Stewart B.E., Qin Q., Chakravarty R., Floyd E.E.,
Jetten A.M., Rice R.H.;
"Primary structure of keratinocyte transglutaminase.";
Proc. Natl. Acad. Sci. U.S.A. 87:9333-9337(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Keratinocyte;
PubMed=1673840; DOI=10.1016/0006-291X(91)91651-R;
Yamanishi K., Liew F.M., Konishi K., Yasuno H., Doi H., Hirano J.,
Fukushima S.;
"Molecular cloning of human epidermal transglutaminase cDNA from
keratinocytes in culture.";
Biochem. Biophys. Res. Commun. 175:906-913(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1670769;
Kim H.C., Idler W.W., Kim I.-G., Han J.H., Chung S.-I., Steinert P.M.;
"The complete amino acid sequence of the human transglutaminase K
enzyme deduced from the nucleic acid sequences of cDNA clones.";
J. Biol. Chem. 266:536-539(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=1346394;
Phillips M.A., Stewart B.E., Rice R.H.;
"Genomic structure of keratinocyte transglutaminase. Recruitment of
new exon for modified function.";
J. Biol. Chem. 267:2282-2286(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1348508;
Kim I.-G., McBride O.W., Wang M., Kim S.-Y., Idler W.W.,
Steinert P.M.;
"Structure and organization of the human transglutaminase 1 gene.";
J. Biol. Chem. 267:7710-7717(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=1381356;
Yamanishi K., Inazawa J., Liew F., Nonomura K., Ariyama T., Yasuno H.,
Abe T., Doi H., Hirano J., Fukushima S.;
"Structure of the gene for human transglutaminase 1.";
J. Biol. Chem. 267:17858-17863(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=1350092; DOI=10.1073/pnas.89.10.4476;
Polakowska R.R., Eickbush T., Falciano V., Razvi F., Goldsmith L.A.;
"Organization and evolution of the human epidermal keratinocyte
transglutaminase I gene.";
Proc. Natl. Acad. Sci. U.S.A. 89:4476-4480(1992).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Esophagus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-42; ILE-372;
MET-518; CYS-607; LEU-755 AND VAL-802.
NIEHS SNPs program;
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-551 (ISOFORM 1).
PubMed=1704039; DOI=10.1111/1523-1747.ep12464554;
Polakowska R., Herting E., Goldsmith L.A.;
"Isolation of cDNA for human epidermal type I transglutaminase.";
J. Invest. Dermatol. 96:285-288(1991).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 375-817 (ISOFORM 1).
TISSUE=Skin;
PubMed=1351505; DOI=10.1111/1523-1747.ep12611394;
Schroeder W., Thacher S., Stewart-Galetka S., Annarella M., Chema D.,
Sicliano M., Davies P., Tang H.Y., Sowa B., Duvic M.;
"Type I keratinocyte transglutaminase: expression in human skin and
psoriasis.";
J. Invest. Dermatol. 99:27-34(1992).
[15]
PHOSPHORYLATION AT SER-24; SER-82; SER-85 AND SER-92.
PubMed=8973564; DOI=10.1042/bj3200547;
Rice R.H., Mehrpouyan M., Quin Q., Phillips M.A., Lee Y.M.;
"Identification of phosphorylation sites in keratinocyte
transglutaminase.";
Biochem. J. 320:547-550(1996).
[16]
REVIEW ON VARIANTS.
PubMed=19241467; DOI=10.1002/humu.20952;
Herman M.L., Farasat S., Steinbach P.J., Wei M.H., Toure O.,
Fleckman P., Blake P., Bale S.J., Toro J.R.;
"Transglutaminase-1 gene mutations in autosomal recessive congenital
ichthyosis: summary of mutations (including 23 novel) and modeling of
TGase-1.";
Hum. Mutat. 30:537-547(2009).
[17]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 693-787.
