Q77375 (VPR_HV1AN) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 66. History...
Names and origin
|Protein names||Recommended name:|
R ORF protein
Viral protein R
|Organism||Human immunodeficiency virus type 1 group O (isolate ANT70) (HIV-1) [Complete proteome]|
|Taxonomic identifier||327105 [NCBI]|
|Taxonomic lineage||Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group ›|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
|Sequence length||97 AA.|
|Protein existence||Inferred from homology|
General annotation (Comments)
Involved in the transport of the viral pre-integration (PIC) complex to the nucleus during the early stages of the infection. This function is crucial for viral infection of non-dividing macrophages. May interact with karyopherin alpha/KPNA1 and KPNA2 to increase their affinity for proteins containing basic-type nuclear localization signal, including the viral matrix protein MA, thus facilitating the translocation of the viral genome into the nucleus. May also act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions By similarity.
May target specific host proteins for degradation by the 26S proteasome. Acts by associating with the cellular CUL4A-DDB1 E3 ligase complex through direct interaction with host VPRPB/DCAF-1. This change in the E3 ligase substrate specificity would result in cell cycle arrest or apoptosis in infected cells. Prevents infected cells from undergoing mitosis and proliferating, by inducing arrest or delay in the G2 phase of the cell cycle. This arrest creates a favorable environment for maximizing viral expression and production by rendering the HIV-1 LTR transcriptionally more active. In this context, Vpr stimulates gene expression driven by the HIV-1 LTR by interacting with human SP1, TFIIB and TFIID. Cell cycle arrest reportedly occurs within hours of infection and is not blocked by antiviral agents, suggesting that it is initiated by the Vpr carried into the virion. Additionally, Vpr induces apoptosis in a cell cycle dependent manner suggesting that these two effects are mechanistically linked. Interacts with mitochondrial permeability transition pore complex (PTPC). This interaction induces a rapid dissipation of the mitochondrial transmembrane potential, and mitochondrial release of apoptogenic proteins such as cytochrome C or apoptosis inducing factors. Detected in the serum and cerebrospinal fluid of AIDS patient, Vpr may also induce cell death to bystander cells By similarity.
Homooligomer, may form homodimer. Interacts with p6-gag region of the Pr55 Gag precursor protein through a (Leu-X-X)4 motif near the C terminus of the P6gag protein. Interacts with host SLC25A4/ANT1, SLC25A5/ANT2, SLC25A6/ANT3, SP1, CDC25C, RAD23A/HHR23A, COPS6/HVIP, TFIIB, UNG, SF3B2/SAP145, KPNA1 and KPNA2. Interacts with host VPRBP/DCAF1, leading to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, mediate ubiquitination of host proteins such as TERT and ZGPAT and arrest the cell cycle in G2 phase. Interacts with ANKHD1 By similarity.
Virion. Host nucleus. Host extracellular space. Note: Incorporation into virion is dependent on p6 GAG sequences. Lacks a canonical nuclear localization signal, thus import into nucleus may function independently of the human importin pathway. Detected in high quantity in the serum and cerebrospinal fluid of AIDS patient By similarity.
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).
Belongs to the HIV-1 VPR protein family.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 97||97||Protein Vpr||PRO_0000246757|
|Region||1 – 42||42||Homooligomerization By similarity|
Amino acid modifications
|Modified residue||79||1||Phosphoserine; by host By similarity|
|Modified residue||95||1||Phosphoserine; by host By similarity|
|Modified residue||97||1||Phosphoserine; by host By similarity|
|||"Genomic cloning and complete sequence analysis of a highly divergent African human immunodeficiency virus isolate."|
Vanden Haesevelde M., Decourt J.L., De Leys R.J., Vanderborght B., van der Groen G., van Heuverswijn H., Saman E.
J. Virol. 68:1586-1596(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|L20587 Genomic RNA. Translation: AAA99881.1.|
3D structure databases
|SMR||Q77375. Positions 1-97. |
Protocols and materials databases
Family and domain databases
|InterPro||IPR000012. RetroV_VpR/X. |
|Pfam||PF00522. VPR. 1 hit. |
|PRINTS||PR00444. HIVVPRVPX. |
|Accession||Primary (citable) accession number: Q77375|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families