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Reviewed, UniProtKB/Swiss-Prot P67877 (GPXC_BRUMA)

Last modified November 25, 2008. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cuticular glutathione peroxidase
    EC=1.11.1.9
Alternative name(s):
    Cuticular glycoprotein gp29
    Major surface antigen gp29
    gp30
OrganismBrugia malayi (Filarial nematode worm)
Taxonomic identifier6279 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeBrugia

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (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 + H(2)O(2) = glutathione disulfide + 2 H(2)O.

Subunit structure

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.

Sequence similarities

Belongs to the glutathione peroxidase family.

Ontologies

Keywords

   Cellular componentSecreted
   DomainSignal
   Molecular functionOxidoreductase
Peroxidase
   PTMGlycoprotein

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to oxidative stress

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglutathione peroxidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 223204Cuticular glutathione peroxidase
PRO_0000013091

Sites

Active site741 By similarity

Amino acid modifications

Glycosylation391N-linked (GlcNAc...)
Glycosylation921N-linked (GlcNAc...)

Sequences

Sequence LengthMass (Da)Tools
P67877-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C46397B8F8C6BF0F

FASTA22325,883
        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 

« Hide

References

[1]"Conservation of primary sequence of gp29, the major soluble cuticular glycoprotein, in three species of lymphatic filariae."
Cookson E., Tang L., Selkirk M.E.
Mol. Biochem. Parasitol. 58:155-160(1993) [PubMed: 8459826] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular modelling and epitope prediction of gp29 from lymphatic filariae."
Zvelebil M.J.J.M., Tang L., Cookson E., Selkirk M.E., Thornton J.M.
Mol. Biochem. Parasitol. 58:145-153(1993) [PubMed: 7681545] [Abstract]
Cited for: 3D-STRUCTURE MODELING, GLYCOSYLATION AT ASN-39 AND ASN-92.

Cross-references

Sequence databases

X69127 Genomic DNA. Translation: CAA48881.1.
PIRS60593.
RefSeqXP_001899550.1.

3D structure databases

HSSPHSSP built from PDB template 1GP1 based on UniProtKB P00435.
ModBaseSearch...

Protein family/group databases

PeroxiBase3749. BmalGPx01.

Genome annotation databases

GeneID6102977.
KEGGbmy:Bm1_40465.

Family and domain databases

InterProIPR000889. Glut_peroxidase.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHERPTHR11592. Glut_peroxidase. 1 hit.
PfamPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFPIRSF000303. Glutathion_perox. 1 hit.
PRINTSPR01011. GLUTPROXDASE.
PROSITEPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPXC_BRUMA
AccessionPrimary (citable) accession number: P67877
Secondary accession number(s): P35665
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 25, 2008
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents