GC_EHV4
ID GC_EHV4 Reviewed; 485 AA.
AC P22596;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Envelope glycoprotein C;
DE AltName: Full=Glycoprotein 13;
DE Flags: Precursor;
GN Name=gC; Synonyms=GP13;
OS Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10333;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2171212; DOI=10.1016/0042-6822(90)90305-b;
RA Nicolson L., Onions D.E.;
RT "The nucleotide sequence of the equine herpesvirus 4 gC gene homologue.";
RL Virology 179:378-387(1990).
RN [2]
RP FUNCTION, AND INTERACTION WITH HOST C3.
RX PubMed=20236610; DOI=10.1016/j.virusres.2010.03.003;
RA Azab W., Tsujimura K., Maeda K., Kobayashi K., Mohamed Y.M., Kato K.,
RA Matsumura T., Akashi H.;
RT "Glycoprotein C of equine herpesvirus 4 plays a role in viral binding to
RT cell surface heparan sulfate.";
RL Virus Res. 151:1-9(2010).
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:0000269|PubMed:20236610}.
CC -!- SUBUNIT: Interacts with host complement component C3; this interaction
CC inhibits host immune response by disregulating complement cascade.
CC {ECO:0000269|PubMed:20236610}.
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; M58031; AAA46083.1; -; Genomic_DNA.
DR PIR; B45343; B45343.
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; 1.
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; 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..32
FT CHAIN 33..485
FT /note="Envelope glycoprotein C"
FT /id="PRO_0000038204"
FT TOPO_DOM 33..444
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..468
FT /note="Helical"
FT TOPO_DOM 469..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 237..330
FT /note="Ig-like"
FT REGION 28..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 92..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 256..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 357..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 361..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 485 AA; 52509 MW; 599AC10EB9C2598E CRC64;
MGLVNIMRFI TFAYIICGGF ILTRTSGTSA SASPATPTTN TGEGTSSPVT PTYTTSTDSN
NSTATNNSTD VNGTEATPTP SHPHSHENTI TCTNSLISVP YYTSVTINCS TTVSVNHSEY
RLEIHLNQRT PFSDTPPGDQ ENYVNHNATK DQTLLLFSTA HSSAKSRRVG QLGVIPDRLP
KRQLFNLPAH TNGGTNFPLN IKSIDWRTAG VYVWYLFAKN GSLINSTSVT VLTYNAPLMD
LSVHPSLKGE NHRAVCVVAS YFPHNSVKLR WYKNAKEVDF TKYVTNASSV WVDGLITRIS
TVSIPADPDE EYPPSLRCSI EWYRDEVSFS RMAKAGTPSV FVAPTVSVNV EDGAAVCTAE
CVPSNGVFVS WVVNDHLPGV PSQDVTTGVC SSHPGLVNMR SSRPLSEENG EREYNCIIEG
YPDGLPMFSD SVVYDASPIV EDMPVLTGII AVTCGAAALA LVVLITAVCF YCSKPSQVPY
KKADF
