GenomeNet

Database: UniProt
Entry: Q09LB1_9HIV1
LinkDB: Q09LB1_9HIV1
Original site: Q09LB1_9HIV1 
ID   Q09LB1_9HIV1            Unreviewed;        81 AA.
AC   Q09LB1;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Protein Vpu {ECO:0000256|ARBA:ARBA00018094, ECO:0000256|RuleBase:RU364058};
DE   AltName: Full=U ORF protein {ECO:0000256|ARBA:ARBA00031215, ECO:0000256|RuleBase:RU364058};
DE   AltName: Full=Viral protein U {ECO:0000256|ARBA:ARBA00030659, ECO:0000256|RuleBase:RU364058};
DE   Flags: Fragment;
GN   Name=vpu {ECO:0000256|RuleBase:RU364058, ECO:0000313|EMBL:ABI50859.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ABI50859.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ABI50859.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2331 {ECO:0000313|EMBL:ABI50859.1};
RA   Sierra S., Kaiser R., Pfister H.;
RT   "Identification of HIV-1 determinants of cytopathogenicity and coreceptor
RT   usage.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Enhances virion budding by targeting host CD4 and
CC       Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents
CC       any unwanted premature interactions between viral Env and its host
CC       receptor CD4 in the endoplasmic reticulum. Degradation of
CC       antiretroviral protein Tetherin/BST2 is important for virion budding,
CC       as BST2 tethers new viral particles to the host cell membrane.
CC       Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate
CC       recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin
CC       ligase, induces their ubiquitination and subsequent proteasomal
CC       degradation. The alteration of the E3 ligase specificity by Vpu seems
CC       to promote the degradation of host IKBKB, leading to NF-kappa-B down-
CC       regulation and subsequent apoptosis. Acts as a viroporin that forms an
CC       oligomeric ion channel in membranes. Modulates the host DNA repair
CC       mechanisms to promote degradation of nuclear viral cDNA in cells that
CC       are already productively infected in order to suppress immune sensing
CC       and proviral hyper-integration (superinfection). Manipulates PML-NBs
CC       and modulates SUMOylation of host BLM protein thereby enhancing its
CC       DNA-end processing activity toward viral unintegrated linear DNA. Also
CC       inhibits RAD52-mediated homologous repair of viral cDNA, preventing the
CC       generation of dead-end circular forms of single copies of the long
CC       terminal repeat and permitting sustained nucleolytic attack.
CC       {ECO:0000256|RuleBase:RU364058}.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000256|RuleBase:RU364058};
CC       Single-pass type I membrane protein {ECO:0000256|RuleBase:RU364058}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the HIV-1 VPU protein family.
CC       {ECO:0000256|RuleBase:RU364058}.
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; DQ874535; ABI50859.1; -; Genomic_DNA.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042609; F:CD4 receptor binding; IEA:InterPro.
DR   GO; GO:0005261; F:monoatomic cation channel activity; IEA:InterPro.
DR   GO; GO:0032801; P:receptor catabolic process; IEA:InterPro.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.195.10; HIV-1 VPU cytoplasmic domain; 1.
DR   HAMAP; MF_04082; HIV_VPU; 1.
DR   InterPro; IPR008187; Vpu.
DR   InterPro; IPR009032; Vpu_cyt_dom_sf.
DR   Pfam; PF00558; Vpu; 1.
DR   SUPFAM; SSF57647; HIV-1 VPU cytoplasmic domain; 1.
PE   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|RuleBase:RU364058};
KW   Host membrane {ECO:0000256|RuleBase:RU364058};
KW   Host-virus interaction {ECO:0000256|RuleBase:RU364058};
KW   Ion channel {ECO:0000256|RuleBase:RU364058};
KW   Ion transport {ECO:0000256|RuleBase:RU364058};
KW   Membrane {ECO:0000256|RuleBase:RU364058};
KW   Transmembrane {ECO:0000256|RuleBase:RU364058};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364058};
KW   Transport {ECO:0000256|RuleBase:RU364058}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364058"
FT   REGION          50..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         81
FT                   /evidence="ECO:0000313|EMBL:ABI50859.1"
SQ   SEQUENCE   81 AA;  9180 MW;  3ABD1C3C8AF38970 CRC64;
     MTPLEIWAIV GLVVALIIAI VVWTLAGIEY KKLLRQRKID RLIKRIRERA EDSGNESEGD
     TDELSQLVEM GNYDLLGDDP L
//
DBGET integrated database retrieval system