CHAC2_MOUSE
ID CHAC2_MOUSE Reviewed; 178 AA.
AC Q9CQG1; Q8R3K5; Q9D1T7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
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:0000269|PubMed:27913623};
DE AltName: Full=Cation transport regulator-like protein 2 {ECO:0000250|UniProtKB:Q9BUX1};
GN Name=Chac2 {ECO:0000250|UniProtKB:Q8WUX2};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Epididymis, Eye, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=27913623; DOI=10.1074/jbc.m116.727479;
RA Kaur A., Gautam R., Srivastava R., Chandel A., Kumar A., Karthikeyan S.,
RA Bachhawat A.K.;
RT "ChaC2, an enzyme for slow turnover of cytosolic glutathione.";
RL J. Biol. Chem. 292:638-651(2017).
CC -!- FUNCTION: Catalyzes the cleavage of glutathione into 5-oxo-L-proline
CC and a Cys-Gly dipeptide (PubMed:27913623). Acts specifically on
CC glutathione, but not on other gamma-glutamyl peptides (By similarity).
CC {ECO:0000250|UniProtKB:Q8WUX2, ECO:0000269|PubMed:27913623}.
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:0000269|PubMed:27913623};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 mM for glutathione {ECO:0000269|PubMed:27913623};
CC Note=kcat is 7.6 min(-1) for glutathione.
CC {ECO:0000269|PubMed:27913623};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8WUX2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8WUX2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CQG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQG1-2; Sequence=VSP_030429;
CC -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family. ChaC
CC subfamily. {ECO:0000305}.
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DR EMBL; AK010914; BAB27264.1; -; mRNA.
DR EMBL; AK021391; BAB32394.1; -; mRNA.
DR EMBL; AK078993; BAC37498.1; -; mRNA.
DR EMBL; AL662891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025100; AAH25100.1; -; mRNA.
DR CCDS; CCDS24510.1; -. [Q9CQG1-1]
DR CCDS; CCDS70154.1; -. [Q9CQG1-2]
DR RefSeq; NP_001277596.1; NM_001290667.1. [Q9CQG1-2]
DR RefSeq; NP_080803.1; NM_026527.3. [Q9CQG1-1]
DR AlphaFoldDB; Q9CQG1; -.
DR SMR; Q9CQG1; -.
DR STRING; 10090.ENSMUSP00000098942; -.
DR PhosphoSitePlus; Q9CQG1; -.
DR EPD; Q9CQG1; -.
DR MaxQB; Q9CQG1; -.
DR PaxDb; Q9CQG1; -.
DR PeptideAtlas; Q9CQG1; -.
DR PRIDE; Q9CQG1; -.
DR ProteomicsDB; 281660; -. [Q9CQG1-1]
DR ProteomicsDB; 281661; -. [Q9CQG1-2]
DR Antibodypedia; 30211; 113 antibodies from 20 providers.
DR DNASU; 68044; -.
DR Ensembl; ENSMUST00000020553; ENSMUSP00000020553; ENSMUSG00000020309. [Q9CQG1-2]
DR Ensembl; ENSMUST00000101394; ENSMUSP00000098942; ENSMUSG00000020309. [Q9CQG1-1]
DR GeneID; 68044; -.
DR KEGG; mmu:68044; -.
DR UCSC; uc007iih.2; mouse. [Q9CQG1-1]
DR UCSC; uc007iii.2; mouse. [Q9CQG1-2]
DR CTD; 494143; -.
DR MGI; MGI:1915294; Chac2.
DR VEuPathDB; HostDB:ENSMUSG00000020309; -.
DR eggNOG; KOG3182; Eukaryota.
DR GeneTree; ENSGT00390000003855; -.
DR HOGENOM; CLU_070703_2_2_1; -.
DR InParanoid; Q9CQG1; -.
DR OMA; LLWYTDF; -.
DR PhylomeDB; Q9CQG1; -.
DR TreeFam; TF313048; -.
DR BRENDA; 4.3.2.7; 3474.
DR Reactome; R-MMU-174403; Glutathione synthesis and recycling.
DR BioGRID-ORCS; 68044; 4 hits in 69 CRISPR screens.
DR ChiTaRS; Chac2; mouse.
DR PRO; PR:Q9CQG1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CQG1; protein.
DR Bgee; ENSMUSG00000020309; Expressed in fetal liver hematopoietic progenitor cell and 233 other tissues.
DR Genevisible; Q9CQG1; MM.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Lyase; Reference proteome.
FT CHAIN 1..178
FT /note="Putative glutathione-specific gamma-
FT glutamylcyclotransferase 2"
FT /id="PRO_0000314913"
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"
FT VAR_SEQ 46..57
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030429"
FT CONFLICT 113
FT /note="C -> Y (in Ref. 3; AAH25100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 20153 MW; 90FC51BB83835B11 CRC64;
MWVFGYGSLI WKVDFPYQDK LVGYITNYSR RFWQGSTDHR GVPGKPGRVV TLVEDPGGSV
WGVAYKLPVG KEEEVKTYLD FREKGGYRTT TVIFYPKDST TKPFSVLLYI GTCDNPNYLG
PAPLEDIAEQ IFNAAGPSGR NTEYLFELAD SVRKLVPEDA DEHLFSLEKL VKERLEGK
