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Protein Vpu (U ORF protein) (Viral protein U)

 A0A1L5K1H2_9HIV1        Unreviewed;        81 AA.
A0A1L5K1H2;
15-MAR-2017, integrated into UniProtKB/TrEMBL.
15-MAR-2017, sequence version 1.
05-DEC-2018, entry version 19.
RecName: Full=Protein Vpu {ECO:0000256|HAMAP-Rule:MF_04082, ECO:0000256|RuleBase:RU364058};
AltName: Full=U ORF protein {ECO:0000256|HAMAP-Rule:MF_04082, ECO:0000256|RuleBase:RU364058};
AltName: Full=Viral protein U {ECO:0000256|HAMAP-Rule:MF_04082, ECO:0000256|RuleBase:RU364058};
Name=vpu {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058, ECO:0000313|EMBL:APO21923.1};
Human immunodeficiency virus 1.
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
NCBI_TaxID=11676 {ECO:0000313|EMBL:APO21923.1};
NCBI_TaxID=9606; Homo sapiens (Human).
[1] {ECO:0000313|EMBL:APO21923.1}
NUCLEOTIDE SEQUENCE.
Bui J.K., Sobolewski M.D., Keele B.F., Spindler J., Musick A.,
Wiegand A., Luke B.T., Shao W., Hughes S.H., Coffin J.M.,
Kearney M.F., Mellors J.W.;
"Proviruses with Identical Sequences Comprise a Large Fraction of the
Replication-Competent HIV Reservoir.";
Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:AQY58235.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Donor4.F6.2.3.p1a11 {ECO:0000313|EMBL:AQY58339.1},
Donor4.F6.2.3.p1a2 {ECO:0000313|EMBL:AQY58323.1},
Donor4.F6.2.3.p1a4 {ECO:0000313|EMBL:AQY58331.1},
Donor4.F6.2.3.p1e15 {ECO:0000313|EMBL:AQY58411.1},
Donor4.F6.2.3.p1e18 {ECO:0000313|EMBL:AQY58403.1},
Donor4.F6.2.3.p1e20 {ECO:0000313|EMBL:AQY58419.1},
Donor4.F6.2.3.p1e6 {ECO:0000313|EMBL:AQY58427.1},
Donor4.F6.2.3.p1e8 {ECO:0000313|EMBL:AQY58435.1},
Donor4.F6.2.3.p1f13 {ECO:0000313|EMBL:AQY58387.1},
Donor4.F6.2.3.p1g1 {ECO:0000313|EMBL:AQY58379.1},
Donor4.F6.2.3.p1h16 {ECO:0000313|EMBL:AQY58395.1},
Donor4.F6.2.3.p4b12 {ECO:0000313|EMBL:AQY58315.1},
Donor4.F6.2.3.p4b17 {ECO:0000313|EMBL:AQY58355.1},
Donor4.F6.2.3.p4b19 {ECO:0000313|EMBL:AQY58347.1},
Donor4.F6.2.3.p4b8 {ECO:0000313|EMBL:AQY58371.1},
Donor4.F6.2.3.p7a7 {ECO:0000313|EMBL:AQY58307.1},
Donor4.F6.2.3.p7b23 {ECO:0000313|EMBL:AQY58363.1},
Donor4.F6.2.p6a19 {ECO:0000313|EMBL:AQY58235.1},
Donor4.F6.2.p6a20 {ECO:0000313|EMBL:AQY58299.1},
Donor4.F6.2.p6b2 {ECO:0000313|EMBL:AQY58243.1},
Donor4.F6.2.p6b20 {ECO:0000313|EMBL:AQY58275.1},
Donor4.F6.2.p6b4 {ECO:0000313|EMBL:AQY58283.1},
Donor4.F6.2.p6c16 {ECO:0000313|EMBL:AQY58291.1},
Donor4.F6.2.p6c2 {ECO:0000313|EMBL:AQY58259.1}, and
Donor4.F6.2.p6d4 {ECO:0000313|EMBL:AQY58251.1};
Bui J.K., Sobolewski M.D., Keele B.F., Spindler J., Musick A.,
Wiegand A., Luke B.T., Shao W., Hughes S.H., Coffin J.M.,
Kearney M.F., Mellors J.W.;
"Clonal Proviruses Comprise a Large Fraction of the Replication-
Competent HIV Reservoir.";
Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Enhances virion budding by targeting host CD4 and
Tetherin/BST2 to proteasome degradation. Degradation of CD4
prevents any unwanted premature interactions between viral Env and
its host receptor CD4 in the endoplasmic reticulum. Degradation of
antiretroviral protein Tetherin/BST2 is important for virion
budding, as BST2 tethers new viral particles to the host cell
membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC,
a substrate recognition subunit of the Skp1/Cullin/F-box protein
E3 ubiquitin ligase, induces their ubiquitination and subsequent
proteasomal degradation. The alteration of the E3 ligase
specificity by Vpu seems to promote the degradation of host IKBKB,
leading to NF-kappa-B down-regulation and subsequent apoptosis.
