P59796 (GPX6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione peroxidase 6
Short name=GPx-6
Short name=GSHPx-6
EC=1.11.1.9

Gene names

Name:

GPX6

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

General annotation (Comments)

Catalytic activity	2 glutathione + H2O2 = glutathione disulfide + 2 H2O.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed in olfactory epithelium and embryos. Ref.1
Sequence similarities	Belongs to the glutathione peroxidase family.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism Selenocysteine
Domain	Signal
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	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 – 221	202	Glutathione peroxidase 6		PRO_0000013081
Sites
	Active site	73	1	By similarity
Amino acid modifications
	Non-standard residue	73	1	Selenocysteine
Natural variations
	Natural variant	6	1	Q → L. Ref.2 Corresponds to variant rs35510314 [ dbSNP | Ensembl ].		VAR_025249
	Natural variant	13	1	F → L. Ref.2 Corresponds to variant rs406113 [ dbSNP | Ensembl ].		VAR_025250
	Natural variant	53	1	Y → H. Ref.2 Corresponds to variant rs34825130 [ dbSNP | Ensembl ].		VAR_025251
	Natural variant	58	1	Q → H. Ref.2 Corresponds to variant rs6922986 [ dbSNP | Ensembl ].		VAR_025252
	Natural variant	72	1	Y → N. Ref.2 Corresponds to variant rs35062161 [ dbSNP | Ensembl ].		VAR_025253
	Natural variant	136	1	E → D. Ref.2 Corresponds to variant rs35394555 [ dbSNP | Ensembl ].		VAR_025254
	Natural variant	140	1	V → M. Ref.2 Corresponds to variant rs36055795 [ dbSNP | Ensembl ].		VAR_025255
	Natural variant	157	1	P → S. Ref.2 Corresponds to variant rs35658392 [ dbSNP | Ensembl ].		VAR_025256
	Natural variant	161	1	D → G. Ref.2 Corresponds to variant rs34955392 [ dbSNP | Ensembl ].		VAR_025257
	Natural variant	188	1	V → A. Ref.2 Corresponds to variant rs35701070 [ dbSNP | Ensembl ].		VAR_025258

Sequences

	Sequence		Length	Mass (Da)
	P59796 [UniParc]. Last modified February 26, 2008. Version 2. Checksum: E9B48AF5F17C3FDD	FASTA	221	24,971
	10 20 30 40 50 60 MFQQFQASCL VLFFLVGFAQ QTLKPQNRKV DCNKGVTGTI YEYGALTLNG EEYIQFKQFA 70 80 90 100 110 120 GKHVLFVNVA AYUGLAAQYP ELNALQEELK NFGVIVLAFP CNQFGKQEPG TNSEILLGLK 130 140 150 160 170 180 YVCPGSGFVP SFQLFEKGDV NGEKEQKVFT FLKNSCPPTS DLLGSSSQLF WEPMKVHDIR 190 200 210 220 WNFEKFLVGP DGVPVMHWFH QAPVSTVKSD ILEYLKQFNT H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of mammalian selenoproteomes." Kryukov G.V., Castellano S., Novoselov S.V., Lobanov A.V., Zehtab O., Guigo R., Gladyshev V.N. Science 300:1439-1443(2003) [PubMed: 12775843] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	NIEHS SNPs program Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-6; LEU-13; HIS-53; HIS-58; ASN-72; ASP-136; MET-140; SER-157; GLY-161 AND ALA-188.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY324826 mRNA. Translation: AAP85543.1. DQ088982 Genomic DNA. Translation: AAY68223.1. AL049543 Genomic DNA. No translation available. Z98745 Genomic DNA. No translation available.
IPI	IPI00335668.
RefSeq	NP_874360.1. NM_182701.1.
UniGene	Hs.448570.
3D structure databases
ProteinModelPortal	P59796.
SMR	P59796. Positions 38-217.
ModBase	Search...
Protein-protein interaction databases
STRING	P59796.
Protein family/group databases
PeroxiBase	3605. HsGPx06.
Polymorphism databases
DMDM	187692196.
Proteomic databases
PRIDE	P59796.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361902; ENSP00000354581; ENSG00000198704.
GeneID	257202.
KEGG	hsa:257202.
Organism-specific databases
CTD	257202.
GeneCards	GC06M028471.
H-InvDB	HIX0032860. HIX0176419.
HGNC	HGNC:4558. GPX6.
MIM	607913. gene.
neXtProt	NX_P59796.
PharmGKB	PA28954.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00550000074312.
HOGENOM	HBG648990.
HOVERGEN	HBG004333.
InParanoid	P59796.
OMA	VIVLAFP.
OrthoDB	EOG4CRM10.
PhylomeDB	P59796.
Gene expression databases
CleanEx	HS_GPX6.
Genevestigator	P59796.
Family and domain databases
InterPro	IPR000889. Glutathione_peroxidase. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K00432.
PANTHER	PTHR11592. Glut_peroxidase. 1 hit.
Pfam	PF00255. GSHPx. 1 hit. [Graphical view]
PIRSF	PIRSF000303. Glutathion_perox. 1 hit.
PRINTS	PR01011. GLUTPROXDASE.
SUPFAM	SSF52833. Thiordxn-like_fd. 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
DrugBank	DB00143. Glutathione.
NextBio	92965.
SOURCE	Search...

Entry information

Entry name

GPX6_HUMAN

Accession

Primary (citable) accession number: P59796
Secondary accession number(s): Q4PJ17

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 4, 2003
Last sequence update:	February 26, 2008
Last modified:	January 25, 2012
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.