GC_HHV2H
ID GC_HHV2H Reviewed; 480 AA.
AC Q89730; O12512;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Envelope glycoprotein C;
DE Flags: Precursor;
GN Name=gC; Synonyms=UL44;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WTW1A;
RA Terhune S.S., Spear P.G.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH HOST C3.
RX PubMed=2849025; DOI=10.1016/0882-4010(87)90012-x;
RA Eisenberg R.J., Ponce de Leon M., Friedman H.M., Fries L.F., Frank M.M.,
RA Hastings J.C., Cohen G.H.;
RT "Complement component C3b binds directly to purified glycoprotein C of
RT herpes simplex virus types 1 and 2.";
RL Microb. Pathog. 3:423-435(1987).
CC -!- FUNCTION: Major attachment protein that mediates binding of the virus
CC to cell surface heparan sulfate or chondroitin sulfate (By similarity).
CC Also plays a role in host immune evasion by inhibiting the host
CC complement cascade activation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host complement component C3b; this interaction
CC inhibits host immune response by disregulating complement cascade.
CC {ECO:0000269|PubMed:2849025}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: There are seven external glycoproteins in HSV-1 and 2:
CC gH, gB, gC, gG, gD, gI, and gE.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein C family.
CC {ECO:0000305}.
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DR EMBL; Z86099; CAB06730.1; -; Genomic_DNA.
DR EMBL; U12179; AAB60551.1; -; Genomic_DNA.
DR EMBL; U12177; AAB60550.1; -; Genomic_DNA.
DR RefSeq; YP_009137196.1; NC_001798.2.
DR PRIDE; Q89730; -.
DR DNASU; 1487331; -.
DR GeneID; 1487331; -.
DR KEGG; vg:1487331; -.
DR Proteomes; UP000001874; Genome.
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; Reference proteome; 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..480
FT /note="Envelope glycoprotein C"
FT /id="PRO_0000038201"
FT TOPO_DOM 28..447
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 236..328
FT /note="Ig-like"
FT REGION 30..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..120
FT /note="Heparin-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 33..55
FT /note="Polar 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 52
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 96..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 255..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 355..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 359..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 480 AA; 51671 MW; C145B4EFEF582B63 CRC64;
MALGRVGLAV GLWGLLWVGV VVVLANASPG RTITVGPRGN ASNAAPSASP RNASAPRTTP
TPPQPRKATK SKASTAKPAP PPKTGPPKTS SEPVRCNRHD PLARYGSRVQ IRCRFPNSTR
TEFRLQIWRY ATATDAEIGT APSLEEVMVN VSAPPGGQLV YDSAPNRTDP HVIWAEGAGP
GASPRLYSVV GPLGRQRLII EELTLETQGM YYWVWGRTDR PSAYGTWVRV RVFRPPSLTI
HPHAVLEGQP FKATCTAATY YPGNRAEFVW FEDGRRVFDP AQIHTQTQEN PDGFSTVSTV
TSAAVGGQGP PRTFTCQLTW HRDSVSFSRR NASGTASVLP RPTITMEFTG DHAVCTAGCV
PEGVTFAWFL GDDSSPAEKV AVASQTSCGR PGTATIRSTL PVSYEQTEYI CRLAGYPDGI
PVLEHHGSHQ PPPRDPTERQ VIRAVEGAGI GVAVLVAVVL AGTAVVYLTH ASSVRYRRLR
