GG_HHV2B
ID GG_HHV2B Reviewed; 697 AA.
AC P81780; Q98VG3; Q9Q0B8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 23-FEB-2022, entry version 47.
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 B4327UR) (HHV-2) (Human herpes simplex virus
OS 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=103921;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-697.
RX PubMed=11101589; DOI=10.1128/jcm.38.12.4517-4522.2000;
RA Liljeqvist J.-A., Svennerholm B., Bergstroem T.;
RT "Conservation of type-specific B-cell epitopes of glycoprotein G in
RT clinical herpes simplex virus type 2 isolates.";
RL J. Clin. Microbiol. 38:4517-4522(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-341.
RX PubMed=11752712; DOI=10.1099/0022-1317-83-1-157;
RA Liljeqvist J.-A., Trybala E., Hoebeke J., Svennerholm B., Bergstroem T.;
RT "Monoclonal antibodies and human sera directed to the secreted glycoprotein
RT G of herpes simplex virus type 2 recognize type-specific antigenic
RT determinants.";
RL J. Gen. Virol. 83:157-165(2002).
RN [3]
RP PROTEIN SEQUENCE OF 23-30.
RX PubMed=10559290; DOI=10.1128/jvi.73.12.9796-9802.1999;
RA Liljeqvist J.A., Svennerholm B., Bergstrom T.;
RT "Herpes simplex virus type 2 glycoprotein G-negative clinical isolates are
RT generated by single frameshift mutations.";
RL J. Virol. 73:9796-9802(1999).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ252261; CAB65674.1; -; Genomic_DNA.
DR EMBL; AJ303204; CAC33573.1; -; Genomic_DNA.
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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:10559290"
FT CHAIN 23..697
FT /note="Envelope glycoprotein G"
FT /id="PRO_0000115768"
FT TOPO_DOM 23..648
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..697
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 298..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..625
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 435
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 697 AA; 72061 MW; E284886C90D1D35E CRC64;
MHAIAPRLLL LFVLSGLPGT RGGSGVPGPI NPPNNDVVFP GGSPVAQYCY AYPRLDDPGP
LGSADAGRQD LPRRVVRHEP LGRSFLTGGL VLLAPPVRGF GAPNATYAAH VTYYRLTRAC
RQPILLRQYG GCRGGEPPSP KTCGSYTYTY QGGGPPTRYA LVNASLLVPI WDRAAETFEY
QIELGGELHV GLLWVEVGGE GPGPTAPPQA ARAEGGPCVP PVPAGRPWRS VPPVWYSAPN
PGFRGLRFRE RCLPPQTPAA PSDLPRVAFA PQSLLVGITG RTFIRMARPT EDGVLPPHWA
PGALDDGPYA PFPPRPRFRR ALRTDPEGVD PDVRAPRTGR RLMALTEDAS SDSPTSAPEK
TPLPVSATAM APSVDPSAEP TAPATTTPPD EMATQAATVA VTPEETAVAS PPATASVESS
PPPAAAATPG AGHTNTSSAS AAKTPPTTPA PTTPPPTSTH ATPRPTTPGP QTTPPGPATP
GPVGASAAPT ADSPLTALPP ATAPGPSAAN VSVAATTATP GTRGTARTPP TDPKTHPHGP
ADAPPGSPAP PPPEHRGGPE EFEGAGDGEP PEDDDSATGL AFRTPNPNKP PPARPGPIRP
TLPPGILGPL APNTPRPPAQ APAKDMPSGP TPQHIPLFWF LTASPALDIL FIISTTIHTA
AFVCLVALAA QLWRGRAGRR RYAHPSVRYV CLPPERD
