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Database: UniProt
Entry: Q8TED1
LinkDB: Q8TED1
Original site: Q8TED1 
ID   GPX8_HUMAN              Reviewed;         209 AA.
AC   Q8TED1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   26-NOV-2014, entry version 114.
DE   RecName: Full=Probable glutathione peroxidase 8;
DE            Short=GPx-8;
DE            Short=GSHPx-8;
DE            EC=1.11.1.9;
GN   Name=GPX8; ORFNames=UNQ847/PRO1785;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-182.
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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-182.
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA   Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA   Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA   Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA   Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA   Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA   Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA   Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA   Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-182.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-182.
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 44-209.
RG   Structural genomics consortium (SGC);
RT   "The structure of human GPX8.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AY358715; AAQ89077.1; -; mRNA.
DR   EMBL; AK074216; BAB85019.1; -; mRNA.
DR   EMBL; AC091977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471123; EAW54908.1; -; Genomic_DNA.
DR   EMBL; BC029424; AAH29424.1; -; mRNA.
DR   CCDS; CCDS34156.1; -.
DR   RefSeq; NP_001008398.2; NM_001008397.2.
DR   UniGene; Hs.289044; -.
DR   PDB; 3CYN; X-ray; 2.00 A; A/B/C=44-209.
DR   PDB; 3KIJ; X-ray; 1.80 A; A/B/C=38-209.
DR   PDBsum; 3CYN; -.
DR   PDBsum; 3KIJ; -.
DR   ProteinModelPortal; Q8TED1; -.
DR   SMR; Q8TED1; 39-209.
DR   BioGrid; 138926; 3.
DR   STRING; 9606.ENSP00000296734; -.
DR   DrugBank; DB00143; Glutathione.
DR   PhosphoSite; Q8TED1; -.
DR   DMDM; 269849565; -.
DR   MaxQB; Q8TED1; -.
DR   PaxDb; Q8TED1; -.
DR   PRIDE; Q8TED1; -.
DR   DNASU; 493869; -.
DR   Ensembl; ENST00000503787; ENSP00000423822; ENSG00000164294.
DR   GeneID; 493869; -.
DR   KEGG; hsa:493869; -.
DR   UCSC; uc003jpq.2; human.
DR   CTD; 493869; -.
DR   GeneCards; GC05P054455; -.
DR   HGNC; HGNC:33100; GPX8.
DR   HPA; HPA036721; -.
DR   neXtProt; NX_Q8TED1; -.
DR   PharmGKB; PA164720300; -.
DR   eggNOG; COG0386; -.
DR   GeneTree; ENSGT00760000119230; -.
DR   HOGENOM; HOG000277054; -.
DR   HOVERGEN; HBG004333; -.
DR   InParanoid; Q8TED1; -.
DR   KO; K00432; -.
DR   OMA; FGDSEPR; -.
DR   OrthoDB; EOG757CZF; -.
DR   PhylomeDB; Q8TED1; -.
DR   TreeFam; TF331942; -.
DR   Reactome; REACT_172715; Detoxification of Reactive Oxygen Species.
DR   EvolutionaryTrace; Q8TED1; -.
DR   GeneWiki; GPX8; -.
DR   GenomeRNAi; 493869; -.
DR   NextBio; 111787; -.
DR   PRO; PR:Q8TED1; -.
DR   Bgee; Q8TED1; -.
DR   CleanEx; HS_GPX8; -.
DR   ExpressionAtlas; Q8TED1; baseline and differential.
DR   Genevestigator; Q8TED1; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004601; F:peroxidase activity; EXP:Reactome.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR013376; Glut_perox_Gpx7.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
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; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Membrane;
KW   Oxidoreductase; Peroxidase; Polymorphism; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    209       Probable glutathione peroxidase 8.
FT                                /FTId=PRO_0000317756.
FT   TRANSMEM     18     40       Helical. {ECO:0000255}.
FT   ACT_SITE     79     79       {ECO:0000250}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000269|PubMed:22814378}.
FT   VARIANT     182    182       K -> R (in dbSNP:rs381852).
FT                                {ECO:0000269|PubMed:12975309,
FT                                ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_060456.
FT   HELIX        47     49       {ECO:0000244|PDB:3KIJ}.
FT   STRAND       51     54       {ECO:0000244|PDB:3KIJ}.
FT   STRAND       59     61       {ECO:0000244|PDB:3KIJ}.
FT   HELIX        62     65       {ECO:0000244|PDB:3KIJ}.
FT   STRAND       68     75       {ECO:0000244|PDB:3KIJ}.
FT   STRAND       77     79       {ECO:0000244|PDB:3KIJ}.
FT   HELIX        82     96       {ECO:0000244|PDB:3KIJ}.
FT   TURN         97     99       {ECO:0000244|PDB:3KIJ}.
FT   STRAND      100    107       {ECO:0000244|PDB:3KIJ}.
FT   HELIX       119    130       {ECO:0000244|PDB:3KIJ}.
FT   HELIX       149    158       {ECO:0000244|PDB:3KIJ}.
FT   STRAND      168    171       {ECO:0000244|PDB:3KIJ}.
FT   STRAND      177    181       {ECO:0000244|PDB:3KIJ}.
FT   HELIX       187    189       {ECO:0000244|PDB:3KIJ}.
FT   HELIX       191    207       {ECO:0000244|PDB:3KIJ}.
SQ   SEQUENCE   209 AA;  23881 MW;  82DACC1A85FDF6D7 CRC64;
     MEPLAAYPLK CSGPRAKVFA VLLSIVLCTV TLFLLQLKFL KPKINSFYAF EVKDAKGRTV
     SLEKYKGKVS LVVNVASDCQ LTDRNYLGLK ELHKEFGPSH FSVLAFPCNQ FGESEPRPSK
     EVESFARKNY GVTFPIFHKI KILGSEGEPA FRFLVDSSKK EPRWNFWKYL VNPEGQVVKF
     WKPEEPIEVI RPDIAALVRQ VIIKKKEDL
//
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