GK_HHV1R
ID GK_HHV1R Reviewed; 338 AA.
AC P68333; P10237;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 1.
DT 23-FEB-2022, entry version 62.
DE RecName: Full=Envelope glycoprotein K;
DE AltName: Full=Syncytial protein;
DE Flags: Precursor;
GN Name=gK; ORFNames=UL53;
OS Human herpesvirus 1 (strain R15) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=36345;
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; S51910; AAB24732.1; -; Genomic_DNA.
DR RefSeq; YP_009137129.1; NC_001806.2.
DR SMR; P68333; -.
DR DNASU; 2703425; -.
DR GeneID; 2703425; -.
DR KEGG; vg:2703425; -.
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 CHAIN 31..338
FT /note="Envelope glycoprotein K"
FT /id="PRO_0000038302"
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; 37573 MW; DC69FE77084E84A1 CRC64;
MLAVRSLQHL STVVLITAYG LVLVWYTVFG ASPLHRCIYA VRPTGTNNDT ALVWMKMNQT
LLFLGAPTHP PNGGWRNHAH ICYANLIAGR VVPFQVPPDA MNRRIMNVHE AVNCLETLWY
TRVRLVVVGW FLYLAFVALH QRRCMFGVVS PAHKMVAPAT YLLNYAGRIV SSVFLQYPYT
KITRLLCELS VQRQNLVQLF ETDPVTFLYH RPAIGVIVGC ELMLRFVAVG LIVGTAFISR
GACAITYPLF LTITTWCFVS TIGLTELYCI LRRGPAPKNA DKAAAPGRSK GLSGVCGRCC
SIILSGIAVR LCYIAVVAGV VLVALHYEQE IQRRLFDV
