GPX6_HUMAN
ID GPX6_HUMAN Reviewed; 221 AA.
AC P59796; Q4PJ17;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glutathione peroxidase 6;
DE Short=GPx-6;
DE Short=GSHPx-6;
DE EC=1.11.1.9;
DE Flags: Precursor;
GN Name=GPX6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12775843; DOI=10.1126/science.1083516;
RA Kryukov G.V., Castellano S., Novoselov S.V., Lobanov A.V., Zehtab O.,
RA Guigo R., Gladyshev V.N.;
RT "Characterization of mammalian selenoproteomes.";
RL Science 300:1439-1443(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-6; LEU-13; HIS-53;
RP HIS-58; ASN-72; ASP-136; MET-140; SER-157; GLY-161 AND ALA-188.
RG NIEHS SNPs program;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in olfactory epithelium and embryos.
CC {ECO:0000269|PubMed:12775843}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gpx6/";
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DR EMBL; AY324826; AAP85543.1; -; mRNA.
DR EMBL; DQ088982; AAY68223.1; -; Genomic_DNA.
DR EMBL; AL049543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS43432.1; -.
DR RefSeq; NP_874360.1; NM_182701.1.
DR STRING; 9606.ENSP00000354581; -.
DR DrugBank; DB09096; Benzoyl peroxide.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR PeroxiBase; 3605; HsGPx06.
DR PhosphoSitePlus; P59796; -.
DR BioMuta; GPX6; -.
DR DMDM; 187692196; -.
DR jPOST; P59796; -.
DR MassIVE; P59796; -.
DR PaxDb; P59796; -.
DR PeptideAtlas; P59796; -.
DR PRIDE; P59796; -.
DR Antibodypedia; 6190; 40 antibodies from 15 providers.
DR DNASU; 257202; -.
DR Ensembl; ENST00000361902.5; ENSP00000354581.1; ENSG00000198704.10.
DR GeneID; 257202; -.
DR KEGG; hsa:257202; -.
DR MANE-Select; ENST00000361902.5; ENSP00000354581.1; NM_182701.1; NP_874360.1.
DR UCSC; uc021yrx.1; human.
DR CTD; 257202; -.
DR DisGeNET; 257202; -.
DR GeneCards; GPX6; -.
DR HGNC; HGNC:4558; GPX6.
DR HPA; ENSG00000198704; Tissue enriched (epididymis).
DR MIM; 607913; gene.
DR neXtProt; NX_P59796; -.
DR OpenTargets; ENSG00000198704; -.
DR PharmGKB; PA28954; -.
DR VEuPathDB; HostDB:ENSG00000198704; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000161098; -.
DR HOGENOM; CLU_029507_2_1_1; -.
DR InParanoid; P59796; -.
DR OMA; VMRWHPR; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; P59796; -.
DR TreeFam; TF105318; -.
DR BRENDA; 1.11.1.9; 2681.
DR PathwayCommons; P59796; -.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR BioGRID-ORCS; 257202; 10 hits in 1067 CRISPR screens.
DR GeneWiki; GPX6; -.
DR GenomeRNAi; 257202; -.
DR Pharos; P59796; Tdark.
DR PRO; PR:P59796; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P59796; protein.
DR Bgee; ENSG00000198704; Expressed in olfactory segment of nasal mucosa and 7 other tissues.
DR ExpressionAtlas; P59796; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 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; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 2: Evidence at transcript level;
KW Oxidoreductase; Peroxidase; Reference proteome; Secreted; Selenocysteine;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..221
FT /note="Glutathione peroxidase 6"
FT /id="PRO_0000013081"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT NON_STD 73
FT /note="Selenocysteine"
FT VARIANT 6
FT /note="Q -> L (in dbSNP:rs35510314)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025249"
FT VARIANT 13
FT /note="F -> L (in dbSNP:rs406113)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025250"
FT VARIANT 53
FT /note="Y -> H (in dbSNP:rs34825130)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025251"
FT VARIANT 58
FT /note="Q -> H (in dbSNP:rs6922986)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025252"
FT VARIANT 72
FT /note="Y -> N (in dbSNP:rs35062161)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025253"
FT VARIANT 136
FT /note="E -> D (in dbSNP:rs35394555)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025254"
FT VARIANT 140
FT /note="V -> M (in dbSNP:rs36055795)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025255"
FT VARIANT 157
FT /note="P -> S (in dbSNP:rs35658392)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025256"
FT VARIANT 161
FT /note="D -> G (in dbSNP:rs34955392)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025257"
FT VARIANT 188
FT /note="V -> A (in dbSNP:rs35701070)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025258"
SQ SEQUENCE 221 AA; 24971 MW; E9B48AF5F17C3FDD CRC64;
MFQQFQASCL VLFFLVGFAQ QTLKPQNRKV DCNKGVTGTI YEYGALTLNG EEYIQFKQFA
GKHVLFVNVA AYUGLAAQYP ELNALQEELK NFGVIVLAFP CNQFGKQEPG TNSEILLGLK
YVCPGSGFVP SFQLFEKGDV NGEKEQKVFT FLKNSCPPTS DLLGSSSQLF WEPMKVHDIR
WNFEKFLVGP DGVPVMHWFH QAPVSTVKSD ILEYLKQFNT H
