ID GPX3_HUMAN Reviewed; 226 AA.
AC P22352; O43787; Q86W78; Q9NZ74; Q9UEL1;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 01-MAY-2013, entry version 141.
DE RecName: Full=Glutathione peroxidase 3;
DE Short=GPx-3;
DE Short=GSHPx-3;
DE EC=1.11.1.9;
DE AltName: Full=Extracellular glutathione peroxidase;
DE AltName: Full=Plasma glutathione peroxidase;
DE Short=GPx-P;
DE Short=GSHPx-P;
DE Flags: Precursor;
GN Name=GPX3; Synonyms=GPXP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fetal liver, and Placenta;
RX PubMed=2229017;
RA Takahashi K., Akasaka M., Yamamoto Y., Kobayashi C., Mizoguchi J.,
RA Koyama J.;
RT "Primary structure of human plasma glutathione peroxidase deduced from
RT cDNA sequences.";
RL J. Biochem. 108:145-148(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=1339300;
RA Chu F.-F., Esworthy R.S., Doroshow J.H., Doan K., Liu X.F.;
RT "Expression of plasma glutathione peroxidase in human liver in
RT addition to kidney, heart, lung, and breast in humans and rodents.";
RL Blood 79:3233-3238(1992).
RN [3]
RP SEQUENCE REVISION TO 73.
RA Chu F.-F.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lymphocyte;
RX PubMed=8056346; DOI=10.1016/0378-1119(94)90023-X;
RA Yoshimura S., Suemizu H., Taniguchi Y., Arimori K., Kawabe N.,
RA Moriuchi T.;
RT "The human plasma glutathione peroxidase-encoding gene: organization,
RT sequence and localization to chromosome 5q32.";
RL Gene 145:293-297(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10970826;
RA Comhair S.A.A., Thomassen M.J., Erzurum S.C.;
RT "Differential induction of extracellular glutathione peroxidase and
RT nitric oxide synthase 2 in airways of healthy individuals exposed to
RT 100% O(2) or cigarette smoke.";
RL Am. J. Respir. Cell Mol. Biol. 23:350-354(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-128.
RG NIEHS SNPs program;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum, Lung, and Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 107-138 AND 148-175, AND CHARACTERIZATION.
RX PubMed=1897960; DOI=10.1016/0003-9861(91)90048-N;
RA Esworthy R.S., Chu F.-F., Paxton R.J., Akman S., Doroshow J.H.;
RT "Characterization and partial amino acid sequence of human plasma
RT glutathione peroxidase.";
RL Arch. Biochem. Biophys. 286:330-336(1991).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 25-223.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human glutathione peroxidase 3 (selenocysteine
RT to glycine mutant).";
RL Submitted (SEP-2007) to the PDB data bank.
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.
CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC disulfide + 2 H(2)O.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Secreted in plasma.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gpx3/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Glutathione peroxidase entry;
CC URL="http://en.wikipedia.org/wiki/Glutathione_peroxidase";
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DR EMBL; D00632; BAA00525.1; -; mRNA.
DR EMBL; X58295; CAA41228.2; -; mRNA.
DR EMBL; D16360; BAA03862.1; -; Genomic_DNA.
DR EMBL; D16361; BAA03863.2; -; Genomic_DNA.
DR EMBL; D16362; BAA03864.1; -; Genomic_DNA.
DR EMBL; AF217787; AAF43005.1; -; mRNA.
DR EMBL; AY310878; AAP50261.1; -; Genomic_DNA.
DR EMBL; AC008641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013601; AAH13601.1; -; mRNA.
DR EMBL; BC035841; AAH35841.1; -; mRNA.
DR EMBL; BC050378; AAH50378.2; -; mRNA.
DR IPI; IPI00026199; -.
DR PIR; I53822; JQ0476.
DR RefSeq; NP_002075.2; NM_002084.3.
DR UniGene; Hs.386793; -.
