ID H0VDJ3_CAVPO Unreviewed; 569 AA.
AC H0VDJ3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Glutathione hydrolase {ECO:0000256|RuleBase:RU368068};
DE EC=2.3.2.2 {ECO:0000256|RuleBase:RU368068};
DE EC=3.4.19.13 {ECO:0000256|RuleBase:RU368068};
DE AltName: Full=Gamma-glutamyltransferase {ECO:0000256|RuleBase:RU368068};
DE AltName: Full=Gamma-glutamyltranspeptidase {ECO:0000256|RuleBase:RU368068};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000008050.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000008050.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000008050.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione and
CC glutathione conjugates. {ECO:0000256|RuleBase:RU368068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:143103; EC=3.4.19.13;
CC Evidence={ECO:0000256|ARBA:ARBA00033643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469;
CC Evidence={ECO:0000256|ARBA:ARBA00033643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC ChEBI:CHEBI:78608; EC=2.3.2.2;
CC Evidence={ECO:0000256|RuleBase:RU368068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC Evidence={ECO:0000256|ARBA:ARBA00033701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808;
CC Evidence={ECO:0000256|ARBA:ARBA00033701};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000256|ARBA:ARBA00005115, ECO:0000256|RuleBase:RU368068}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU368068}; Single-
CC pass type II membrane protein {ECO:0000256|RuleBase:RU368068}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009381}.
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DR EMBL; AAKN02007190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02007191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003478050.1; XM_003478002.3.
DR RefSeq; XP_012997544.1; XM_013142090.1.
DR RefSeq; XP_012997545.1; XM_013142091.1.
DR RefSeq; XP_012997546.1; XM_013142092.1.
DR RefSeq; XP_012997547.1; XM_013142093.1.
DR STRING; 10141.ENSCPOP00000025838; -.
DR Ensembl; ENSCPOT00000009038.3; ENSCPOP00000008050.2; ENSCPOG00000008956.4.
DR Ensembl; ENSCPOT00000047776.1; ENSCPOP00000025838.1; ENSCPOG00000008956.4.
DR GeneID; 100717316; -.
DR KEGG; cpoc:100717316; -.
DR CTD; 2678; -.
DR VEuPathDB; HostDB:ENSCPOG00000008956; -.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000154601; -.
DR HOGENOM; CLU_014813_4_1_1; -.
DR OMA; KATKNMF; -.
DR OrthoDB; 2910309at2759; -.
DR TreeFam; TF313608; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000008956; Expressed in adult mammalian kidney and 11 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:Ensembl.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0002682; P:regulation of immune system process; IEA:Ensembl.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR000101; GGT_peptidase.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR NCBIfam; TIGR00066; g_glut_trans; 1.
DR PANTHER; PTHR11686; GAMMA GLUTAMYL TRANSPEPTIDASE; 1.
DR PANTHER; PTHR11686:SF56; GLUTATHIONE HYDROLASE 1 PROENZYME-RELATED; 1.
DR Pfam; PF01019; G_glu_transpept; 1.
DR PRINTS; PR01210; GGTRANSPTASE.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU368068};
KW Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684};
KW Hydrolase {ECO:0000256|RuleBase:RU368068};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Transferase {ECO:0000256|RuleBase:RU368068}.
FT ACT_SITE 381
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 569 AA; 61199 MW; 9EFDA4C1F785A801 CRC64;
MKKQFVVLGL LAVVLILVII GLCLWLPSAS STQPDHVYAK AAVAADAKRC SEIGRDMLLD
GGSAVDAAIA GLLCTGLMNA HSMGIGGGLF LTIYDSATGK AEIINAREVA PRMAHASMFN
SSQQSEEGGL SVAVPGEIRG YELAHQRHGR LPWHRLFQPS IQLAREGFPV GKGLAGALER
TRTVIEQSPA LCEVFCRHGK VLKEGDTVTM PRLADTYETL AREGAQAFYN GSLTAQIVKD
IRDAGGIMTT EDLNNYRAEL IEHPLSISLG DSVLYTPSAP LSGPVLVLIL NILKGYNFSS
ASVSTPEQKA LTYHRIVEAF RFAYAKRTLL GDPKFVDVTK VIHNMSSEFF AAQLQGRISD
DTTYPVSYYE PEYYTPNDGG TAHLSVVSED GSAVSATSTI NLYFGSKLIS QVSGILFNNE
MDDFSSPNFT NQFGVSPSPA NFIEPGKQPL SSMCPSIIVG KDGKVQMVVG ASGGTQITTS
TALTIIHSLW FGYDMKRAVE EPRLHNQLLP NTTTLEKDVD EAVVAGLKTR HHETAFTSTF
IAVVQAIART ARGWAAASDS RKGGEPAGY
//
