ID A0A2I3RIV0_PANTR Unreviewed; 205 AA.
AC A0A2I3RIV0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU003494};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU003494};
GN Name=GSTM5 {ECO:0000313|Ensembl:ENSPTRP00000064569.1,
GN ECO:0000313|VGNC:VGNC:6852};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000064569.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000064569.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000064569.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000256|RuleBase:RU003494};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family.
CC {ECO:0000256|ARBA:ARBA00005861, ECO:0000256|RuleBase:RU003494}.
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DR EMBL; AC199716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3RIV0; -.
DR Ensembl; ENSPTRT00000082877.1; ENSPTRP00000064569.1; ENSPTRG00000001062.5.
DR VGNC; VGNC:6852; GSTM5.
DR GeneTree; ENSGT00940000155416; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001062; Expressed in fibroblast and 9 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:UniProt.
DR CDD; cd03075; GST_N_Mu; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF249; GLUTATHIONE S-TRANSFERASE MU 5; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Transferase {ECO:0000256|RuleBase:RU003494}.
FT DOMAIN 1..84
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 86..205
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 205 AA; 23708 MW; F99A55CEC616D6E0 CRC64;
MTLCVCLGLA HAIRLLLEYT DSSYVEKKYT LGDAPDYDRS QWLNEKFKLG LDFPNLPYLI
DGAHKITQSN AILRYIARKH NLCGETEEEK IRVDILENQV MDNHMELVRL CYDPDFEKLK
PKYLEELPEK LKLYSEFLEK QPWFAGDKIT FVDFLAYDVL DMKRIFEPKC LDAFLNLKDF
ISLSCGLASS SRAGDVVGAQ GHREI
//
