GC_HHV1K
ID GC_HHV1K Reviewed; 511 AA.
AC P28986; Q68982;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Envelope glycoprotein C;
DE Flags: Precursor;
GN Name=gC; Synonyms=UL44;
OS Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10306;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6300426; DOI=10.1128/jvi.45.2.634-647.1983;
RA Frink R.J., Eisenberg R.J., Cohen G.H., Wagner E.K.;
RT "Detailed analysis of the portion of the herpes simplex virus type 1 genome
RT encoding glycoprotein C.";
RL J. Virol. 45:634-647(1983).
RN [2]
RP HEPARIN BINDING DOMAIN.
RX PubMed=7512117; DOI=10.1099/0022-1317-75-4-743;
RA Trybala E., Bergstrom T., Svennerholm B., Jeansson S., Glorioso J.C.,
RA Olofsson S.;
RT "Localization of a functional site on herpes simplex virus type 1
RT glycoprotein C involved in binding to cell surface heparan sulphate.";
RL J. Gen. Virol. 75:743-752(1994).
RN [3]
RP FUNCTION.
RX PubMed=11807221; DOI=10.1099/0022-1317-83-2-291;
RA Mardberg K., Trybala E., Tufaro F., Bergstrom T.;
RT "Herpes simplex virus type 1 glycoprotein C is necessary for efficient
RT infection of chondroitin sulfate-expressing gro2C cells.";
RL J. Gen. Virol. 83:291-300(2002).
RN [4]
RP FUNCTION.
RC STRAIN=NS;
RX PubMed=18480440; DOI=10.1128/jvi.02599-07;
RA Hook L.M., Huang J., Jiang M., Hodinka R., Friedman H.M.;
RT "Blocking antibody access to neutralizing domains on glycoproteins involved
RT in entry as a novel mechanism of immune evasion by herpes simplex virus
RT type 1 glycoproteins C and E.";
RL J. Virol. 82:6935-6941(2008).
RN [5]
RP ALTERNATIVE SPLICING.
RX PubMed=18495765; DOI=10.1128/jvi.00388-08;
RA Sedlackova L., Perkins K.D., Lengyel J., Strain A.K., van Santen V.L.,
RA Rice S.A.;
RT "Herpes simplex virus type 1 ICP27 regulates expression of a variant,
RT secreted form of glycoprotein C by an intron retention mechanism.";
RL J. Virol. 82:7443-7455(2008).
RN [6]
RP FUNCTION.
RX PubMed=20176392; DOI=10.1016/j.virol.2010.01.032;
RA Adamiak B., Trybala E., Mardberg K., Johansson M., Liljeqvist J.A.,
RA Olofsson S., Grabowska A., Bienkowska-Szewczyk K., Szewczyk B.,
RA Bergstrom T.;
RT "Human antibodies to herpes simplex virus type 1 glycoprotein C are
RT neutralizing and target the heparan sulfate-binding domain.";
RL Virology 400:197-206(2010).
CC -!- FUNCTION: Major attachment protein that mediates binding of the virus
CC to cell surface heparan sulfate or chondroitin sulfate. Also plays
CC several roles in host immune evasion by inhibiting the host complement
CC cascade activation, and by providing a shield against neutralizing
CC antibodies that interfere with gB-gD, gB-gH/gL or gD-gH/gL
CC interactions. {ECO:0000269|PubMed:11807221,
CC ECO:0000269|PubMed:18480440, ECO:0000269|PubMed:20176392}.
CC -!- SUBUNIT: Interacts with host complement component C3b; 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=2;
CC Name=gC;
CC IsoId=P28986-1; Sequence=Displayed;
CC Name=gCsec;
CC IsoId=P28986-2; Sequence=VSP_040893;
CC -!- MISCELLANEOUS: There are seven external glycoproteins in HSV-1 and 2:
CC gH, gB, gC, gG, gD, gI, and gE.
CC -!- MISCELLANEOUS: [Isoform gC]: Membrane-bound gC.
CC -!- MISCELLANEOUS: [Isoform gCsec]: Secreted. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein C family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA45780.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J02216; AAA45779.1; -; Genomic_DNA.
DR EMBL; J02216; AAA45780.1; ALT_INIT; Genomic_DNA.
DR PIR; A20857; VGBE1K.
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 Alternative initiation; Alternative splicing; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Immunoglobulin domain;
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..511
FT /note="Envelope glycoprotein C"
FT /id="PRO_0000038198"
FT TOPO_DOM 25..480
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 267..359
FT /note="Ig-like"
FT REGION 41..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..151
FT /note="Heparin-binding domain"
FT COMPBIAS 41..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
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 148
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 127..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 286..347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 386..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 390..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 472..511
FT /note="VIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR -> VILGRSRT
FT THGVEQNASP (in isoform gCsec)"
FT /evidence="ECO:0000305"
FT /id="VSP_040893"
SQ SEQUENCE 511 AA; 55011 MW; B53CFC89DA62566F CRC64;
MAPGRVGLAV VLWGLLWLGA GVAGGSETAS TGPTITAGAV TNASEAPTSG SPGSAASPEV
TPTSTPNPNN VTQNKTTPTE PASPPTTPKP TSTPKSPPTS TPDPKPKNNT TPAKSGRPTK
PPGPVWCDRR DPLARYGSRV QIRCRFRNST RMEFRLQIWR YSMGPSPPIA PAPDLEEVLT
NITAPPGGLL VYDSAPNLTD PHVLWAEGAG PGADPPLYSV TGPLPTQRLI IGEVTPATQG
MYYLAWGRMD SPHEYGTWVR VRMFRPPSLT LQPHAVMEGQ PFKATCTAAA YYPRNPVEFD
WFEDDRQVFN PGQIDTQTHE HPDGFTTVST VTSEAVGGQV PPRTFTCQMT WHRDSVTFSR
RNATGLALVL PRPTITMEFG VRHVVCTAGC VPEGVTFAWF LGDDPSPAAK SAVTAQESCD
HPGLATVRST LPISYDYSEY ICRLTGYPAG IPVLEHHGSH QPPPRDPTER QVIEAIEWVG
IGIGVLAAGV LVVTAIVYVV RTSQSRQRHR R
