Reviewed, UniProtKB/Swiss-Prot Q96SL4 (GPX7_HUMAN)

Names and origin

Protein names

Recommended name:
    Glutathione peroxidase 7
    EC=1.11.1.9
Alternative name(s):
    CL683

Gene names

Name:	GPX7
Synonyms:	GPX6
ORF Names:	UNQ469/PRO828

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	2 glutathione + H2O2 = glutathione disulfide + 2 H2O.
Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the glutathione peroxidase family.
Sequence caution	The sequence AAC72961.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione peroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Chain

20 – 187

168

Glutathione peroxidase 7

PRO_0000013084

Sites

Active site

57

1

By similarity

Experimental info

Sequence conflict

75 – 77

3

GPH → HED Ref.7

Secondary structure

1

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187

Helix Strand Turn

Details...

Helix

25 – 27

3

Beta strand

29 – 32

4

Beta strand

37 – 39

3

Helix

40 – 43

4

Beta strand

46 – 53

8

Beta strand

55 – 57

3

Helix

60 – 74

15

Helix

75 – 77

3

Beta strand

79 – 85

7

Helix

97 – 108

12

Helix

127 – 136

10

Beta strand

146 – 149

4

Beta strand

155 – 159

5

Helix

165 – 173

9

Sequences

	Sequence		Length	Mass (Da)
	Q96SL4-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 0ACB80AC2522EFCD	FASTA	187	20,996
	10 20 30 40 50 60 MVAATVAAAW LLLWAAACAQ QEQDFYDFKA VNIRGKLVSL EKYRGSVSLV VNVASECGFT 70 80 90 100 110 120 DQHYRALQQL QRDLGPHHFN VLAFPCNQFG QQEPDSNKEI ESFARRTYSV SFPMFSKIAV 130 140 150 160 170 180 TGTGAHPAFK YLAQTSGKEP TWNFWKYLVA PDGKVVGAWD PTVSVEEVRP QITALVRKLI LLKREDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] 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: 14702039] [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: 16710414] [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: 15489334] [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]	"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.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00045798.

RefSeq

NP_056511.2.

UniGene

Hs.43728

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2P31	X-ray	2.00	A/B	20-177	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96SL4. 2 interactions.

Protein family/group databases

PeroxiBase

3606. HsGPx07.

Proteomic databases

PRIDE

Q96SL4.

Genome annotation databases

Ensembl

ENSG00000116157. Homo sapiens. [Contig view]

GeneID

2882.

KEGG

hsa:2882.

NMPDR

fig|9606.3.peg.1172.

Organism-specific databases

GeneCards

GC01P052840.

H-InvDB

HIX0004864.

HGNC

HGNC:4559. GPX7.

PharmGKB

PA28955.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q96SL4.

HOVERGEN

Q96SL4.

OMA

Q96SL4. ETSGKEP.

Enzyme and pathway databases

BRENDA

1.11.1.9. 247.

Gene expression databases

ArrayExpress

Q96SL4.

Bgee

Q96SL4.

CleanEx

HS_GPX6.
HS_GPX7.

GermOnline

ENSG00000116157. Homo sapiens.

Family and domain databases

InterPro

IPR013376. Glut_perox_Gpx7.
IPR000889. Glutathione_peroxidase.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR11592. Glut_peroxidase. 1 hit.

Pfam

PF00255. GSHPx. 1 hit.
[Graphical view]

PIRSF

PIRSF000303. Glutathion_perox. 1 hit.

PRINTS

PR01011. GLUTPROXDASE.

TIGRFAMs

TIGR02540. gpx7. 1 hit.

PROSITE

PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

11381.

Entry information

Entry name

GPX7_HUMAN

Accession

Primary (citable) accession number: Q96SL4
Secondary accession number(s): O95337, Q5T501

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 4, 2003
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)