Structural genomics consortium (SGC);
"Crystal structure of the human transglutaminase 1 beta-barrel
domain.";
Submitted (JAN-2011) to the PDB data bank.
[18]
VARIANTS ARCI1 TYR-42 AND GLN-323, AND INVOLVEMENT IN ARC11.
PubMed=7824952; DOI=10.1126/science.7824952;
Huber M., Rettler I., Bernasconi K., Frenk E., Lavrijsen S.P.M.,
Ponec M., Bon A., Lautenschlager S., Schorderet D.F., Hohl D.;
"Mutations of keratinocyte transglutaminase in lamellar ichthyosis.";
Science 267:525-528(1995).
[19]
VARIANTS ARCI1 HIS-142 AND HIS-143.
PubMed=7773290; DOI=10.1038/ng0395-279;
Russell L.J., Digiovanna J.J., Rogers G.R., Steinert P.M., Hashem N.,
Compton J.G., Bale S.J.;
"Mutations in the gene for transglutaminase 1 in autosomal recessive
lamellar ichthyosis.";
Nat. Genet. 9:279-283(1995).
[20]
VARIANTS ARCI1 HIS-142; CYS-143; SER-218; LEU-379 AND LEU-396.
PubMed=9326318; DOI=10.1086/515498;
Laiho E., Ignatius J., Mikkola H., Yee V.C., Teller D.C., Niemi K.-M.,
Saarialho-Kere U., Kere J., Palotie A.;
"Transglutaminase 1 mutations in autosomal recessive congenital
ichthyosis: private and recurrent mutations in an isolated
population.";
Am. J. Hum. Genet. 61:529-538(1997).
[21]
VARIANT ARCI1 HIS-389.
PubMed=11251583; DOI=10.1046/j.1365-2133.2001.04037.x;
Akiyama M., Takizawa Y., Kokaji T., Shimizu H.;
"Novel mutations of TGM1 in a child with congenital ichthyosiform
erythroderma.";
Br. J. Dermatol. 144:401-407(2001).
[22]
VARIANTS ARCI1 VAL-102; THR-289 AND TRP-307.
PubMed=11511296; DOI=10.1046/j.0022-202x.2001.01429.x;
Yang J.M., Ahn K.S., Cho M.O., Yoneda K., Lee C.H., Lee J.H.,
Lee E.S., Candi E., Melino G., Ahvazi B., Steinert P.M.;
"Novel mutations of the transglutaminase 1 gene in lamellar
ichthyosis.";
J. Invest. Dermatol. 117:214-218(2001).
[23]
VARIANT ARCI1 GLY-307.
PubMed=19890349; DOI=10.1038/jid.2009.346;
Vahlquist A., Bygum A., Gaanemo A., Virtanen M., Hellstroem-Pigg M.,
Strauss G., Brandrup F., Fischer J.;
"Genotypic and clinical spectrum of self-improving collodion
ichthyosis: ALOX12B, ALOXE3, and TGM1 mutations in Scandinavian
patients.";
J. Invest. Dermatol. 130:438-443(2010).
[24]
VARIANTS ARCI1 CYS-143 AND PHE-212, CHARACTERIZATION OF VARIANTS ARCI1
CYS-143 AND PHE-212, AND FUNCTION.
PubMed=26220141; DOI=10.1111/ijd.12806;
Zhang S.Q., Li C.X., Gao X.Q., Qiu W.Y., Chen Q., Li X.M., Zhou X.,
Tian X., Tang Z.P., Zhao T., Zhang F., Zhang X.B.;
"Identification and functional characterization of a novel
transglutaminase 1 gene mutation associated with autosomal recessive
congenital ichthyosis.";
Int. J. Dermatol. 55:201-207(2016).
-!- FUNCTION: Catalyzes the cross-linking of proteins and the
conjugation of polyamines to proteins. Responsible for cross-
linking epidermal proteins during formation of the stratum
corneum. Involved in cell proliferation (PubMed:26220141).
{ECO:0000269|PubMed:26220141}.
