ID   GK_HHV19                Reviewed;         338 AA.
AC   Q07005;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   23-FEB-2022, entry version 69.
DE   RecName: Full=Envelope glycoprotein K;
DE   AltName: Full=Syncytial protein;
DE   Flags: Precursor;
GN   Name=gK; ORFNames=UL53;
OS   Human herpesvirus 1 (strain R19) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=36346;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1335675; DOI=10.1016/0168-1702(92)90150-8;
RA   Moyal M., Berkowitz C., Rosen-Wolff A., Darai G., Becker Y.;
RT   "Mutations in the UL53 gene of HSV-1 abolish virus neurovirulence to mice
RT   by the intracerebral route of infection.";
RL   Virus Res. 26:99-112(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. Also plays a
CC       role, together with gB, in virus-induced cell-to-cell fusion (syncytia
CC       formation). Seems to block fusion of virions with infected cell
CC       membranes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via UL20 interaction region) with protein UL20 (via
CC       N-terminus); this interaction probably plays a role in the coordinate
CC       transport of protein UL20 and gK to the trans-Golgi network (TGN), and
CC       is required for the cell surface expression of gK. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus
CC       membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC       Note=During virion morphogenesis, this protein probably accumulates in
CC       the endosomes and trans-Golgi where secondary envelopment occurs. It is
CC       probably transported with UL20 to the cell surface from where it is
CC       endocytosed and directed to the trans-Golgi network (TGN). Cell surface
CC       expression of gK is required for virus-induced cell-to-cell fusion.
CC       Probably not present in extracellular virions (By similarity).
CC       {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; S51912; AAB24733.1; -; Genomic_DNA.
DR   SMR; Q07005; -.
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..30
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..338
FT                   /note="Envelope glycoprotein K"
FT                   /id="PRO_0000038299"
FT   TOPO_DOM        31..121
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..212
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..243
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        265..301
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        323..338
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          31..121
FT                   /note="Involved in fusion"
FT                   /evidence="ECO:0000255"
FT   REGION          265..301
FT                   /note="Interaction with UL20"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   338 AA;  37524 MW;  C0DAF5B316DE84A1 CRC64;
     MLAVRSLQHL STVVLITAYG LVLVWYTVFG ASPLHRCIYA VRPTGTNNDT ALVWMKMNQT
     LLFLGAPTHP PNGGWRNHAH ISYANLIAGR VVPFQVPPDA MNRRIMNVHE AVNCLETLWY
     TRVRLVVVGW FLYLAFVALH QRRCMFGVVS PAHKMVAPAT YLLNYAGRIV SSVFLQYPYT
     KITRLLCELS VQRQNLVQLF ETDPVTFLYH RPAIGVIVGC ELIVRFVAVG LIVGTAFISR
     GACAITYPLF LTITTWCFVS TIGLTELYCI LRRGPAPKNA DKAAAPGRSK GLSGVCGRCC
     SIILSGIAVR LCYIAVVAGV VLVALHYEQE IQRRLFDV