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Phospholipid hydroperoxide glutathione peroxidase, mitochondrial (PHGPx) (EC 1.11.1.12) (Glutathione peroxidase 4) (GPx-4) (GSHPx-4)

 GPX4_HUMAN              Reviewed;         197 AA.
P36969; O43381; Q6PJ59; Q9UPK2;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 3.
25-OCT-2017, entry version 185.
RecName: Full=Phospholipid hydroperoxide glutathione peroxidase, mitochondrial;
Short=PHGPx;
EC=1.11.1.12;
AltName: Full=Glutathione peroxidase 4;
Short=GPx-4;
Short=GSHPx-4;
Flags: Precursor;
Name=GPX4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=8039723; DOI=10.1016/0378-1119(94)90400-6;
Esworthy R.S., Doan K., Doroshow J.H., Chu F.-F.;
"Cloning and sequencing of the cDNA encoding a human testis
phospholipid hydroperoxide glutathione peroxidase.";
Gene 144:317-318(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9705830; DOI=10.1006/bbrc.1998.9086;
Kelner M.J., Montoya M.A.;
"Structural organization of the human selenium-dependent phospholipid
hydroperoxide glutathione peroxidase gene (GPX4): chromosomal
localization to 19p13.3.";
Biochem. Biophys. Res. Commun. 249:53-55(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-2.
NIEHS SNPs program;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, Lung, Pancreas, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[9]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 29-197 (ISOFORM
CYTOPLASMIC), SUBUNIT, AND MUTAGENESIS OF SEC-73.
PubMed=17630701; DOI=10.1021/bi700840d;
Scheerer P., Borchert A., Krauss N., Wessner H., Gerth C., Hoehne W.,
Kuhn H.;
"Structural basis for catalytic activity and enzyme polymerization of
phospholipid hydroperoxide glutathione peroxidase-4 (GPx4).";
Biochemistry 46:9041-9049(2007).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 36-197.
Structural genomics consortium (SGC);
"Crystal structure of the selenocysteine to glycine mutant of human
glutathione peroxidase 4 (GPX4).";
Submitted (FEB-2009) to the PDB data bank.
[11]
VARIANTS ASN-2 AND THR-120.
PubMed=12606444; DOI=10.1095/biolreprod.102.007500;
Maiorino M., Bosello V., Ursini F., Foresta C., Garolla A., Scapin M.,
Sztajer H., Flohe L.;
"Genetic variations of gpx-4 and male infertility in humans.";
Biol. Reprod. 68:1134-1141(2003).
[12]
INVOLVEMENT IN SMDS.
PubMed=24706940; DOI=10.1136/jmedgenet-2013-102218;
FORGE Canada Consortium;
Smith A.C., Mears A.J., Bunker R., Ahmed A., MacKenzie M.,
Schwartzentruber J.A., Beaulieu C.L., Ferretti E., Majewski J.,
Bulman D.E., Celik F.C., Boycott K.M., Graham G.E.;
"Mutations in the enzyme glutathione peroxidase 4 cause Sedaghatian-
type spondylometaphyseal dysplasia.";
J. Med. Genet. 51:470-474(2014).
-!- FUNCTION: Protects cells against membrane lipid peroxidation and
cell death. Required for normal sperm development and male
fertility. Could play a major role in protecting mammals from the
toxicity of ingested lipid hydroperoxides. Essential for embryonic
development. Protects from radiation and oxidative damage.
Essential for maturation and survival of photoreceptor cells.
Plays a role in a primary T cell response to viral and parasitic
infection by protecting T cells from ferroptosis, a cell death
resulting from an iron-dependent accumulation of lipid reactive
oxygen species, and by supporting T cell expansion.
{ECO:0000250|UniProtKB:O70325}.
-!- CATALYTIC ACTIVITY: 2 glutathione + a hydroperoxy-fatty-acyl-
[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] +
H(2)O. {ECO:0000250|UniProtKB:P36968}.
-!- SUBUNIT: Monomer. Has a tendency to form higher mass oligomers.
{ECO:0000269|PubMed:17630701}.
-!- SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion.
-!- SUBCELLULAR LOCATION: Isoform Cytoplasmic: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Mitochondrial;
IsoId=P36969-1; Sequence=Displayed;
Name=Cytoplasmic;
IsoId=P36969-2; Sequence=VSP_018740;
-!- TISSUE SPECIFICITY: Present primarily in testis.
