ID   GG_HHV2H                Reviewed;         699 AA.
AC   P13290;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   23-FEB-2022, entry version 81.
DE   RecName: Full=Envelope glycoprotein G;
DE            Short=gG;
DE   AltName: Full=gG-2;
DE   Flags: Precursor;
GN   Name=gG; ORFNames=US4;
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 [GENOMIC DNA].
RX   PubMed=3027242; DOI=10.1099/0022-1317-68-1-19;
RA   McGeoch D.J., Moss H.W.M., McNab D., Frame M.C.;
RT   "DNA sequence and genetic content of the HindIII l region in the short
RT   unique component of the herpes simplex virus type 2 genome: identification
RT   of the gene encoding glycoprotein G, and evolutionary comparisons.";
RL   J. Gen. Virol. 68:19-38(1987).
RN   [2]
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).
CC   -!- FUNCTION: Chemokine-binding protein that inhibits neutrophils'
CC       chemotaxis. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Glycoprotein G is much larger in HSV-2 than in HSV-1.
CC   -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein G family.
CC       {ECO:0000305}.
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DR   EMBL; X04798; CAA28490.1; -; Genomic_DNA.
DR   EMBL; Z86099; CAB06711.1; -; Genomic_DNA.
DR   PIR; C43674; C43674.
DR   RefSeq; YP_009137216.1; NC_001798.2.
DR   GlyConnect; 171; 3 O-Linked glycans.
DR   PRIDE; P13290; -.
DR   DNASU; 1487356; -.
DR   GeneID; 1487356; -.
DR   KEGG; vg:1487356; -.
DR   Proteomes; UP000001874; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR002896; Herpes_glycop_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   Pfam; PF01537; Herpes_glycop_D; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..699
FT                   /note="Envelope glycoprotein G"
FT                   /id="PRO_0000115769"
FT   TOPO_DOM        23..650
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        651..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        672..699
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          302..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..484
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..557
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..627
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        512
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   699 AA;  72244 MW;  612BA7B345E75540 CRC64;
     MHAIAPRLLL LFVLSGLPGT RGGSGVPGPI NPPNSDVVFP GGSPVAQYCY AYPRLDDPGP
     LGSADAGRQD LPRRVVRHEP LGRSFLTGGL VLLAPPVRGF GAPNATYAAR VTYYRLTRAC
     RQPILLRQYG GCRGGEPPSP KTCGSYTYTY QGGGPPTRYA LVNASLLVPI WDRAAETFEY
     QIELGGELHV GLLWVEVGGE GPGPTAPPQA ARAEGGPCVP PVPAGRPWRS VPPVWYSAPN
     PGFRGLRFRE RCLPPQTPAA PSDLPRVAFA PQSLLVGITG RTFIRMARPT EDVGVLPPHW
     APGALDDGPY APFPPRPRFR RALRTDPEGV DPDVRAPRTG RRLMALTEDT SSDSPTSAPE
     KTPLPVSATA MAPSVDPSAE PTAPATTTPP DEMATQAATV AVTPEETAVA SPPATASVES
     SPLPAAAAAT PGAGHTNTSS ASAAKTPPTT PAPTTPPPTS THATPRPTTP GPQTTPPGPA
     TPGPVGASAA PTADSPLTAS PPATAPGPSA ANVSVAATTA TPGTRGTART PPTDPKTHPH
     GPADAPPGSP APPPPEHRGG PEEFEGAGDG EPPEDDDSAT GLAFRTPNPN KPPPARPGPI
     RPTLPPGILG PLAPNTPRPP AQAPAKDMPS GPTPQHIPLF WFLTASPALD ILFIISTTIH
     TAAFVCLVAL AAQLWRGRAG RRRYAHPSVR YVCLPPERD