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Database: UniProt/SWISS-PROT
Entry: TGM1_MOUSE
LinkDB: TGM1_MOUSE
Original site: TGM1_MOUSE 
ID   TGM1_MOUSE              Reviewed;         815 AA.
AC   Q9JLF6; Q8R0T9;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   05-DEC-2018, entry version 133.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX   PubMed=10567386; DOI=10.1074/jbc.274.48.34148;
RA   Hiiragi T., Sasaki H., Nagafuchi A., Sabe H., Shen S.C., Matsuki M.,
RA   Yamanishi K., Tsukita S.;
RT   "Transglutaminase type 1 and its cross-linking activity are
RT   concentrated at adherens junctions in simple epithelial cells.";
RL   J. Biol. Chem. 274:34148-34154(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-94 AND SER-803,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21; SER-23 AND SER-803,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
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 (By similarity).
CC       {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(+);
CC         Xref=Rhea:RHEA:54816, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207,
CC         Rhea:RHEA-COMP:14005, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:30011, ChEBI:CHEBI:138370; EC=2.3.2.13;
CC         Evidence={ECO:0000255|PROSITE-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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in large amounts in epithelial
CC       tissues (lung, liver and kidney). {ECO:0000269|PubMed:10567386}.
CC   -!- PTM: Tyrosine-phosphorylated. {ECO:0000269|PubMed:10567386}.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
DR   EMBL; AF186373; AAF35986.1; -; mRNA.
DR   EMBL; BC026422; AAH26422.1; -; mRNA.
DR   CCDS; CCDS36932.1; -.
DR   RefSeq; NP_001155186.1; NM_001161714.1.
DR   RefSeq; NP_001155187.1; NM_001161715.1.
DR   RefSeq; NP_064368.3; NM_019984.3.
DR   RefSeq; XP_006518871.1; XM_006518808.2.
DR   RefSeq; XP_006518872.1; XM_006518809.3.
DR   UniGene; Mm.41964; -.
DR   ProteinModelPortal; Q9JLF6; -.
DR   SMR; Q9JLF6; -.
DR   BioGrid; 204167; 1.
DR   IntAct; Q9JLF6; 3.
DR   MINT; Q9JLF6; -.
DR   STRING; 10090.ENSMUSP00000002389; -.
DR   iPTMnet; Q9JLF6; -.
DR   PhosphoSitePlus; Q9JLF6; -.
DR   SwissPalm; Q9JLF6; -.
DR   EPD; Q9JLF6; -.
DR   MaxQB; Q9JLF6; -.
DR   PaxDb; Q9JLF6; -.
DR   PeptideAtlas; Q9JLF6; -.
DR   PRIDE; Q9JLF6; -.
DR   GeneID; 21816; -.
DR   KEGG; mmu:21816; -.
DR   UCSC; uc007uag.2; mouse.
DR   CTD; 7051; -.
DR   MGI; MGI:98730; Tgm1.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; Q9JLF6; -.
DR   KO; K05619; -.
DR   PhylomeDB; Q9JLF6; -.
DR   TreeFam; TF324278; -.
DR   BRENDA; 2.3.2.13; 3474.
DR   PRO; PR:Q9JLF6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   CleanEx; MM_TGM1; -.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0031224; C:intrinsic component of membrane; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; ISO:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISO:MGI.
DR   GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
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   GO; GO:0019538; P:protein metabolic process; TAS:MGI.
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   Acyltransferase; Calcium; Complete proteome; Keratinization; Membrane;
KW   Metal-binding; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1    815       Protein-glutamine gamma-
FT                                glutamyltransferase K.
FT                                /FTId=PRO_0000213702.
FT   ACT_SITE    376    376       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    435    435       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    458    458       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       498    498       Calcium. {ECO:0000250}.
FT   METAL       500    500       Calcium. {ECO:0000250}.
FT   METAL       547    547       Calcium. {ECO:0000250}.
FT   METAL       552    552       Calcium. {ECO:0000250}.
FT   MOD_RES      21     21       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES      23     23       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES      71     71       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P23606}.
FT   MOD_RES      83     83       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22735}.
FT   MOD_RES      91     91       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355}.
FT   MOD_RES      94     94       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:18630941}.
FT   MOD_RES     803    803       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   CONFLICT     29     29       E -> V (in Ref. 1; AAF35986).
FT                                {ECO:0000305}.
SQ   SEQUENCE   815 AA;  89826 MW;  326DD4E512AEA23E CRC64;
     MEGPRSDVGR WGRSPWQPPT TPSPEPEPEP EPDRRSRSRR GGGRSFWARC CGCCSCGNRG
     DDDWGPEPSG SRSRGTSSRG RDSRGGRRPE SRGSGVNAAG DGTIREGMLV VTGVDLLCSR
     SDQNRREHHT DEFEYDELIV RRGQPFHMIL FLNREYESSD RIALELLIGS NPEVGKGTHV
     IIPVGKGGSG GWKAQVTKNN GHNLNLRVHT SPNAIIGKFQ FTVRTRSEAG EFQLPFDPRN
     EIYILFNPWC PEDIVYVDHE DWRQEYVLNE SGRIYYGTEA QIGERTWNYG QFDHGVLDAC
     LYILDRRGMP YGGRGDPVSV SRVVSAMVNS LDDNGVLIGN WTGDYSRGTN PSAWVGSVEI
     LLSYLRTGYS VPYGQCWVFA GVTTTVLRCL GFATRTVTNF NSAHDTDTSL TMDIYFDENM
     KPLEHLNHDS VWNFHVWNDC WMKRPDLPSG FDGWQVVDAT PQETSSGIFC CGPCSVESVK
     NGLVYMKYDT PFIFAEVNSD KVYWQRQDDG SFKIVYVEEK AIGTLIVTKA IHSNNREDIT
     HIYKHPEGSE AERRAVEKAA AHGSKPNVYA TRDSAEDVAM QVEAQDAVMG QDLAVSVVLT
     NRGSSRRTVK LHLYLCVTYY TGVSGPTFKE AKKEVTLAPG ASDSVTMPVA YKEYKPHLVD
     QGAMLLNVSG HVKESGQVLA KQHTFRLRTP DLSLTLLGAA VVGQECGVQI VFKNPLPVTL
     TNVVFRLEGS GLQRPKVLNV GDIGGNETVT LRQTFVPVRP GPRQLIASLD SPQLSQVHGV
     IQVDVAPASG GSGFSDAGGD SRSGENIPMA YRGGA
//
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