GPXC_BRUMA
ID GPXC_BRUMA Reviewed; 223 AA.
AC P67877; P35665;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279;
RN [1]
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 [2]
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; X69127; CAA48881.1; -; Genomic_DNA.
DR PIR; S60593; S60593.
DR RefSeq; XP_001899550.1; XM_001899515.1.
DR AlphaFoldDB; P67877; -.
DR SMR; P67877; -.
DR STRING; 6279.P67877; -.
DR PeroxiBase; 3749; BmalGPx01.
DR iPTMnet; P67877; -.
DR EnsemblMetazoa; Bm2151a.1; Bm2151a.1; WBGene00222412.
DR GeneID; 6102977; -.
DR KEGG; bmy:BM_BM2151; -.
DR WBParaSite; Bm2151a.1; Bm2151a.1; WBGene00222412.
DR CTD; 6102977; -.
DR HOGENOM; CLU_029507_2_1_1; -.
DR OrthoDB; 1483113at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..223
FT /note="Cuticular glutathione peroxidase"
FT /id="PRO_0000013091"
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"
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
