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Database: UniProt/SWISS-PROT
Entry: TGM2_BOVIN
LinkDB: TGM2_BOVIN
Original site: TGM2_BOVIN 
ID   TGM2_BOVIN              Reviewed;         687 AA.
AC   P51176; Q3ZBH7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   22-NOV-2017, entry version 137.
DE   RecName: Full=Protein-glutamine gamma-glutamyltransferase 2;
DE            EC=2.3.2.13;
DE   AltName: Full=Tissue transglutaminase;
DE   AltName: Full=Transglutaminase C;
DE            Short=TG(C);
DE            Short=TGC;
DE            Short=TGase C;
DE   AltName: Full=Transglutaminase-2;
DE            Short=TGase-2;
GN   Name=TGM2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 79-95; 157-166;
RP   242-251 AND 581-587.
RC   TISSUE=Artery;
RX   PubMed=1682150; DOI=10.1111/j.1432-1033.1991.tb16338.x;
RA   Nakanishi K., Nara K., Hagiwara H., Aoyama Y., Ueno H., Hirose S.;
RT   "Cloning and sequence analysis of cDNA clones for bovine aortic-
RT   endothelial-cell transglutaminase.";
RL   Eur. J. Biochem. 202:15-21(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 79-95; 157-166 AND 242-251.
RX   PubMed=2572599;
RA   Nara K., Nakanishi K., Hagiwara H., Wakita K., Kojima S., Hirose S.;
RT   "Retinol-induced morphological changes of cultured bovine endothelial
RT   cells are accompanied by a marked increase in transglutaminase.";
RL   J. Biol. Chem. 264:19308-19312(1989).
CC   -!- FUNCTION: Catalyzes the cross-linking of proteins and the
CC       conjugation of polyamines to proteins.
CC   -!- CATALYTIC ACTIVITY: A protein-L-glutamine + a protein-L-lysine = a
CC       protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3).
CC       {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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highest levels are detected in the lung. Lower
CC       levels are found in the liver, spleen and heart, but not in the
CC       brain.
CC   -!- INDUCTION: By retinoic acid.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
DR   EMBL; X60686; CAA43097.1; -; mRNA.
DR   EMBL; BC103290; AAI03291.1; -; mRNA.
DR   PIR; S19680; S19680.
DR   RefSeq; NP_803473.1; NM_177507.2.
DR   UniGene; Bt.5401; -.
DR   ProteinModelPortal; P51176; -.
DR   SMR; P51176; -.
DR   STRING; 9913.ENSBTAP00000021569; -.
DR   PaxDb; P51176; -.
DR   PeptideAtlas; P51176; -.
DR   PRIDE; P51176; -.
DR   GeneID; 281528; -.
DR   KEGG; bta:281528; -.
DR   CTD; 7052; -.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; P51176; -.
DR   KO; K05625; -.
DR   TreeFam; TF324278; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
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; 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; SSF81296; SSF81296; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Calcium; Complete proteome;
KW   Direct protein sequencing; Metal-binding; Reference proteome;
KW   Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P08587}.
FT   CHAIN         2    687       Protein-glutamine gamma-
FT                                glutamyltransferase 2.
FT                                /FTId=PRO_0000213705.
FT   ACT_SITE    277    277       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    335    335       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    358    358       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       398    398       Calcium. {ECO:0000250}.
FT   METAL       400    400       Calcium. {ECO:0000250}.
FT   METAL       447    447       Calcium. {ECO:0000250}.
FT   METAL       452    452       Calcium. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:P08587}.
FT   MOD_RES     468    468       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P21981}.
FT   CONFLICT    638    638       V -> I (in Ref. 2; AAI03291).
FT                                {ECO:0000305}.
SQ   SEQUENCE   687 AA;  77112 MW;  7BBA00F15E779944 CRC64;
     MAEELVLERC DLELEANGRD HHTADLCRER LVVRRGQPFW LTLHFEGRNY EASVDSLTFC
     AVTGPDPSEE AGTKALFRLS DATEEGAWAA VAADQRDSTL SLHLSTPANA PVGHYRLSLE
     ASTGYQGSSF MLGQFTLLFN SWCPADAVYL DSDEERQEYV LTQQGFIYQG SAKFIKNIPW
     NFGQFEEGIL DICLMLLDVN PKFLRNAGRD CSRRSSPVYV GRVVSGMVNC NDDQGVLLGR
     WDNNYADGIS PMSWIGSVDI LRRWKRDGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN
     YNSAHDQNSN LLIEYFRNEF GEIQSDKSEM IWNFHCWVES WMTRPDLQPG YEGWQALDPT
     PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVFAEVNAD VVDWIRQDDG SLHKSINHSL
     VVGLKISTKC VGRDDREDIT HSYKYPEGSP EEREAFTRAN HLNKLVNKEE TGVAMRIRVG
     EGMNRGCDFD VFAHITNSTP EEHTGRLLLC ARTVSYNGIL GPECGTKDLL SLSLEPYSEK
     SIPLRILYEK YCDCLTESNL IKVRGLLIEP AANSYLLAER DIYLENPEIK IRILGEPKQN
     RKLVAEISLQ NPLTVALSGC TFTVEGAGLI EEQKTVDVPD PVEAGEEVKV RVDLLPLYVG
     RHKLVVNFES DRLKAVKGFR NVIVGPS
//
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