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Protein

Glutathione peroxidase 7

Gene

GPX7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

It protects esophageal epithelia from hydrogen peroxide-induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks.1 Publication

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei57 – 571By similarity

GO - Molecular functioni

  • catalase activity Source: CACAO
  • glutathione peroxidase activity Source: UniProtKB-EC
  • peroxidase activity Source: Reactome

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.9. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei3606. HsGPx07.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 7 (EC:1.11.1.9)
Short name:
GPx-7
Short name:
GSHPx-7
Alternative name(s):
CL683
Gene namesi
Name:GPX7
Synonyms:GPX6
ORF Names:UNQ469/PRO828
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4559. GPX7.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Barrett esophagus (BE)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. The pathologic mechanisms leading to Barrett esophagus involve GPX7 dysfunction that results in higher levels of hydrogen peroxide and ROS-induced oxidative stress and DNA damage in esophageal cells.
Disease descriptionA condition characterized by a metaplastic change in which normal esophageal squamous epithelium is replaced by a columnar and intestinal-type epithelium. Patients with Barrett esophagus have an increased risk of esophageal adenocarcinoma. The main cause of Barrett esophagus is gastroesophageal reflux. The retrograde movement of acid and bile salts from the stomach into the esophagus causes prolonged injury to the esophageal epithelium and induces chronic esophagitis, which in turn is believed to trigger the pathologic changes.
See also OMIM:614266

Organism-specific databases

MIMi614266. phenotype.
PharmGKBiPA28955.

Chemistry

DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGPX7.
DMDMi33516901.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 187168Glutathione peroxidase 7PRO_0000013084Add
BLAST

Proteomic databases

EPDiQ96SL4.
MaxQBiQ96SL4.
PaxDbiQ96SL4.
PeptideAtlasiQ96SL4.
PRIDEiQ96SL4.

PTM databases

iPTMnetiQ96SL4.

Expressioni

Tissue specificityi

Expressed in esophageal epithelial cells; expression is up-regulated after exposure to acidic bile acids.1 Publication

Gene expression databases

BgeeiQ96SL4.
CleanExiHS_GPX6.
HS_GPX7.
GenevisibleiQ96SL4. HS.

Organism-specific databases

HPAiHPA025829.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ASNA1O436813EBI-749411,EBI-2515857
CEP70Q8NHQ13EBI-749411,EBI-739624

Protein-protein interaction databases

BioGridi109139. 36 interactions.
IntActiQ96SL4. 4 interactions.
MINTiMINT-1466561.
STRINGi9606.ENSP00000354677.

Structurei

Secondary structure

1
187
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 273Combined sources
Beta strandi29 – 324Combined sources
Beta strandi37 – 393Combined sources
Helixi40 – 434Combined sources
Beta strandi46 – 538Combined sources
Beta strandi55 – 573Combined sources
Helixi60 – 7415Combined sources
Helixi75 – 773Combined sources
Beta strandi79 – 857Combined sources
Helixi97 – 10812Combined sources
Helixi127 – 13610Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi155 – 1595Combined sources
Helixi165 – 1739Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P31X-ray2.00A/B20-177[»]
ProteinModelPortaliQ96SL4.
SMRiQ96SL4. Positions 23-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96SL4.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277054.
HOVERGENiHBG004333.
InParanoidiQ96SL4.
KOiK00432.
OMAiCAQREQD.
OrthoDBiEOG757CZF.
PhylomeDBiQ96SL4.
TreeFamiTF331942.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR013376. Glut_perox_Gpx7.
IPR000889. 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.
TIGRFAMsiTIGR02540. gpx7. 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.

Q96SL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAATVAAAW LLLWAAACAQ QEQDFYDFKA VNIRGKLVSL EKYRGSVSLV
60 70 80 90 100
VNVASECGFT DQHYRALQQL QRDLGPHHFN VLAFPCNQFG QQEPDSNKEI
110 120 130 140 150
ESFARRTYSV SFPMFSKIAV TGTGAHPAFK YLAQTSGKEP TWNFWKYLVA
160 170 180
PDGKVVGAWD PTVSVEEVRP QITALVRKLI LLKREDL
Length:187
Mass (Da):20,996
Last modified:December 1, 2001 - v1
Checksum:i0ACB80AC2522EFCD
GO

Sequence cautioni

The sequence AAC72961.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 773GPH → HED (Ref. 7) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320068 mRNA. Translation: AAN76501.1.
AY358402 mRNA. Translation: AAQ88768.1.
AK027683 mRNA. Translation: BAB55294.1.
DQ096732 Genomic DNA. Translation: AAY88741.1.
AL356976 Genomic DNA. Translation: CAI22476.1.
BC032788 mRNA. Translation: AAH32788.1.
AF091092 mRNA. Translation: AAC72961.1. Sequence problems.
CCDSiCCDS569.1.
RefSeqiNP_056511.2. NM_015696.4.
UniGeneiHs.43728.

