ID   GK_SUHVK                Reviewed;         312 AA.
AC   Q85230;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Envelope glycoprotein K;
DE   AltName: Full=Syncytial protein;
DE   Flags: Precursor;
GN   Name=gK; ORFNames=UL53;
OS   Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS   Kaplan)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=33703;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7637001; DOI=10.1128/jvi.69.9.5560-5567.1995;
RA   Baumeister J., Klupp B.G., Mettenleiter T.C.;
RT   "Pseudorabies virus and equine herpesvirus 1 share a nonessential gene
RT   which is absent in other herpesviruses and located adjacent to a highly
RT   conserved gene cluster.";
RL   J. Virol. 69:5560-5567(1995).
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; X87246; CAA60692.1; -; Genomic_DNA.
DR   SMR; Q85230; -.
DR   PRIDE; Q85230; -.
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; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..312
FT                   /note="Envelope glycoprotein K"
FT                   /id="PRO_0000038307"
FT   TOPO_DOM        21..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..187
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        209..227
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        249..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..312
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   312 AA;  33796 MW;  02AC2C1B5C1DF2CC CRC64;
     MLLGGRPLHL LVLGVMGAYA GLGAYYATVA RLPHPVVYAA LPLGEDAAGG APDWEAFNAT
     AIYVAPNETD ALSPALRDRA RVVYARRDCR AYLWDVHFRL AAVAWLLYAA FVYARQERRM
     FGPFRDPAEF LTPEKYTLNY AASVLAATVI GCSYTKFAWY MAELATRRAA LSRDLREDPI
     TLAHRHPTLI ALILLELGLR LGARMALFTT LGVTRAPCAL VFPLYARALV WIFVLAVGAL
     ELLAATLPHI ARVSGATATP ARSDGGRAAL GVCGACCSTV LAGIFAKALY LCLLVGGVLL
     FLHYERHITI FG