GPX7_HUMAN
ID GPX7_HUMAN Reviewed; 187 AA.
AC Q96SL4; O95337; Q5T501;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Glutathione peroxidase 7;
DE Short=GPx-7;
DE Short=GSHPx-7;
DE EC=1.11.1.9;
DE AltName: Full=CL683;
DE Flags: Precursor;
GN Name=GPX7; Synonyms=GPX6; ORFNames=UNQ469/PRO828;
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].
RC TISSUE=Fetal brain;
RA Gu S., Lin S., Ying K., Xie Y., Mao Y.;
RT "Cloning and characterizing a novel human glutathione peroxidase-GPX6.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-187.
RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
RT "Full-insert sequence of mapped XREF EST.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN BE.
RX PubMed=22157330; DOI=10.1136/gutjnl-2011-301078;
RA Peng D., Belkhiri A., Hu T., Chaturvedi R., Asim M., Wilson K.T., Zaika A.,
RA El-Rifai W.;
RT "Glutathione peroxidase 7 protects against oxidative DNA damage in
RT oesophageal cells.";
RL Gut 61:1250-1260(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-177.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human glutathione peroxidase 7.";
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: It protects esophageal epithelia from hydrogen peroxide-
CC induced oxidative stress. It suppresses acidic bile acid-induced
CC reactive oxigen species (ROS) and protects against oxidative DNA damage
CC and double-strand breaks. {ECO:0000269|PubMed:22157330}.
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 -!- INTERACTION:
CC Q96SL4; Q12797-6: ASPH; NbExp=3; IntAct=EBI-749411, EBI-12092171;
CC Q96SL4; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-749411, EBI-739624;
CC Q96SL4; Q9UBL6-2: CPNE7; NbExp=5; IntAct=EBI-749411, EBI-12012272;
CC Q96SL4; G5E9A7: DMWD; NbExp=3; IntAct=EBI-749411, EBI-10976677;
CC Q96SL4; O43681: GET3; NbExp=6; IntAct=EBI-749411, EBI-2515857;
CC Q96SL4; P42858: HTT; NbExp=3; IntAct=EBI-749411, EBI-466029;
CC Q96SL4; P61601: NCALD; NbExp=3; IntAct=EBI-749411, EBI-749635;
CC Q96SL4; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-749411, EBI-741158;
CC Q96SL4; O43765: SGTA; NbExp=7; IntAct=EBI-749411, EBI-347996;
CC Q96SL4; Q96EQ0: SGTB; NbExp=5; IntAct=EBI-749411, EBI-744081;
CC Q96SL4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-749411, EBI-5235340;
CC Q96SL4; Q9BQ70: TCF25; NbExp=3; IntAct=EBI-749411, EBI-745182;
CC Q96SL4; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-749411, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in esophageal epithelial cells;
CC expression is up-regulated after exposure to acidic bile acids.
CC {ECO:0000269|PubMed:22157330}.
CC -!- DISEASE: Barrett esophagus (BE) [MIM:614266]: A condition characterized
CC by a metaplastic change in which normal esophageal squamous epithelium
CC is replaced by a columnar and intestinal-type epithelium. Patients with
CC Barrett esophagus have an increased risk of esophageal adenocarcinoma.
CC The main cause of Barrett esophagus is gastroesophageal reflux. The
CC retrograde movement of acid and bile salts from the stomach into the
CC esophagus causes prolonged injury to the esophageal epithelium and
CC induces chronic esophagitis, which in turn is believed to trigger the
CC pathologic changes. {ECO:0000269|PubMed:22157330}. Note=The disease is
CC caused by variants affecting the gene represented in this entry. The
CC pathologic mechanisms leading to Barrett esophagus involve GPX7
CC dysfunction that results in higher levels of hydrogen peroxide and ROS-
CC induced oxidative stress and DNA damage in esophageal cells.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72961.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gpx7/";
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DR EMBL; AF320068; AAN76501.1; -; mRNA.
DR EMBL; AY358402; AAQ88768.1; -; mRNA.
DR EMBL; AK027683; BAB55294.1; -; mRNA.
DR EMBL; DQ096732; AAY88741.1; -; Genomic_DNA.
DR EMBL; AL356976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032788; AAH32788.1; -; mRNA.
DR EMBL; AF091092; AAC72961.1; ALT_SEQ; mRNA.
