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CHAC2_RAT
ID   CHAC2_RAT               Reviewed;         178 AA.
AC   Q641Z5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Putative glutathione-specific gamma-glutamylcyclotransferase 2 {ECO:0000250|UniProtKB:Q8WUX2};
DE            Short=Gamma-GCG 2 {ECO:0000250|UniProtKB:Q8WUX2};
DE            EC=4.3.2.7 {ECO:0000250|UniProtKB:Q8WUX2};
DE   AltName: Full=Cation transport regulator-like protein 2 {ECO:0000250|UniProtKB:Q9BUX1};
GN   Name=Chac2 {ECO:0000250|UniProtKB:Q8WUX2};
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 [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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).
CC   -!- FUNCTION: Catalyzes the cleavage of glutathione into 5-oxo-L-proline
CC       and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on
CC       other gamma-glutamyl peptides. {ECO:0000250|UniProtKB:Q8WUX2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione = 5-oxo-L-proline + L-cysteinylglycine;
CC         Xref=Rhea:RHEA:47724, ChEBI:CHEBI:57925, ChEBI:CHEBI:58402,
CC         ChEBI:CHEBI:61694; EC=4.3.2.7;
CC         Evidence={ECO:0000250|UniProtKB:Q8WUX2};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8WUX2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q8WUX2}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family. ChaC
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC082031; AAH82031.1; -; mRNA.
DR   RefSeq; NP_001020187.1; NM_001025016.1.
DR   AlphaFoldDB; Q641Z5; -.
DR   SMR; Q641Z5; -.
DR   STRING; 10116.ENSRNOP00000002094; -.
DR   jPOST; Q641Z5; -.
DR   PaxDb; Q641Z5; -.
DR   Ensembl; ENSRNOT00000115752; ENSRNOP00000097905; ENSRNOG00000070799.
DR   GeneID; 360994; -.
DR   KEGG; rno:360994; -.
DR   UCSC; RGD:1309120; rat.
DR   CTD; 494143; -.
DR   RGD; 1309120; Chac2.
DR   eggNOG; KOG3182; Eukaryota.
DR   GeneTree; ENSGT00390000003855; -.
DR   HOGENOM; CLU_070703_2_2_1; -.
DR   InParanoid; Q641Z5; -.
DR   OMA; LLWYTDF; -.
DR   OrthoDB; 1392423at2759; -.
DR   PhylomeDB; Q641Z5; -.
DR   TreeFam; TF313048; -.
DR   Reactome; R-RNO-174403; Glutathione synthesis and recycling.
DR   PRO; PR:Q641Z5; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000001531; Expressed in stomach and 20 other tissues.
DR   Genevisible; Q641Z5; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IBA:GO_Central.
DR   GO; GO:0061928; F:glutathione specific gamma-glutamylcyclotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
DR   CDD; cd06661; GGCT_like; 1.
DR   InterPro; IPR006840; ChaC.
DR   InterPro; IPR013024; GGCT-like.
DR   InterPro; IPR036568; GGCT-like_sf.
DR   PANTHER; PTHR12192; PTHR12192; 1.
DR   Pfam; PF04752; ChaC; 1.
DR   SUPFAM; SSF110857; SSF110857; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Reference proteome.
FT   CHAIN           1..178
FT                   /note="Putative glutathione-specific gamma-
FT                   glutamylcyclotransferase 2"
FT                   /id="PRO_0000314914"
FT   ACT_SITE        83
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O75223"
FT   BINDING         3..8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O75223"
SQ   SEQUENCE   178 AA;  20167 MW;  90FC4F4A6C835B11 CRC64;
     MWVFGYGSLI WKVDFPYQDK LVGYITNYSR RFWQGSTDHR GVPGKPGRVV TLVEDPGGSV
     WGVAYKLPVG KEEEVKTYLD FREKGGYRTT TVIFYPKDST TKPFSVLLYI GTCDNPNYLG
     PAPLEDIAEQ IFNAAGPSGR NTEYLFELAD SIRKLVPEDA DEHLFSLEKL VKERLEGK
 
 
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