TGM1_RABIT
ID TGM1_RABIT Reviewed; 836 AA.
AC P22758;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 137.
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;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Tracheobronchial epithelium;
RX PubMed=8097865; DOI=10.1210/mend.7.3.8097865;
RA Saunders N.A., Bernacki S.H., Vollberg T.M., Jetten A.M.;
RT "Regulation of transglutaminase type I expression in squamous
RT differentiating rabbit tracheal epithelial cells and human epidermal
RT keratinocytes: effects of retinoic acid and phorbol esters.";
RL Mol. Endocrinol. 7:387-398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 368-749.
RX PubMed=2574824; DOI=10.1128/mcb.9.11.4846-4851.1989;
RA Floyd E.E., Jetten A.M.;
RT "Regulation of type I (epidermal) transglutaminase mRNA levels during
RT squamous differentiation: down regulation by retinoids.";
RL Mol. Cell. Biol. 9:4846-4851(1989).
RN [3]
RP SEQUENCE REVISION.
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).
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 (By similarity). {ECO:0000250|UniProtKB:P22735}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by retinoic acid, but phorbol ester
CC treatment activates it.
CC -!- SUBUNIT: Interacts with PLAAT4. {ECO:0000250|UniProtKB:P22735}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P22735}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P22735}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:P22735}.
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:0000250|UniProtKB:P22735}.
CC -!- PTM: Tyrosine-phosphorylated. {ECO:0000250|UniProtKB:Q9JLF6}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
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DR EMBL; L10714; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M30468; AAA31475.1; -; mRNA.
DR PIR; A33477; A33477.
DR PIR; A54269; A54269.
DR AlphaFoldDB; P22758; -.
DR SMR; P22758; -.
DR PRIDE; P22758; -.
DR InParanoid; P22758; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; ISS: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 2: Evidence at transcript level;
KW Acyltransferase; Calcium; Keratinization; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..836
FT /note="Protein-glutamine gamma-glutamyltransferase K"
FT /id="PRO_0000213703"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 568
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 573
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLF6"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22735"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23606"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22735"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLF6"
SQ SEQUENCE 836 AA; 91935 MW; B3D281F7BECB9C00 CRC64;
MDGPRSDMGR SDVSRSDMSR SDMGRSDMGR SDVGRCGGGP LQPSATPSPE PEPEPEPEPD
RGSRSRGGRG RSFWARCCGC CSCRNAADDD WGREPSDSRD RGSSSRGGRP DSRGGGVNAA
GDGTIREGML VVTGVDLLSS RSDQNRREHH TDEFEYEELI VRRGQPFHLV LFLSRPYESS
DRIALELQIG NNPEVGKGTH VIIPVGKGNS GGWKAQVTKA SGQTLNLRVH SPASAIIGKF
QFTVRTRTEA GEFQLPFDPR NEIYILFNPW CPEDIVYVDH EDWRQDYVLN ESGRIYYGTE
AQIGERTWNY GQFDHGVLDA CLYILDRRGM PYGGRGDPVS VSRVISAMVN SLDDNGVLIG
NWSGDYSRGT NPSAWVGSVE ILLSYLRTGY SVPYGQCWVF AGVTTTVLRC LGLATRTVTN
FNSAHDTDTS LTMDIYFDEN MKPLEHLNRD SVWNFHVWND CWMKRPDLPS GFDGWQVVDA
TPQETSSGIF CCGPCSVESV KNGLVYMKYD TPFIFAEVNS DKVYWQRQDD GSFKIVYVEE
KAIGTLIVTK AVRSHMREDI THIYKHPEGS DAERKAVETA AAHGSKPNVY DSRDSAEDVA
MQVEAQDAVM GQDLTVSVVL TNRSSSRRTV KLHLYLSVTF YTGVTGSIFK ESKKEVVLAA
GSSDSVVMPV AYKEYRPHLV DQGAMLLNVS GHVKESGQVL AKQHTFRVRT PDLSLTLLGA
AVVGQECEVQ IVFRNPLPIT LTNVVFRLEG SGLQRPKILN VGDIGGNETV TLRQTFVPVR
PGPRQLIASL DSPQLSQVHG VIQVDVAPAS GGRGFLHAGG DSYSGETIPM TSRGEA
