GL18A_MDBVW
ID GL18A_MDBVW Reviewed; 515 AA.
AC Q4ZJZ0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 23-FEB-2022, entry version 35.
DE RecName: Full=Mucin-like protein Glc1.8a;
DE Flags: Precursor;
GN Name=O9;
OS Microplitis demolitor bracovirus (isolate Webb) (MdBV).
OC Viruses; Polydnaviridae; Bracovirus.
OX NCBI_TaxID=654919;
OH NCBI_TaxID=69319; Microplitis demolitor.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16380146; DOI=10.1016/j.virol.2005.11.010;
RA Webb B.A., Strand M.R., Dickey S.E., Beck M.H., Hilgarth R.S., Barney W.E.,
RA Kadash K., Kroemer J.A., Lindstrom K.G., Rattanadechakul W., Shelby K.S.,
RA Thoetkiattikul H., Turnbull M.W., Witherell R.A.;
RT "Polydnavirus genomes reflect their dual roles as mutualists and
RT pathogens.";
RL Virology 347:160-174(2006).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11086136; DOI=10.1099/0022-1317-81-12-3049;
RA Trudeau D., Witherell R.A., Strand M.R.;
RT "Characterization of two novel Microplitis demolitor polydnavirus mRNAs
RT expressed in Pseudoplusia includens haemocytes.";
RL J. Gen. Virol. 81:3049-3058(2000).
RN [3]
RP FUNCTION.
RX PubMed=16482578; DOI=10.1002/arch.20107;
RA Strand M.R., Beck M.H., Lavine M.D., Clark K.D.;
RT "Microplitis demolitor bracovirus inhibits phagocytosis by hemocytes from
RT Pseudoplusia includens.";
RL Arch. Insect Biochem. Physiol. 61:134-145(2006).
CC -!- FUNCTION: Involved in suppression of the insect cellular immune
CC response. Inhibits host hemocyte adhesion and phagocytosis.
CC {ECO:0000269|PubMed:16482578}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polydnaviridae Glc1.8 protein family.
CC {ECO:0000305}.
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DR EMBL; DQ000240; AAY24528.1; -; Genomic_DNA.
DR RefSeq; YP_239419.1; NC_007044.1.
DR GeneID; 3416071; -.
DR KEGG; vg:3416071; -.
DR Proteomes; UP000008168; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Glycoprotein; Host membrane; Host-virus interaction;
KW Inhibition of host innate immune response by virus; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral immunoevasion.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..515
FT /note="Mucin-like protein Glc1.8a"
FT /id="PRO_0000405391"
FT TOPO_DOM 21..467
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 80..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 515 AA; 56241 MW; 4DF79CE89B8E9E07 CRC64;
MSQITLIILI LAIGFSCTKS HPINSTRDGE DSGTDLKNLL TEPANTTYAT NSTLTRKELN
STIQPERNDE GSAIRKIMAS KKDENITGQS EINTSAKSQP INSTRDGEDS GTDLKNLLTE
PANTTYATNS TLTRKELNSS IPPERNDEGS AIRKIMASKK DEIITGQSEI NTIAKSQPIN
STRDGEDSGT DLKNLLTEPA NTTYATNSTL TRKELNSSIP PERNDEGSAI RKIMASKKDE
IITGQSEINT IAKSQPINST RDGEDSGTDL KNLLTELANT TYLTNSTLTR KELNSIIQPE
RNDESSAIRK IMASKKDENV TGQSEINTSA KSQPINSTRD GEDSGTDLKN LLTDPANTTY
ATNSTLTRKE LNSTIQPERN DETSAIRKIM ASRKDENVTG QSEFNISTNS NLNTTTHHED
AVVSPTEKVY VPNNASSAEL NVSSTIQPKE ADATTSSAND IKKPAFPYCI ILITFQIVTV
GMIIYLVFRT MRKPCQSERA IPLNTFGFGN NSSHE