-!- CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N(5)-
alkylglutamine + NH(3). {ECO:0000255|PROSITE-ProRule:PRU10024}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 1 Ca(2+) ion per subunit.;
-!- INTERACTION:
B2R4U6:-; NbExp=4; IntAct=EBI-2562368, EBI-10175477;
-!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P22735-1; Sequence=Displayed;
Name=2;
IsoId=P22735-2; Sequence=VSP_056840;
Note=No experimental confirmation available.;
-!- PTM: The membrane anchorage region possesses a cluster of five
cysteines within which fatty acid(s) may become thioester-linked.
It is subject to phorbol ester-stimulated phosphorylation and is
hypersensitive to proteolysis, which releases the enzyme in a
soluble form. {ECO:0000269|PubMed:8973564}.
-!- DISEASE: Ichthyosis, congenital, autosomal recessive 1 (ARCI1)
[MIM:242300]: A form of autosomal recessive congenital ichthyosis,
a disorder of keratinization with abnormal differentiation and
desquamation of the epidermis, resulting in abnormal skin scaling
over the whole body. The main skin phenotypes are lamellar
ichthyosis (LI) and non-bullous congenital ichthyosiform
erythroderma (NCIE), although phenotypic overlap within the same
patient or among patients from the same family can occur. Lamellar
ichthyosis is a condition often associated with an embedment in a
collodion-like membrane at birth; skin scales later develop,
covering the entire body surface. Non-bullous congenital
ichthyosiform erythroderma characterized by fine whitish scaling
on an erythrodermal background; larger brownish scales are present
on the buttocks, neck and legs. {ECO:0000269|PubMed:11251583,
ECO:0000269|PubMed:11511296, ECO:0000269|PubMed:19890349,
ECO:0000269|PubMed:26220141, ECO:0000269|PubMed:7773290,
ECO:0000269|PubMed:7824952, ECO:0000269|PubMed:9326318}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the transglutaminase superfamily.
Transglutaminase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA61166.1; Type=Frameshift; Positions=16; Evidence={ECO:0000305};
Sequence=M86360; Type=Frameshift; Positions=16, 421, 651; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tgm1/";
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EMBL; M55183; AAA59474.1; -; mRNA.
EMBL; D90287; BAA14329.1; -; mRNA.
EMBL; M62925; AAA61166.1; ALT_FRAME; mRNA.
EMBL; M83230; AAA61156.1; -; Genomic_DNA.
EMBL; M83227; AAA61156.1; JOINED; Genomic_DNA.
EMBL; M83228; AAA61156.1; JOINED; Genomic_DNA.
EMBL; M83229; AAA61156.1; JOINED; Genomic_DNA.
EMBL; M86360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D10353; BAA34203.1; -; Genomic_DNA.
EMBL; M98447; AAA96667.1; -; Genomic_DNA.
EMBL; AK301652; BAG63129.1; -; mRNA.
EMBL; AK315843; BAF98734.1; -; mRNA.
EMBL; DQ640500; ABF70204.1; -; Genomic_DNA.
EMBL; AL096870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW66047.1; -; Genomic_DNA.
EMBL; BC034699; AAH34699.1; -; mRNA.
EMBL; X57974; CAA41040.1; -; mRNA.
CCDS; CCDS9622.1; -. [P22735-1]
PIR; A43401; TGHUM1.
RefSeq; NP_000350.1; NM_000359.2. [P22735-1]
UniGene; Hs.508950; -.
PDB; 2XZZ; X-ray; 2.30 A; A=693-787.
PDBsum; 2XZZ; -.
ProteinModelPortal; P22735; -.
SMR; P22735; -.
BioGrid; 112909; 43.
IntAct; P22735; 34.
STRING; 9606.ENSP00000206765; -.
BindingDB; P22735; -.
ChEMBL; CHEMBL2810; -.
DrugBank; DB00130; L-Glutamine.
iPTMnet; P22735; -.
