ID   GG_EHV1V                Reviewed;         411 AA.
AC   P84393; Q6S6W1;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   02-JUN-2021, entry version 49.
DE   RecName: Full=Envelope glycoprotein G;
DE            Short=gG;
DE   Flags: Precursor;
GN   Name=gG; OrderedLocusNames=70;
OS   Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=310273;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAS45958.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein G family.
CC       {ECO:0000305}.
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DR   EMBL; AY464052; AAS45958.1; -; Genomic_DNA.
DR   RefSeq; YP_053114.1; NC_001491.2.
DR   GeneID; 2948582; -.
DR   KEGG; vg:2948582; -.
DR   Proteomes; UP000008296; 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; Signal; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..411
FT                   /note="Envelope glycoprotein G"
FT                   /id="PRO_0000038291"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          306..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   411 AA;  45270 MW;  CC6349C38D0E12E2 CRC64;
     MLTVLAALSL LSLLTSATGR LAPDELCYAE PRRTGSPPNT QPERPPVIFE PPTIAIKAES
     KGCELILLDP PIDVSYRRED KVNASIAWFF DFGACRMPIA YREYYGCIGN AVPSPETCDA
     YSFTLIRTEG IVEFTIVNMS LLFQPGIYDS GNFIYSVLLD YHIFTGRVTL EVEKDTNYPC
     GMIHGLTAYG NINVDETMDN ASPHPRAVGC FPEPIDNEAW ANVTFTELGI PDPNSFLDDE
     GDYPNISDCH SWESYTYPNT LRQATGPQTL LVGAVGLRIL AQAWKFVGDE TYDTIRAEAK
     NLETHVPSSA AESSLENQST QEESNSPEVA HLRSVNSDDS THTGGASNGI QDCDSQLKTV
     YACLALIGLG TCAMIGLIVY ICVLRSKLSS RNFSRAQNVK HRNYQRLEYV A