ID   CHAC2_DANRE             Reviewed;         182 AA.
AC   Q4KMJ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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}; ORFNames=zgc:110055;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Larval eye, and Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family. ChaC
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC098541; AAH98541.1; -; mRNA.
DR   EMBL; BC154137; AAI54138.1; -; mRNA.
DR   RefSeq; NP_001025128.1; NM_001029957.1.
DR   AlphaFoldDB; Q4KMJ1; -.
DR   SMR; Q4KMJ1; -.
DR   STRING; 7955.ENSDARP00000050830; -.
DR   PaxDb; Q4KMJ1; -.
DR   Ensembl; ENSDART00000050831; ENSDARP00000050830; ENSDARG00000055078.
DR   GeneID; 557614; -.
DR   KEGG; dre:557614; -.
DR   CTD; 494143; -.
DR   ZFIN; ZDB-GENE-050706-146; chac2.
DR   eggNOG; KOG3182; Eukaryota.
DR   GeneTree; ENSGT00390000003855; -.
DR   HOGENOM; CLU_070703_2_2_1; -.
DR   InParanoid; Q4KMJ1; -.
DR   OMA; LLWYTDF; -.
DR   OrthoDB; 1238273at2759; -.
DR   PhylomeDB; Q4KMJ1; -.
DR   TreeFam; TF313048; -.
DR   Reactome; R-DRE-174403; Glutathione synthesis and recycling.
DR   PRO; PR:Q4KMJ1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 12.
DR   Bgee; ENSDARG00000055078; Expressed in testis and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   Lyase; Reference proteome.
FT   CHAIN           1..182
FT                   /note="Putative glutathione-specific gamma-
FT                   glutamylcyclotransferase 2"
FT                   /id="PRO_0000314916"
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   182 AA;  20762 MW;  AE20AC786C798523 CRC64;
     MWVFGYGSLI WKVDFPYEDK RVGFVKGFSR RFWQGSTDHR GVPGKPGRVV TLIEDPEGCV
     WGVAYKLPSG QEQEVKEYLD YREKGGYGVI TVTFHPKDEQ QQPMQDTLLY IGSCDNPNYL
     GPAPLETIAQ QIVKSVGPSG KNTDYLFELA DALRQLVPED LDDHLFSLER LVKQLQEQED
     MD