ID   GK_EHV1B                Reviewed;         343 AA.
AC   Q6S6R5; P28933;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-FEB-2022, entry version 82.
DE   RecName: Full=Envelope glycoprotein K;
DE   AltName: Full=Syncytial protein;
DE   Flags: Precursor;
GN   Name=gK; OrderedLocusNames=ORF6;
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).
CC   -!- FUNCTION: Glycoprotein that probably modulates membrane fusion events
CC       during secondary envelopment of cytoplasmic capsids that bud into
CC       specific trans-Golgi network (TGN)-derived membranes. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via UL20 interaction region) with protein UL20
CC       homolog (via N-terminus); this interaction probably plays a role in the
CC       coordinate transport of protein UL20 homolog and gK to the trans-Golgi
CC       network (TGN), and is required for the cell surface expression of gK.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane protein.
CC       Host endosome membrane {ECO:0000250}; Multi-pass membrane protein
CC       {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=During virion morphogenesis, this
CC       protein probably accumulates in the endosomes and trans-Golgi where
CC       secondary envelopment occurs. It is probably transported with UL20 to
CC       the cell surface from where it is endocytosed and directed to the
CC       trans-Golgi network (TGN). Cell surface expression of gK is required
CC       for virus-induced cell-to-cell fusion. Likely not present in
CC       extracellular virions (By similarity). {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein K family.
CC       {ECO:0000305}.
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DR   EMBL; AY665713; AAT67263.1; -; Genomic_DNA.
DR   PIR; G36795; MMBEA5.
DR   RefSeq; YP_053051.1; NC_001491.2.
DR   SMR; Q6S6R5; -.
DR   PRIDE; Q6S6R5; -.
DR   GeneID; 1487514; -.
DR   KEGG; vg:1487514; -.
DR   Proteomes; UP000001189; Genome.
DR   GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039700; P:fusion of viral membrane with host outer nuclear membrane; IEA:UniProtKB-KW.
DR   GO; GO:0060141; P:positive regulation of syncytium formation by virus; IEA:UniProtKB-KW.
DR   InterPro; IPR002567; GK.
DR   Pfam; PF01621; Fusion_gly_K; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Host cell membrane; Host endosome; Host Golgi apparatus;
KW   Host membrane; Membrane; Reference proteome; Signal;
KW   Syncytium formation induced by viral infection; Transmembrane;
KW   Transmembrane helix;
KW   Viral primary envelope fusion with host outer nuclear membrane;
KW   Viral release from host cell.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..343
FT                   /note="Envelope glycoprotein K"
FT                   /id="PRO_0000038304"
FT   TOPO_DOM        32..118
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..251
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..303
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..343
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   343 AA;  38045 MW;  05662C27BD8E3833 CRC64;
     MLLGGRTAYL SVLGLITAYA AFTIWYTLTA QLHNPCVYAT VSIDSKDGIA AKWEVYNSTI
     VYAYPENGAK RFSDGLSGFD YVCRENWVNE SKLDVLKNMK ELHDKVRIVV GTRNCRAYLW
     SVQLQMITGA WLIYIAFLCL RQERRLLGPF RNQNEFLSPT GYTFNYATYT LATTVLKTHY
     TKFALLLCEA SLRRVALSRT FKRDPIGFLC EHSAALALIG LEVGTHFVAR LLVVGTVTLV
     HTPCSQIYPI YLKLASWGFV VAVTIVEIVA IIYEKPPKTG SSANPPTPAT HGVKGLCTSC
     CSTVLANLCG KLVYLLLVIG AVSILLHYEQ RIQIGLLGES FSS