PhosphoSitePlus; P22735; -.
SwissPalm; P22735; -.
BioMuta; TGM1; -.
DMDM; 57015359; -.
EPD; P22735; -.
MaxQB; P22735; -.
PaxDb; P22735; -.
PeptideAtlas; P22735; -.
PRIDE; P22735; -.
DNASU; 7051; -.
Ensembl; ENST00000206765; ENSP00000206765; ENSG00000092295. [P22735-1]
Ensembl; ENST00000544573; ENSP00000439446; ENSG00000092295. [P22735-2]
GeneID; 7051; -.
KEGG; hsa:7051; -.
UCSC; uc001wod.3; human. [P22735-1]
CTD; 7051; -.
DisGeNET; 7051; -.
EuPathDB; HostDB:ENSG00000092295.11; -.
GeneCards; TGM1; -.
GeneReviews; TGM1; -.
HGNC; HGNC:11777; TGM1.
HPA; CAB015159; -.
HPA; HPA040171; -.
MalaCards; TGM1; -.
MIM; 190195; gene.
MIM; 242300; phenotype.
neXtProt; NX_P22735; -.
OpenTargets; ENSG00000092295; -.
Orphanet; 281127; Acral self-healing collodion baby.
Orphanet; 100976; Bathing suit ichthyosis.
Orphanet; 79394; Congenital non-bullous ichthyosiform erythroderma.
Orphanet; 313; Lamellar ichthyosis.
Orphanet; 281122; Self-healing collodion baby.
PharmGKB; PA36490; -.
eggNOG; ENOG410IFMV; Eukaryota.
eggNOG; ENOG410XQEZ; LUCA.
GeneTree; ENSGT00760000119108; -.
HOGENOM; HOG000231695; -.
HOVERGEN; HBG004342; -.
InParanoid; P22735; -.
KO; K05619; -.
OMA; DDDWGPE; -.
OrthoDB; EOG091G030K; -.
PhylomeDB; P22735; -.
TreeFam; TF324278; -.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
SIGNOR; P22735; -.
GeneWiki; Keratinocyte_transglutaminase; -.
GenomeRNAi; 7051; -.
PRO; PR:P22735; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000092295; -.
CleanEx; HS_TGM1; -.
ExpressionAtlas; P22735; baseline and differential.
Genevisible; P22735; HS.
GO; GO:0001533; C:cornified envelope; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IDA:UniProtKB.
GO; GO:0043163; P:cell envelope organization; TAS:UniProtKB.
GO; GO:0006464; P:cellular protein modification process; NAS:UniProtKB.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
GO; GO:0018149; P:peptide cross-linking; IDA:CAFA.
GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IMP:UniProtKB.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.90.260.10; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002931; Transglutaminase-like.
InterPro; IPR036985; Transglutaminase-like_sf.
InterPro; IPR023608; Transglutaminase_animal.
InterPro; IPR013808; Transglutaminase_AS.
InterPro; IPR008958; Transglutaminase_C.
InterPro; IPR036238; Transglutaminase_C_sf.
InterPro; IPR001102; Transglutaminase_N.
Pfam; PF00927; Transglut_C; 2.
Pfam; PF01841; Transglut_core; 1.
Pfam; PF00868; Transglut_N; 1.
PIRSF; PIRSF000459; TGM_EBP42; 1.
SMART; SM00460; TGc; 1.
SUPFAM; SSF49309; SSF49309; 2.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS00547; TRANSGLUTAMINASES; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Alternative splicing; Calcium;
Complete proteome; Disease mutation; Ichthyosis; Keratinization;
Lipoprotein; Membrane; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Transferase.
CHAIN 1 817 Protein-glutamine gamma-
glutamyltransferase K.
/FTId=PRO_0000213701.
REGION 1 100 Membrane anchorage region.
ACT_SITE 377 377 {ECO:0000255|PROSITE-ProRule:PRU10024}.
