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Database: UniProt
Entry: G1T569_RABIT
LinkDB: G1T569_RABIT
Original site: G1T569_RABIT 
ID   G1T569_RABIT            Unreviewed;       154 AA.
AC   G1T569;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Glutathione peroxidase 1 {ECO:0000256|ARBA:ARBA00040407};
DE            EC=1.11.1.9 {ECO:0000256|ARBA:ARBA00012310};
DE   AltName: Full=Cellular glutathione peroxidase {ECO:0000256|ARBA:ARBA00042292};
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:ENSOCUP00000011468.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000011468.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000011468.3,
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:ENSOCUP00000011468.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000011468.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2
CC         glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate +
CC         glutathione disulfide + H2O; Xref=Rhea:RHEA:50708, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57444, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC         ChEBI:CHEBI:90680; Evidence={ECO:0000256|ARBA:ARBA00036482};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709;
CC         Evidence={ECO:0000256|ARBA:ARBA00036482};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC         Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00036108};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834;
CC         Evidence={ECO:0000256|ARBA:ARBA00036108};
CC   -!- SUBUNIT: Homotetramer. Interacts with MIEN1.
CC       {ECO:0000256|ARBA:ARBA00038541}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926}.
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DR   EMBL; AAGW02041418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1T569; -.
DR   SMR; G1T569; -.
DR   STRING; 9986.ENSOCUP00000011468; -.
DR   Ensembl; ENSOCUT00000013325.3; ENSOCUP00000011468.3; ENSOCUG00000013331.3.
DR   eggNOG; KOG1651; Eukaryota.
DR   GeneTree; ENSGT00940000156150; -.
DR   HOGENOM; CLU_029507_2_0_1; -.
DR   InParanoid; G1T569; -.
DR   TreeFam; TF105318; -.
DR   Proteomes; UP000001811; Chromosome X.
DR   Bgee; ENSOCUG00000013331; Expressed in smooth muscle tissue and 14 other cell types or tissues.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF41; GLUTATHIONE PEROXIDASE 1; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811}.
SQ   SEQUENCE   154 AA;  16835 MW;  75A40CE07210E90A CRC64;
     MCAARMAAAA QSVYSFSAHP LACGEPMNLG SLRGKENAKN EEILNSLKYV RPGGGFEPNF
     MLFQKCEVNG AKAHPLFAFL REALPAPSDD PTALMTDPKF ITWSPVCRND VSWNFEKFLV
     GPDGVPVRRY SRRFPTIDIE PDIQALLSKG SGGA
//
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