ID G1SXQ0_RABIT Unreviewed; 279 AA.
AC G1SXQ0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 63.
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|Ensembl:ENSOCUP00000008346.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000008346.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000008346.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000008346.3,
RC ECO:0000313|Proteomes:UP000001811};
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:ENSOCUP00000008346.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000008346.3};
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 -!- SIMILARITY: Belongs to the GST superfamily. Mu family.
CC {ECO:0000256|ARBA:ARBA00005861, ECO:0000256|RuleBase:RU003494}.
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DR EMBL; AAGW02000960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02000961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02000962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02000963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1SXQ0; -.
DR SMR; G1SXQ0; -.
DR STRING; 9986.ENSOCUP00000008346; -.
DR PaxDb; 9986-ENSOCUP00000008346; -.
DR Ensembl; ENSOCUT00000009687.4; ENSOCUP00000008346.3; ENSOCUG00000023703.2.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000157663; -.
DR HOGENOM; CLU_039475_2_0_1; -.
DR InParanoid; G1SXQ0; -.
DR OMA; KIANYMQ; -.
DR TreeFam; TF353040; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000023703; Expressed in testis and 14 other cell types or tissues.
DR ExpressionAtlas; G1SXQ0; baseline.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0035686; C:sperm fibrous sheath; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0043295; F:glutathione binding; IEA:Ensembl.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; IEA:Ensembl.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR GO; GO:0018916; P:nitrobenzene metabolic process; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0042178; P:xenobiotic catabolic process; IEA:Ensembl.
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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Transferase {ECO:0000256|RuleBase:RU003494}.
FT DOMAIN 59..146
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 148..266
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 32773 MW; D0D22B8DE5063AD9 CRC64;
MRVAPLARGE GARGRRGEDK ELTLTPPTYV DYKPSLPAGR RSSKIRWRRS GGLTMSSTSS
MLLGYWDIRG LAHAIRLLLE FTDTCYEEKR YTCGEAPDYD RSQWLDVKFK LDLDFPNLPY
LMDGNNKITQ SNAILRYIAR KHNMCGDTEE EKIRVDIMEN QIMDFRMQLV RLCYNSDHEK
MKPQYLEQLP GQLKQFSLFL GKYSWFAGEK LTFVDFLTYD VLDQNRMFEP KCLDEFPNLK
AFMCRFEALE KIAAYMQSDR FFKMPINNKM AKWGNRSLC
//