-!- DISEASE: Spondylometaphyseal dysplasia, Sedaghatian type (SMDS)
[MIM:250220]: A form of spondylometaphyseal dysplasia, a group of
short stature disorders distinguished by abnormalities in the
vertebrae and the metaphyses of the tubular bones. SMDS is a
neonatal lethal form characterized by severe metaphyseal
chondrodysplasia with mild limb shortening, platyspondyly, cardiac
conduction defects, and central nervous system abnormalities.
{ECO:0000269|PubMed:24706940}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the glutathione peroxidase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/gpx4/";
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EMBL; X71973; CAA50793.1; -; mRNA.
EMBL; AF060972; AAC32261.1; -; Genomic_DNA.
EMBL; AY324108; AAP72965.1; -; Genomic_DNA.
EMBL; AC004151; AAC03239.1; -; Genomic_DNA.
EMBL; AC005390; AAC28920.1; -; Genomic_DNA.
EMBL; BC011836; AAH11836.1; -; mRNA.
EMBL; BC021567; AAH21567.1; -; mRNA.
EMBL; BC022071; AAH22071.1; -; mRNA.
EMBL; BC032695; AAH32695.3; -; mRNA.
EMBL; BC039849; AAH39849.1; -; mRNA.
CCDS; CCDS42457.1; -. [P36969-1]
PIR; T02747; T02747.
RefSeq; NP_001034936.1; NM_001039847.2.
RefSeq; NP_002076.2; NM_002085.4. [P36969-1]
UniGene; Hs.433951; -.
PDB; 2GS3; X-ray; 1.90 A; A=36-197.
PDB; 2OBI; X-ray; 1.55 A; A=29-197.
PDB; 5H5Q; X-ray; 1.10 A; A=29-197.
PDB; 5H5R; X-ray; 1.20 A; A=29-197.
PDB; 5H5S; X-ray; 1.85 A; A=29-197.
PDBsum; 2GS3; -.
PDBsum; 2OBI; -.
PDBsum; 5H5Q; -.
PDBsum; 5H5R; -.
PDBsum; 5H5S; -.
ProteinModelPortal; P36969; -.
SMR; P36969; -.
BioGrid; 109137; 39.
DIP; DIP-53543N; -.
IntAct; P36969; 8.
STRING; 9606.ENSP00000346103; -.
DrugBank; DB00143; Glutathione.
SwissLipids; SLP:000001633; -.
MoonProt; P36969; -.
PeroxiBase; 3603; HsGPx04-A.
PeroxiBase; 3632; HsGPx04-B.
PeroxiBase; 3633; HsGPx04-C.
iPTMnet; P36969; -.
PhosphoSitePlus; P36969; -.
SwissPalm; P36969; -.
BioMuta; GPX4; -.
DMDM; 172045844; -.
REPRODUCTION-2DPAGE; IPI00304814; -.
UCD-2DPAGE; P36969; -.
EPD; P36969; -.
MaxQB; P36969; -.
PaxDb; P36969; -.
PeptideAtlas; P36969; -.
PRIDE; P36969; -.
DNASU; 2879; -.
Ensembl; ENST00000354171; ENSP00000346103; ENSG00000167468. [P36969-1]
Ensembl; ENST00000611653; ENSP00000483655; ENSG00000167468. [P36969-2]
GeneID; 2879; -.
KEGG; hsa:2879; -.
UCSC; uc021umg.3; human. [P36969-1]
CTD; 2879; -.
DisGeNET; 2879; -.
EuPathDB; HostDB:ENSG00000167468.16; -.
GeneCards; GPX4; -.
HGNC; HGNC:4556; GPX4.
HPA; CAB008630; -.
HPA; HPA047224; -.
HPA; HPA058546; -.
MalaCards; GPX4; -.
MIM; 138322; gene.
MIM; 250220; phenotype.
neXtProt; NX_P36969; -.
OpenTargets; ENSG00000167468; -.
Orphanet; 93317; Spondylometaphyseal dysplasia, Sedaghatian type.
PharmGKB; PA28952; -.
eggNOG; KOG1651; Eukaryota.
eggNOG; COG0386; LUCA.
GeneTree; ENSGT00900000141111; -.
HOGENOM; HOG000277054; -.
HOVERGEN; HBG004333; -.
InParanoid; P36969; -.
KO; K05361; -.
OMA; GTDESIH; -.
PhylomeDB; P36969; -.
TreeFam; TF338735; -.
BioCyc; MetaCyc:HS09562-MONOMER; -.
BRENDA; 1.11.1.12; 2681.
Reactome; R-HSA-2142688; Synthesis of 5-eicosatetraenoic acids.
Reactome; R-HSA-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
Reactome; R-HSA-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
SABIO-RK; P36969; -.
ChiTaRS; GPX4; human.
