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Protein

Glutathione peroxidase 3

Gene

Gpx3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731

GO - Molecular functioni

  1. glutathione peroxidase activity Source: UniProtKB
  2. selenium binding Source: UniProtKB

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: MGI
  2. protein homotetramerization Source: UniProtKB
  3. response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei3711. MmGPx03.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 3 (EC:1.11.1.9)
Short name:
GPx-3
Short name:
GSHPx-3
Alternative name(s):
Plasma glutathione peroxidase
Short name:
GPx-P
Short name:
GSHPx-P
Gene namesi
Name:Gpx3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:105102. Gpx3.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 226202Glutathione peroxidase 3PRO_0000013063Add
BLAST

Proteomic databases

MaxQBiP46412.
PaxDbiP46412.
PRIDEiP46412.

Expressioni

Tissue specificityi

Secreted in plasma.

Gene expression databases

BgeeiP46412.
CleanExiMM_GPX3.
GenevestigatoriP46412.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP46412. 3 interactions.
MINTiMINT-4096578.
STRINGi10090.ENSMUSP00000081011.

Structurei

3D structure databases

ProteinModelPortaliP46412.
SMRiP46412. Positions 36-221.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP46412.
KOiK00432.
OMAiIMRWHHR.
PhylomeDBiP46412.
TreeFamiTF105318.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARILRASCL LSLLLAGFVP PGRGQEKSKT DCHGGMSGTI YEYGALTIDG
60 70 80 90 100
EEYIPFKQYA GKYILFVNVA SYUGLTDQYL ELNALQEELG PFGLVILGFP
110 120 130 140 150
SNQFGKQEPG ENSEILPSLK YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT
160 170 180 190 200
FLKNSCPPTA ELLGSPGRLF WEPMKIHDIR WNFEKFLVGP DGIPVMRWYH
210 220
RTTVSNVKMD ILSYMRRQAA LSARGK
Length:226
Mass (Da):25,424
Last modified:February 26, 2008 - v2
Checksum:iD9706574929E3F86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 72RA → Q (PubMed:8566787).Curated
Sequence conflicti21 – 211P → A (PubMed:8566787).Curated
Sequence conflicti24 – 296GQEKSK → DKRSLR (PubMed:8566787).Curated

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei73 – 731Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13705 mRNA. Translation: AAA62283.2.
AK002219 mRNA. Translation: BAC55243.1.
AK004942 mRNA. Translation: BAC55250.1.
AK146760 mRNA. Translation: BAE27413.1.
BC003339 mRNA. Translation: AAH03339.1.
BC037027 mRNA. Translation: AAH37027.1.
BC049235 mRNA. Translation: AAH49235.1.
BC061950 mRNA. Translation: AAH61950.1.
X84742 Genomic DNA. No translation available.
CCDSiCCDS24703.1.
PIRiA55086.
RefSeqiNP_032187.2. NM_008161.3.
UniGeneiMm.200916.

Genome annotation databases

EnsembliENSMUST00000082430; ENSMUSP00000081011; ENSMUSG00000018339.
GeneIDi14778.
KEGGimmu:14778.
UCSCiuc007iyk.2. mouse.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13705 mRNA. Translation: AAA62283.2.
AK002219 mRNA. Translation: BAC55243.1.
AK004942 mRNA. Translation: BAC55250.1.
AK146760 mRNA. Translation: BAE27413.1.
BC003339 mRNA. Translation: AAH03339.1.
BC037027 mRNA. Translation: AAH37027.1.
BC049235 mRNA. Translation: AAH49235.1.
BC061950 mRNA. Translation: AAH61950.1.
X84742 Genomic DNA. No translation available.
CCDSiCCDS24703.1.
PIRiA55086.
RefSeqiNP_032187.2. NM_008161.3.
UniGeneiMm.200916.

3D structure databases

ProteinModelPortaliP46412.
SMRiP46412. Positions 36-221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP46412. 3 interactions.
MINTiMINT-4096578.
STRINGi10090.ENSMUSP00000081011.

Protein family/group databases

PeroxiBasei3711. MmGPx03.

Proteomic databases

MaxQBiP46412.
PaxDbiP46412.
PRIDEiP46412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000082430; ENSMUSP00000081011; ENSMUSG00000018339.
GeneIDi14778.
KEGGimmu:14778.
UCSCiuc007iyk.2. mouse.

Organism-specific databases

CTDi2878.
MGIiMGI:105102. Gpx3.

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP46412.
KOiK00432.
OMAiIMRWHHR.
PhylomeDBiP46412.
TreeFamiTF105318.

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiGpx3. mouse.
NextBioi286887.
PROiP46412.
SOURCEiSearch...

Gene expression databases

BgeeiP46412.
CleanExiMM_GPX3.
GenevestigatoriP46412.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion."
    Maser R.L., Magenheimer B.S., Calvet J.P.
    J. Biol. Chem. 269:27066-27073(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Heart, Kidney and Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N and NMRI.
    Tissue: Colon, Kidney and Mammary tumor.
  4. "Cloning of the mouse gene encoding plasma glutathione peroxidase: organization, sequence and chromosomal localization."
    Schwaab V., Baud E., Ghyselinck N.B., Mattei M.-G., Dufaure J.-P., Drevet J.R.
    Gene 167:25-31(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.

Entry informationi

Entry nameiGPX3_MOUSE
AccessioniPrimary (citable) accession number: P46412
Secondary accession number(s): Q5XKR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: February 26, 2008
Last modified: March 4, 2015
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.