GK_GAHVM
ID GK_GAHVM Reviewed; 354 AA.
AC Q9E6M3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 23-FEB-2022, entry version 67.
DE RecName: Full=Envelope glycoprotein K;
DE Flags: Precursor;
GN Name=gK; ORFNames=MDV067;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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 {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein K family.
CC {ECO:0000305}.
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DR EMBL; AF243438; AAG14247.1; -; Genomic_DNA.
DR RefSeq; YP_001033983.1; NC_002229.3.
DR SMR; Q9E6M3; -.
DR GeneID; 4811528; -.
DR KEGG; vg:4811528; -.
DR Proteomes; UP000008072; 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..354
FT /note="Envelope glycoprotein K"
FT /id="PRO_0000406578"
FT TOPO_DOM 32..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 354 AA; 39517 MW; D3913E70168E17C2 CRC64;
MSIRTSIALI GILFAISIYT VLLVVYVSTL SQNGSGCIYA TLVDSSLYDA KNFTWEQYNS
TLIYTALGNK LPLDGGFDDF SDVCRTYLVN LTSISGLASH VSTKPKIRSV VGTRNCVTYL
WRIHIQSLSS SLGLYTIFYV IREWRRMFGV VRFEDDAIST ARYTKNYAAR VISSVLLNTT
YTKMSRFMCE IMIYKNALSR TFKDDPISFL FHHPIAAVLI ITEGLVRLGA QCLCLATLSM
YFVPCEKVLS KWFLSITGIF IGIIICIELS LLLAPGPVDG AAMLGETKQV KKDECALETS
PSGVHVFCSN CCASLISNIL IKVLYILFMI ILIVTIVRYE RTLQIALFGR AYLP