EvolutionaryTrace; P36969; -.
GeneWiki; GPX4; -.
GenomeRNAi; 2879; -.
PRO; PR:P36969; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000167468; -.
CleanEx; HS_GPX4; -.
ExpressionAtlas; P36969; baseline and differential.
Genevisible; P36969; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0004602; F:glutathione peroxidase activity; IMP:CAFA.
GO; GO:0042802; F:identical protein binding; IMP:CAFA.
GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IEA:UniProtKB-EC.
GO; GO:0019372; P:lipoxygenase pathway; TAS:Reactome.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0055114; P:oxidation-reduction process; TAS:UniProtKB.
GO; GO:0006644; P:phospholipid metabolic process; TAS:UniProtKB.
GO; GO:0051258; P:protein polymerization; IMP:CAFA.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
CDD; cd00340; GSH_Peroxidase; 1.
InterPro; IPR000889; Glutathione_peroxidase.
InterPro; IPR029759; GPX_AS.
InterPro; IPR029760; GPX_CS.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR11592; PTHR11592; 1.
Pfam; PF00255; GSHPx; 1.
PIRSF; PIRSF000303; Glutathion_perox; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Complete proteome; Cytoplasm;
Developmental protein; Dwarfism; Mitochondrion; Oxidoreductase;
Peroxidase; Polymorphism; Reference proteome; Selenocysteine;
Transit peptide.
TRANSIT 1 ? Mitochondrion. {ECO:0000255}.
CHAIN ? 197 Phospholipid hydroperoxide glutathione
peroxidase, mitochondrial.
/FTId=PRO_0000013067.
ACT_SITE 73 73
NON_STD 73 73 Selenocysteine.
VAR_SEQ 1 27 Missing (in isoform Cytoplasmic).
{ECO:0000305}.
/FTId=VSP_018740.
VARIANT 2 2 S -> N (in dbSNP:rs8178967).
{ECO:0000269|PubMed:12606444,
ECO:0000269|Ref.3}.
/FTId=VAR_017063.
VARIANT 120 120 A -> T (in a patient affected by
cryptorchidism; dbSNP:rs76201145).
{ECO:0000269|PubMed:12606444}.
/FTId=VAR_017064.
MUTAGEN 73 73 U->A: Loss of enzyme activity.
{ECO:0000269|PubMed:17630701}.
MUTAGEN 73 73 U->C: Almost complete loss of enzyme
activity. {ECO:0000269|PubMed:17630701}.
HELIX 35 37 {ECO:0000244|PDB:5H5Q}.
HELIX 41 43 {ECO:0000244|PDB:5H5Q}.
STRAND 45 48 {ECO:0000244|PDB:5H5Q}.
STRAND 53 55 {ECO:0000244|PDB:5H5Q}.
HELIX 56 59 {ECO:0000244|PDB:5H5Q}.
STRAND 64 69 {ECO:0000244|PDB:5H5Q}.
STRAND 71 73 {ECO:0000244|PDB:5H5Q}.
HELIX 76 90 {ECO:0000244|PDB:5H5Q}.
HELIX 91 93 {ECO:0000244|PDB:5H5Q}.
STRAND 96 101 {ECO:0000244|PDB:5H5Q}.
TURN 104 107 {ECO:0000244|PDB:5H5Q}.
HELIX 113 122 {ECO:0000244|PDB:5H5Q}.
STRAND 127 130 {ECO:0000244|PDB:5H5Q}.
STRAND 134 137 {ECO:0000244|PDB:2GS3}.
HELIX 142 148 {ECO:0000244|PDB:5H5Q}.
TURN 151 153 {ECO:0000244|PDB:5H5Q}.
STRAND 156 160 {ECO:0000244|PDB:5H5R}.
STRAND 167 170 {ECO:0000244|PDB:5H5Q}.
STRAND 176 180 {ECO:0000244|PDB:5H5Q}.
HELIX 186 191 {ECO:0000244|PDB:5H5Q}.
HELIX 193 196 {ECO:0000244|PDB:5H5Q}.
SEQUENCE 197 AA; 22175 MW; 1AE3BC7AE42FDDB1 CRC64;
MSLGRLCRLL KPALLCGALA APGLAGTMCA SRDDWRCARS MHEFSAKDID GHMVNLDKYR
GFVCIVTNVA SQUGKTEVNY TQLVDLHARY AECGLRILAF PCNQFGKQEP GSNEEIKEFA
AGYNVKFDMF SKICVNGDDA HPLWKWMKIQ PKGKGILGNA IKWNFTKFLI DKNGCVVKRY
GPMEEPLVIE KDLPHYF


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