DR UniGene; Hs.725787; -.
DR PDB; 2R37; X-ray; 1.85 A; A/B=25-223.
DR PDBsum; 2R37; -.
DR ProteinModelPortal; P22352; -.
DR IntAct; P22352; 6.
DR STRING; 9606.ENSP00000373477; -.
DR PeroxiBase; 3602; HsGPx03.
DR DMDM; 172046796; -.
DR REPRODUCTION-2DPAGE; IPI00026199; -.
DR SWISS-2DPAGE; P22352; -.
DR PaxDb; P22352; -.
DR PRIDE; P22352; -.
DR DNASU; 2878; -.
DR Ensembl; ENST00000388825; ENSP00000373477; ENSG00000211445.
DR GeneID; 2878; -.
DR KEGG; hsa:2878; -.
DR UCSC; uc021yga.1; human.
DR CTD; 2878; -.
DR GeneCards; GC05P150381; -.
DR H-InvDB; HIX0024803; -.
DR HGNC; HGNC:4555; GPX3.
DR MIM; 138321; gene.
DR neXtProt; NX_P22352; -.
DR PharmGKB; PA28951; -.
DR eggNOG; COG0386; -.
DR HOGENOM; HOG000277055; -.
DR HOVERGEN; HBG004333; -.
DR InParanoid; P22352; -.
DR KO; K00432; -.
DR OMA; SNVKMDI; -.
DR OrthoDB; EOG4CRM10; -.
DR PhylomeDB; P22352; -.
DR BioCyc; MetaCyc:HS08224-MONOMER; -.
DR ChiTaRS; GPX3; human.
DR DrugBank; DB00143; Glutathione.
DR EvolutionaryTrace; P22352; -.
DR GenomeRNAi; 2878; -.
DR NextBio; 11363; -.
DR ArrayExpress; P22352; -.
DR Bgee; P22352; -.
DR CleanEx; HS_GPX3; -.
DR Genevestigator; P22352; -.
DR GermOnline; ENSG00000211445; Homo sapiens.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:UniProtKB.
DR GO; GO:0008430; F:selenium binding; IDA:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; TAS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0006982; P:response to lipid hydroperoxide; TAS:UniProtKB.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR PANTHER; PTHR11592; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thiordxn-like_fd; 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 3D-structure; Complete proteome; Direct protein sequencing;
KW Oxidoreductase; Peroxidase; Polymorphism; Reference proteome;
KW Secreted; Selenocysteine; Signal.
FT SIGNAL 1 20 Potential.
FT CHAIN 21 226 Glutathione peroxidase 3.
FT /FTId=PRO_0000013062.
FT ACT_SITE 73 73
FT NON_STD 73 73 Selenocysteine.
FT VARIANT 128 128 F -> L (in dbSNP:rs8177445).
FT /FTId=VAR_020943.
FT HELIX 40 42
FT STRAND 44 47
FT STRAND 53 55
FT HELIX 56 59
FT STRAND 62 69
FT STRAND 71 73
FT TURN 74 77
FT HELIX 78 89
FT HELIX 90 92
FT STRAND 94 100
FT HELIX 112 114
FT HELIX 115 121
FT STRAND 131 135
FT STRAND 140 142
FT HELIX 147 155
FT HELIX 166 168
FT STRAND 185 188
FT STRAND 194 198
FT HELIX 204 223
SQ SEQUENCE 226 AA; 25552 MW; A839E87A5CDB51A9 CRC64;
MARLLQASCL LSLLLAGFVS QSRGQEKSKM DCHGGISGTI YEYGALTIDG EEYIPFKQYA
GKYVLFVNVA SYUGLTGQYI ELNALQEELA PFGLVILGFP CNQFGKQEPG ENSEILPTLK
YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR
WNFEKFLVGP DGIPIMRWHH RTTVSNVKMD ILSYMRRQAA LGVKRK
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