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   27-MAR-2024, entry version 158.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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 concentrated at
RT   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 project:
RT   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, AND
RP   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 BY
RP   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 affinity
RT   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, AND
RP   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 expression.";
RL   Cell 143:1174-1189(2010).
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   -!- SUBUNIT: Interacts with PLAAT4. {ECO:0000250|UniProtKB:P22735}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P22735}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:P22735}.
CC   -!- TISSUE SPECIFICITY: Expressed in large amounts in epithelial tissues
CC       (lung, liver and kidney). {ECO:0000269|PubMed:10567386}.
CC   -!- PTM: Tyrosine-phosphorylated. {ECO:0000269|PubMed:10567386}.
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   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
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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   AlphaFoldDB; Q9JLF6; -.
DR   SMR; Q9JLF6; -.
DR   BioGRID; 204167; 3.
DR   IntAct; Q9JLF6; 2.
DR   MINT; Q9JLF6; -.
DR   STRING; 10090.ENSMUSP00000128090; -.
DR   GlyGen; Q9JLF6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9JLF6; -.
DR   PhosphoSitePlus; Q9JLF6; -.
DR   SwissPalm; Q9JLF6; -.
DR   EPD; Q9JLF6; -.
DR   jPOST; Q9JLF6; -.
DR   MaxQB; Q9JLF6; -.
DR   PaxDb; 10090-ENSMUSP00000128090; -.
DR   PeptideAtlas; Q9JLF6; -.
DR   ProteomicsDB; 263052; -.
DR   Pumba; Q9JLF6; -.
DR   DNASU; 21816; -.
DR   GeneID; 21816; -.
DR   KEGG; mmu:21816; -.
DR   UCSC; uc007uag.2; mouse.
DR   AGR; MGI:98730; -.
DR   CTD; 7051; -.
DR   MGI; MGI:98730; Tgm1.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   InParanoid; Q9JLF6; -.
DR   OrthoDB; 5344745at2759; -.
DR   PhylomeDB; Q9JLF6; -.
DR   TreeFam; TF324278; -.
DR   BRENDA; 2.3.2.13; 3474.
DR   Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR   BioGRID-ORCS; 21816; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; Tgm1; mouse.
DR   PRO; PR:Q9JLF6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9JLF6; Protein.
DR   GO; GO:0005912; C:adherens junction; IDA:MGI.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; 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: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; Immunoglobulins; 3.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 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   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11590:SF49; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE K; 1.
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; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Calcium; Keratinization; Lipoprotein; Membrane;
KW   Metal-binding; Palmitate; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..815
FT                   /note="Protein-glutamine gamma-glutamyltransferase K"
FT                   /id="PRO_0000213702"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          791..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        376
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   ACT_SITE        458
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   BINDING         498
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         500
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         547
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         552
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         21
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23606"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P22735"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:18630941"
FT   MOD_RES         803
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   CONFLICT        29
FT                   /note="E -> V (in Ref. 1; AAF35986)"
FT                   /evidence="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
//