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Virion infectivity factor

 K0H249_9HIV1            Unreviewed;       192 AA.
K0H249;
28-NOV-2012, integrated into UniProtKB/TrEMBL.
28-NOV-2012, sequence version 1.
28-MAR-2018, entry version 25.
RecName: Full=Virion infectivity factor {ECO:0000256|HAMAP-Rule:MF_04081};
Short=Vif {ECO:0000256|HAMAP-Rule:MF_04081};
AltName: Full=SOR protein {ECO:0000256|HAMAP-Rule:MF_04081};
Contains:
RecName: Full=p17 {ECO:0000256|HAMAP-Rule:MF_04081};
Contains:
RecName: Full=p7 {ECO:0000256|HAMAP-Rule:MF_04081};
Name=vif {ECO:0000256|HAMAP-Rule:MF_04081,
ECO:0000313|EMBL:AFU33767.1};
Human immunodeficiency virus 1.
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11676 {ECO:0000313|EMBL:AFU33767.1};
NCBI_TaxID=9606; Homo sapiens (Human).
[1] {ECO:0000313|EMBL:AFU33767.1}
NUCLEOTIDE SEQUENCE.
STRAIN=AA122a01R {ECO:0000313|EMBL:AFU33792.1},
AA122a02R {ECO:0000313|EMBL:AFU33774.1},
AA122a04L {ECO:0000313|EMBL:AFU33759.1},
AA122a05L {ECO:0000313|EMBL:AFU33755.1},
AA122a06L {ECO:0000313|EMBL:AFU33767.1},
AA122a08R {ECO:0000313|EMBL:AFU33780.1}, and
AA122a09L {ECO:0000313|EMBL:AFU33751.1};
PubMed=22960785; DOI=10.1038/nature11519;
Rolland M., Edlefsen P.T., Larsen B.B., Tovanabutra S.,
Sanders-Buell E., Hertz T., de Camp A.C., Carrico C., Menis S.,
Magaret C.A., Ahmed H., Juraska M., Chen L., Konopa P., Nariya S.,
Stoddard J.N., Wong K., Zhao H., Deng W., Maust B.S., Bose M.,
Howell S., Bates A., Lazzaro M., O'Sullivan A., Lei E., Bradfield A.,
Ibitamuno G., Assawadarachai V., O'Connell R.J., de Souza M.S.,
Nitayaphan S., Rerks-Ngarm S., Robb M.L., McLellan J.S., Georgiev I.,
Kwong P.D., Carlson J.M., Michael N.L., Schief W.R., Gilbert P.B.,
Mullins J.I., Kim J.H.;
"Increased HIV-1 vaccine efficacy against viruses with genetic
signatures in Env V2.";
Nature 490:417-420(2012).
[2] {ECO:0000313|EMBL:AFU33767.1}
NUCLEOTIDE SEQUENCE.
STRAIN=AA122a01R {ECO:0000313|EMBL:AFU33792.1},
AA122a02R {ECO:0000313|EMBL:AFU33774.1},
AA122a04L {ECO:0000313|EMBL:AFU33759.1},
AA122a05L {ECO:0000313|EMBL:AFU33755.1},
AA122a06L {ECO:0000313|EMBL:AFU33767.1},
AA122a08R {ECO:0000313|EMBL:AFU33780.1}, and
AA122a09L {ECO:0000313|EMBL:AFU33751.1};
PubMed=25646817;
RV144 Sequencing Team;
Edlefsen P.T., Rolland M., Hertz T., Tovanabutra S., Gartland A.J.,
deCamp A.C., Magaret C.A., Ahmed H., Gottardo R., Juraska M.,
McCoy C., Larsen B.B., Sanders-Buell E., Carrico C., Menis S.,
Kijak G.H., Bose M., Arroyo M.A., O'Connell R.J., Nitayaphan S.,
Pitisuttithum P., Kaewkungwal J., Rerks-Ngarm S., Robb M.L., Kirys T.,
Georgiev I.S., Kwong P.D., Scheffler K., Pond S.L., Carlson J.M.,
Michael N.L., Schief W.R., Mullins J.I., Kim J.H., Gilbert P.B.;
"Comprehensive sieve analysis of breakthrough HIV-1 sequences in the
RV144 vaccine efficacy trial.";
PLoS Comput. Biol. 11:E1003973-E1003973(2015).
