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
//
