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UniProtKB/Swiss-Prot entry P67877


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPXC_BRUMA
Primary accession number P67877
Secondary accession number P35665
Integrated into Swiss-Prot on October 11, 2004
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 28)
Name and origin of the protein
Protein name Cuticular glutathione peroxidase [Precursor]
Synonyms EC 1.11.1.9
Cuticular glycoprotein gp29
Major surface antigen gp29
gp30
Gene name None
From
Brugia malayi (Filarial nematode worm) [TaxID: 6279] 
Taxonomy Eukaryota; Metazoa; Nematoda; Chromadorea; Spirurida; Filarioidea; Onchocercidae; Brugia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0166-6851(93)90099-J; PubMed=8459826 [NCBI, ExPASy, EBI, Israel, Japan]
Cookson E., Tang L., Selkirk M.E.;
"Conservation of primary sequence of gp29, the major soluble cuticular glycoprotein, in three species of lymphatic filariae.";
Mol. Biochem. Parasitol. 58:155-160(1993).
[2]
3D-STRUCTURE MODELING, AND GLYCOSYLATION AT ASN-39 AND ASN-92.
DOI=10.1016/0166-6851(93)90098-I; PubMed=7681545 [NCBI, ExPASy, EBI, Israel, Japan]
Zvelebil M.J.J.M., Tang L., Cookson E., Selkirk M.E., Thornton J.M.;
"Molecular modelling and epitope prediction of gp29 from lymphatic filariae.";
Mol. Biochem. Parasitol. 58:145-153(1993).
Comments
  • FUNCTION: Could inhibit the oxidative burst of leukocytes and neutralize the secondary products of lipid peroxidation, thus providing the resistance of these parasites to immune effector mechanisms and their persistence in the mammalian host. It may also be involved in the formation of cross-linking residues such as dityrosine, trityrosine and isotrityrosine identified in cuticular collagen. Highly cross-linked external cortex may also serve to protect the parasite from immune attack.
  • CATALYTIC ACTIVITY: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O.
  • SUBUNIT: Homotetramer.
  • SUBCELLULAR LOCATION: Secreted. Note=Secreted into the cuticle and ultimately released into the medium.
  • DEVELOPMENTAL STAGE: Up-regulated in the third stage larvae following infection of host. Concomitant synthesis occurs at a high level through the adult stage. Not detected in microfilariae.
  • SIMILARITY: Belongs to the glutathione peroxidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X69127; CAA48881.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S60593; S60593.
RefSeq XP_001899550.1; -.
3D structure databases
HSSP P00435; 1GP1. [HSSP ENTRY / PDB]
ModBase P67877.
Protein family/group databases
PeroxiBase 3749; BmalGPx01.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004602; Molecular function: glutathione peroxidase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979; Biological process: response to oxidative stress (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000889; Glut_peroxidase.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
PANTHER PTHR11592; Glut_peroxidase; 1.
Pfam PF00255; GSHPx; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000303; Glutathion_perox; 1.
PRINTS PR01011; GLUTPROXDASE.
PROSITE PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P67877.
Genome annotation databases
GeneID 6102977; -.
KEGG bmy:Bm1_40465; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycoprotein; Oxidoreductase; Peroxidase; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
SIGNAL   1    19  19     Potential. 
CHAIN   20   223  204     Cuticular glutathione peroxidase. PRO_0000013091
ACT_SITE   74    74        By similarity. 
CARBOHYD   39    39        N-linked (GlcNAc...). 
CARBOHYD   92    92        N-linked (GlcNAc...). 
Sequence information
Length: 223 AA [This is the length of the unprocessed precursor] Molecular weight: 25883 Da [This is the MW of the unprocessed precursor] CRC64: C46397B8F8C6BF0F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAQLLILSH MVLLQLIVAQ LGPKIGKQFL KPKQCEITNQ TVYDFQVQML NGAQKSLAEY 

        70         80         90        100        110        120 
RNKVLLIVNV ATYCAYTMQY RDFNPILESN SNGTLNILGF PCNQFYLQEP AENHELLSGL 

       130        140        150        160        170        180 
KYVRPGHGWE PHKNMHIFGK LEVNGENDHP LYKFLKERCP PTVPVIGKRH QLIYDPIGTN 

       190        200        210        220 
DVIWNFEKFL VDKKGRPRYR FHPENWVQGT AVKPYIDELE REI 

P67877 in FASTA format

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