ID   GG_EHV4                 Reviewed;         405 AA.
AC   P32650;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-DEC-2020, entry version 69.
DE   RecName: Full=Envelope glycoprotein G;
DE            Short=gG;
DE   Flags: Precursor;
GN   Name=gG;
OS   Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10333;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1529525; DOI=10.1016/0042-6822(92)91200-e;
RA   Crabb B.S., Nagesha H.S., Studdert M.J.;
RT   "Identification of equine herpesvirus 4 glycoprotein G: a type-specific,
RT   secreted glycoprotein.";
RL   Virology 190:143-154(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8380320; DOI=10.1007/bf01309795;
RA   Nagesha H.S., Studdert M.J., Crabb B.S.;
RT   "Analysis of the nucleotide sequence of five genes at the left end of the
RT   unique short region of the equine herpesvirus 4 genome.";
RL   Arch. Virol. 128:143-154(1993).
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; S44796; AAB23267.1; -; Genomic_DNA.
DR   EMBL; M89634; AAA46103.1; -; Genomic_DNA.
DR   PIR; A43375; VGBEGF.
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..405
FT                   /note="Envelope glycoprotein G"
FT                   /id="PRO_0000038292"
FT   TRANSMEM        389..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
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        174
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   405 AA;  44804 MW;  D05D10C798B27B37 CRC64;
     MLAVGATLCL LSFLTGATGR LAPDDLCYAE PRKTGPMPRS KPKHQPLLFE APKVALTAES
     KGCQLILLDP PIDMGYRLED KINASIAWFF DFGNCRMPIA YREYYDCVGN AIPSPETCDG
     YSFTLVKTEG VVEFTIVNMS LLLQPGIYDS GSFIYSALLD MDVLTGRVIL NVENDTNYPC
     GMTHGLTADG NINVDETTHT TPHPRAVGCF PELINFDAWE NVTFEEMGIP DPNSFLDDES
     DYPNTMDCYS WDLYTYPKSL KQAEGPQTLL IGAVGLRILA QAWKFVENET YSQHTRTYTR
     DAKEVDVTQP SPVQADSVLA KKRTSMKNNP IYSEGKPHAK PFSTIDSIHT EGMKNNPVYS
     ESLMLNVQHS DSITTGGVLH GLQDCDNQLK TVYICLALIG LAHVP