ID A0A0B5KPZ3_9HIV1 Unreviewed; 192 AA. AC A0A0B5KPZ3; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 10-APR-2019, entry version 22. DE RecName: Full=Virion infectivity factor {ECO:0000256|HAMAP-Rule:MF_04081}; DE Short=Vif {ECO:0000256|HAMAP-Rule:MF_04081}; DE AltName: Full=SOR protein {ECO:0000256|HAMAP-Rule:MF_04081}; DE Contains: DE RecName: Full=p7 {ECO:0000256|HAMAP-Rule:MF_04081}; DE Contains: DE RecName: Full=p17 {ECO:0000256|HAMAP-Rule:MF_04081}; GN Name=vif {ECO:0000256|HAMAP-Rule:MF_04081, GN ECO:0000313|EMBL:AJG38616.1}; OS Human immunodeficiency virus 1. OC Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus. OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AJG38616.1, ECO:0000313|Proteomes:UP000101665}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:AJG38616.1, ECO:0000313|Proteomes:UP000101665} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R463MPL_I32 {ECO:0000313|EMBL:AJG38616.1}; RX PubMed=25569444; RA Yue L., Pfafferott K.J., Baalwa J., Conrod K., Dong C.C., Chui C., RA Rong R., Claiborne D.T., Prince J.L., Tang J., Ribeiro R.M., RA Cormier E., Hahn B.H., Perelson A.S., Shaw G.M., Karita E., RA Gilmour J., Goepfert P., Derdeyn C.A., Allen S.A., Borrow P., RA Hunter E.; RT "Transmitted Virus Fitness and Host T Cell Responses Collectively RT Define Divergent Infection Outcomes in Two HIV-1 Recipients."; RL PLoS Pathog. 11:E1004565-E1004565(2015). CC -!- FUNCTION: Counteracts the innate antiviral activity of host CC APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and CC APOBEC3G thus preventing the entry of these lethally hypermutating CC enzymes into progeny virions. Recruits an active E3 ubiquitin CC ligase complex composed of elongin BC, CUL5, and RBX2 to induce CC polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are CC directed to the 26S proteasome for degradation. Vif interaction CC with APOBEC3G also blocks its cytidine deaminase activity in a CC proteasome-independent manner, suggesting a dual inhibitory CC mechanism. May interact directly with APOBEC3G mRNA in order to CC inhibit its translation. Seems to play a role in viral morphology CC by affecting the stability of the viral nucleoprotein core. CC Finally, Vif also contributes to the G2 cell cycle arrest observed CC in HIV infected cells. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- SUBUNIT: Homomultimer; in vitro and presumably in vivo. Interacts CC with viral RNA and Pr55Gag precursor; these interactions mediate CC Vif incorporation into the virion. Interacts with the viral CC reverse transcriptase. Interacts with human APOBEC3F and APOBEC3G. CC Interacts with host UBCE7IP1 isoform 3/ZIN and possibly with SAT. CC Interacts with host tyrosine kinases HCK and FYN; these CC interactions may decrease level of phosphorylated APOBEC3G CC incorporation into virions. Interacts with host ABCE1; this CC interaction may play a role in protecting viral RNA from damage CC during viral assembly. Forms an E3 ligase complex by interacting CC with host CUL5 and elongin BC complex (ELOB and ELOC). Interacts CC with host MDM2; this interaction targets Vif for degradation by CC the proteasome. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000256|HAMAP- CC Rule:MF_04081, ECO:0000256|SAAS:SAAS01059686}; Peripheral membrane CC protein {ECO:0000256|HAMAP-Rule:MF_04081, CC ECO:0000256|SAAS:SAAS01059686}; Cytoplasmic side CC {ECO:0000256|HAMAP-Rule:MF_04081, ECO:0000256|SAAS:SAAS01059686}. CC Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04081}. Virion CC {ECO:0000256|HAMAP-Rule:MF_04081, ECO:0000256|SAAS:SAAS01059682}. CC Note=In the cytoplasm, seems to colocalize with intermediate CC filament vimentin. A fraction is associated with the cytoplasmic CC side of cellular membranes, presumably via the interaction with CC Pr55Gag precursor. Incorporated in virions at a ratio of CC approximately 7 to 20 molecules per virion. {ECO:0000256|HAMAP- CC Rule:MF_04081}. CC -!- INDUCTION: Expressed late during infection in a Rev-dependent CC manner. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- DOMAIN: The BC-like-box motif mediates the interaction with CC elongin BC complex. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- DOMAIN: The HCCH motif (H-x(5)-C-x(18)-C-x(5)-H) mediates the CC interaction with CUL5. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- PTM: Highly phosphorylated on serine and threonine residues. CC {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- PTM: Polyubiquitinated and degraded by the proteasome in the CC presence of APOBEC3G. