位置:首页 > 蛋白库 > GSTM3_HUMAN
GSTM3_HUMAN
ID   GSTM3_HUMAN             Reviewed;         225 AA.
AC   P21266; O60550; Q96HA3;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 220.
DE   RecName: Full=Glutathione S-transferase Mu 3;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-mu 3;
DE   AltName: Full=GSTM3-3;
DE            Short=hGSTM3-3;
GN   Name=GSTM3; Synonyms=GST5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Brain, and Testis;
RX   PubMed=2345169; DOI=10.1016/s0021-9258(19)38830-1;
RA   Campbell E., Takahashi Y., Abramovitz M., Peretz M., Listowsky I.;
RT   "A distinct human testis and brain mu-class glutathione S-transferase.
RT   Molecular cloning and characterization of a form present even in
RT   individuals lacking hepatic type mu isoenzymes.";
RL   J. Biol. Chem. 265:9188-9193(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9882431; DOI=10.1006/abbi.1998.0964;
RA   Patskovsky Y.V., Huang M.Q., Takayama T., Listowsky I., Pearson W.R.;
RT   "Distinctive structure of the human GSTM3 gene-inverted orientation
RT   relative to the mu class glutathione transferase gene cluster.";
RL   Arch. Biochem. Biophys. 361:85-93(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-224.
RC   TISSUE=Brain, and Uterus;
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   [5]
RP   PROTEIN SEQUENCE OF N-TERMINUS.
RC   TISSUE=Testis;
RX   PubMed=8373352; DOI=10.1042/bj2940373;
RA   Ross V.L., Board P.G.;
RT   "Molecular cloning and heterologous expression of an alternatively spliced
RT   human Mu class glutathione S-transferase transcript.";
RL   Biochem. J. 294:373-380(1993).
RN   [6]
RP   PROTEIN SEQUENCE OF 190-209.
RX   PubMed=8218382; DOI=10.1016/0167-4838(93)90047-u;
RA   Hussey A.J., Hayes J.D.;
RT   "Human Mu-class glutathione S-transferases present in liver, skeletal
RT   muscle and testicular tissue.";
RL   Biochim. Biophys. Acta 1203:131-141(1993).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-54 AND LYS-73, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), CATALYTIC ACTIVITY, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF TYR-120 AND
RP   ASN-213.
RX   PubMed=10587441; DOI=10.1021/bi991714t;
RA   Patskovsky Y.V., Patskovska L.N., Listowsky I.;
RT   "An asparagine-phenylalanine substitution accounts for catalytic
RT   differences between hGSTM3-3 and other human class mu glutathione S-
RT   transferases.";
RL   Biochemistry 38:16187-16194(1999).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. May govern uptake
CC       and detoxification of both endogenous compounds and xenobiotics at the
CC       testis and brain blood barriers. {ECO:0000269|PubMed:10587441}.
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:0000269|PubMed:10587441};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.1 mM for 1-chloro-2,4-dinitrobenzene
CC         {ECO:0000269|PubMed:10587441};
CC         KM=0.084 mM for glutathione {ECO:0000269|PubMed:10587441};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10587441}.
CC   -!- INTERACTION:
CC       P21266; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-350350, EBI-12357161;
CC       P21266; P21266: GSTM3; NbExp=10; IntAct=EBI-350350, EBI-350350;
CC       P21266; Q03013: GSTM4; NbExp=4; IntAct=EBI-350350, EBI-713363;
CC       P21266; P46439: GSTM5; NbExp=12; IntAct=EBI-350350, EBI-4312072;
CC       P21266; Q12836: ZP4; NbExp=2; IntAct=EBI-350350, EBI-11783805;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Testis and brain.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J05459; AAA60964.1; -; mRNA.
DR   EMBL; AF043105; AAC17866.1; -; Genomic_DNA.
DR   EMBL; BT019945; AAV38748.1; -; mRNA.
DR   EMBL; BC000088; AAH00088.1; -; mRNA.
DR   EMBL; BC008790; AAH08790.1; -; mRNA.
DR   CCDS; CCDS812.1; -.
DR   PIR; A35295; A35295.
DR   RefSeq; NP_000840.2; NM_000849.4.
DR   PDB; 3GTU; X-ray; 2.80 A; B/D=2-225.
DR   PDBsum; 3GTU; -.
DR   AlphaFoldDB; P21266; -.
DR   SMR; P21266; -.
DR   BioGRID; 109202; 94.
DR   IntAct; P21266; 24.
DR   MINT; P21266; -.
DR   STRING; 9606.ENSP00000256594; -.
DR   ChEMBL; CHEMBL2242; -.
DR   DrugBank; DB14001; alpha-Tocopherol succinate.
DR   DrugBank; DB14002; D-alpha-Tocopherol acetate.
DR   DrugBank; DB00143; Glutathione.
DR   DrugBank; DB03310; Glutathione disulfide.
DR   DrugBank; DB00163; Vitamin E.
DR   MoonProt; P21266; -.
DR   GlyGen; P21266; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P21266; -.
DR   MetOSite; P21266; -.
DR   PhosphoSitePlus; P21266; -.
DR   BioMuta; GSTM3; -.
DR   DMDM; 21264423; -.
DR   OGP; P21266; -.
