Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 116 (12 Aug 2020)
Sequence version 1 (01 Oct 1989)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Virion infectivity factor

Gene

vif

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.UniRule annotation1 Publication

Miscellaneous

The infectious clone pNL4-3 is a chimeric provirus that consists of DNA from HIV isolates NY5 (5' half) and BRU (3' half).
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.UniRule annotation
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).UniRule annotation
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.UniRule annotation

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding
Biological processHost-virus interaction, Ubl conjugation pathway

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Virion infectivity factorUniRule annotation
Short name:
VifUniRule annotation
Alternative name(s):
SOR proteinUniRule annotation
Cleaved into the following 2 chains:
p17UniRule annotation
p7UniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:vifUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri11698 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesOrterviralesRetroviridaeOrthoretrovirinaeLentivirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host cytoplasm, Host membrane, Membrane, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi5 – 6WQ → AA: 44% loss of viral infectivity. 1 Publication2
Mutagenesisi12 – 13QV → AA: No effect on viral infectivity. 1 Publication2
Mutagenesisi16 – 18MRI → AAA: 29% loss of viral infectivity. 1 Publication3
Mutagenesisi23 – 24RL → AA: 14% loss of viral infectivity. 1 Publication2
Mutagenesisi29 – 31MYI → AAV: 59% loss of viral infectivity. 1 Publication3
Mutagenesisi33 – 34RK → AA: 35% loss of viral infectivity. 1 Publication2
Mutagenesisi38 – 40WFY → AAA: 94% loss of viral infectivity. 1 Publication3
Mutagenesisi43 – 44HY → AA: 95% loss of viral infectivity. 1 Publication2
Mutagenesisi53 – 54SE → AA: 39% loss of viral infectivity. 1 Publication2
Mutagenesisi58 – 59PL → AA: 45% loss of viral infectivity. 1 Publication2
Mutagenesisi69 – 70YW → AA: 97% loss of viral infectivity. 1 Publication2
Mutagenesisi73 – 74HT → AA: No effect onviral infectivity. 1 Publication2
Mutagenesisi80 – 81HL → AA: 19% loss of viral infectivity. 1 Publication2
Mutagenesisi86 – 87SI → AA: 42% loss of viral infectivity. 1 Publication2
Mutagenesisi90 – 92RKK → AAA: No effect on viral infectivity. 1 Publication3
Mutagenesisi97 – 98QV → AA: 27% loss of viral infectivity. 1 Publication2
Mutagenesisi105 – 107QLI → AAV: 98% loss of viral infectivity. 1 Publication3
Mutagenesisi108H → L: Complete loss of interaction with CUL5. 1 Publication1
Mutagenesisi111 – 112YF → AA: 93% loss of viral infectivity. 1 Publication2
Mutagenesisi114C → S: 98% loss of viral infectivity. Complete loss of interaction with CUL5. 3 Publications1
Mutagenesisi121 – 123RNT → AAA: 35% increase of viral infectivity. 1 Publication3
Mutagenesisi127 – 128RI → AA: 10% loss of viral infectivity. 1 Publication2
Mutagenesisi133C → S: 95% loss of viral infectivity. Complete loss of interaction with CUL5. 3 Publications1
Mutagenesisi135 – 136YQ → AA: 73% loss of viral infectivity. 1 Publication2
Mutagenesisi139H → L: Complete loss of interaction with CUL5. 1 Publication1
Mutagenesisi140 – 141NK → AA: 68% loss of viral infectivity. 1 Publication2
Mutagenesisi144 – 146SLQ → AAA: 93% loss of viral infectivity. 1 Publication3
Mutagenesisi144S → A: 25% loss of interaction with CUL5y. 1 Publication1
Mutagenesisi145L → A: Complete loss of interaction with CUL5. 1 Publication1
Mutagenesisi146Q → A: 90% loss of interaction with CUL5. 1 Publication1
Mutagenesisi147 – 148YL → AA: 40% loss of viral infectivity. 1 Publication2
Mutagenesisi147Y → A: 40% loss of interaction with CUL5. 1 Publication1
Mutagenesisi148L → A: 35% loss of interaction with CUL5. 1 Publication1
Mutagenesisi149 – 151ALA → RKS: Complete loss of processing between p17 and p7. Complete loss of replication. 1 Publication3
Mutagenesisi149A → G: 75% loss of CUL5 binding activity. 1 Publication1
Mutagenesisi150L → A: 90% loss of CUL5 binding activity. 1 Publication1
Mutagenesisi151A → E: No effect on processing between p17 and p7. 1
Mutagenesisi151A → N: Slightly increased processing between p17 and p7. 1
Mutagenesisi151A → P: Increased processing between p17 and p7. 1
Mutagenesisi151A → Y: Partial loss of processing between p17 and p7. 1
Mutagenesisi156 – 158PKQ → AAA: No effect on viral infectivity. 1 Publication3
Mutagenesisi157K → A: No effect viral infectivity. 1 Publication1
Mutagenesisi158 – 160QIK → AAA: 9% loss of viral infectivity. 1 Publication3
Mutagenesisi160K → A: 33% loss of viral infectivity. 1
Mutagenesisi161 – 164PPLP → APLA: 88% loss of viral infectivity. 1 Publication4
Mutagenesisi161 – 163PPL → AAA: 97% loss of viral infectivity. 3
Mutagenesisi161P → A: 27% loss of viral infectivity. 1
Mutagenesisi162P → A: No effect viral infectivity. 1
Mutagenesisi163L → A: 26% loss of viral infectivity. 1
Mutagenesisi164P → A: 63% loss of viral infectivity. 1
Mutagenesisi165S → A: 67% loss of viral infectivity. 1 Publication1
Mutagenesisi166V → A: 20% loss of viral infectivity. 1 Publication1
Mutagenesisi169 – 170LT → AA: 42% loss of viral infectivity. 1 Publication2
Mutagenesisi180 – 181TK → AA: 5% loss of viral infectivity. 1 Publication2
Mutagenesisi189 – 190MN → AA: 4% loss of viral infectivity. 1 Publication2

