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   03-AUG-2022, entry version 93.
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; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
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   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   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