GC_EHV1D
ID GC_EHV1D Reviewed; 468 AA.
AC P68325; P12889; P36321;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Envelope glycoprotein C;
DE Short=gC;
DE AltName: Full=Glycoprotein 13;
DE Flags: Precursor;
GN Name=gC; Synonyms=GP13;
OS Equine herpesvirus 1 (strain Kentucky D) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10330;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2455821; DOI=10.1128/jvi.62.8.2850-2858.1988;
RA Allen G.P., Coogle L.D.;
RT "Characterization of an equine herpesvirus type 1 gene encoding a
RT glycoprotein (gp13) with homology to herpes simplex virus glycoprotein C.";
RL J. Virol. 62:2850-2858(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2550665; DOI=10.1128/jvi.63.10.4189-4198.1989;
RA Guo P., Goebel S.J., Davis S., Perkus M.E., Languet B., Desmettre P.,
RA Allen G., Paoletti E.;
RT "Expression in recombinant vaccinia virus of the equine herpesvirus 1 gene
RT encoding glycoprotein gp13 and protection of immunized animals.";
RL J. Virol. 63:4189-4198(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8384760; DOI=10.1006/viro.1993.1200;
RA Matsumura T., Smith R.H., O'Callaghan D.J.;
RT "DNA sequence and transcriptional analyses of the region of the equine
RT herpesvirus type 1 Kentucky A strain genome encoding glycoprotein C.";
RL Virology 193:910-923(1993).
RN [4]
RP INTERACTION WITH HOST C3.
RX PubMed=7483825; DOI=10.1016/0168-1702(95)00027-n;
RA Huemer H.P., Nowotny N., Crabb B.S., Meyer H., Hubert P.H.;
RT "gp13 (EHV-gC): a complement receptor induced by equine herpesviruses.";
RL Virus Res. 37:113-126(1995).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host complement component C3; this interaction
CC inhibits host immune response by disregulating complement cascade.
CC {ECO:0000269|PubMed:7483825}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L07272; AAA46078.1; -; Genomic_DNA.
DR EMBL; M19966; AAA46077.1; -; Genomic_DNA.
DR EMBL; M29234; AAA46085.1; -; Genomic_DNA.
DR EMBL; S57839; AAB25944.1; -; Genomic_DNA.
DR PIR; A28149; VGBEEH.
DR PIR; B46114; B46114.
DR RefSeq; YP_053061.1; NC_001491.2.
DR GeneID; 1487561; -.
DR KEGG; vg:1487561; -.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Host-virus interaction;
KW Immunoglobulin domain; Inhibition of host complement factors by virus;
KW Membrane; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host adhesion receptor; Viral attachment to host cell;
KW Viral immunoevasion; Virion; 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_0000038203"
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"
FT CONFLICT 107
FT /note="E -> K (in Ref. 3; AAA46078/AAB25944)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="E -> K (in Ref. 3; AAA46078/AAB25944)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="V -> A (in Ref. 3; AAA46078/AAB25944)"
FT /evidence="ECO:0000305"
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
