VPR_HV1Z2
ID VPR_HV1Z2 Reviewed; 96 AA.
AC P12519;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein Vpr {ECO:0000255|HAMAP-Rule:MF_04080};
DE AltName: Full=R ORF protein {ECO:0000255|HAMAP-Rule:MF_04080};
DE AltName: Full=Viral protein R {ECO:0000255|HAMAP-Rule:MF_04080};
GN Name=vpr {ECO:0000255|HAMAP-Rule:MF_04080};
OS Human immunodeficiency virus type 1 group M subtype D (isolate Z2/CDC-Z34)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11683;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Theodore T., Buckler-White A.J.;
RL Submitted (JUL-1989) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_04080}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_04080}.
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. {ECO:0000255|HAMAP-Rule:MF_04080}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04080}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04080}. Host extracellular space
CC {ECO:0000255|HAMAP-Rule:MF_04080}. Note=Incorporation into virion is
CC dependent on p6 GAG sequences. Lacks a canonical nuclear localization
CC signal, thus import into nucleus may function independently of the
CC human importin pathway. Detected in high quantity in the serum and
CC cerebrospinal fluid of AIDS patient. {ECO:0000255|HAMAP-Rule:MF_04080}.
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. {ECO:0000255|HAMAP-Rule:MF_04080}.
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 {ECO:0000255|HAMAP-Rule:MF_04080}.
CC -!- SIMILARITY: Belongs to the HIV-1 VPR protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04080}.
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DR EMBL; M22639; AAA45368.1; -; Genomic_RNA.
DR PIR; S54380; S54380.
DR BMRB; P12519; -.
DR SMR; P12519; -.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043655; C:host extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0019051; P:induction by virus of host apoptotic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-UniRule.
DR GO; GO:0051260; P:protein homooligomerization; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0039592; P:suppression by virus of G2/M transition of host mitotic cell cycle; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04080; HIV_VPR; 1.
DR InterPro; IPR000012; RetroV_VpR/X.
DR Pfam; PF00522; VPR; 1.
DR PRINTS; PR00444; HIVVPRVPX.
PE 3: Inferred from homology;
KW Activator; AIDS; Apoptosis; Cell cycle;
KW Host G2/M cell cycle arrest by virus; Host nucleus; Host-virus interaction;
KW Ion channel; Ion transport; Modulation of host cell cycle by virus;
KW Phosphoprotein; Transcription; Transcription regulation; Transport;
KW Viral penetration into host nucleus; Virion; Virus entry into host cell.
FT CHAIN 1..96
FT /note="Protein Vpr"
FT /id="PRO_0000085437"
FT REGION 1..42
FT /note="Homooligomerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04080"
FT MOD_RES 79
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04080"
FT MOD_RES 94
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04080"
FT MOD_RES 96
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04080"
SQ SEQUENCE 96 AA; 11380 MW; 85BC4E4D959BA944 CRC64;
MEQAPEDQGP QREPYNEWTL ELLEELKSEA VRHFPRIWLH SLGQYIYETY GDTWAGVEAL
IRILQQLLFI HFRIGCQHSR IGITRQRRAR NGSSRS
