ID   TGM2_CAVCU              Reviewed;         690 AA.
AC   P08587;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   16-JUN-2009, entry version 81.
DE   RecName: Full=Protein-glutamine gamma-glutamyltransferase 2;
DE            EC=2.3.2.13;
DE   AltName: Full=Tissue transglutaminase;
DE   AltName: Full=TGase C;
DE            Short=TGC;
DE            Short=TG(C);
DE   AltName: Full=Transglutaminase-2;
GN   Name=TGM2;
OS   Cavia cutleri (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Caviidae; Cavia.
OX   NCBI_TaxID=10144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=88294033; PubMed=2900023; DOI=10.1021/bi00408a035;
RA   Ikura K., Nasu T.-A., Yokota H., Tsuchiya Y., Sasaki R., Chiba H.;
RT   "Amino acid sequence of guinea pig liver transglutaminase from its
RT   cDNA sequence.";
RL   Biochemistry 27:2898-2905(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 189-632.
RC   TISSUE=Liver;
RA   Ikura K., Nasu T.-A., Yokota H., Sasaki R., Chiba H.;
RT   "Cloning of cDNA coding for guinea pig liver transglutaminase.";
RL   Agric. Biol. Chem. 51:957-961(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-5.
RC   TISSUE=Liver;
RX   MEDLINE=71111415; PubMed=5543674;
RA   Connellan J.M., Chung S.I., Whetzel N.K., Bradley L.M., Folk J.E.;
RT   "Structural properties of guinea pig liver transglutaminase.";
RL   J. Biol. Chem. 246:1093-1098(1971).
CC   -!- FUNCTION: Catalyzes the cross-linking of proteins and the
CC       conjugation of polyamines to proteins.
CC   -!- CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N(5)-
CC       alkylglutamine + NH(3).
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family.
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DR   EMBL; M19646; AAA37056.1; -; mRNA.
DR   EMBL; D00114; BAA00068.1; -; mRNA.
DR   PIR; A29996; A29996.
DR   HSSP; P21980; 1KV3.
DR   SMR; P08587; 15-690.
DR   HOVERGEN; P08587; -.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase...; IEA:EC.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
DR   InterPro; IPR008957; Fibronectin_typ-III-like_fold.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR013808; Transglutaminase_CS.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   Gene3D; G3DSA:2.60.40.30; FN_III-like; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00927; Transglut_C; 2.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   SMART; SM00460; TGc; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Calcium; Direct protein sequencing;
KW   Metal-binding; Phosphoprotein; Transferase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    690       Protein-glutamine gamma-
FT                                glutamyltransferase 2.
FT                                /FTId=PRO_0000213706.
FT   ACT_SITE    277    277       By similarity.
FT   ACT_SITE    335    335       By similarity.
FT   ACT_SITE    358    358       By similarity.
FT   METAL       398    398       Calcium (By similarity).
FT   METAL       400    400       Calcium (By similarity).
FT   METAL       446    446       Calcium (By similarity).
FT   METAL       451    451       Calcium (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     219    219       Phosphotyrosine (By similarity).
FT   MOD_RES     369    369       Phosphotyrosine (By similarity).
FT   MOD_RES     426    426       Phosphoserine (By similarity).
FT   CONFLICT      2      3       AE -> EA (in Ref. 3; AA sequence).
FT   CONFLICT    292    292       G -> A (in Ref. 2; BAA00068).
FT   CONFLICT    336    354       CWVESWMTRPDLEPGYEGW -> SLLGGVVDDQAGPGAWVR
FT                                GV (in Ref. 2; BAA00068).
SQ   SEQUENCE   690 AA;  77141 MW;  047223D38DBEA4A4 CRC64;
     MAEDLILERC DLQLEVNGRD HRTADLCRER LVLRRGQPFW LTLHFEGRGY EAGVDTLTFN
     AVTGPDPSEE AGTMARFSLS SAVEGGTWSA SAVDQQDSTV SLLLSTPADA PIGLYRLSLE
     ASTGYQGSSF VLGHFILLYN PRCPADAVYM DSDQERQEYV LTQQGFIYQG SAKFINGIPW
     NFGQFEDGIL DICLMLLDTN PKFLKNAGQD CSRRSRPVYV GRVVSAMVNC NDDQGVLQGR
     WDNNYSDGVS PMSWIGSVDI LRRWKDYGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN
     FNSAHDQNSN LLIEYFRNES GEIEGNKSEM IWNFHCWVES WMTRPDLEPG YEGWQALDPT
     PQEKSEGTYC CGPVPVRAIK EGHLNVKYDA PFVFAEVNAD VVNWIRQKDG SLRKSINHLV
     VGLKISTKSV GRDEREDITH TYKYPEGSEE EREAFVRANH LNKLATKEEA QEETGVAMRI
     RVGQNMTMGS DFDIFAYITN GTAESHECQL LLCARIVSYN GVLGPVCSTN DLLNLTLDPF
     SENSIPLHIL YEKYGDYLTE SNLIKVRGLL IEPAANSYVL AERDIYLENP EIKIRVLGEP
     KQNRKLIAEV SLKNPLPVPL LGCIFTVEGA GLTKDQKSVE VPDPVEAGEQ AKVRVDLLPT
     EVGLHKLVVN FECDKLKAVK GYRNVIIGPA
//