-!- FUNCTION: Counteracts the innate antiviral activity of host
APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and
APOBEC3G thus preventing the entry of these lethally hypermutating
enzymes into progeny virions. Recruits an active E3 ubiquitin
ligase complex composed of elongin BC, CUL5, and RBX2 to induce
polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are
directed to the 26S proteasome for degradation. Vif interaction
with APOBEC3G also blocks its cytidine deaminase activity in a
proteasome-independent manner, suggesting a dual inhibitory
mechanism. May interact directly with APOBEC3G mRNA in order to
inhibit its translation. Seems to play a role in viral morphology
by affecting the stability of the viral nucleoprotein core.
Finally, Vif also contributes to the G2 cell cycle arrest observed
in HIV infected cells. {ECO:0000256|HAMAP-Rule:MF_04081}.
-!- SUBUNIT: Homomultimer; in vitro and presumably in vivo. Interacts
with viral RNA and Pr55Gag precursor; these interactions mediate
Vif incorporation into the virion. Interacts with the viral
reverse transcriptase. Interacts with human APOBEC3F and APOBEC3G.
Interacts with host UBCE7IP1 isoform 3/ZIN and possibly with SAT.
Interacts with host tyrosine kinases HCK and FYN; these
interactions may decrease level of phosphorylated APOBEC3G
incorporation into virions. Interacts with host ABCE1; this
interaction may play a role in protecting viral RNA from damage
during viral assembly. Forms an E3 ligase complex by interacting
with host CUL5 and elongin BC complex (ELOB and ELOC). Interacts
with host MDM2; this interaction targets Vif for degradation by
the proteasome. {ECO:0000256|HAMAP-Rule:MF_04081}.
-!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000256|HAMAP-
Rule:MF_04081, ECO:0000256|SAAS:SAAS00594051}; Peripheral membrane
protein {ECO:0000256|HAMAP-Rule:MF_04081,
ECO:0000256|SAAS:SAAS00594051}; Cytoplasmic side
{ECO:0000256|HAMAP-Rule:MF_04081, ECO:0000256|SAAS:SAAS00594051}.
Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04081}. Virion
{ECO:0000256|HAMAP-Rule:MF_04081, ECO:0000256|SAAS:SAAS00594062}.
Note=In the cytoplasm, seems to colocalize with intermediate
filament vimentin. A fraction is associated with the cytoplasmic
side of cellular membranes, presumably via the interaction with
Pr55Gag precursor. Incorporated in virions at a ratio of
approximately 7 to 20 molecules per virion. {ECO:0000256|HAMAP-
Rule:MF_04081}.
-!- INDUCTION: Expressed late during infection in a Rev-dependent
manner. {ECO:0000256|HAMAP-Rule:MF_04081}.
-!- DOMAIN: The BC-like-box motif mediates the interaction with
elongin BC complex. {ECO:0000256|HAMAP-Rule:MF_04081}.
-!- DOMAIN: The HCCH motif (H-x(5)-C-x(18)-C-x(5)-H) mediates the
interaction with CUL5. {ECO:0000256|HAMAP-Rule:MF_04081}.
-!- PTM: Highly phosphorylated on serine and threonine residues.
{ECO:0000256|HAMAP-Rule:MF_04081}.
-!- PTM: Polyubiquitinated and degraded by the proteasome in the
presence of APOBEC3G. {ECO:0000256|HAMAP-Rule:MF_04081}.
-!- PTM: Processed in virion by the viral protease.
{ECO:0000256|HAMAP-Rule:MF_04081}.
-!- MISCELLANEOUS: 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). {ECO:0000256|HAMAP-Rule:MF_04081}.
-!- MISCELLANEOUS: Required for replication in 'nonpermissive' cells,
including primary T-cells, macrophages and certain T-cell lines,
but is dispensable for replication in 'permissive' cell lines,
such as 293T cells. In nonpermissive cells, Vif-defective viruses
can produce virions, but they fail to complete reverse
transcription and cannot successfully infect new cells.
{ECO:0000256|HAMAP-Rule:MF_04081}.
-!- MISCELLANEOUS: Vif-defective viruses show catastrophic failure in
reverse transcription due to APOBEC-induced mutations that
initiate a DNA base repair pathway and compromise the structural
integrity of the ssDNA. In the absence of Vif, the virion is
morphologically abnormal. {ECO:0000256|HAMAP-Rule:MF_04081}.
