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   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.
DR   Genevisible; P23606; RN.
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
//