ID   US9_EHV4                Reviewed;         220 AA.
AC   P18348;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   02-JUN-2021, entry version 71.
DE   RecName: Full=Envelope protein US9 homolog;
DE   AltName: Full=Envelope protein 76;
DE   AltName: Full=ORF76 protein;
GN   OrderedLocusNames=76;
OS   Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10333;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2839595; DOI=10.1099/0022-1317-69-7-1575;
RA   Cullinane A.A., Rixon F.J., Davison A.J.;
RT   "Characterization of the genome of equine herpesvirus 1 subtype 2.";
RL   J. Gen. Virol. 69:1575-1590(1988).
CC   -!- FUNCTION: Essential for the anterograde spread of the infection
CC       throughout the host nervous system. Together with the gE/gI
CC       heterodimer, US9 is involved in the sorting and transport of viral
CC       structural components toward axon tips (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type
CC       II membrane protein {ECO:0000250}. Host Golgi apparatus membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Host
CC       smooth endoplasmic reticulum membrane {ECO:0000250}; Single-pass type
CC       II membrane protein {ECO:0000250}. Host cell membrane {ECO:0000305};
CC       Single-pass type II membrane protein {ECO:0000305}. 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 to the cell surface from where it is endocytosed and
CC       directed to the trans-Golgi network (TGN), maybe through an interaction
CC       with PACS-1 sorting protein.
CC   -!- PTM: Phosphorylated on serines within the acidic cluster.
CC       Phosphorylation determines whether endocytosed viral US9 traffics to
CC       the trans-Golgi network or recycles to the cell membrane.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the alphaherpesvirinae envelope protein US9
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D00318; BAA00219.1; -; Genomic_DNA.
DR   SMR; P18348; -.
DR   PRIDE; P18348; -.
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:0044171; C:host cell smooth endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0075733; P:intracellular transport of virus; IEA:InterPro.
DR   InterPro; IPR009278; Herpes_US9.
DR   Pfam; PF06072; Herpes_US9; 1.
PE   3: Inferred from homology;
KW   Host cell membrane; Host endoplasmic reticulum; Host Golgi apparatus;
KW   Host membrane; Membrane; Phosphoprotein; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   CHAIN           1..220
FT                   /note="Envelope protein US9 homolog"
FT                   /id="PRO_0000116137"
FT   TOPO_DOM        1..194
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        195..215
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        216..220
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000250"
FT   REGION          151..169
FT                   /note="Acidic"
FT   MOTIF           145..146
FT                   /note="Di-leucine internalization motif"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         164
FT                   /note="Phosphoserine; by host CK2"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         166
FT                   /note="Phosphoserine; by host CK2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   220 AA;  22923 MW;  A43940EB0F1D38BD CRC64;
     MGEPEPVVAL TEDAPLSVYN PNYRSDNALI ADGDSSPIGG DCCPAEAVAA AEEVATAALA
     SEEIYEMHIK SCISSTTCGD HNNSIGVTSG LTVRAAECHP PSPEAVGIED VVVVQTAATT
     NGPSDTVPAS AAASVISDDN GCVPLLGSRL ELENYDLESG CYYSESDNET ASLFIQRVGR
     RQARRHRRRR VALTVAGVVL VAVLCAISGI VGAFLARVFQ