Genome annotation databases

EnsembliENST00000361314; ENSP00000354677; ENSG00000116157.
GeneIDi2882.
KEGGihsa:2882.
UCSCiuc001cue.4. human.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320068 mRNA. Translation: AAN76501.1.
AY358402 mRNA. Translation: AAQ88768.1.
AK027683 mRNA. Translation: BAB55294.1.
DQ096732 Genomic DNA. Translation: AAY88741.1.
AL356976 Genomic DNA. Translation: CAI22476.1.
BC032788 mRNA. Translation: AAH32788.1.
AF091092 mRNA. Translation: AAC72961.1. Sequence problems.
CCDSiCCDS569.1.
RefSeqiNP_056511.2. NM_015696.4.
UniGeneiHs.43728.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P31X-ray2.00A/B20-177[»]
ProteinModelPortaliQ96SL4.
SMRiQ96SL4. Positions 23-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109139. 36 interactions.
IntActiQ96SL4. 4 interactions.
MINTiMINT-1466561.
STRINGi9606.ENSP00000354677.

Chemistry

DrugBankiDB00143. Glutathione.

Protein family/group databases

PeroxiBasei3606. HsGPx07.

PTM databases

iPTMnetiQ96SL4.

Polymorphism and mutation databases

BioMutaiGPX7.
DMDMi33516901.

Proteomic databases

EPDiQ96SL4.
MaxQBiQ96SL4.
PaxDbiQ96SL4.
PeptideAtlasiQ96SL4.
PRIDEiQ96SL4.

Protocols and materials databases

DNASUi2882.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361314; ENSP00000354677; ENSG00000116157.
GeneIDi2882.
KEGGihsa:2882.
UCSCiuc001cue.4. human.

Organism-specific databases

CTDi2882.
GeneCardsiGPX7.
HGNCiHGNC:4559. GPX7.
HPAiHPA025829.
MIMi614266. phenotype.
615784. gene.
neXtProtiNX_Q96SL4.
PharmGKBiPA28955.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277054.
HOVERGENiHBG004333.
InParanoidiQ96SL4.
KOiK00432.
OMAiCAQREQD.
OrthoDBiEOG757CZF.
PhylomeDBiQ96SL4.
TreeFamiTF331942.

Enzyme and pathway databases

BRENDAi1.11.1.9. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiGPX7. human.
EvolutionaryTraceiQ96SL4.
GeneWikiiGPX7.
GenomeRNAii2882.
PROiQ96SL4.
SOURCEiSearch...

Gene expression databases

BgeeiQ96SL4.
CleanExiHS_GPX6.
HS_GPX7.
GenevisibleiQ96SL4. HS.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR013376. Glut_perox_Gpx7.
IPR000889. 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.
TIGRFAMsiTIGR02540. gpx7. 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. "Cloning and characterizing a novel human glutathione peroxidase-GPX6."
    Gu S., Lin S., Ying K., Xie Y., Mao Y.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. NIEHS SNPs program
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Blood.
  7. "Full-insert sequence of mapped XREF EST."
    Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-187.
  8. "Glutathione peroxidase 7 protects against oxidative DNA damage in oesophageal cells."
    Peng D., Belkhiri A., Hu T., Chaturvedi R., Asim M., Wilson K.T., Zaika A., El-Rifai W.
    Gut 61:1250-1260(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN BE.
  9. "Crystal structure of human glutathione peroxidase 7."
    Structural genomics consortium (SGC)
    Submitted (MAR-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-177.

Entry informationi

Entry nameiGPX7_HUMAN
AccessioniPrimary (citable) accession number: Q96SL4
Secondary accession number(s): O95337, Q5T501
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.