CHAC2_CHICK
ID CHAC2_CHICK Reviewed; 186 AA.
AC Q5ZI66;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=RCJMB04_29n19;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720918; CAG32577.1; -; mRNA.
DR AlphaFoldDB; Q5ZI66; -.
DR SMR; Q5ZI66; -.
DR STRING; 9031.ENSGALP00000013307; -.
DR PaxDb; Q5ZI66; -.
DR VEuPathDB; HostDB:geneid_421221; -.
DR eggNOG; KOG3182; Eukaryota.
DR HOGENOM; CLU_070703_2_2_1; -.
DR InParanoid; Q5ZI66; -.
DR PhylomeDB; Q5ZI66; -.
DR Proteomes; UP000000539; Unplaced.
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..186
FT /note="Putative glutathione-specific gamma-
FT glutamylcyclotransferase 2"
FT /id="PRO_0000314915"
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 186 AA; 21094 MW; BBD9435FFE0D55E5 CRC64;
MWVFGYGSLI WKVDFPYQEK MVGRIRGYSR RFWQGSTDHR GVPGKPGRVV TLVEDPEGCV
WGVAYRLPAG QECEVKAYLD FREKGGYRTT TVVFYPKDSS IKPFDVLLYI GTRDNPNYLG
PAPLQEIAEQ IIDAVGPSGR NTEYLFELAN SMRNLVPEDV DEHLFSLEET SKGTPGKRTK
PKLPLE
