Reviewed, UniProtKB/Swiss-Prot P67878 (GPXC_BRUPA)

Names and origin

Protein names	Recommended name:     Cuticular glutathione peroxidase     EC=1.11.1.9 Alternative name(s):     Cuticular glycoprotein gp29     Major surface antigen gp29     gp30
Organism	Brugia pahangi (Filarial nematode worm)
Taxonomic identifier	6280 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Nematoda › Chromadorea › Spirurida › Filarioidea › Onchocercidae › Brugia

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Oxidoreductase Peroxidase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glutathione peroxidase activity Inferred from electronic annotation. Source: InterPro
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 – 223	204	Cuticular glutathione peroxidase		PRO_0000013092
Sites
	Active site	74	1	By similarity
Amino acid modifications
	Glycosylation	39	1	N-linked (GlcNAc...)
	Glycosylation	92	1	N-linked (GlcNAc...)
Experimental info
	Sequence conflict	96	1	N → I in CAA48882. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P67878-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: C46397B8F8C6BF0F	FASTA	223	25,883
	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

References

[1]	"Identification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase." Cookson E., Blaxter M.L., Selkirk M.E. Proc. Natl. Acad. Sci. U.S.A. 89:5837-5841(1992) [PubMed: 1631065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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].
[3]	"Stage specific differences in steady state levels of mRNA encoding the major surface glycoprotein of Brugia pahangi." Cox-Singh J., Paine M., Martin S.A., Devaney E. Trop. Med. Parasitol. 45:352-354(1994) [PubMed: 7716403] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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
EMBLGenBankDDBJ	X63365 mRNA. Translation: CAA44965.1. X69128 Genomic DNA. Translation: CAA48882.1. X73232 mRNA. Translation: CAA51704.1.
PIR	S23062.
3D structure databases
HSSP	HSSP built from PDB template 1GP1 based on UniProtKB P00435.
ModBase	Search...
Protein family/group databases
PeroxiBase	3750. BpaGPx01.
Family and domain databases
InterPro	IPR000889. Glut_peroxidase. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHER	PTHR11592. Glut_peroxidase. 1 hit.
Pfam	PF00255. GSHPx. 1 hit. [Graphical view]
PIRSF	PIRSF000303. Glutathion_perox. 1 hit.
PRINTS	PR01011. GLUTPROXDASE.
PROSITE	PS00460. GLUTATHIONE_PEROXID_1. 1 hit. PS00763. GLUTATHIONE_PEROXID_2. 1 hit. PS51355. GLUTATHIONE_PEROXID_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPXC_BRUPA

Accession

Primary (citable) accession number: P67878
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 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)