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- PTM: Processed in virion by the viral protease. CC {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M CC (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). CC The vast majority of strains found worldwide belong to the group CC M. Group O seems to be endemic to and largely confined to Cameroon CC and neighboring countries in West Central Africa, where these CC viruses represent a small minority of HIV-1 strains. The group N CC is represented by a limited number of isolates from Cameroonian CC persons. The group M is further subdivided in 9 clades or subtypes CC (A to D, F to H, J and K). {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- MISCELLANEOUS: Required for replication in 'nonpermissive' cells, CC including primary T-cells, macrophages and certain T-cell lines, CC but is dispensable for replication in 'permissive' cell lines, CC such as 293T cells. In nonpermissive cells, Vif-defective viruses CC can produce virions, but they fail to complete reverse CC transcription and cannot successfully infect new cells. CC {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- MISCELLANEOUS: Vif-defective viruses show catastrophic failure in CC reverse transcription due to APOBEC-induced mutations that CC initiate a DNA base repair pathway and compromise the structural CC integrity of the ssDNA. In the absence of Vif, the virion is CC morphologically abnormal. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein CC family. {ECO:0000256|HAMAP-Rule:MF_04081, CC ECO:0000256|RuleBase:RU003341, ECO:0000256|SAAS:SAAS01059764}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KP223781; AJG38616.1; -; Genomic_RNA. DR Proteomes; UP000101665; Genome. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0019058; P:viral life cycle; IEA:InterPro. DR HAMAP; MF_04081; HIV_VIF; 1. DR InterPro; IPR000475; Viral_infect. DR Pfam; PF00559; Vif; 1. DR PRINTS; PR00349; VIRIONINFFCT. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000101665}; KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04081, KW ECO:0000256|SAAS:SAAS01059755}; KW Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04081, KW ECO:0000256|SAAS:SAAS01059745}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04081, KW ECO:0000256|SAAS:SAAS01059757}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04081, KW ECO:0000256|SAAS:SAAS01059733}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04081, KW ECO:0000256|SAAS:SAAS01059748}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04081}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_04081}; KW Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_04081}; KW Ubl conjugation pathway {ECO:0000256|HAMAP-Rule:MF_04081, KW ECO:0000256|SAAS:SAAS01059744}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04081, KW ECO:0000256|SAAS:SAAS01059762}. FT REGION 14 17 Interaction with host APOBEC3F; F1-box. FT {ECO:0000256|HAMAP-Rule:MF_04081}. FT REGION 40 44 Interaction with host APOBEC3G; G-box. FT {ECO:0000256|HAMAP-Rule:MF_04081}. FT REGION 54 72 Interaction with host APOBEC3F and FT APOBEC3G; FG-box. {ECO:0000256|HAMAP- FT Rule:MF_04081}. FT REGION 74 79 Interaction with host APOBEC3F; F2-box. FT {ECO:0000256|HAMAP-Rule:MF_04081}. FT REGION 75 114 RNA-binding. {ECO:0000256|HAMAP-Rule: FT MF_04081}. FT REGION 151 164 Multimerization. {ECO:0000256|HAMAP-Rule: FT MF_04081}. FT REGION 171 172 Membrane association. {ECO:0000256|HAMAP- FT Rule:MF_04081}. FT MOTIF 108 139 HCCH motif. {ECO:0000256|HAMAP-Rule: FT MF_04081}. FT MOTIF 144 153 BC-box-like motif. {ECO:0000256|HAMAP- FT Rule:MF_04081}. FT SITE 150 151 Cleavage in virion (by viral protease). FT {ECO:0000256|HAMAP-Rule:MF_04081}. FT MOD_RES 96 96 Phosphothreonine; by host MAP4K1. FT {ECO:0000256|HAMAP-Rule:MF_04081}. FT MOD_RES 144 144 Phosphoserine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04081}. FT MOD_RES 155 155 Phosphothreonine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04081}. FT MOD_RES 165 165 Phosphoserine; by host MAP4K1. FT {ECO:0000256|HAMAP-Rule:MF_04081}. FT MOD_RES 188 188 Phosphothreonine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04081}. SQ SEQUENCE 192 AA; 22769 MW; 1B52F005D0341A48 CRC64; MENRWQVMIV WQVDRMRIRT WNSLVKYHMY RSKKAKRWFY RHHYESNHPK VSSEVHIPLG EARLVVRTYW GLHTGERDWQ LGHGVSIEWR LRRYNTQIDP ELADQLIHLH YFACFSESAI RKAILGQVVS PSCEYQAGHN KVGSLQYLAL KALVTPTREK PPLPSVRKLT EDRWNKPQKT RGHRGSHTMN GC //