DR CCDS; CCDS569.1; -.
DR RefSeq; NP_056511.2; NM_015696.4.
DR PDB; 2P31; X-ray; 2.00 A; A/B=20-177.
DR PDBsum; 2P31; -.
DR AlphaFoldDB; Q96SL4; -.
DR SMR; Q96SL4; -.
DR BioGRID; 109139; 67.
DR IntAct; Q96SL4; 40.
DR STRING; 9606.ENSP00000354677; -.
DR DrugBank; DB09096; Benzoyl peroxide.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR PeroxiBase; 3606; HsGPx07.
DR GlyGen; Q96SL4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96SL4; -.
DR PhosphoSitePlus; Q96SL4; -.
DR BioMuta; GPX7; -.
DR DMDM; 33516901; -.
DR EPD; Q96SL4; -.
DR jPOST; Q96SL4; -.
DR MassIVE; Q96SL4; -.
DR MaxQB; Q96SL4; -.
DR PaxDb; Q96SL4; -.
DR PeptideAtlas; Q96SL4; -.
DR PRIDE; Q96SL4; -.
DR ProteomicsDB; 78126; -.
DR Antibodypedia; 19147; 236 antibodies from 36 providers.
DR DNASU; 2882; -.
DR Ensembl; ENST00000361314.5; ENSP00000354677.4; ENSG00000116157.6.
DR GeneID; 2882; -.
DR KEGG; hsa:2882; -.
DR MANE-Select; ENST00000361314.5; ENSP00000354677.4; NM_015696.5; NP_056511.2.
DR UCSC; uc001cue.4; human.
DR CTD; 2882; -.
DR DisGeNET; 2882; -.
DR GeneCards; GPX7; -.
DR HGNC; HGNC:4559; GPX7.
DR HPA; ENSG00000116157; Low tissue specificity.
DR MIM; 614266; phenotype.
DR MIM; 615784; gene.
DR neXtProt; NX_Q96SL4; -.
DR OpenTargets; ENSG00000116157; -.
DR PharmGKB; PA28955; -.
DR VEuPathDB; HostDB:ENSG00000116157; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000159127; -.
DR HOGENOM; CLU_029507_0_1_1; -.
DR InParanoid; Q96SL4; -.
DR OMA; LAPFKGQ; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; Q96SL4; -.
DR TreeFam; TF331942; -.
DR BRENDA; 1.11.1.9; 2681.
DR PathwayCommons; Q96SL4; -.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR SignaLink; Q96SL4; -.
DR BioGRID-ORCS; 2882; 6 hits in 1063 CRISPR screens.
DR ChiTaRS; GPX7; human.
DR EvolutionaryTrace; Q96SL4; -.
DR GeneWiki; GPX7; -.
DR GenomeRNAi; 2882; -.
DR Pharos; Q96SL4; Tbio.
DR PRO; PR:Q96SL4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96SL4; protein.
DR Bgee; ENSG00000116157; Expressed in adrenal tissue and 123 other tissues.
DR Genevisible; Q96SL4; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004096; F:catalase activity; IDA:CACAO.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; EXP:Reactome.
DR GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR InterPro; IPR013376; Glut_perox_Gpx7.
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 TIGRFAMs; TIGR02540; gpx7; 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; Oxidoreductase; Peroxidase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..187
FT /note="Glutathione peroxidase 7"
FT /id="PRO_0000013084"
FT ACT_SITE 57
FT /evidence="ECO:0000250"
FT CONFLICT 75..77
FT /note="GPH -> HED (in Ref. 7)"
FT /evidence="ECO:0000305"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2P31"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2P31"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2P31"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2P31"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:2P31"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2P31"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:2P31"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2P31"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:2P31"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:2P31"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:2P31"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2P31"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:2P31"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:2P31"
SQ SEQUENCE 187 AA; 20996 MW; 0ACB80AC2522EFCD CRC64;
MVAATVAAAW LLLWAAACAQ QEQDFYDFKA VNIRGKLVSL EKYRGSVSLV VNVASECGFT
DQHYRALQQL QRDLGPHHFN VLAFPCNQFG QQEPDSNKEI ESFARRTYSV SFPMFSKIAV
TGTGAHPAFK YLAQTSGKEP TWNFWKYLVA PDGKVVGAWD PTVSVEEVRP QITALVRKLI
LLKREDL
