ID GC_HHV23 Reviewed; 480 AA.
AC P06475;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=Envelope glycoprotein C;
DE Flags: Precursor;
GN Name=gC; Synonyms=UL44;
OS Human herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC Simplexvirus humanalpha2; Human herpesvirus 2.
OX NCBI_TaxID=10313;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2982036; DOI=10.1128/jvi.53.2.561-569.1985;
RA Swain M.A., Peet R.W., Galloway D.A.;
RT "Characterization of the gene encoding herpes simplex virus type 2
RT glycoprotein C and comparison with the type 1 counterpart.";
RL J. Virol. 53:561-569(1985).
CC -!- FUNCTION: Major attachment protein that mediates binding of the virus
CC to cell surface heparan sulfate or chondroitin sulfate. Also plays a
CC role in host immune evasion by inhibiting the host complement cascade
CC activation (By similarity). {ECO:0000250}.
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 -!- 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; U12178; AAA20532.1; -; Genomic_DNA.
DR EMBL; X01996; CAA26025.1; -; Genomic_DNA.
DR EMBL; M10053; AAA66442.1; -; Genomic_DNA.
DR GlyCosmos; P06475; 6 sites, No reported glycans.
DR GO; GO:0016020; C: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; Immunoglobulins; 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; Immunoglobulin; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 3: Inferred from homology;
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..480
FT /note="Envelope glycoprotein C"
FT /id="PRO_0000038199"
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; 51611 MW; CBEB0F5BFE4A2AB5 CRC64;
MALGRVGLAV GLWGLLWVGV VVVLANASPG RTITVGPRGN ASNAAPSASP RNASAPRTTP
TPPQPRKATK SKASTAKPAP PPKTGPPKTS SEPVRCNRHD PLARYGSRVQ IRCRFPNSTR
TESRLQIWRY 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
//
