CHAC1_DANRE
ID CHAC1_DANRE Reviewed; 196 AA.
AC Q5SPB6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Glutathione-specific gamma-glutamylcyclotransferase 1 {ECO:0000250|UniProtKB:Q9BUX1};
DE Short=Gamma-GCG 1 {ECO:0000250|UniProtKB:Q9BUX1};
DE EC=4.3.2.7 {ECO:0000250|UniProtKB:Q9BUX1};
DE AltName: Full=Cation transport regulator-like protein 1 {ECO:0000250|UniProtKB:Q9BUX1};
GN Name=chac1 {ECO:0000250|UniProtKB:Q9BUX1};
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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. Glutathione depletion is an important
CC factor for apoptosis initiation and execution. Acts as a pro-apoptotic
CC component of the unfolded protein response pathway by mediating the
CC pro-apoptotic effects of the ATF4-ATF3-DDIT3/CHOP cascade. Negative
CC regulator of Notch signaling pathway involved in embryonic
CC neurogenesis: acts by inhibiting Notch cleavage by furin, maintaining
CC Notch in an immature inactive form, thereby promoting neurogenesis in
CC embryos. {ECO:0000250|UniProtKB:Q9BUX1}.
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:Q9BUX1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9BUX1}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q8R3J5}.
CC -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family. ChaC
CC subfamily. {ECO:0000305}.
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DR EMBL; AL929049; CAI20656.1; -; Genomic_DNA.
DR EMBL; BX897725; CAI11900.1; -; Genomic_DNA.
DR RefSeq; NP_001103596.2; NM_001110126.2.
DR AlphaFoldDB; Q5SPB6; -.
DR SMR; Q5SPB6; -.
DR STRING; 7955.ENSDARP00000094107; -.
DR PaxDb; Q5SPB6; -.
DR Ensembl; ENSDART00000103330; ENSDARP00000094107; ENSDARG00000070426.
DR GeneID; 563855; -.
DR KEGG; dre:563855; -.
DR CTD; 79094; -.
DR ZFIN; ZDB-GENE-030131-1957; chac1.
DR eggNOG; KOG3182; Eukaryota.
DR GeneTree; ENSGT00390000003855; -.
DR HOGENOM; CLU_070703_2_2_1; -.
DR InParanoid; Q5SPB6; -.
DR OMA; TVCGGYV; -.
DR OrthoDB; 1238273at2759; -.
DR PhylomeDB; Q5SPB6; -.
DR TreeFam; TF313048; -.
DR Reactome; R-DRE-174403; Glutathione synthesis and recycling.
DR PRO; PR:Q5SPB6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000070426; Expressed in swim bladder and 48 other tissues.
DR ExpressionAtlas; Q5SPB6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
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:0005112; F:Notch binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IDA:ZFIN.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0010955; P:negative regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Apoptosis; Cytoplasm; Golgi apparatus; Lyase; Neurogenesis;
KW Notch signaling pathway; Reference proteome; Unfolded protein response.
FT CHAIN 1..196
FT /note="Glutathione-specific gamma-glutamylcyclotransferase
FT 1"
FT /id="PRO_0000239012"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O75223"
FT BINDING 15..20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O75223"
SQ SEQUENCE 196 AA; 22016 MW; 9433BC64051BA364 CRC64;
MKPQDIVAGK SSLWIFGYGS LVWKPDFKYK RSKVGYIKGY KRRFWHGDNF HRGDDEMPGR
VVTLIEEDDV CTWGVAFEVT GSQMEESLKY LNVREAVRGG YLTRAVDFFP RGTNQPPVQA
LVYIATPDNP IYLGPASTEE IASQIAVCKG NSGHNIEYLL RLAEFMRVSC PDVDDPHLFS
IEAALLATIR PILLAA