-!- SIMILARITY: Belongs to the primate lentivirus group Vif protein
family. {ECO:0000256|HAMAP-Rule:MF_04081,
ECO:0000256|RuleBase:RU003341, ECO:0000256|SAAS:SAAS00594061}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04081}.
-----------------------------------------------------------------------
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EMBL; JX448211; AFU33751.1; -; Genomic_RNA.
EMBL; JX448212; AFU33755.1; -; Genomic_RNA.
EMBL; JX448213; AFU33759.1; -; Genomic_RNA.
EMBL; JX448215; AFU33767.1; -; Genomic_RNA.
EMBL; JX448217; AFU33774.1; -; Genomic_RNA.
EMBL; JX448218; AFU33780.1; -; Genomic_RNA.
EMBL; JX448220; AFU33792.1; -; Genomic_RNA.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
GO; GO:0019058; P:viral life cycle; IEA:InterPro.
HAMAP; MF_04081; HIV_VIF; 1.
InterPro; IPR000475; Viral_infect.
Pfam; PF00559; Vif; 1.
PRINTS; PR00349; VIRIONINFFCT.
2: Evidence at transcript level;
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04081,
ECO:0000256|SAAS:SAAS00135760};
Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04081,
ECO:0000256|SAAS:SAAS00487388};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04081,
ECO:0000256|SAAS:SAAS00135760};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04081,
ECO:0000256|SAAS:SAAS00487339};
Membrane {ECO:0000256|HAMAP-Rule:MF_04081,
ECO:0000256|SAAS:SAAS00135760};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04081};
RNA-binding {ECO:0000256|HAMAP-Rule:MF_04081};
Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_04081};
Ubl conjugation pathway {ECO:0000256|HAMAP-Rule:MF_04081,
ECO:0000256|SAAS:SAAS00487332};
Virion {ECO:0000256|HAMAP-Rule:MF_04081,
ECO:0000256|SAAS:SAAS00487311}.
REGION 14 17 Interaction with host APOBEC3F; F1-box.
{ECO:0000256|HAMAP-Rule:MF_04081}.
REGION 40 44 Interaction with host APOBEC3G; G-box.
{ECO:0000256|HAMAP-Rule:MF_04081}.
REGION 54 72 Interaction with host APOBEC3F and
APOBEC3G; FG-box. {ECO:0000256|HAMAP-
Rule:MF_04081}.
REGION 74 79 Interaction with host APOBEC3F; F2-box.
{ECO:0000256|HAMAP-Rule:MF_04081}.
REGION 75 114 RNA-binding. {ECO:0000256|HAMAP-
Rule:MF_04081}.
REGION 151 164 Multimerization. {ECO:0000256|HAMAP-
Rule:MF_04081}.
REGION 171 172 Membrane association. {ECO:0000256|HAMAP-
Rule:MF_04081}.
MOTIF 108 139 HCCH motif. {ECO:0000256|HAMAP-
Rule:MF_04081}.
MOTIF 144 153 BC-box-like motif. {ECO:0000256|HAMAP-
Rule:MF_04081}.
SITE 150 151 Cleavage in virion (by viral protease).
{ECO:0000256|HAMAP-Rule:MF_04081}.
MOD_RES 96 96 Phosphothreonine; by host MAP4K1.
{ECO:0000256|HAMAP-Rule:MF_04081}.
MOD_RES 144 144 Phosphoserine; by host.
{ECO:0000256|HAMAP-Rule:MF_04081}.
MOD_RES 165 165 Phosphoserine; by host MAP4K1.
{ECO:0000256|HAMAP-Rule:MF_04081}.
MOD_RES 188 188 Phosphothreonine; by host.
{ECO:0000256|HAMAP-Rule:MF_04081}.
SEQUENCE 192 AA; 22716 MW; 64B6592EE0C72D52 CRC64;
MENKWQVMIV WQVDRMRIRT WNSIVKHHMY TSKKAKEWVY RHHYESQHPK VSSEVHIPLG
KAKLIIRTYW GLQTGEKDWH LGHGVSIEWR QRNYSTQIDP DLADKLIHLQ YFDCFSDSAI
RRAILGQVVR HRCEYPSGHN KVGSLQYLAL KALAAPKRIK PPLPSVKKLT EDRWNKPQKI
RGHKENPTMN GH


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