ACT_SITE 436 436 {ECO:0000255|PROSITE-ProRule:PRU10024}.
ACT_SITE 459 459 {ECO:0000255|PROSITE-ProRule:PRU10024}.
METAL 499 499 Calcium. {ECO:0000250}.
METAL 501 501 Calcium. {ECO:0000250}.
METAL 548 548 Calcium. {ECO:0000250}.
METAL 553 553 Calcium. {ECO:0000250}.
MOD_RES 22 22 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9JLF6}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000269|PubMed:8973564}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000250|UniProtKB:P23606}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000269|PubMed:8973564}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000269|PubMed:8973564}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000269|PubMed:8973564}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JLF6}.
VAR_SEQ 1 442 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056840.
VARIANT 42 42 S -> Y (in ARCI1; skin phenotype
consistent with lamellar ichthyosis;
dbSNP:rs41295338).
{ECO:0000269|PubMed:7824952,
ECO:0000269|Ref.9}.
/FTId=VAR_015220.
VARIANT 53 53 C -> S (in ARCI1).
/FTId=VAR_058638.
VARIANT 94 94 G -> D (in ARCI1; dbSNP:rs121918729).
/FTId=VAR_058639.
VARIANT 102 102 D -> V (in ARCI1; skin phenotype
consistent with lamellar ichthyosis;
dbSNP:rs398122901).
{ECO:0000269|PubMed:11511296}.
/FTId=VAR_020918.
VARIANT 126 126 R -> C (in ARCI1; dbSNP:rs397514524).
/FTId=VAR_058640.
VARIANT 126 126 R -> H (in ARCI1; dbSNP:rs200491579).
/FTId=VAR_058641.
VARIANT 132 132 D -> N (in dbSNP:rs2229462).
/FTId=VAR_029268.
VARIANT 134 134 Y -> C (in ARCI1; dbSNP:rs147916609).
/FTId=VAR_058642.
VARIANT 142 142 R -> C (in ARCI1; dbSNP:rs121918716).
/FTId=VAR_058643.
VARIANT 142 142 R -> H (in ARCI1; skin phenotype
consistent with lamellar ichthyosis;
dbSNP:rs121918718).
{ECO:0000269|PubMed:7773290,
ECO:0000269|PubMed:9326318}.
/FTId=VAR_007476.
VARIANT 142 142 R -> P (in ARCI1).
/FTId=VAR_058644.
VARIANT 143 143 R -> C (in ARCI1; compound heterozygote
with F-212; inhibits cell proliferation;
dbSNP:rs531650682).
{ECO:0000269|PubMed:26220141,
ECO:0000269|PubMed:9326318}.
/FTId=VAR_007477.
VARIANT 143 143 R -> H (in ARCI1; skin phenotype
consistent with lamellar ichthyosis;
dbSNP:rs121918719).
{ECO:0000269|PubMed:7773290}.
/FTId=VAR_007478.
VARIANT 144 144 G -> E (in ARCI1).
/FTId=VAR_058645.
VARIANT 144 144 G -> R (in ARCI1; dbSNP:rs778635368).
/FTId=VAR_058646.
VARIANT 160 160 S -> C (in ARCI1; dbSNP:rs121918728).
/FTId=VAR_058647.
VARIANT 205 205 L -> Q (in ARCI1; dbSNP:rs878853259).
/FTId=VAR_058648.
VARIANT 209 209 V -> F (in ARCI1).
/FTId=VAR_058649.
VARIANT 212 212 S -> F (in ARCI1; compound heterozygote
with C-143; inhibits cell proliferation).
{ECO:0000269|PubMed:26220141}.
/FTId=VAR_075227.
VARIANT 218 218 G -> S (in ARCI1; skin phenotype
consistent with lamellar ichthyosis;
dbSNP:rs121918732).
{ECO:0000269|PubMed:9326318}.
/FTId=VAR_007479.
VARIANT 225 225 R -> H (in ARCI1; dbSNP:rs549195122).