DR   REPRODUCTION-2DPAGE; IPI00246975; -.
DR   EPD; P21266; -.
DR   jPOST; P21266; -.
DR   MassIVE; P21266; -.
DR   PaxDb; P21266; -.
DR   PeptideAtlas; P21266; -.
DR   PRIDE; P21266; -.
DR   ProteomicsDB; 53855; -.
DR   Antibodypedia; 33773; 218 antibodies from 32 providers.
DR   CPTC; P21266; 3 antibodies.
DR   DNASU; 2947; -.
DR   Ensembl; ENST00000256594.7; ENSP00000256594.3; ENSG00000134202.12.
DR   Ensembl; ENST00000361066.7; ENSP00000354357.2; ENSG00000134202.12.
DR   GeneID; 2947; -.
DR   KEGG; hsa:2947; -.
DR   MANE-Select; ENST00000361066.7; ENSP00000354357.2; NM_000849.5; NP_000840.2.
DR   CTD; 2947; -.
DR   DisGeNET; 2947; -.
DR   GeneCards; GSTM3; -.
DR   HGNC; HGNC:4635; GSTM3.
DR   HPA; ENSG00000134202; Tissue enhanced (testis).
DR   MIM; 138390; gene.
DR   neXtProt; NX_P21266; -.
DR   OpenTargets; ENSG00000134202; -.
DR   Orphanet; 586; Cystic fibrosis.
DR   PharmGKB; PA29024; -.
DR   VEuPathDB; HostDB:ENSG00000134202; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000157663; -.
DR   HOGENOM; CLU_039475_2_0_1; -.
DR   InParanoid; P21266; -.
DR   OMA; KWANKRA; -.
DR   OrthoDB; 1162336at2759; -.
DR   PhylomeDB; P21266; -.
DR   TreeFam; TF353040; -.
DR   BRENDA; 2.5.1.18; 2681.
DR   PathwayCommons; P21266; -.
DR   Reactome; R-HSA-156590; Glutathione conjugation.
DR   SABIO-RK; P21266; -.
DR   SignaLink; P21266; -.
DR   BioGRID-ORCS; 2947; 5 hits in 1074 CRISPR screens.
DR   EvolutionaryTrace; P21266; -.
DR   GeneWiki; GSTM3; -.
DR   GenomeRNAi; 2947; -.
DR   Pharos; P21266; Tbio.
DR   PRO; PR:P21266; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P21266; protein.
DR   Bgee; ENSG00000134202; Expressed in right testis and 207 other tissues.
DR   ExpressionAtlas; P21266; baseline and differential.
DR   Genevisible; P21266; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0035686; C:sperm fibrous sheath; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR   GO; GO:0043295; F:glutathione binding; IDA:BHF-UCL.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
DR   GO; GO:0070458; P:cellular detoxification of nitrogen compound; IDA:BHF-UCL.
DR   GO; GO:0008065; P:establishment of blood-nerve barrier; TAS:ProtInc.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR   GO; GO:0018916; P:nitrobenzene metabolic process; IDA:BHF-UCL.
DR   GO; GO:0043627; P:response to estrogen; IEP:UniProtKB.
DR   GO; GO:0042178; P:xenobiotic catabolic process; IDA:BHF-UCL.
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   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; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW   Reference proteome; Transferase; Ubl conjugation.
FT   CHAIN           1..225
FT                   /note="Glutathione S-transferase Mu 3"
FT                   /id="PRO_0000185822"
FT   DOMAIN          5..92
FT                   /note="GST N-terminal"
FT   DOMAIN          94..212
FT                   /note="GST C-terminal"
FT   BINDING         11..12
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         50..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         63..64
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         76..77
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        54
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        73
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         224
FT                   /note="V -> I (in dbSNP:rs7483)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_014498"
FT   MUTAGEN         120
FT                   /note="Y->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:10587441"
FT   MUTAGEN         120
FT                   /note="Y->F: Strongly increased catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:10587441"
FT   MUTAGEN         213
FT                   /note="N->F: Strongly increased catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:10587441"
FT   MUTAGEN         213
FT                   /note="N->G: No effect."
FT                   /evidence="ECO:0000269|PubMed:10587441"
FT   CONFLICT        147
FT                   /note="G -> W (in Ref. 1; AAA60964)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..15
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           16..18
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           19..27
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           48..54
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   STRAND          72..76
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           77..87
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           95..120
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           124..146
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           159..174
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           176..179
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           183..193
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           196..203
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   HELIX           205..208
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:3GTU"
FT   STRAND          217..220
FT                   /evidence="ECO:0007829|PDB:3GTU"
SQ   SEQUENCE   225 AA;  26560 MW;  79093161ECEF5396 CRC64;
     MSCESSMVLG YWDIRGLAHA IRLLLEFTDT SYEEKRYTCG EAPDYDRSQW LDVKFKLDLD
     FPNLPYLLDG KNKITQSNAI LRYIARKHNM CGETEEEKIR VDIIENQVMD FRTQLIRLCY
     SSDHEKLKPQ YLEELPGQLK QFSMFLGKFS WFAGEKLTFV DFLTYDILDQ NRIFDPKCLD
     EFPNLKAFMC RFEALEKIAA YLQSDQFCKM PINNKMAQWG NKPVC
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024