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Protein

Protein Vpr

Gene

vpr

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

During virus entry, plays a role in the transport of the viral pre-integration (PIC) complex to the host nucleus. This function is crucial for viral infection of non-dividing macrophages. May act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions.UniRule annotation16 Publications
During virus replication, may deplete host UNG protein, and incude G2-M cell cycle arrest. Acts by targeting specific host proteins for degradation by the 26S proteasome, through association with the cellular CUL4A-DDB1 E3 ligase complex by direct interaction with host VPRPB/DCAF-1. 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. Detected in the serum and cerebrospinal fluid of AIDS patient, VPR may also induce cell death to bystander cells.UniRule annotation

Miscellaneous

The infectious clone pNL4-3 is a chimeric provirus that consists of DNA from HIV isolates NY5 (5' half) and BRU (3' half).
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).UniRule annotation

GO - Biological processi

Keywordsi

Molecular functionActivator, Ion channel
Biological processApoptosis, Cell cycle, Host G2/M cell cycle arrest by virus, Host-virus interaction, Ion transport, Modulation of host cell cycle by virus, Transcription, Transcription regulation, Transport, Viral penetration into host nucleus, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Protein VprUniRule annotation
Alternative name(s):
R ORF proteinUniRule annotation
Viral protein RUniRule annotation
Gene namesi
Name:vprUniRule annotation
OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
Taxonomic identifieri11686 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007692 Componenti: Genome

Subcellular locationi

P05928:
  • Virion UniRule annotation
  • Host nucleus UniRule annotation
  • Host extracellular space UniRule annotation
  • 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.UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Host nucleus, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17E → D: No effect. 1 Publication1
Mutagenesisi18W → R: Partial loss of cell killing. 1 Publication1
Mutagenesisi20 – 26LELLEEL → AEAAEEA: Partial loss of nuclear localization. 1 Publication7
Mutagenesisi21E → Q: Partial loss of Na(+) permeability for ion channel function. 1 Publication1
Mutagenesisi23L → F: 80% loss incorporation into virion. 10% loss of LTR transactivation. 1 Publication1
Mutagenesisi24E → G: Partial loss of cell killing. 2 Publications1
Mutagenesisi24E → Q: Partial loss of Na(+) permeability for ion channel function. 2 Publications1
Mutagenesisi25E → K: 75% loss incorporation into virion. Perinuclear localization. Partial loss of cell killing. No effect on human TFIIB binding. 3 Publications1
Mutagenesisi30A → F: 80% loss incorporation into virion. Perinuclear localization. 56% loss of LTR transactivation. No effect on human TFIIB binding. 3 Publications1
Mutagenesisi30A → L: Complete loss of G2/M cell cycle arrest. 3 Publications1
Mutagenesisi32R → A: No effect on incorporation in virion. 1 Publication1
Mutagenesisi33H → R: Partial loss of nuclear localization, cell killing and G2/M cell cycle arrest. 1 Publication1
Mutagenesisi34F → I: Partial loss of cell killing and nuclear localization. 1 Publication1
Mutagenesisi54W → R: Partial loss of cell killing. 1 Publication1
Mutagenesisi57V → L: 25% loss incorporation into virion. Perinuclear localization. No effect on human TFIIB binding. 2 Publications1
Mutagenesisi58E → Q: No effect on ion channel activity. 1 Publication1
Mutagenesisi59A → P: Complete loss of G2/M cell cycle arrest. 1 Publication1
Mutagenesisi62R → A: No effect on incorporation in virion. 2 Publications1
Mutagenesisi62R → P: 30% loss incorporation into virion. Perinuclear localization. 8% loss of LTR transactivation. 2 Publications1
Mutagenesisi63I → F: 10% loss incorporation into virion. Perinuclear localization. 31% loss of LTR transactivation. 1 Publication1
Mutagenesisi63I → K: 35% loss incorporation into virion. Perinuclear localization. 22% loss of LTR transactivation. 1 Publication1
Mutagenesisi67L → S: Partial loss of nuclear localization. Complete loss of G2/M cell cycle arrest. 1 Publication1
Mutagenesisi68 – 70LFI → KFR: Complete loss of G2/M cell cycle arrest. Perinuclear localization. 66% loss of LTR transactivation. 1 Publication3
Mutagenesisi71H → C: Complete loss of G2/M cell cycle arrest. 2 Publications1
Mutagenesisi71H → R: Partial loss of nuclear localization, cell killing and G2/M cell cycle arrest. 2 Publications1
Mutagenesisi73R → A or S: Complete loss of LTR transactivation and of G2/M cell cycle arrest. Transdominant mutation. 1 Publication1
Mutagenesisi75G → A: Complete loss of G2/M cell cycle arrest. 1 Publication1
Mutagenesisi76C → A: Complete loss of incorporation in virion. 2 Publications1
Mutagenesisi76C → S: Complete loss of G2/M cell cycle arrest. 2 Publications1
Mutagenesisi78H → R: Partial loss of G2/M cell cycle arrest. 1 Publication1
Mutagenesisi79S → A: Complete loss of cell cycle arrest. 2 Publications1
Mutagenesisi80 – 90RIGVTQQRRAR → NIGVTNQNNAN: Partial loss of nuclear localization. 1 PublicationAdd BLAST11
Mutagenesisi80R → A: Complete loss of G2/M cell cycle arrest. 66% loss of LTR transactivation. Complete loss of human TFIIB binding. 2 Publications1
Mutagenesisi88R → K: Partial loss of G2/M cell cycle arrest. 1 Publication1
Mutagenesisi89A → T: No effect. 1 Publication1
Mutagenesisi90R → K: Partial loss of cell killing and G2/M cell cycle arrest. 1 Publication1
Mutagenesisi94S → G: Partial loss of cell cycle arrest. 1 Publication1
Mutagenesisi95R → Q: No effect on ion channel activity. 1 Publication1
Mutagenesisi96S → P: No effect on cell cycle arrest. 1 Publication1

