ID   GG_EHV1K                Reviewed;         411 AA.
AC   P32514;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   23-FEB-2022, entry version 65.
DE   RecName: Full=Envelope glycoprotein G;
DE            Short=gG;
DE   Flags: Precursor;
GN   Name=gG; OrderedLocusNames=70;
OS   Equine herpesvirus 1 (strain Kentucky A) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10329;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1316673; DOI=10.1016/0042-6822(92)90509-n;
RA   Colle C.F. III, Flowers C.C., O'Callaghan D.J.;
RT   "Open reading frames encoding a protein kinase, homolog of glycoprotein gX
RT   of pseudorabies virus, and a novel glycoprotein map within the unique short
RT   segment of equine herpesvirus type 1.";
RL   Virology 188:545-557(1992).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Kinkou M., Fukushi H., Matsumura T., Kim S.K., O'Callaghan D.J.;
RL   Submitted (SEP-2001) 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; M87497; AAA46071.2; -; Genomic_DNA.
DR   PIR; B42538; VGBEKA.
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_0000038293"
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"
SQ   SEQUENCE   411 AA;  45327 MW;  CE5DB8348CAC1144 CRC64;
     MLTVLAALSL LSLLTSATGR LAPDELCYAE PRRTGSPPNT QPERPPVIFE PPTIAIKAES
     KGCELILLDP PIDVSYRRED KVNASIAWFF DFGACRMPIA YREYYGCIGN AVPSPETCDA
     YSFTLIRTEG IVEFTIVNMS LLFQPGIYDS GNFIYSVLLD YHIFTGRVTL EVEKDTNYPC
     GMIHGLTAYG NINVDETMDN ASPHPRAVGC FPEPIDNEAW GNVTFTELGI PDPNSFLDDE
     GDYPNISDCH SWESYTYPNT LRQATGPQTL LVGAVGLRIL AQAWKFVGDE TYDTIRAEAK
     NLETHVPSSA AESSLENQST QEESNSPEVA HLRSVNSDDS THTGGASNGI QDCDSQLKTV
     YACLALIGLG TCAMIGLIVY ICVLRSKLSS LEFWRAQNVK HRNYQRLEYV A