AC MF_04080; DC Protein; auto TR HAMAP; MF_04080; -; 1; level=0 XX Names: HIV_VPR XX ID VPR DE RecName: Full=Protein Vpr; DE AltName: Full=R ORF protein; DE AltName: Full=Viral protein R; GN Name=vpr; XX CC -!- FUNCTION: During virus entry, plays a role in the transport of the CC viral pre-integration (PIC) complex to the host nucleus. This function CC is crucial for viral infection of non-dividing macrophages. May act CC directly at the nuclear pore complex, by binding nucleoporins CC phenylalanine-glycine (FG)-repeat regions. CC -!- FUNCTION: During virus replication, may deplete host UNG protein, and CC incude G2-M cell cycle arrest. Acts by targeting specific host proteins CC for degradation by the 26S proteasome, through association with the CC cellular CUL4A-DDB1 E3 ligase complex by direct interaction with host CC VPRPB/DCAF-1. Cell cycle arrest reportedly occurs within hours of CC infection and is not blocked by antiviral agents, suggesting that it is CC initiated by the VPR carried into the virion. Additionally, VPR induces CC apoptosis in a cell cycle dependent manner suggesting that these two CC effects are mechanistically linked. Detected in the serum and CC cerebrospinal fluid of AIDS patient, VPR may also induce cell death to CC bystander cells. CC -!- SUBUNIT: Homooligomer, may form homodimer. Interacts with p6-gag region CC of the Pr55 Gag precursor protein through a (Leu-X-X)4 motif near the CC C-terminus of the P6gag protein. Interacts with host UNG. May interact CC with host RAD23A/HHR23A. Interacts with host VPRBP/DCAF1, leading to CC hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, mediating CC ubiquitination of host proteins such as TERT and ZGPAT and arrest of CC the cell cycle in G2 phase. CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus. Host extracellular space. CC Note=Incorporation into virion is dependent on p6 GAG sequences. Lacks CC a canonical nuclear localization signal, thus import into nucleus may CC function independently of the human importin pathway. Detected in high CC quantity in the serum and cerebrospinal fluid of AIDS patient. CC -!- PTM: Phosphorylated on several residues by host. These phosphorylations CC regulate VPR activity for the nuclear import of the HIV-1 pre- CC integration complex. CC -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for CC Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast CC majority of strains found worldwide belong to the group M. Group O CC seems to be endemic to and largely confined to Cameroon and neighboring CC countries in West Central Africa, where these viruses represent a small CC minority of HIV-1 strains. The group N is represented by a limited CC number of isolates from Cameroonian persons. The group M is further CC subdivided in 9 clades or subtypes (A to D, F to H, J and K). CC -!- SIMILARITY: Belongs to the HIV-1 VPR protein family. XX DR Pfam; PF00522; VPR; 1; trigger=no DR PRINTS; PR00444; HIVVPRVPX; 1; trigger=no XX KW Activator KW Apoptosis KW Cell cycle KW Host G2/M cell cycle arrest by virus KW Host nucleus KW Host-virus interaction KW Ion channel KW Ion transport KW Modulation of host cell cycle by virus KW Phosphoprotein KW Transcription KW Transcription regulation KW Transport KW Viral penetration into host nucleus KW Virion KW Virus entry into host cell XX GO GO:0043655; C:host extracellular space GO GO:0042025; C:host cell nucleus GO GO:0044423; C:virion component GO GO:0000278; P:mitotic cell cycle GO GO:0019051; P:induction by virus of host apoptotic process GO GO:0051701; P:biological process involved in interaction with host GO GO:0006811; P:monoatomic ion transport GO GO:0051260; P:protein homooligomerization GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0039592; P:perturbation by virus of G2/M transition of host mitotic cell cycle GO GO:0006351; P:DNA-templated transcription GO GO:0075732; P:viral penetration into host nucleus XX FT From: VPR_HV1H2 (P69726) FT REGION 1..42 FT /note="Homooligomerization" FT MOD_RES 79 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 94 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 96 FT /note="Phosphoserine; by host" FT Condition: S XX Size: 78-100; Related: None; Template: P69726; Scope: Viruses; Lentivirus Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.12 2023/07/28 //