ID A0A286MM87_9ALPH Unreviewed; 539 AA.
AC A0A286MM87;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Envelope glycoprotein E {ECO:0000256|ARBA:ARBA00013988};
GN Name=US8 {ECO:0000313|EMBL:ASW27113.1};
OS Beluga whale alphaherpesvirus 1.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC Varicellovirus monodontidalpha1; Monodontid alphaherpesvirus 1.
OX NCBI_TaxID=1434720 {ECO:0000313|EMBL:ASW27113.1};
RN [1] {ECO:0000313|EMBL:ASW27113.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LN3131-1 {ECO:0000313|EMBL:ASW27113.1};
RA Davison A.J., Nielsen O., Subramaniam K., Jacob J.M., Romero C.H.,
RA Burek-Huntington K.A., Waltzek T.B.;
RT "Genome sequence of an alphaherpesvirus from a beluga whale (Delphinapterus
RT leucas).";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In epithelial cells, the heterodimer gE/gI is required for
CC the cell-to-cell spread of the virus, by sorting nascent virions to
CC cell junctions. Once the virus reaches the cell junctions, virus
CC particles can spread to adjacent cells extremely rapidly through
CC interactions with cellular receptors that accumulate at these
CC junctions. Implicated in basolateral spread in polarized cells. In
CC neuronal cells, gE/gI is essential for the anterograde spread of the
CC infection throughout the host nervous system. Together with US9, the
CC heterodimer gE/gI is involved in the sorting and transport of viral
CC structural components toward axon tips.
CC {ECO:0000256|ARBA:ARBA00025134}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Endosome membrane {ECO:0000256|ARBA:ARBA00004190}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004190}. Host Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004152}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004152}. Host cell junction
CC {ECO:0000256|ARBA:ARBA00004315}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004402}. Host endosome membrane
CC {ECO:0000256|ARBA:ARBA00004235}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004235}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004563}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein E family.
CC {ECO:0000256|ARBA:ARBA00008101}.
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DR EMBL; MF678601; ASW27113.1; -; Genomic_DNA.
DR Proteomes; UP000297205; Genome.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
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:0044156; C:host cell junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003404; Herpes_glycopE_Fc.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF02480; Herpes_gE; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
PE 3: Inferred from homology;
KW Host cell junction {ECO:0000256|ARBA:ARBA00023081};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host endosome {ECO:0000256|ARBA:ARBA00023046};
KW Host Golgi apparatus {ECO:0000256|ARBA:ARBA00022812};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000297205};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879,
KW ECO:0000313|EMBL:ASW27113.1}; Virion {ECO:0000256|ARBA:ARBA00022844}.
FT TRANSMEM 399..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..372
FT /note="Envelope glycoprotein E Fc-binding"
FT /evidence="ECO:0000259|Pfam:PF02480"
FT REGION 449..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 58077 MW; 54649AC2022C5BB8 CRC64;
MGSSTRVGPG LSAALLALLA PVALTVTRVT VGLNETLLIG HNFSVTPTSP TNVTVGWSVL
YADAHPFHDT LVCLRHAQCE TELVFANESL SSLRALPEAF LKLRLLNGST EILAAVADDG
VEFDVSNVSV GLNVSIDSPL NRLYLLDVVY ENGSAAHEAV VVTVTGPGPG DADANASANA
TLAPHLHVVH AITPHAHGAH FSTRGYHSHL YAVGEAFNVS VHLESSIYDS DGFTANLEWY
FVKPDDSCPL LTIYEPCLYH PNVPACLHPH NARCAFASPY RATTLFSRLY IQCDRRTRDW
TAACVGTVYA HPRDYVVQAP NNVDLIFRRT PDAASGTYVF VLRYNDHVET WSYVTVTTSE
HLVNAEVVRH LPARGRDHEP DASTPPTLVI PRPGRVGSVV FLGLAVAVLI AASVAVAALG
VWLYRRCARR RRLTKPTLLP VYGRLPTTDY RPLAESDTSE DSFEDDSGGE DGSDDGDGSD
GGDDEDRVLY TRPAFKKAPP AAPRPAPARS GFKFWLRGRG GGAARSSATY SLLGDGAPY
//
