ID   GK_PSHV1                Reviewed;         358 AA.
AC   Q6UDM3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-DEC-2020, entry version 55.
DE   RecName: Full=Envelope glycoprotein K;
DE   AltName: Full=Syncytial protein;
DE   Flags: Precursor;
GN   Name=gK; ORFNames=UL53;
OS   Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS   (Pacheco's disease virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX   NCBI_TaxID=670426;
OH   NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA   Thureen D.R., Keeler C.L. Jr.;
RT   "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT   Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL   J. Virol. 80:7863-7872(2006).
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       Likely not present in extracellular virions (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein K family.
CC       {ECO:0000305}.
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DR   EMBL; AY372243; AAQ73687.1; -; Genomic_DNA.
DR   RefSeq; NP_944381.1; NC_005264.1.
DR   GeneID; 2656957; -.
DR   KEGG; vg:2656957; -.
DR   Proteomes; UP000006840; 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..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..358
FT                   /note="Envelope glycoprotein K"
FT                   /id="PRO_0000406831"
FT   TOPO_DOM        34..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..273
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..323
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        345..358
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   358 AA;  40383 MW;  E3E033905DDD4D1D CRC64;
     MSRVQCLRLA AVIASISHLI FLVWFVCWNS VLENNEDCVY ATRSLAAQVQ LGELGANMST
     ETRLRIRGAA AEPVSVGPFN RSLVYVINSD ASLLYSPRET QDGRCFANTF HKTDMAAVMK
     VYPDGKNVVL VLEMADCMAY LWFFQVRTAT AALLMYLAFL CVNRQRRGFG PWLDSASRVS
     AEAYYLNYWT TLAARVFLKV RYLKLSRFLR EIEYRREQTW RQFSIDTLGF YLMHPLALLL
     RAIETILYFA SLVASATVLR VNFDPCSVVL PNHVKVFAWV FVAALGALEV VSAIDHLRRE
     TRSARDAAAV IRPTNIIAAC CANIISHVLL RMLYGAALVL VVIGALKYER EIQTRLLG