GP2_EHV1B
ID GP2_EHV1B Reviewed; 797 AA.
AC P28968; Q66VC3; Q6DLE0;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 29-SEP-2021, entry version 83.
DE RecName: Full=Glycoprotein gp2;
DE AltName: Full=Glycoprotein X;
DE Short=GpX;
DE Flags: Precursor;
GN Name=EUs4; OrderedLocusNames=71;
OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=RacL11;
RX PubMed=15795295; DOI=10.1128/jvi.79.8.5105-5115.2005;
RA Smith P.M., Kahan S.M., Rorex C.B., von Einem J., Osterrieder N.,
RA O'Callaghan D.J.;
RT "Expression of the full-length form of gp2 of equine herpesvirus 1 (EHV-1)
RT completely restores respiratory virulence to the attenuated EHV-1 strain
RT KyA in CBA mice.";
RL J. Virol. 79:5105-5115(2005).
CC -!- FUNCTION: Virulence factor. {ECO:0000305|PubMed:15795295}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
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DR EMBL; AY665713; AAT67328.1; -; Genomic_DNA.
DR EMBL; AY702017; AAU09476.1; -; Genomic_DNA.
DR PIR; H36802; VGBEX1.
DR RefSeq; YP_053115.1; NC_001491.2.
DR GeneID; 2948560; -.
DR KEGG; vg:2948560; -.
DR Proteomes; UP000001189; Genome.
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:0016032; P:viral process; IEA:InterPro.
DR InterPro; IPR010278; Varicellovirus_Gp2_glycop.
DR Pfam; PF05955; Herpes_gp2; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Virion; Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..797
FT /note="Glycoprotein gp2"
FT /id="PRO_0000038296"
FT TRANSMEM 766..790
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 24..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VARIANT 221..222
FT /note="TA -> SS (in strain: RacL11)"
FT VARIANT 226..238
FT /note="SSATTAATTTAAT -> AATTSSA (in strain: RacL11)"
FT VARIANT 430
FT /note="T -> A (in strain: RacL11)"
FT VARIANT 441
FT /note="E -> G (in strain: RacL11)"
SQ SEQUENCE 797 AA; 80343 MW; 50C9ED9211F5E5B2 CRC64;
MGFIYARKLL LCMAVSIYAI GSTTTTETTT SSSSTSGSGQ STSSGTTNSS SSPTTSPPTT
SSSPPTSTHT SSPSSTSTQS SSTAATSSSA PSTASSTTSI PTSTSTETTT TTPTASTTTP
TTTTAAPTTA ATTTAVTTAA STSAETTTAT ATATSTPTTT TPTSTTTTTA TTTVPTTAST
TTDTTTAATT TAATTTAATT TAATTTAATT TAATTTAATT TAATTSSATT AATTTAATTT
AATTTAATTT AATTTAATTT GSPTSGSTST TGASTSTPSA STATSATPTS TSTSAAATTS
TPTPTSAATS AESTTEAPTS TPTTDTTTPS EATTATTSPE STTVSASTTS ATTTAFTTES
HTSPDSSTGS TSTAEPSSTF TLTPSTATPS TDQFTGSSAS TESDSTDSST VPTTGTESIT
ESSSTTEAST NLGSSTYEST EALETPDGNT TSGNTTPSPS PRTPSFADTQ QTPDNGVSTQ
HTTINDHTTA NAQKHAGHHR GRAGGRRGSP QGGSHTTPHP DRLTPSPDDT YDDDTNHPNG
RNNSIEIVPQ LPPDRPIIEL GVATLRKNFM EASCTVETNS GLAIFWKIGN ASVDAFNRGT
THTRLMRNGV PVYALVSTLR VPWLNVIPLT KITCAACPTN LVAGDGVDLN SCTTKSTTIP
CPGQQRTHIF FSAKGDRAVC ITSELVSQPT ITWSVGSDRL RNDGFSQTWY GIQPGVCGIL
RSEVRIHRTT WRFGSTSKDY LCEVSASDSK TSDYKVLPNA HSTSNFALVA ATTLTVTILC
LLCCLYCMLT RPRASVY