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Database: UniProt/SWISS-PROT
Entry: TGM2_CHICK
LinkDB: TGM2_CHICK
Original site: TGM2_CHICK 
ID   TGM2_CHICK              Reviewed;         689 AA.
AC   Q01841;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 3.
DT   22-NOV-2017, entry version 122.
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=TGL2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 9-22; 181-191;
RP   242-262; 383-401; 406-416; 430-448 AND 457-483.
RC   TISSUE=Erythrocyte;
RX   PubMed=1357669; DOI=10.1073/pnas.89.20.9804;
RA   Weraarchakul-Boonmark N., Jeong J.M., Murthy S.N.P., Engel J.D.,
RA   Lorand L.;
RT   "Cloning and expression of chicken erythrocyte transglutaminase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:9804-9808(1992).
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.
CC   -!- TISSUE SPECIFICITY: Predominates in mature erythrocytes. Also
CC       found in kidney and cardiac muscle.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA49104.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; L02270; AAA49104.1; ALT_INIT; mRNA.
DR   PIR; A47203; A47203.
DR   RefSeq; NP_990779.1; NM_205448.1.
DR   UniGene; Gga.1035; -.
DR   UniGene; Gga.31956; -.
DR   ProteinModelPortal; Q01841; -.
DR   SMR; Q01841; -.
DR   STRING; 9031.ENSGALP00000038435; -.
DR   PaxDb; Q01841; -.
DR   PRIDE; Q01841; -.
DR   GeneID; 396432; -.
DR   KEGG; gga:396432; -.
DR   CTD; 7052; -.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; Q01841; -.
DR   KO; K05625; -.
DR   PhylomeDB; Q01841; -.
DR   PRO; PR:Q01841; -.
DR   Proteomes; UP000000539; 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   Acyltransferase; Calcium; Complete proteome;
KW   Direct protein sequencing; Metal-binding; Reference proteome;
KW   Transferase.
FT   CHAIN         1    689       Protein-glutamine gamma-
FT                                glutamyltransferase 2.
FT                                /FTId=PRO_0000213709.
FT   ACT_SITE    278    278       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    336    336       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    359    359       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       399    399       Calcium. {ECO:0000250}.
FT   METAL       401    401       Calcium. {ECO:0000250}.
FT   METAL       447    447       Calcium. {ECO:0000250}.
FT   METAL       452    452       Calcium. {ECO:0000250}.
SQ   SEQUENCE   689 AA;  77970 MW;  ACA3FA84B48A5AB3 CRC64;
     MAEELVLETC DLQCERNGRE HRTEEMGSQQ LVVRRGQPFT ITLNFAGRGY EEGVDKLAFD
     VETGPCPVET SGTRSHFTLT DCPEEGTWSA VLQQQDGATL CVSLCSPSIA RVGRYRLTLE
     ASTGYQGSSF HLGDFVLLFN AWHPEDAVYL KEEDERREYV LSQQGLIYMG SRDYITSTPW
     NFGQFEDEIL AICLEMLDIN PKFLRDQNLD CSRRNDPVYI GRVVSAMVNC NDEDHGVLLG
     RWDNHYEDGM SPMAWIGSVD ILKRWRRLGC QPVKYGQCWV FAAVACTVMR CLGVPSRVVT
     NYNSAHDTNG NLVIDRYLSE TGMEERRSTD MIWNFHCWVE CWMTRPDLAP GYDGWQALDP
     TPQEKSEGVY CCGPAPVKAI KEGDLQVQYD IPFVFAEVNA DVVYWIVQSD GEKKKSTHSS
     VVGKNISTKS VGRDSREDIT HTYKYPEGSE KEREVFSKAE HEKSSLGEQE EGLHMRIKLS
     EGANNGSDFD VFAFISNDTD KERECRLRLC ARTASYNGEV GPQCGFKDLL NLSLQPHMEQ
     SVPLRILYEQ YGPNLTQDNM IKVVALLTEY ETGDSVVAIR DVYIQNPEIK IRILGEPMQE
     RKLVAEIRLV NPLAEPLNNC IFVVEGAGLT EGQRIEELED PVEPQAEAKF RMEFVPRQAG
     LHKLMVDFES DKLTGVKGYR NVIIAPLPK
//
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