CHAC1_RAT
ID CHAC1_RAT Reviewed; 222 AA.
AC B3STU3;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Blocks Notch protein {ECO:0000250|UniProtKB:Q9BUX1};
DE Short=Botch {ECO:0000250|UniProtKB:Q9BUX1};
DE AltName: Full=Cation transport regulator-like protein 1 {ECO:0000250|UniProtKB:Q9BUX1};
DE AltName: Full=Neuroprotective protein 7 {ECO:0000303|PubMed:21124846};
GN Name=Chac1 {ECO:0000250|UniProtKB:Q9BUX1};
GN Synonyms=Botch {ECO:0000250|UniProtKB:Q9BUX1},
GN Npg7 {ECO:0000303|PubMed:21124846};
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 [MRNA].
RC STRAIN=CD Charles River;
RX PubMed=21124846; DOI=10.1371/journal.pone.0015008;
RA Dai C., Liang D., Li H., Sasaki M., Dawson T.M., Dawson V.L.;
RT "Functional identification of neuroprotective molecules.";
RL PLoS ONE 5:E15008-E15008(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
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. 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 -!- SUBUNIT: Interacts with NOTCH1 (via extracellular region).
CC {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; EF688602; ABX10438.1; -; mRNA.
DR EMBL; CH473949; EDL79903.1; -; Genomic_DNA.
DR RefSeq; NP_001166908.1; NM_001173437.1.
DR AlphaFoldDB; B3STU3; -.
DR SMR; B3STU3; -.
DR STRING; 10116.ENSRNOP00000019392; -.
DR iPTMnet; B3STU3; -.
DR PhosphoSitePlus; B3STU3; -.
DR PaxDb; B3STU3; -.
DR ABCD; B3STU3; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000019392; ENSRNOP00000019392; ENSRNOG00000014387.
DR GeneID; 362196; -.
DR KEGG; rno:362196; -.
DR UCSC; RGD:1307153; rat.
DR CTD; 79094; -.
DR RGD; 1307153; Chac1.
DR eggNOG; KOG3182; Eukaryota.
DR GeneTree; ENSGT00390000003855; -.
DR HOGENOM; CLU_070703_2_2_1; -.
DR InParanoid; B3STU3; -.
DR OMA; RPECTAV; -.
DR OrthoDB; 1238273at2759; -.
DR PhylomeDB; B3STU3; -.
DR TreeFam; TF313048; -.
DR Reactome; R-RNO-174403; Glutathione synthesis and recycling.
DR PRO; PR:B3STU3; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000014387; Expressed in skeletal muscle tissue and 18 other tissues.
DR Genevisible; B3STU3; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
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:0006751; P:glutathione catabolic process; IBA:GO_Central.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD.
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 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Golgi apparatus; Lyase; Neurogenesis;
KW Notch signaling pathway; Reference proteome; Unfolded protein response.
FT CHAIN 1..222
FT /note="Glutathione-specific gamma-glutamylcyclotransferase
FT 1"
FT /id="PRO_0000417990"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O75223"
FT BINDING 35..40
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O75223"
SQ SEQUENCE 222 AA; 24457 MW; 3F6D2CDFA14BA3FF CRC64;
MKQESAAQST PPPSLSPAPS AQPSWEDGDP QALWIFGYGS LVWKPDFAYS DSRVGFVRGY
SRRFWQGDTF HRGSDKMPGR VVTLLEDHEG CTWGVAYQVR GEQVSEALKY LNVREAVLGG
YDTKEVTFYP QDTPDQPLTA LAYVATPQNP GYLGPAPEEV IATQILACRG FSGHNLEYLL
RLADFMQLCG PQAQDEHLEA IVDAVGSLLP CSYLSEQPLA LI