/FTId=VAR_058650.
VARIANT 225 225 R -> P (in ARCI1).
/FTId=VAR_058651.
VARIANT 243 243 I -> S (in ARCI1).
/FTId=VAR_058652.
VARIANT 249 249 P -> L (in ARCI1).
/FTId=VAR_058653.
VARIANT 264 264 R -> Q (in ARCI1; dbSNP:rs781006633).
/FTId=VAR_058654.
VARIANT 264 264 R -> W (in ARCI1; dbSNP:rs201868387).
/FTId=VAR_058655.
VARIANT 272 272 S -> P (in ARCI1; dbSNP:rs764040146).
/FTId=VAR_058656.
VARIANT 276 276 Y -> N (in ARCI1; dbSNP:rs397514523).
/FTId=VAR_058657.
VARIANT 278 278 G -> R (in ARCI1; dbSNP:rs121918725).
/FTId=VAR_058658.
VARIANT 285 285 E -> K (in ARCI1; dbSNP:rs749721551).
/FTId=VAR_058659.
VARIANT 286 286 R -> Q (in ARCI1; dbSNP:rs121918727).
/FTId=VAR_058660.
VARIANT 289 289 N -> T (in ARCI1; skin phenotype
consistent with lamellar ichthyosis;
dbSNP:rs121918730).
{ECO:0000269|PubMed:11511296}.
/FTId=VAR_020919.
VARIANT 293 293 F -> V (in ARCI1).
/FTId=VAR_058661.
VARIANT 304 304 I -> F (in ARCI1; dbSNP:rs753798494).
/FTId=VAR_058662.
VARIANT 307 307 R -> G (in ARCI1; dbSNP:rs121918731).
{ECO:0000269|PubMed:19890349}.
/FTId=VAR_058663.
VARIANT 307 307 R -> W (in ARCI1; skin phenotype
consistent with lamellar ichthyosis;
dbSNP:rs121918731).
{ECO:0000269|PubMed:11511296}.
/FTId=VAR_020920.
VARIANT 315 315 R -> C (in ARCI1; dbSNP:rs397514525).
/FTId=VAR_058664.
VARIANT 315 315 R -> H (in ARCI1; dbSNP:rs143473912).
/FTId=VAR_058665.
VARIANT 315 315 R -> L (in ARCI1; dbSNP:rs143473912).
/FTId=VAR_058666.
VARIANT 323 323 R -> Q (in ARCI1; skin phenotype
consistent with lamellar ichthyosis;
dbSNP:rs121918717).
{ECO:0000269|PubMed:7824952}.
/FTId=VAR_015221.
VARIANT 323 323 R -> W (in ARCI1; dbSNP:rs771820315).
/FTId=VAR_058667.
VARIANT 330 330 N -> H (in ARCI1).
/FTId=VAR_058668.
VARIANT 331 331 S -> P (in ARCI1).
/FTId=VAR_058669.
VARIANT 342 342 W -> R (in ARCI1).
/FTId=VAR_058670.
VARIANT 358 358 S -> R (in ARCI1; dbSNP:rs779287673).
/FTId=VAR_058671.
VARIANT 359 359 V -> M (in ARCI1; dbSNP:rs202037016).
/FTId=VAR_058672.
VARIANT 365 365 Y -> D (in ARCI1).
/FTId=VAR_058673.
VARIANT 366 366 L -> P (in ARCI1).
/FTId=VAR_058674.
VARIANT 372 372 V -> I (in dbSNP:rs41293794).
{ECO:0000269|Ref.9}.
/FTId=VAR_055374.
VARIANT 379 379 V -> L (in ARCI1; dbSNP:rs121918720).
{ECO:0000269|PubMed:9326318}.
/FTId=VAR_007480.
VARIANT 382 382 G -> R (in ARCI1).
/FTId=VAR_058675.
VARIANT 383 383 V -> M (in ARCI1; dbSNP:rs121918722).
