Reviewed,
UniProtKB/Swiss-Prot P05949 (VPU_HV1A2)
Last modified
February 9, 2010.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein Vpu Alternative name(s): Viral protein U U ORF protein | ||
| Gene names |
| ||
| Organism | Human immunodeficiency virus type 1 (isolate ARV2/SF2 group M subtype B) (HIV-1) | ||
| Taxonomic identifier | 11685 [NCBI] | ||
| Taxonomic lineage | Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 81 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Enhances virion budding, by targeting human CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its receptor human CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to interfere with the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis By similarity. |
| Enzyme regulation | Ion channel activity is inhibited by hexamethylene amiloride in vitro By similarity. |
| Subunit structure | May form pentamers or hexamers. Forms ternary complexes, by interacting with human CD4 and BTRC, and with human BST2 and BTRC By similarity. |
| Subcellular location | Host membrane; Single-pass type I membrane protein By similarity. |
| Domain | The N-terminal and transmembrane domains are required for proper virion budding, whereas the cytoplasmic domain is required for CD4 degradation. The cytoplasmic domain is composed of 2 amphipathic alpha helix By similarity. |
| Post-translational modification | Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BTRC and degradation of CD4 By similarity. |
| Miscellaneous | HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K). |
| Sequence similarities | Belongs to the HIV-1 VPU protein family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 81 | 81 | Protein Vpu | PRO_0000085416 | |||||
Regions | |||||||||
| Topological domain | 1 – 5 | 5 | Extracellular Potential | ||||||
| Transmembrane | 6 – 26 | 21 | Potential | ||||||
| Topological domain | 27 – 81 | 55 | Cytoplasmic Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 53 | 1 | Phosphoserine; by host CK2 By similarity | ||||||
| Modified residue | 57 | 1 | Phosphoserine; by host CK2 By similarity | ||||||
Sequences
References
| [1] | "Host range, replicative, and cytopathic properties of human immunodeficiency virus type 1 are determined by very few amino acid changes in tat and gp120." Cheng-Mayer C., Shioda T., Levy J.A. J. Virol. 65:6931-6941(1991) [PubMed: 1658383] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate SF13. |
| [2] | "Nucleotide sequence and expression of an AIDS-associated retrovirus (ARV-2)." Sanchez-Pescador R., Power M.D., Barr P.J., Steimer K.S., Stempien M.M., Brown-Shimer S.L., Gee W.W., Renard A., Randolph A., Levy J.A., Dina D., Luciw P.A. Science 227:484-492(1985) [PubMed: 2578227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-38. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L07422 Genomic RNA. Translation: AAA80323.1. K02007 Genomic RNA. Translation: AAB59881.1. Different termination. |
3D structure databases | |
| SMR | P05949. Positions 38-81. |
| ModBase | Search... |
Enzyme and pathway databases | |
| Reactome | REACT_6185. HIV Infection. |
Family and domain databases | |
| InterPro | IPR008187. Vpu. IPR009032. Vpu_cyt. [Graphical view] |
| Gene3D | G3DSA:1.10.195.10. Vpu_cyt. 1 hit. |
| Pfam | PF00558. Vpu. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | VPU_HV1A2 | ||||||||
| Accession | Primary (citable) accession number: P05949 Secondary accession number(s): Q80160 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||

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