GenomeNet

Database: UniProt/SWISS-PROT
Entry: TGM1_RAT
LinkDB: TGM1_RAT
Original site: TGM1_RAT 
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   05-DEC-2018, entry version 142.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   project: 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;
RP   SER-103 AND SER-812, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
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   UniGene; Rn.10039; -.
DR   ProteinModelPortal; P23606; -.
DR   SMR; P23606; -.
DR   BioGrid; 248784; 2.
DR   STRING; 10116.ENSRNOP00000027315; -.
DR   iPTMnet; P23606; -.
DR   PhosphoSitePlus; P23606; -.
DR   PaxDb; P23606; -.
DR   PRIDE; P23606; -.
DR   Ensembl; ENSRNOT00000027315; ENSRNOP00000027315; ENSRNOG00000020136.
DR   GeneID; 60335; -.
DR   KEGG; rno:60335; -.
DR   UCSC; RGD:61838; rat.
DR   CTD; 7051; -.
DR   RGD; 61838; Tgm1.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   GeneTree; ENSGT00940000154933; -.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; P23606; -.
DR   KO; K05619; -.
DR   OMA; NMREDIT; -.
DR   OrthoDB; EOG091G030K; -.
DR   PhylomeDB; P23606; -.
DR   TreeFam; TF324278; -.
DR   Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR   PRO; PR:P23606; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000020136; Expressed in 9 organ(s), highest expression level in spleen.
DR   Genevisible; P23606; RN.
DR   GO; GO:0031224; C:intrinsic component of membrane; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; NAS:RGD.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   GO; GO:0018149; P:peptide cross-linking; NAS: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; -; 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    824       Protein-glutamine gamma-
FT                                glutamyltransferase K.
FT                                /FTId=PRO_0000213704.
FT   ACT_SITE    385    385       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    444    444       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    467    467       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       507    507       Calcium. {ECO:0000250}.
FT   METAL       509    509       Calcium. {ECO:0000250}.
FT   METAL       556    556       Calcium. {ECO:0000250}.
FT   METAL       561    561       Calcium. {ECO:0000250}.
FT   MOD_RES      20     20       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9JLF6}.
FT   MOD_RES      22     22       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES      70     70       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES      92     92       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22735}.
FT   MOD_RES     100    100       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     103    103       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     812    812       Phosphoserine.
FT                                {ECO:0000244|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
//
DBGET integrated database retrieval system