ID   GPXC_BRUPA              Reviewed;         223 AA.
AC   P67878; P35665;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Cuticular glutathione peroxidase;
DE            EC=1.11.1.9;
DE   AltName: Full=Cuticular glycoprotein gp29;
DE   AltName: Full=Major surface antigen gp29;
DE   AltName: Full=gp30;
DE   Flags: Precursor;
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1631065; DOI=10.1073/pnas.89.13.5837;
RA   Cookson E., Blaxter M.L., Selkirk M.E.;
RT   "Identification of the major soluble cuticular glycoprotein of lymphatic
RT   filarial nematode parasites (gp29) as a secretory homolog of glutathione
RT   peroxidase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:5837-5841(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8459826; DOI=10.1016/0166-6851(93)90099-j;
RA   Cookson E., Tang L., Selkirk M.E.;
RT   "Conservation of primary sequence of gp29, the major soluble cuticular
RT   glycoprotein, in three species of lymphatic filariae.";
RL   Mol. Biochem. Parasitol. 58:155-160(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7716403;
RA   Cox-Singh J., Paine M., Martin S.A., Devaney E.;
RT   "Stage specific differences in steady state levels of mRNA encoding the
RT   major surface glycoprotein of Brugia pahangi.";
RL   Trop. Med. Parasitol. 45:352-354(1994).
RN   [4]
RP   3D-STRUCTURE MODELING, AND GLYCOSYLATION AT ASN-39 AND ASN-92.
RX   PubMed=7681545; DOI=10.1016/0166-6851(93)90098-i;
RA   Zvelebil M.J.J.M., Tang L., Cookson E., Selkirk M.E., Thornton J.M.;
RT   "Molecular modelling and epitope prediction of gp29 from lymphatic
RT   filariae.";
RL   Mol. Biochem. Parasitol. 58:145-153(1993).
CC   -!- FUNCTION: Could inhibit the oxidative burst of leukocytes and
CC       neutralize the secondary products of lipid peroxidation, thus providing
CC       the resistance of these parasites to immune effector mechanisms and
CC       their persistence in the mammalian host. It may also be involved in the
CC       formation of cross-linking residues such as dityrosine, trityrosine and
CC       isotrityrosine identified in cuticular collagen. Highly cross-linked
CC       external cortex may also serve to protect the parasite from immune
CC       attack.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC         Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted into the cuticle and
CC       ultimately released into the medium.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated in the third stage larvae following
CC       infection of host. Concomitant synthesis occurs at a high level through
CC       the adult stage. Not detected in microfilariae.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; X63365; CAA44965.1; -; mRNA.
DR   EMBL; X69128; CAA48882.1; -; Genomic_DNA.
DR   EMBL; X73232; CAA51704.1; -; mRNA.
DR   PIR; S23062; S23062.
DR   AlphaFoldDB; P67878; -.
DR   SMR; P67878; -.
DR   STRING; 6280.P67878; -.
DR   PeroxiBase; 3750; BpaGPx01.
DR   iPTMnet; P67878; -.
DR   BRENDA; 1.11.1.9; 999.
DR   Proteomes; UP000038020; Genome Assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
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   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Oxidoreductase; Peroxidase; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..223
FT                   /note="Cuticular glutathione peroxidase"
FT                   /id="PRO_0000013092"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:7681545"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:7681545"
FT   CONFLICT        96
FT                   /note="N -> I (in Ref. 2; CAA48882)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   223 AA;  25883 MW;  C46397B8F8C6BF0F CRC64;
     MSAQLLILSH MVLLQLIVAQ LGPKIGKQFL KPKQCEITNQ TVYDFQVQML NGAQKSLAEY
     RNKVLLIVNV ATYCAYTMQY RDFNPILESN SNGTLNILGF PCNQFYLQEP AENHELLSGL
     KYVRPGHGWE PHKNMHIFGK LEVNGENDHP LYKFLKERCP PTVPVIGKRH QLIYDPIGTN
     DVIWNFEKFL VDKKGRPRYR FHPENWVQGT AVKPYIDELE REI