Ion channel activity has also been suggested, however, formation
of cation-selective channel has been reconstituted ex-vivo in
lipid bilayers. It is thus unsure that this activity plays a role
in vivo. {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058}.
-!- ACTIVITY REGULATION: Ion channel activity is inhibited by
hexamethylene amiloride in vitro. {ECO:0000256|HAMAP-
Rule:MF_04082}.
-!- SUBUNIT: Forms pentamers or hexamers. Interacts with host CD4 and
BRTC; these interactions induce proteasomal degradation of CD4.
Interacts with host BST2; this interaction leads to the
degradation of host BST2. Interacts with host FBXW11. Interacts
with host AP1M1; this interaction plays a role in the
mistrafficking and subsequent degradation of host BST2.
{ECO:0000256|HAMAP-Rule:MF_04082}.
-!- SUBCELLULAR LOCATION: Host membrane {ECO:0000256|HAMAP-
Rule:MF_04082, ECO:0000256|RuleBase:RU364058}; Single-pass type I
membrane protein {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058}.
-!- DOMAIN: The N-terminal and transmembrane domains are required for
proper virion budding, whereas the cytoplasmic domain is required
for CD4 degradation. The cytoplasmic domain is composed of 2
amphipathic alpha helix. {ECO:0000256|HAMAP-Rule:MF_04082}.
-!- PTM: Phosphorylated by host CK2. This phosphorylation is necessary
for interaction with human BTRC and degradation of CD4.
{ECO:0000256|HAMAP-Rule:MF_04082}.
-!- 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_04082}.
-!- SIMILARITY: Belongs to the HIV-1 VPU protein family.
{ECO:0000256|HAMAP-Rule:MF_04082, ECO:0000256|RuleBase:RU364058}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; KY057570; APO21891.1; -; Genomic_RNA.
EMBL; KY057572; APO21907.1; -; Genomic_RNA.
EMBL; KY057573; APO21915.1; -; Genomic_RNA.
EMBL; KY057574; APO21923.1; -; Genomic_RNA.
EMBL; KY057575; APO21931.1; -; Genomic_RNA.
EMBL; KY057576; APO21939.1; -; Genomic_RNA.
EMBL; KY057577; APO21947.1; -; Genomic_RNA.
EMBL; KY057578; APO21955.1; -; Genomic_RNA.
EMBL; KY748393; AQY58235.1; -; Genomic_RNA.
EMBL; KY748394; AQY58243.1; -; Genomic_RNA.
EMBL; KY748395; AQY58251.1; -; Genomic_RNA.
EMBL; KY748396; AQY58259.1; -; Genomic_RNA.
EMBL; KY748398; AQY58275.1; -; Genomic_RNA.
EMBL; KY748399; AQY58283.1; -; Genomic_RNA.
EMBL; KY748400; AQY58291.1; -; Genomic_RNA.
EMBL; KY748401; AQY58299.1; -; Genomic_RNA.
EMBL; KY748402; AQY58307.1; -; Genomic_RNA.
EMBL; KY748403; AQY58315.1; -; Genomic_RNA.
EMBL; KY748404; AQY58323.1; -; Genomic_RNA.
EMBL; KY748405; AQY58331.1; -; Genomic_RNA.
EMBL; KY748406; AQY58339.1; -; Genomic_RNA.
EMBL; KY748407; AQY58347.1; -; Genomic_RNA.
EMBL; KY748408; AQY58355.1; -; Genomic_RNA.
EMBL; KY748409; AQY58363.1; -; Genomic_RNA.
EMBL; KY748410; AQY58371.1; -; Genomic_RNA.
EMBL; KY748411; AQY58379.1; -; Genomic_RNA.
EMBL; KY748412; AQY58387.1; -; Genomic_RNA.