Keywords - Diseasei

AIDS

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000427621 – 192Virion infectivity factorUniRule annotationAdd BLAST192
ChainiPRO_00004410791 – 150p17UniRule annotationAdd BLAST150
ChainiPRO_0000441080151 – 192p7UniRule annotationAdd BLAST42

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei96Phosphothreonine; by host MAP4K1UniRule annotation1
Modified residuei144Phosphoserine; by hostUniRule annotation1
Modified residuei165Phosphoserine; by host MAP4K1UniRule annotation1
Modified residuei188Phosphothreonine; by hostUniRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Highly phosphorylated on serine and threonine residues. Thr-96 and Ser-165 are phosphorylated by the mitogen activated kinase MAP4K1. As the HIV-1 replication can be activated by stress and mitogens, these phosphorylations could be involved in this process. Ser-144 phosphorylation may inhibit elongin BC complex binding.1 Publication
Processed in virion by the viral protease.UniRule annotation
Highly phosphorylated on serine and threonine residues.UniRule annotation
Polyubiquitinated and degraded by the proteasome in the presence of APOBEC3G.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei150 – 151Cleavage in virion (by viral protease)UniRule annotation2

Keywords - PTMi

Phosphoprotein, Ubl conjugation

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expressed late during infection in a Rev-dependent manner.UniRule annotation1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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.

UniRule annotation

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P12504

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P12504

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni14 – 17Interaction with host APOBEC3F; F1-boxUniRule annotation4
Regioni40 – 44Interaction with host APOBEC3G; G-boxUniRule annotation5
Regioni54 – 72Interaction with host APOBEC3F and APOBEC3G; FG-boxUniRule annotationAdd BLAST19
Regioni74 – 79Interaction with host APOBEC3F; F2-boxUniRule annotation6
Regioni75 – 114RNA-bindingUniRule annotationAdd BLAST40
Regioni151 – 164MultimerizationUniRule annotationAdd BLAST14
Regioni171 – 172Membrane associationUniRule annotation2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi108 – 139HCCH motifUniRule annotationAdd BLAST32
Motifi144 – 153BC-box-like motifUniRule annotation10

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The BC-like-box motif mediates the interaction with elongin BC complex.UniRule annotation
The HCCH motif (H-x5-C-x(18)-C-x5-H) mediates the interaction with CUL5.UniRule annotation

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the primate lentivirus group Vif protein family.UniRule annotationCurated

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_04081, HIV_VIF, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000475, Vif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00559, Vif, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00349, VIRIONINFFCT

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P12504-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MENRWQVMIV WQVDRMRINT WKRLVKHHMY ISRKAKDWFY RHHYESTNPK
60 70 80 90 100
ISSEVHIPLG DAKLVITTYW GLHTGERDWH LGQGVSIEWR KKRYSTQVDP
110 120 130 140 150
DLADQLIHLH YFDCFSESAI RNTILGRIVS PRCEYQAGHN KVGSLQYLAL
160 170 180 190
AALIKPKQIK PPLPSVRKLT EDRWNKPQKT KGHRGSHTMN GH
Length:192
Mass (Da):22,699
Last modified:October 1, 1989 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2830B3233E8ECD16
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti90 – 93RKKR → KKRK in strain: Clinical isolate; from an asymptomatic patient; Vif is mislocalized to the nucleus and non functional. 4

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M19921 Genomic RNA Translation: AAA44989.1
M38431 Genomic RNA Translation: AAB04038.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19921 Genomic RNA Translation: AAA44989.1
M38431 Genomic RNA Translation: AAB04038.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MA9NMR-A139-174[»]
3DCGX-ray2.40E/F139-176[»]
4N9FX-ray3.301/2/7/G/M/S/b/d/j/p/q/v1-176[»]
6NILelectron microscopy3.90C/F/I/L1-113[»]
C/F/I/L158-176[»]
SMRiP12504
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-36069N
IntActiP12504, 29 interactors

Chemistry databases

BindingDBiP12504

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P12504, 1 sequenced antibody

Miscellaneous databases

EvolutionaryTraceiP12504

Family and domain databases

HAMAPiMF_04081, HIV_VIF, 1 hit
InterProiView protein in InterPro
IPR000475, Vif
PfamiView protein in Pfam
PF00559, Vif, 1 hit
PRINTSiPR00349, VIRIONINFFCT

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVIF_HV1N5
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P12504
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: August 12, 2020
This is version 116 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again