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GC_EHV1B
ID   GC_EHV1B                Reviewed;         468 AA.
AC   Q6S6Q5; P12889; P36321;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Envelope glycoprotein C;
DE            Short=gC;
DE   AltName: Full=Glycoprotein 13;
DE   Flags: Precursor;
GN   Name=gC; Synonyms=GP13; OrderedLocusNames=16;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
CC   -!- FUNCTION: Essential for the initial attachment to heparan sulfate
CC       moieties of the host cell surface proteoglycans. Also plays a role in
CC       host immune evasion by inhibiting the host complement cascade
CC       activation. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with host complement component C3; this interaction
CC       inhibits host immune response by disregulating complement cascade.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein C family.
CC       {ECO:0000305}.
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DR   EMBL; AY665713; AAT67273.1; -; Genomic_DNA.
DR   PIR; A28149; VGBEEH.
DR   RefSeq; YP_053061.1; NC_001491.2.
DR   GeneID; 1487561; -.
DR   KEGG; vg:1487561; -.
DR   Proteomes; UP000001189; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039573; P:suppression by virus of host complement activation; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR001038; GA_GC.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   Pfam; PF02124; Marek_A; 1.
DR   PRINTS; PR00668; GLYCPROTEINC.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Host-virus interaction;
KW   Immunoglobulin domain; Inhibition of host complement factors by virus;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Viral attachment to host adhesion receptor;
KW   Viral attachment to host cell; Viral immunoevasion; Virion;
KW   Virus entry into host cell.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..468
FT                   /note="Envelope glycoprotein C"
FT                   /id="PRO_0000038202"
FT   TOPO_DOM        31..431
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        432..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        452..468
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          220..311
FT                   /note="Ig-like 1"
FT   DOMAIN          321..416
FT                   /note="Ig-like 2"
FT   REGION          31..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        239..301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        340..399
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        344..373
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   468 AA;  50889 MW;  86F67AFD15AF1C89 CRC64;
     MWLPNLVRFV AVAYLICAGA ILTYASGASA SSSQSTPATP THTTPNLTTA HGAGSDNTTN
     ANGTESTHSH ETTITCTKSL ISVPYYKSVD MNCTTSVGVN YSEYRLEIYL NQRTPFSGTP
     PGDEENYINH NATKDQTLLL FSTAERKKSR RGGQLGVIPD RLPKRQLFNL PLHTEGGTKF
     PLTIKSVDWR TAGIYVWSLY AKNGTLVNST SVTVSTYNAP LLDLSVHPSL KGENYRATCV
     VASYFPHSSV KLRWYKNARE VDFTKYVTNA SSVWVDGLIT RISTVSIPVD PEEEYTPSLR
     CSIDWYRDEV SFARIAKAGT PSVFVAPTVS VSVEDGDAVC TAKCVPSTGV FVSWSVNDHL
     PGVPSQDMTT GVCPSHSGLV NMQSRRPLSE ENGEREYSCI IEGYPDGLPM FSDTVVYDAS
     PIVEDRPVLT SIIAVTCGAA ALALVVLITA VCFYCSKPSQ APYKKSDF
 
 
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