EMBL; KY748413; AQY58395.1; -; Genomic_RNA.
EMBL; KY748414; AQY58403.1; -; Genomic_RNA.
EMBL; KY748415; AQY58411.1; -; Genomic_RNA.
EMBL; KY748416; AQY58419.1; -; Genomic_RNA.
EMBL; KY748417; AQY58427.1; -; Genomic_RNA.
EMBL; KY748418; AQY58435.1; -; Genomic_RNA.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0005261; F:cation channel activity; IEA:UniProtKB-UniRule.
GO; GO:0042609; F:CD4 receptor binding; IEA:UniProtKB-UniRule.
GO; GO:0032801; P:receptor catabolic process; IEA:UniProtKB-UniRule.
GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-UniRule.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-UniRule.
GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
Gene3D; 1.10.195.10; -; 1.
HAMAP; MF_04082; HIV_VPU; 1.
InterPro; IPR008187; Vpu.
InterPro; IPR009032; Vpu_cyt_dom_sf.
Pfam; PF00558; Vpu; 1.
SUPFAM; SSF57647; SSF57647; 1.
3: Inferred from homology;
Apoptosis {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04082};
Inhibition of host innate immune response by virus {ECO:0000256|HAMAP-
Rule:MF_04082};
Inhibition of host interferon signaling pathway by virus
{ECO:0000256|HAMAP-Rule:MF_04082};
Inhibition of host tetherin by virus {ECO:0000256|HAMAP-
Rule:MF_04082};
Ion channel {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058};
Ion transport {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058};
Membrane {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04082};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058};
Transport {ECO:0000256|HAMAP-Rule:MF_04082,
ECO:0000256|RuleBase:RU364058};
Viral immunoevasion {ECO:0000256|HAMAP-Rule:MF_04082}.
TOPO_DOM 1 4 Extracellular. {ECO:0000256|HAMAP-
Rule:MF_04082}.
TRANSMEM 6 28 Helical. {ECO:0000256|RuleBase:RU364058}.
TOPO_DOM 29 81 Cytoplasmic. {ECO:0000256|HAMAP-
Rule:MF_04082}.
MOD_RES 53 53 Phosphoserine; by host CK2.
{ECO:0000256|HAMAP-Rule:MF_04082}.
MOD_RES 57 57 Phosphoserine; by host CK2.
{ECO:0000256|HAMAP-Rule:MF_04082}.
SEQUENCE 81 AA; 9086 MW; CAAF0E8A6DEC22E5 CRC64;
MQSLTILAIV ALVVAAILAI VVWTIVLIEY RKILRQRKID KLLSRIAERA EDSGNESDGD
QEELSTLVDM GHLAPWDIED L


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Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
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Related Genes :
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu env] Multifunctional fusion protein [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)] [Includes: Envelope glycoprotein gp160 (Env polyprotein); Protein Vpu (U ORF protein) (Viral protein U)]
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag] Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]
[POL RR33_62180gpPOL RR33_62181gpPOL] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[HNRNPU C1orf199 HNRPU SAFA U21.1] Heterogeneous nuclear ribonucleoprotein U (hnRNP U) (GRIP120) (Nuclear p120 ribonucleoprotein) (Scaffold-attachment factor A) (SAF-A) (p120) (pp120)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] Genome polyprotein [Cleaved into: P1 proteinase (N-terminal protein) (EC 3.4.-.-); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[U2AF1L4 U2AF1-RS3 U2AF1L3] Splicing factor U2AF 26 kDa subunit (U2 auxiliary factor 26) (U2 small nuclear RNA auxiliary factor 1-like protein 4) (U2AF1-like 4) (U2(RNU2) small nuclear RNA auxiliary factor 1-like protein 3) (U2 small nuclear RNA auxiliary factor 1-like protein 3) (U2AF1-like protein 3)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)

Bibliography :
[15165822] Fusion of the upstream vpu sequences to the env of simian human immunodeficiency virus (SHIV(KU-1bMC33)) results in the synthesis of two envelope precursor proteins, increased numbers of virus particles associated with the cell surface and is pathogenic for pig-tailed macaques.
[12885901] Feline immunodeficiency virus ORF-Ais required for virus particle formation and virus infectivity.
[1729599] Mechanism of translation of monocistronic and multicistronic human immunodeficiency virus type 1 mRNAs.
[3043230] Identification of a protein encoded by the vpu gene of HIV-1.