ID GPX3_MOUSE Reviewed; 226 AA.
AC P46412; Q5XKR0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 185.
DE RecName: Full=Glutathione peroxidase 3 {ECO:0000305};
DE Short=GPx-3;
DE Short=GSHPx-3;
DE EC=1.11.1.9 {ECO:0000250|UniProtKB:P22352};
DE AltName: Full=Plasma glutathione peroxidase;
DE Short=GPx-P;
DE Short=GSHPx-P;
DE Flags: Precursor;
GN Name=Gpx3 {ECO:0000312|MGI:MGI:105102};
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=7929449; DOI=10.1016/s0021-9258(18)47126-8;
RA Maser R.L., Magenheimer B.S., Calvet J.P.;
RT "Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal
RT proximal tubular expression and secretion.";
RL J. Biol. Chem. 269:27066-27073(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Kidney, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and NMRI; TISSUE=Colon, Kidney, and 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=8566787; DOI=10.1016/0378-1119(95)00551-x;
RA Schwaab V., Baud E., Ghyselinck N.B., Mattei M.-G., Dufaure J.-P.,
RA Drevet J.R.;
RT "Cloning of the mouse gene encoding plasma glutathione peroxidase:
RT organization, sequence and chromosomal localization.";
RL Gene 167:25-31(1995).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Spleen, and Testis;
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 -!- FUNCTION: Protects cells and enzymes from oxidative damage, by
CC catalyzing the reduction of hydrogen peroxide, lipid peroxides and
CC organic hydroperoxide, by glutathione. {ECO:0000250|UniProtKB:P22352}.
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:0000250|UniProtKB:P22352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + tert-butyl hydroperoxide = glutathione
CC disulfide + H2O + tert-butanol; Xref=Rhea:RHEA:69412,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:45895, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297, ChEBI:CHEBI:64090;
CC Evidence={ECO:0000250|UniProtKB:P22352};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Secreted in plasma.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; U13705; AAA62283.2; -; mRNA.
DR EMBL; AK002219; BAC55243.1; -; mRNA.
DR EMBL; AK004942; BAC55250.1; -; mRNA.
DR EMBL; AK146760; BAE27413.1; -; mRNA.
DR EMBL; BC003339; AAH03339.1; -; mRNA.
DR EMBL; BC037027; AAH37027.1; -; mRNA.
DR EMBL; BC049235; AAH49235.1; -; mRNA.
DR EMBL; BC061950; AAH61950.1; -; mRNA.
DR EMBL; X84742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24703.1; -.
DR PIR; A55086; A55086.
DR RefSeq; NP_001316789.1; NM_001329860.1.
DR RefSeq; NP_032187.2; NM_008161.4.
DR BioGRID; 200040; 3.
DR IntAct; P46412; 1.
DR STRING; 10090.ENSMUSP00000081011; -.
DR PeroxiBase; 3711; MmGPx03.
DR iPTMnet; P46412; -.
DR PhosphoSitePlus; P46412; -.
DR SwissPalm; P46412; -.
DR CPTAC; non-CPTAC-3540; -.
DR jPOST; P46412; -.
DR MaxQB; P46412; -.
DR PaxDb; 10090-ENSMUSP00000081011; -.
DR PeptideAtlas; P46412; -.
DR ProteomicsDB; 271014; -.
DR Antibodypedia; 8091; 288 antibodies from 32 providers.
DR DNASU; 14778; -.
DR Ensembl; ENSMUST00000082430.11; ENSMUSP00000081011.5; ENSMUSG00000018339.13.
DR GeneID; 14778; -.
DR KEGG; mmu:14778; -.
DR UCSC; uc007iyk.2; mouse.
DR AGR; MGI:105102; -.
DR CTD; 2878; -.
DR MGI; MGI:105102; Gpx3.
DR VEuPathDB; HostDB:ENSMUSG00000018339; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000161754; -.
DR InParanoid; P46412; -.
DR OMA; KTDCHAG; -.
DR OrthoDB; 67394at2759; -.
DR PhylomeDB; P46412; -.
DR TreeFam; TF105318; -.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR BioGRID-ORCS; 14778; 5 hits in 80 CRISPR screens.
DR ChiTaRS; Gpx3; mouse.
DR PRO; PR:P46412; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P46412; Protein.
DR Bgee; ENSMUSG00000018339; Expressed in right kidney and 278 other cell types or tissues.
DR ExpressionAtlas; P46412; baseline and differential.
DR Genevisible; P46412; MM.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0045340; F:mercury ion binding; ISO:MGI.
DR GO; GO:0008430; F:selenium binding; ISS:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF32; GLUTATHIONE PEROXIDASE 3; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase; Peroxidase; Reference proteome; Secreted; Selenocysteine;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..226
FT /note="Glutathione peroxidase 3"
FT /id="PRO_0000013063"
FT ACT_SITE 73
FT NON_STD 73
FT /note="Selenocysteine"
FT CONFLICT 6..7
FT /note="RA -> Q (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="P -> A (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 24..29
FT /note="GQEKSK -> DKRSLR (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 25424 MW; D9706574929E3F86 CRC64;
MARILRASCL LSLLLAGFVP PGRGQEKSKT DCHGGMSGTI YEYGALTIDG EEYIPFKQYA
GKYILFVNVA SYUGLTDQYL ELNALQEELG PFGLVILGFP SNQFGKQEPG ENSEILPSLK
YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTA ELLGSPGRLF WEPMKIHDIR
WNFEKFLVGP DGIPVMRWYH RTTVSNVKMD ILSYMRRQAA LSARGK
//
