ID   GC_HHV2G                Reviewed;         479 AA.
AC   P03173;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Envelope glycoprotein C;
DE   AltName: Full=Glycoprotein F;
DE   Flags: Precursor;
GN   Name=gC; Synonyms=UL44;
OS   Human herpesvirus 2 (strain G) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10314;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6090692; DOI=10.1128/jvi.52.1.154-163.1984;
RA   Dowbenko D.J., Lasky L.A.;
RT   "Extensive homology between the herpes simplex virus type 2 glycoprotein F
RT   gene and the herpes simplex virus type 1 glycoprotein C gene.";
RL   J. Virol. 52:154-163(1984).
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; X01456; CAA25687.1; -; Genomic_DNA.
DR   PIR; A03734; VGBEF2.
DR   PRIDE; P03173; -.
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..479
FT                   /note="Envelope glycoprotein C"
FT                   /id="PRO_0000038200"
FT   TOPO_DOM        28..446
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        468..479
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          235..327
FT                   /note="Ig-like"
FT   REGION          30..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..119
FT                   /note="Heparin-binding domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        33..54
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        51
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        254..315
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        354..410
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        358..387
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   479 AA;  51668 MW;  9EDF4075108A4933 CRC64;
     MALGRVGLTV GLWGLLWVGV VVVLANASPG RTITVGPRGN ASNAAPSVPR NRSAPRTTPT
     PPQPRKATKS KASTAKPAPP PKTGPPKTSS EPVRCNRHDP LARYGSRVQI RCRFPNSTRT
     ESRLQIWRYA TATDAEIGTA PSLEEVMVNV SAPPGGQLVY DSAPNRTDPH VIWAEGAGPG
     ASPRLYSVVG PLGRQRLIIE ELTLETQGMY YWVWGRTDRP SAYGTWVRVR VFRPPSLTIH
     PHAVLEGQPF KATCTAATYY PGNRAEFVWF EDGRRVFDPA QIHTQTQENP DGFSTVSTVT
     SAAVGGQGPP RTFTCQLTWH RDSVSFSRRN ASGTASVLPR PTITMEFTGD HAVCTAGCVP
     EGVTFAWFLG DDSSPAEKVA VASQTSCGRP GTATIRSTLP VSYEQTEYIC RLAGYPDGIP
     VLEHHGSHQP PPRDPTERQV IRAVEGAGIG VAVLVAVVLA GTAVVYLTHA SSVRYRRLR