US9_VZVD
ID US9_VZVD Reviewed; 102 AA.
AC P09312;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 02-JUN-2021, entry version 80.
DE RecName: Full=Envelope protein US9;
DE AltName: Full=Envelope protein 65;
DE AltName: Full=ORF65 protein;
GN ORFNames=ORF65;
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 [GENOMIC DNA].
RX PubMed=6321154; DOI=10.1002/j.1460-2075.1983.tb01724.x;
RA Davison A.J.;
RT "DNA sequence of the US component of the varicella-zoster virus genome.";
RL EMBO J. 2:2203-2209(1983).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=11162819; DOI=10.1006/viro.2000.0741;
RA Cohen J.I., Sato H., Srinivas S., Lekstrom K.;
RT "Varicella-zoster virus (VZV) ORF65 virion protein is dispensable for
RT replication in cell culture and is phosphorylated by casein kinase II, but
RT not by the VZV protein kinases.";
RL Virology 280:62-71(2001).
RN [4]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=19420087; DOI=10.1128/jvi.00598-09;
RA Lyman M.G., Kemp C.D., Taylor M.P., Enquist L.W.;
RT "Comparison of the pseudorabies virus Us9 protein with homologs from other
RT veterinary and human alphaherpesviruses.";
RL J. Virol. 83:6978-6986(2009).
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.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:11162819};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:19420087}.
CC Host Golgi apparatus membrane {ECO:0000269|PubMed:11162819}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:19420087}. Host Golgi
CC apparatus, host trans-Golgi network {ECO:0000269|PubMed:19420087}. Host
CC cell membrane {ECO:0000269|PubMed:11162819}; Single-pass type II
CC membrane protein {ECO:0000269|PubMed:19420087}. Note=During virion
CC morphogenesis, this protein accumulates in the trans-Golgi where
CC secondary envelopment occurs. {ECO:0000305}.
CC -!- PTM: Phosphorylated on serines within the acidic cluster, possibly by
CC host CK2. Phosphorylation determines whether endocytosed viral US9
CC traffics to 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}.
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DR EMBL; X04370; CAA27948.1; -; Genomic_DNA.
DR EMBL; X00208; CAA25030.1; -; Genomic_DNA.
DR PIR; D27345; WZBE65.
DR RefSeq; NP_040187.1; NC_001348.1.
DR PRIDE; P09312; -.
DR GeneID; 1487702; -.
DR KEGG; vg:1487702; -.
DR Proteomes; UP000002602; Genome.
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: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 1: Evidence at protein level;
KW Host cell membrane; Host Golgi apparatus; Host membrane; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion.
FT CHAIN 1..102
FT /note="Envelope protein US9"
FT /id="PRO_0000116142"
FT TOPO_DOM 1..75
FT /note="Intravirion"
FT /evidence="ECO:0000250"
FT TRANSMEM 76..96
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000250"
FT TOPO_DOM 97..102
FT /note="Virion surface"
FT /evidence="ECO:0000250"
FT REGION 41..55
FT /note="Acidic"
FT MOTIF 14..15
FT /note="Di-leucine internalization motif"
FT /evidence="ECO:0000255"
FT MOD_RES 46
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 48
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 102 AA; 11436 MW; 18801A669057A3A3 CRC64;
MAGQNTMEGE AVALLMEAVV TPRAQPNNTT ITAIQPSRSA EKCYYSDSEN ETADEFLRRI
GKYQHKIYHR KKFCYITLII VFVFAMTGAA FALGYITSQF VG