ID TGM1_RAT Reviewed; 824 AA.
AC P23606; Q4QRA6;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 24-JAN-2024, entry version 167.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1979171; DOI=10.1073/pnas.87.23.9333;
RA Phillips M.A., Stewart B.E., Qin Q., Chakravarty R., Floyd E.E.,
RA Jetten A.M., Rice R.H.;
RT "Primary structure of keratinocyte transglutaminase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9333-9337(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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-22; SER-70; SER-100; SER-103
RP AND SER-812, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- 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; M57263; AAA63495.1; -; mRNA.
DR EMBL; BC097305; AAH97305.1; -; mRNA.
DR PIR; B38423; B38423.
DR RefSeq; NP_113847.1; NM_031659.1.
DR RefSeq; XP_006252076.1; XM_006252014.3.
DR RefSeq; XP_008768913.1; XM_008770691.2.
DR AlphaFoldDB; P23606; -.
DR SMR; P23606; -.
DR BioGRID; 248784; 3.
DR IntAct; P23606; 1.
DR MINT; P23606; -.
DR STRING; 10116.ENSRNOP00000027315; -.
DR iPTMnet; P23606; -.
DR PhosphoSitePlus; P23606; -.
DR PaxDb; 10116-ENSRNOP00000027315; -.
DR Ensembl; ENSRNOT00000027315.6; ENSRNOP00000027315.2; ENSRNOG00000020136.8.
DR Ensembl; ENSRNOT00055021557; ENSRNOP00055017471; ENSRNOG00055012630.
DR Ensembl; ENSRNOT00060041879; ENSRNOP00060034730; ENSRNOG00060024135.
DR Ensembl; ENSRNOT00065057484; ENSRNOP00065047325; ENSRNOG00065033433.
DR GeneID; 60335; -.
DR KEGG; rno:60335; -.
DR UCSC; RGD:61838; rat.
DR AGR; RGD:61838; -.
DR CTD; 7051; -.
DR RGD; 61838; Tgm1.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR GeneTree; ENSGT01050000244939; -.
DR HOGENOM; CLU_013435_0_2_1; -.
DR InParanoid; P23606; -.
DR OrthoDB; 5344745at2759; -.
DR PhylomeDB; P23606; -.
DR TreeFam; TF324278; -.
DR PRO; PR:P23606; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000020136; Expressed in esophagus and 14 other cell types or tissues.
DR Genevisible; P23606; RN.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; ISO:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
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; 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..824
FT /note="Protein-glutamine gamma-glutamyltransferase K"
FT /id="PRO_0000213704"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 509
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 556
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 561
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLF6"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22735"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 824 AA; 90770 MW; A7D81C148CEFD938 CRC64;
MEGPRSDVGR WGRSPWQPTT PSPEPEPEPE PDRSSRSRRG GGRSFWARCC GCCSCGNRAD
DDWGPEPSGS RSRGTSSRGG GSRGGDSRGR DSRGGRRPES RGSGVNAAGD GTIREGMLVV
NGVDLLCSRS DQNRREHHTD EFEYDELILR RGQPFHIILF LNREYESSDR IALELLIGNN
PEVGKGTHVI IPVGKGGSGG WKAQVTKTNG HNLTLRVHTS PNAIIGKFQF TVRTRSEAGE
FQLPFDPRNE IYILFNPWCP EDIVYVDHED WRQEYVLNES GRIYYGTEAQ IGERTWNYGQ
FDHGVLDACL YILDRRGMPY GGRGDPVSVS RVVSAMVNSL DDNGVLIGNW TGDYSRGTNP
SAWVGSVEIL LSYLRTGYSV PYGQCWVFAG VTTTVLRCLG LATRTVTNFN SAHDTDTSLT
MDIYFDENMK PLEHLNHDSV WNFHVWNDCW MKRPDLPSGF DGWQVVDATP QETSSGIFCC
GPCSVESIKN GLVYMKYDTP FIFAEVNSDK VYWQRQDDGS FKIVYVEEKA IGTLIVTKAI
NSNMREDITH IYKHPEGSEA ERKAVEKAAA HGSKPNVYAT RDSAEDVAMQ VEAQDAVMGQ
DLTVSVVLTN RGSSRRTVKL HLYLCVTYYT GVSGPTFKET KKEVVLAPGA SDTVAMPVAY
KEYKPHLVDQ GAMLLNVSGH VKESGQVLAK QHTFRLRTPD LSLTLLGAAV VGQECEVQIV
FKNPLPITLT NVVFRLEGSG LQRPKVLNVG DIGGNETVTL RQTFVPVRPG PRQLIASLDS
PQLSQVHGVI QVDVAPSSGG RGFSEAVGDS RSGENIPMAF RGGA
//
