GPX8_MOUSE
ID GPX8_MOUSE Reviewed; 209 AA.
AC Q9D7B7; Q8VE68;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable glutathione peroxidase 8;
DE Short=GPx-8;
DE Short=GSHPx-8;
DE EC=1.11.1.9;
GN Name=Gpx8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; AK009378; BAB26254.1; -; mRNA.
DR EMBL; BC019664; AAH19664.1; -; mRNA.
DR CCDS; CCDS26781.1; -.
DR RefSeq; NP_081403.1; NM_027127.2.
DR AlphaFoldDB; Q9D7B7; -.
DR SMR; Q9D7B7; -.
DR BioGRID; 213554; 3.
DR STRING; 10090.ENSMUSP00000022282; -.
DR PhosphoSitePlus; Q9D7B7; -.
DR EPD; Q9D7B7; -.
DR MaxQB; Q9D7B7; -.
DR PaxDb; Q9D7B7; -.
DR PeptideAtlas; Q9D7B7; -.
DR PRIDE; Q9D7B7; -.
DR ProteomicsDB; 271084; -.
DR Antibodypedia; 23390; 120 antibodies from 22 providers.
DR DNASU; 69590; -.
DR Ensembl; ENSMUST00000022282; ENSMUSP00000022282; ENSMUSG00000021760.
DR GeneID; 69590; -.
DR KEGG; mmu:69590; -.
DR UCSC; uc007rxb.1; mouse.
DR CTD; 493869; -.
DR MGI; MGI:1916840; Gpx8.
DR VEuPathDB; HostDB:ENSMUSG00000021760; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000159371; -.
DR HOGENOM; CLU_029507_0_1_1; -.
DR InParanoid; Q9D7B7; -.
DR OMA; KVVRFWR; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; Q9D7B7; -.
DR TreeFam; TF331942; -.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR BioGRID-ORCS; 69590; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Gpx8; mouse.
DR PRO; PR:Q9D7B7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9D7B7; protein.
DR Bgee; ENSMUSG00000021760; Expressed in humerus cartilage element and 244 other tissues.
DR ExpressionAtlas; Q9D7B7; baseline and differential.
DR Genevisible; Q9D7B7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR InterPro; IPR013376; Glut_perox_Gpx7.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02540; gpx7; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Oxidoreductase; Peroxidase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..209
FT /note="Probable glutathione peroxidase 8"
FT /id="PRO_0000317757"
FT TRANSMEM 18..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 79
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8TED1"
FT CONFLICT 88
FT /note="T -> I (in Ref. 2; AAH19664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 24148 MW; 8DA93ED11B4ECF21 CRC64;
MEPFAAYPLK CSGPKAKIFA VLLSMVLCTV MLFLLQLKFL KPRTNSFYSF EVKDAKGRTV
SLEKFKGKAS LVVNVASDCR FTDKSYQTLR ELHKEFGPYH FNVLAFPCNQ FGESEPKSSK
EVESFARQNY GVTFPIFHKI KILGPEAEPA FRFIVDSSKK EPRWNFWKYL VNPEGQVVKF
WRPEEPLEAI RPHVSQMIGQ IILKKKEDL
