GC_BHV1C
ID GC_BHV1C Reviewed; 521 AA.
AC P14378;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 02-JUN-2021, entry version 98.
DE RecName: Full=Envelope glycoprotein C homolog;
DE AltName: Full=Glycoprotein GIII;
DE Flags: Precursor;
GN Name=gC; ORFNames=GIII;
OS Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10323;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2554578; DOI=10.1016/0042-6822(89)90220-1;
RA Fitzpatrick D.R., Babiuk L.A., Zamb T.J.;
RT "Nucleotide sequence of bovine herpesvirus type 1 glycoprotein gIII, a
RT structural model for gIII as a new member of the immunoglobulin
RT superfamily, and implications for the homologous glycoproteins of other
RT herpesviruses.";
RL Virology 173:46-57(1989).
RN [2]
RP INTERACTION WITH HOST C3.
RX PubMed=8390825; DOI=10.1007/bf01309666;
RA Huemer H.P., Larcher C., van Drunen Littel-van den Hurk S., Babiuk L.A.;
RT "Species selective interaction of Alphaherpesvirinae with the 'unspecific'
RT immune system of the host.";
RL Arch. Virol. 130:353-364(1993).
CC -!- FUNCTION: Essential for the initial attachment to heparan sulfate
CC moieties of the host cell surface proteoglycans (By similarity). Plays
CC also a role in host immune evasion by inhibiting the host complement
CC cascade activation. {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:8390825}.
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; M27491; AAA46054.1; -; Genomic_DNA.
DR PIR; A32593; VGBEHB.
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 Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR001038; GA_GC.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
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..21
FT CHAIN 22..521
FT /note="Envelope glycoprotein C homolog"
FT /id="PRO_0000038205"
FT TOPO_DOM 22..475
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 155..227
FT /note="Ig-like V-type"
FT DOMAIN 386..451
FT /note="Ig-like C2-type"
FT REGION 24..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
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 DISULFID 142..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 290..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 390..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 394..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 521 AA; 55384 MW; 72E87266A5AEBEA5 CRC64;
MGPLGRAWLI AAIFAWALLS ARRGLAEEAE ASPSPPPSPC PTETESSAGT TGATPPTPNS
PDATPEDSTP GATTPVGTPE PPSVSEHDPP VTNSTPPPAP PEDGRPGGAG NASRDGRPSG
GGRPRPPRPS KAPPKERKWM LCEREAVAAS YAEPLYVHCG VADNATGGAR LELWFQRVGR
FRSTRGDDEA VRNPFPRAPP VLLFVAQNGS IAYRSAELGD NYIFPSPADP RNLPLTVRSL
TAATEGVYTW RRDMGTKSQR KVVTVTTHRA PAVSVEPQPA LEGAGYAAVC RAAEYYPPRS
TRLHWFRNGY PVEARHARDV FTVDDSGLFS RTSVLTLEDA TPTAHPPNLR CDVSWFQSAN
MERRFYAAGT PAVYRPPELR VYFEGGEAVC EARCVPEGRV SLRWTVRDGI APSRTEQTGV
CAERPGLVNL RGVRLLSTTD GPVDYTCTAT GYPAPLPEFS ATATYDASPG LIGSPVLVSV
VAVACGLGAV GLLLVAASCL RRKARVIQPG LTRARALGSA P
