ID GPXC_DIRIM Reviewed; 221 AA. AC P52033; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 25-NOV-2008, entry version 45. DE RecName: Full=Glutathione peroxidase; DE EC=1.11.1.9; DE AltName: Full=Di29; DE Flags: Precursor; OS Dirofilaria immitis (Canine heartworm). OC Eukaryota; Metazoa; Nematoda; Chromadorea; Spirurida; Filarioidea; OC Onchocercidae; Dirofilaria. OX NCBI_TaxID=6287; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Venkatakrishnaiah L., James E.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=98162489; PubMed=9501847; DOI=10.1006/expr.1998.4217; RA Tripp C.A., Frank R.S., Selkirk M.E., Tang L., Mika-Grieve M., RA Frank G.R., Grieve R.B.; RT "Dirofilaria immitis: molecular cloning and expression of a cDNA RT encoding a selenium-independent secreted glutathione peroxidase."; RL Exp. Parasitol. 88:43-50(1998). CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space (By CC similarity). CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U04693; AAA16224.1; -; mRNA. DR EMBL; U87457; AAB58573.1; -; mRNA. DR EMBL; U87458; AAB58574.1; -; Genomic_DNA. DR HSSP; P00435; 1GP1. DR PeroxiBase; 3752; DiGPx01. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR InterPro; IPR000889; Glut_peroxidase. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR PANTHER; PTHR11592; Glut_peroxidase; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 2: Evidence at transcript level; KW Glycoprotein; Oxidoreductase; Peroxidase; Secreted; Signal. FT SIGNAL 1 19 Potential. FT CHAIN 20 221 Glutathione peroxidase. FT /FTId=PRO_0000013094. FT ACT_SITE 72 72 By similarity. FT CARBOHYD 28 28 N-linked (GlcNAc...) (Potential). FT CARBOHYD 87 87 N-linked (GlcNAc...) (Potential). FT CARBOHYD 90 90 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 221 AA; 25453 MW; 88FFF848D567CF28 CRC64; MFIQLLILSY AILLQLIATQ VADKQLPNLT KQCEPTSQTI YDFHVPTLDG SEKSLAEYRG KVLLLVNVAT YCAYTFQYND FNPMLENNSN GTLKILAFPC NQFLLQEPAE NHELLNGLKY VRPGNGWEPH GNMHIFGKVE VNGDDHHPLY KFLKEHCPQT VPIIGDRHQL MYNPIGTNDI IWNFEKFLID KKGHPRYRFH PSAWVQGSVI APFIDELERE I //