|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1631065 [NCBI, ExPASy, EBI, Israel, Japan]
Cookson E.,
Blaxter M.L.,
Selkirk M.E.;
"Identification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase.";
Proc. Natl. Acad. Sci. U.S.A. 89:5837-5841(1992).
|
[2]
|
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).
|
[3]
|
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7716403 [NCBI, ExPASy, EBI, Israel, Japan]
Cox-Singh J.,
Paine M.,
Martin S.A.,
Devaney E.;
"Stage specific differences in steady state levels of mRNA encoding the major surface glycoprotein of Brugia pahangi.";
Trop. Med. Parasitol. 45:352-354(1994).
|
[4]
|
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).
|
|
|
|
- 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.
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| 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
|
P67878 in FASTA format |
|
ExPASy Home page
SIB Switzerland