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 24-JAN-2024, entry version 95.
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; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC Varicellovirus equidalpha1; Equid alphaherpesvirus 1.
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 GlyCosmos; Q6S6Q5; 9 sites, No reported glycans.
DR GeneID; 1487561; -.
DR KEGG; vg:1487561; -.
DR Proteomes; UP000001189; Segment.
DR GO; GO:0016020; C: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; Immunoglobulin; 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
//