/FTId=VAR_058676.
VARIANT 389 389 R -> H (in ARCI1; skin phenotype
consistent with non-bullous congenital
ichthyosiform erythroderma;
dbSNP:rs121918723).
{ECO:0000269|PubMed:11251583}.
/FTId=VAR_015222.
VARIANT 389 389 R -> P (in ARCI1; dbSNP:rs121918723).
/FTId=VAR_058677.
VARIANT 392 392 G -> D (in ARCI1; dbSNP:rs121918726).
/FTId=VAR_058678.
VARIANT 396 396 R -> H (in ARCI1; dbSNP:rs121918721).
/FTId=VAR_058679.
VARIANT 396 396 R -> L (in ARCI1; skin phenotype
consistent with non-bullous congenital
ichthyosiform erythroderma;
dbSNP:rs121918721).
{ECO:0000269|PubMed:9326318}.
/FTId=VAR_007481.
VARIANT 396 396 R -> S (in ARCI1).
/FTId=VAR_058680.
VARIANT 401 401 F -> V (in ARCI1).
/FTId=VAR_058681.
VARIANT 430 430 D -> V (in ARCI1).
/FTId=VAR_058682.
VARIANT 473 473 G -> S (in ARCI1).
/FTId=VAR_058683.
VARIANT 490 490 D -> G (in ARCI1; dbSNP:rs121918724).
/FTId=VAR_058684.
VARIANT 518 518 V -> M (in dbSNP:rs35312232).
{ECO:0000269|Ref.9}.
/FTId=VAR_052550.
VARIANT 520 520 E -> G (in ARCI1; dbSNP:rs142404759).
/FTId=VAR_058685.
VARIANT 544 544 Y -> C (in ARCI1).
/FTId=VAR_058686.
VARIANT 607 607 R -> C (in dbSNP:rs2229464).
{ECO:0000269|Ref.9}.
/FTId=VAR_052551.
VARIANT 687 687 R -> C (in ARCI1; dbSNP:rs147516124).
/FTId=VAR_058687.
VARIANT 687 687 R -> H (in ARCI1).
/FTId=VAR_058688.
VARIANT 755 755 S -> L (in dbSNP:rs35926651).
{ECO:0000269|Ref.9}.
/FTId=VAR_052552.
VARIANT 764 764 R -> C (in ARCI1; dbSNP:rs201853046).
/FTId=VAR_058689.
VARIANT 802 802 D -> V (in dbSNP:rs2228337).
{ECO:0000269|Ref.9}.
/FTId=VAR_024660.
CONFLICT 119 120 Missing (in Ref. 5; M86360).
{ECO:0000305}.
CONFLICT 301 301 C -> A (in Ref. 4; AAA61156).
{ECO:0000305}.
CONFLICT 508 508 Q -> H (in Ref. 5; M86360).
{ECO:0000305}.
CONFLICT 551 551 D -> E (in Ref. 5; M86360).
{ECO:0000305}.
CONFLICT 554 554 R -> A (in Ref. 3; AAA61166).
{ECO:0000305}.
CONFLICT 669 669 V -> I (in Ref. 3; AAA61166).
{ECO:0000305}.
STRAND 693 699 {ECO:0000244|PDB:2XZZ}.
STRAND 703 705 {ECO:0000244|PDB:2XZZ}.
STRAND 707 714 {ECO:0000244|PDB:2XZZ}.
STRAND 717 719 {ECO:0000244|PDB:2XZZ}.
STRAND 723 730 {ECO:0000244|PDB:2XZZ}.
TURN 731 733 {ECO:0000244|PDB:2XZZ}.
STRAND 734 741 {ECO:0000244|PDB:2XZZ}.
STRAND 749 756 {ECO:0000244|PDB:2XZZ}.
STRAND 767 771 {ECO:0000244|PDB:2XZZ}.
HELIX 773 776 {ECO:0000244|PDB:2XZZ}.
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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