GK_VZVD
ID GK_VZVD Reviewed; 340 AA.
AC P09261;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 84.
DE RecName: Full=Envelope glycoprotein K;
DE AltName: Full=Syncytial protein;
DE Flags: Precursor;
GN Name=gK; ORFNames=ORF5;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=17010406; DOI=10.1016/j.virol.2006.08.021;
RA Hall S.L., Govero J.L., Heineman T.C.;
RT "Intracellular transport and stability of varicella-zoster virus
RT glycoprotein K.";
RL Virology 358:283-290(2007).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=17027059; DOI=10.1016/j.virol.2006.08.055;
RA Govero J.L., Hall S.L., Heineman T.C.;
RT "Intracellular localization of varicella-zoster virus ORF39 protein and its
RT functional relationship to glycoprotein K.";
RL Virology 358:291-302(2007).
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), which is extensive during VZV infection in cultured cells
CC (By similarity). {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; Multi-pass membrane protein. Host Golgi
CC apparatus membrane; Multi-pass membrane protein. Note=During virion
CC morphogenesis, this protein probably accumulates in the endosomes and
CC trans-Golgi where secondary envelopment occurs. It is probably
CC transported with UL20 to the cell surface from where it is endocytosed
CC and directed to the trans-Golgi network (TGN). Cell surface expression
CC of gK is required for virus-induced cell-to-cell fusion. Likely not
CC present in extracellular virions (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein K family.
CC {ECO:0000305}.
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DR EMBL; X04370; CAA27888.1; -; Genomic_DNA.
DR PIR; E27212; MMBE5.
DR SMR; P09261; -.
DR PRIDE; P09261; -.
DR Proteomes; UP000002602; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..340
FT /note="Envelope glycoprotein K"
FT /id="PRO_0000038306"
FT TOPO_DOM 22..114
FT /note="Extracellular"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 340 AA; 38577 MW; 0387FE00EC39C946 CRC64;
MQALGIKTEH FIIMCLLSGH AVFTLWYTAR VKFEHECVYA TTVINGGPVV WGSYNNSLIY
VTFVNHSTFL DGLSGYDYSC RENLLSGDTM VKTAISTPLH DKIRIVLGTR NCHAYFWCVQ
LKMIFFAWFV YGMYLQFRRI RRMFGPFRSS CELISPTSYS LNYVTRVISN ILLGYPYTKL
ARLLCDVSMR RDGMSKVFNA DPISFLYMHK GVTLLMLLEV IAHISSGCIV LLTLGVAYTP
CALLYPTYIR ILAWVVVCTL AIVELISYVR PKPTKDNHLN HINTGGIRGI CTTCCATVMS
GLAIKCFYIV IFAIAVVIFM HYEQRVQVSL FGESENSQKH
