ID   G2HFY3_PANTR            Unreviewed;       225 AA.
AC   G2HFY3; A0A2J8JXM6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU003494};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU003494};
GN   Name=GSTM3 {ECO:0000313|EMBL:JAA02585.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000081279.1};
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|EMBL:BAK62641.1};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000067283.1, 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|EMBL:BAK62641.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Testis {ECO:0000313|EMBL:BAK62641.1};
RX   PubMed=21484476; DOI=10.1007/s10142-011-0220-9;
RA   Kim R.N., Kim D.W., Choi S.H., Chae S.H., Nam S.H., Kim D.W., Kim A.,
RA   Kang A., Park K.H., Lee Y.S., Hirai M., Suzuki Y., Sugano S., Hashimoto K.,
RA   Kim D.S., Park H.S.;
RT   "Major chimpanzee-specific structural changes in sperm development-
RT   associated genes.";
RL   Funct. Integr. Genomics 11:507-517(2011).
RN   [3] {ECO:0000313|EMBL:JAA02585.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA02585.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Ensembl:ENSPTRP00000067283.1}
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|ARBA:ARBA00000710,
CC         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   EMBL; AK305647; BAK62641.1; -; mRNA.
DR   EMBL; GABC01008753; JAA02585.1; -; mRNA.
DR   RefSeq; NP_001233497.1; NM_001246568.1.
DR   RefSeq; XP_009427417.1; XM_009429142.1.
DR   RefSeq; XP_016781448.1; XM_016925959.1.
DR   STRING; 9598.ENSPTRP00000067283; -.
DR   PaxDb; 9598-ENSPTRP00000001838; -.
DR   Ensembl; ENSPTRT00000092461.1; ENSPTRP00000067283.1; ENSPTRG00000042967.1.
DR   Ensembl; ENSPTRT00000092937.1; ENSPTRP00000081279.1; ENSPTRG00000043733.1.
DR   GeneID; 457128; -.
DR   KEGG; ptr:457128; -.
DR   CTD; 2947; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000157663; -.
DR   HOGENOM; CLU_039475_2_0_1; -.
DR   OMA; KIANYMQ; -.
DR   OrthoDB; 5488107at2759; -.
DR   TreeFam; TF353040; -.
DR   Proteomes; UP000002277; Chromosome 1.
DR   Bgee; ENSPTRG00000042967; Expressed in testis and 15 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; cd03209; GST_C_Mu; 1.
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:SF133; GLUTATHIONE S-TRANSFERASE MU 3; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01267; GSTRNSFRASEM.
DR   SFLD; SFLDG01205; AMPS.1; 1.
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   2: Evidence at transcript level;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Transferase {ECO:0000256|RuleBase:RU003494, ECO:0000313|EMBL:BAK62641.1}.
FT   DOMAIN          5..92
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          94..212
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   225 AA;  26604 MW;  790F87D1ECEF5396 CRC64;
     MSCESSMVLG YWDIRGLAHA IRLLLEFTDT SYEEKRYTCG EAPDYDRSQW LDVKFKLDLD
     FPNLPYLLDG KNKITQSNAI LRYIARKHNM CGETEEEKIR VDIIENQVMD FRTQLIRLCY
     SSDHEKLKPQ YLEELPGQLK QFSMFLGKFS WFAGEKLTFV DFLTYDILDQ NRIFDPKCLD
     EFPNLKAFMC RFEALEKIAA YLQSDQFFKM PINNKMAQWG NKPVC
//