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-FEB-2021, entry version 31. 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=p17 {ECO:0000256|HAMAP-Rule:MF_04081}; DE Contains: DE RecName: Full=p7 {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; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC 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., Rong R., RA Claiborne D.T., Prince J.L., Tang J., Ribeiro R.M., Cormier E., Hahn B.H., RA Perelson A.S., Shaw G.M., Karita E., Gilmour J., Goepfert P., Derdeyn C.A., RA Allen S.A., Borrow P., Hunter E.; RT "Transmitted Virus Fitness and Host T Cell Responses Collectively Define RT Divergent Infection Outcomes in Two HIV-1 Recipients."; RL PLoS Pathog. 11:E1004565-E1004565(2015). CC -!- FUNCTION: Counteracts the innate antiviral activity of host APOBEC3F CC and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus CC preventing the entry of these lethally hypermutating enzymes into CC progeny virions. Recruits an active E3 ubiquitin ligase complex CC composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of CC APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome CC for degradation. Vif interaction with APOBEC3G also blocks its cytidine CC deaminase activity in a proteasome-independent manner, suggesting a CC dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in CC order to inhibit its translation. Seems to play a role in viral CC morphology by affecting the stability of the viral nucleoprotein core. CC Finally, Vif also contributes to the G2 cell cycle arrest observed in CC HIV infected cells. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- SUBUNIT: Homomultimer; in vitro and presumably in vivo. Interacts with CC viral RNA and Pr55Gag precursor; these interactions mediate Vif CC incorporation into the virion. Interacts with the viral reverse CC transcriptase. Interacts with human APOBEC3F and APOBEC3G. Interacts CC with host UBCE7IP1 isoform 3/ZIN and possibly with SAT. Interacts with CC host tyrosine kinases HCK and FYN; these interactions may decrease CC level of phosphorylated APOBEC3G incorporation into virions. Interacts CC with host ABCE1; this interaction may play a role in protecting viral CC RNA from damage during viral assembly. Forms an E3 ligase complex by CC interacting with host CUL5 and elongin BC complex (ELOB and ELOC). CC Interacts with host MDM2; this interaction targets Vif for degradation CC by the proteasome. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Host cell membrane CC {ECO:0000256|ARBA:ARBA00004501, ECO:0000256|HAMAP-Rule:MF_04081}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004501, CC ECO:0000256|HAMAP-Rule:MF_04081}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004501, ECO:0000256|HAMAP-Rule:MF_04081}. Host CC cytoplasm {ECO:0000256|HAMAP-Rule:MF_04081}. Virion {ECO:0000256|HAMAP- CC Rule:MF_04081}. Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral CC membrane protein {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004287}. Note=In the cytoplasm, seems to CC colocalize with intermediate filament vimentin. A fraction is CC associated with the cytoplasmic side of cellular membranes, presumably CC via the interaction with Pr55Gag precursor. Incorporated in virions at CC a ratio of approximately 7 to 20 molecules per virion. CC {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- INDUCTION: Expressed late during infection in a Rev-dependent manner. CC {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- DOMAIN: The BC-like-box motif mediates the interaction with elongin BC CC 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 presence CC of APOBEC3G. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- PTM: Processed in virion by the viral protease. {ECO:0000256|HAMAP- CC Rule:MF_04081}. 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:0000256|HAMAP-Rule:MF_04081}. CC -!- MISCELLANEOUS: Required for replication in 'nonpermissive' cells, CC including primary T-cells, macrophages and certain T-cell lines, but is CC dispensable for replication in 'permissive' cell lines, such as 293T CC cells. In nonpermissive cells, Vif-defective viruses can produce CC virions, but they fail to complete reverse transcription and cannot CC successfully infect new cells. {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- MISCELLANEOUS: Vif-defective viruses show catastrophic failure in CC reverse transcription due to APOBEC-induced mutations that initiate a CC DNA base repair pathway and compromise the structural integrity of the CC ssDNA. In the absence of Vif, the virion is morphologically abnormal. CC {ECO:0000256|HAMAP-Rule:MF_04081}. CC -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family. CC {ECO:0000256|ARBA:ARBA00006372, ECO:0000256|HAMAP-Rule:MF_04081, CC ECO:0000256|RuleBase:RU003341}. 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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; Vif. DR Pfam; PF00559; Vif; 1. DR PRINTS; PR00349; VIRIONINFFCT. PE 2: Evidence at transcript level; KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04081}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, ECO:0000256|HAMAP- KW Rule:MF_04081}; Host membrane {ECO:0000256|HAMAP-Rule:MF_04081}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04081}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04081}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04081}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_04081}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843, ECO:0000256|HAMAP- KW Rule:MF_04081}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, ECO:0000256|HAMAP- KW Rule:MF_04081}; Virion {ECO:0000256|HAMAP-Rule:MF_04081}. FT CHAIN 1..192 FT /note="Virion infectivity factor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT /id="PRO_5023471801" FT CHAIN 1..150 FT /note="p17" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT /id="PRO_5023471798" FT CHAIN 151..192 FT /note="p7" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT /id="PRO_5023471800" FT REGION 14..17 FT /note="Interaction with host APOBEC3F; F1-box" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT REGION 40..44 FT /note="Interaction with host APOBEC3G; G-box" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT REGION 54..72 FT /note="Interaction with host APOBEC3F and APOBEC3G; FG-box" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT REGION 74..79 FT /note="Interaction with host APOBEC3F; F2-box" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT REGION 75..114 FT /note="RNA-binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT REGION 151..164 FT /note="Multimerization" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT REGION 159..192 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 171..172 FT /note="Membrane association" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT MOTIF 108..139 FT /note="HCCH motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT MOTIF 144..153 FT /note="BC-box-like motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT COMPBIAS 164..179 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 150..151 FT /note="Cleavage in virion (by viral protease)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT MOD_RES 96 FT /note="Phosphothreonine; by host MAP4K1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT MOD_RES 144 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT MOD_RES 155 FT /note="Phosphothreonine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT MOD_RES 165 FT /note="Phosphoserine; by host MAP4K1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04081" FT MOD_RES 188 FT /note="Phosphothreonine; by host" FT /evidence="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 //