Keywords - Diseasei

AIDS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000854391 – 96Protein VprAdd BLAST96

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei79Phosphoserine; by hostUniRule annotation2 Publications1
Modified residuei94Phosphoserine; by hostUniRule annotation1 Publication1
Modified residuei96Phosphoserine; by hostUniRule annotation1 Publication1

Post-translational modificationi

Phosphorylated on several residues by host. These phosphorylations regulate VPR activity for the nuclear import of the HIV-1 pre-integration complex.UniRule annotation2 Publications

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiP05928.

Interactioni

Subunit structurei

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 UNG. May interact with host RAD23A/HHR23A. Interacts with host VPRBP/DCAF1, leading to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, mediating ubiquitination of host proteins such as TERT and ZGPAT and arrest of the cell cycle in G2 phase.UniRule annotation15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DCAF1Q9Y4B6-32EBI-9210238,EBI-9915372From a different organism.

Protein-protein interaction databases

IntActiP05928. 13 interactors.

Structurei

3D structure databases

ProteinModelPortaliP05928.
SMRiP05928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 42HomooligomerizationUniRule annotationAdd BLAST42

Sequence similaritiesi

Belongs to the HIV-1 VPR protein family.UniRule annotation

Phylogenomic databases

OrthoDBiVOG090001DK.

Family and domain databases

HAMAPiMF_04080. HIV_VPR. 1 hit.
InterProiView protein in InterPro
IPR000012. RetroV_VpR/X.
PfamiView protein in Pfam
PF00522. VPR. 1 hit.
PRINTSiPR00444. HIVVPRVPX.

Sequencei

Sequence statusi: Complete.

P05928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQAPEDQGP QREPHNEWTL ELLEELKNEA VRHFPRIWLH GLGQHIYETY
60 70 80 90
GDTWAGVEAI IRILQQLLFI HFRIGCRHSR IGVTQQRRAR NGASRS
Length:96
Mass (Da):11,295
Last modified:November 1, 1988 - v1
Checksum:i42892A4186E83D3E
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti15H → Y in strain: Clone pNL4-3. 1
Natural varianti28N → S in strain: Clone pNL4-3. 1
Natural varianti41G → N in strain: Clone pNL4-3. 1
Natural varianti85Q → R in strain: Clone pNL4-3. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02013 Genomic RNA. Translation: AAB59749.1.

Similar proteinsi

Entry informationi

Entry nameiVPR_HV1BR
AccessioniPrimary (citable) accession number: P05928
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: October 25, 2017
This is version 120 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families