GC_SUHVF
ID GC_SUHVF Reviewed; 479 AA.
AC P06024;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 02-JUN-2021, entry version 88.
DE RecName: Full=Envelope glycoprotein C homolog;
DE AltName: Full=Glycoprotein GIII;
DE Flags: Precursor;
GN Name=gC;
OS Suid herpesvirus 1 (strain Indiana-Funkhauser / Becker) (SuHV-1)
OS (Pseudorabies virus (strain Indiana-Funkhauser / Becker)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31523;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3009851; DOI=10.1128/jvi.58.2.339-347.1986;
RA Robbins A.K., Watson R.J., Whealy M.E., Hays W.W., Enquist L.W.;
RT "Characterization of a pseudorabies virus glycoprotein gene with homology
RT to herpes simplex virus type 1 and type 2 glycoprotein C.";
RL J. Virol. 58:339-347(1986).
RN [2]
RP INTERACTION WITH HOST C3.
RX PubMed=1320797; DOI=10.1016/0168-1702(92)90113-n;
RA Huemer H.P., Larcher C., Coe N.E.;
RT "Pseudorabies virus glycoprotein III derived from virions and infected
RT cells binds to the third component of complement.";
RL Virus Res. 23:271-280(1992).
RN [3]
RP HEPARIN BINDING DOMAIN.
RX PubMed=8627651; DOI=10.1128/jvi.70.3.1355-1364.1996;
RA Flynn S.J., Ryan P.;
RT "The receptor-binding domain of pseudorabies virus glycoprotein gC is
RT composed of multiple discrete units that are functionally redundant.";
RL J. Virol. 70:1355-1364(1996).
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:1320797}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The three heparin-binding domains (HDB1, HDB2 and HDB3) mediate
CC virus attachment through specific arrangements of basic residues.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein C family.
CC {ECO:0000305}.
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DR EMBL; M12778; AAA47464.1; -; mRNA.
DR PIR; A26097; VGBEPB.
DR IntAct; P06024; 1.
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; IPR036179; Ig-like_dom_sf.
DR Pfam; PF02124; Marek_A; 1.
DR PRINTS; PR00668; GLYCPROTEINC.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Host-virus interaction;
KW Inhibition of host complement factors by virus; Membrane; Signal;
KW 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..22
FT CHAIN 23..479
FT /note="Envelope glycoprotein C homolog"
FT /id="PRO_0000038212"
FT TOPO_DOM 23..451
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 26..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..82
FT /note="HDB1"
FT REGION 95..101
FT /note="HDB2"
FT REGION 135..140
FT /note="HDB3"
FT COMPBIAS 26..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
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 228
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 103..120
FT /evidence="ECO:0000250"
FT DISULFID 256..326
FT /evidence="ECO:0000250"
FT DISULFID 365..418
FT /evidence="ECO:0000250"
FT DISULFID 369..392
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 51207 MW; DE8FEA4B2521D17F CRC64;
MASLARAMLA LLALYAAAIA AAPSTTTALD TTPNGGGGGN SSEGELSPSP PPTPAPASPE
AGAVSTPPVP PPSVSRRKPP RNNNRTRVHG DKATAHGRKR IVCRERLFSA RVGDAVSFGC
AVFPRAGETF EVRFYRRGRF RSPDADPEYF DEPPRPELPR ERLLFSSANA SLAHADALAP
VVVEGERATV ANVSGEVSVR VAAADAETEG VYTWRVLSAN GTEVRSANVS LLLYSQPEFG
LSAPPVLFGE PFRAVCVVRD YYPRRSVRLR WFADEHPVDA AFVTNSTVAD ELGRRTRVSV
VNVTRADVPG LAAADAADAL APSLRCEAVW YRDSVASQRF SEALRPHVYH PAAVSVRFVE
GFAVCDGLCV PPEARLAWSD HAADTVYHLG ACAEHPGLLN VRSARPLSDL DGPVDYTCRL
EGLPSQLPVF EDTQRYDASP ASVSWPVVSS MIVVIAGIGI LAIVLVIMAT CVYYRQAGP
