US09_HCMVM
ID US09_HCMVM Reviewed; 247 AA.
AC F5HC33;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Membrane glycoprotein US9;
DE Flags: Precursor;
GN Name=US9;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
CC -!- FUNCTION: Influences cell-to-cell spread of virus in polarized cells.
CC Promotes dissemination of virus across cell-cell junctions of polarized
CC epithelial cells, maybe through the association with the cytoskeletal
CC matrix (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane; Single-pass
CC type I membrane protein. Host cytoplasm, host cytoskeleton
CC {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Single-pass
CC type I membrane protein {ECO:0000250}. Note=In polarized cells,
CC colocalizes with F-actin in the cortical cytoskeleton which underlies
CC lateral membranes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytomegalovirus US6 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; AY446894; AAR31698.1; -; Genomic_DNA.
DR RefSeq; YP_081594.1; NC_006273.2.
DR PRIDE; F5HC33; -.
DR DNASU; 3077455; -.
DR GeneID; 3077455; -.
DR KEGG; vg:3077455; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Proteomes; UP000000938; Genome.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044386; C:integral to host endoplasmic reticulum membrane; IEA:InterPro.
DR InterPro; IPR012536; CMV_US.
DR Pfam; PF08001; CMV_US; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host cytoplasm; Host cytoskeleton;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..247
FT /note="Membrane glycoprotein US9"
FT /id="PRO_0000416724"
FT TOPO_DOM 28..192
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 72..168
FT /note="Ig-like H-type"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 81..164
FT /evidence="ECO:0000250"
SQ SEQUENCE 247 AA; 28053 MW; D8B0EBA23A8B7067 CRC64;
MILWSPSTCS FFWHWCLIAV SVLSSRSKES LRLSWSSDES SASSSSRICP LSNSKSVRLP
QYPRGFGDVS GYRVSSSVSE CYVQHGVLVA AWLVRGNFSD TAPRAYGTWG NERSATHFKV
GAPQLENDGA LRYETELPQV DARLSYVMLT VYPCSACNRS VLHCRPASRL PWLPLRVTPS
DLERLFAERR YLTFLYVVLV QFVKHVALFS FGVQVACCVY LRWIRPWVRG RHRATGRTSR
EEEAKDD
