Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]

 NEF_HV1H2               Reviewed;         206 AA.
P04601; O09780; Q85587;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 5.
30-AUG-2017, entry version 142.
RecName: Full=Protein Nef {ECO:0000255|HAMAP-Rule:MF_04078};
AltName: Full=3'ORF {ECO:0000255|HAMAP-Rule:MF_04078};
AltName: Full=Negative factor {ECO:0000255|HAMAP-Rule:MF_04078};
Short=F-protein {ECO:0000255|HAMAP-Rule:MF_04078};
Contains:
RecName: Full=C-terminal core protein {ECO:0000255|HAMAP-Rule:MF_04078};
Name=nef {ECO:0000255|HAMAP-Rule:MF_04078};
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
(HIV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11706;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2999715; DOI=10.1093/nar/13.22.8219;
Ratner L., Starcich B.R., Josephs S.F., Hahn B.H., Reddy E.P.,
Livak K.J., Petteway S.R. Jr., Pearson M.L., Haseltine W.A.,
Arya S.K., Wong-staal F.;
"Polymorphism of the 3' open reading frame of the virus associated
with the acquired immune deficiency syndrome, human T-lymphotropic
virus type III.";
Nucleic Acids Res. 13:8219-8229(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3040055; DOI=10.1089/aid.1987.3.57;
Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S.,
Gallo R.C., Wong-Staal F.;
"Complete nucleotide sequences of functional clones of the AIDS
virus.";
AIDS Res. Hum. Retroviruses 3:57-69(1987).
[3]
SEQUENCE REVISION.
Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S.,
Gallo R.C., Wong-Staal F.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[4]
INDUCTION.
PubMed=1707154;
Hewlett I.K., Geyer S.J., Hawthorne C.A., Ruta M., Epstein J.S.;
"Kinetics of early HIV-1 gene expression in infected H9 cells assessed
by PCR.";
Oncogene 6:491-493(1991).
[5]
FUNCTION, AND DILEUCINE MOTIF.
STRAIN=Isolate HXB2-R7;
PubMed=8124721; DOI=10.1016/0092-8674(94)90360-3;
Aiken C., Konner J., Landau N.R., Lenburg M.E., Trono D.;
"Nef induces CD4 endocytosis: requirement for a critical dileucine
motif in the membrane-proximal CD4 cytoplasmic domain.";
Cell 76:853-864(1994).
[6]
FUNCTION.
PubMed=9450757; DOI=10.1038/34929;
Collins K.L., Chen B.K., Kalams S.A., Walker B.D., Baltimore D.;
"HIV-1 Nef protein protects infected primary cells against killing by
cytotoxic T lymphocytes.";
Nature 391:397-401(1998).
[7]
FUNCTION.
STRAIN=Isolate HXB2-R7;
PubMed=9971776;
Mangasarian A., Piguet V., Wang J.-K., Chen Y.-L., Trono D.;
"Nef-induced CD4 and major histocompatibility complex class I (MHC-I)
down-regulation are governed by distinct determinants: N-terminal
alpha helix and proline repeat of Nef selectively regulate MHC-I
trafficking.";
J. Virol. 73:1964-1973(1999).
[8]
FUNCTION, INTERACTION WITH HOST PACS1, AND SUBCELLULAR LOCATION.
STRAIN=Isolate HXB2-R7;
PubMed=10707087; DOI=10.1038/35004038;
Piguet V., Wan L., Borel C., Mangasarian A., Demaurex N., Thomas G.,
Trono D.;
"HIV-1 Nef protein binds to the cellular protein PACS-1 to
downregulate class I major histocompatibility complexes.";
Nat. Cell Biol. 2:163-167(2000).
[9]
FUNCTION.
PubMed=11593029; DOI=10.1073/pnas.221256498;
Stumptner-Cuvelette P., Morchoisne S., Dugast M., Le Gall S.,
Raposo G., Schwartz O., Benaroch P.;
"HIV-1 Nef impairs MHC class II antigen presentation and surface
expression.";
Proc. Natl. Acad. Sci. U.S.A. 98:12144-12149(2001).
[10]
FUNCTION, MUTAGENESIS OF MET-20; 63-GLU--GLU-65; PRO-72 AND PRO-75,
AND REGION ACIDIC.
STRAIN=Isolate HXB2D;
PubMed=12526811; DOI=10.1016/S0092-8674(02)01162-5;
Blagoveshchenskaya A.D., Thomas L., Feliciangeli S.F., Hung C.-H.,
Thomas G.;
"HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6
endocytic pathway.";
Cell 111:853-866(2002).
[11]
IDENTIFICATION IN A AP1-NEF-MHC-I COMPLEX.
PubMed=15569716; DOI=10.1083/jcb.200407031;
Roeth J.F., Williams M., Kasper M.R., Filzen T.M., Collins K.L.;
"HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I
cytoplasmic tail.";
J. Cell Biol. 167:903-913(2004).
[12]
ACIDIC REGION, INTERACTION WITH HOST PACS1, AND MUTAGENESIS OF
62-GLU--GLU-65.
PubMed=18653452; DOI=10.1128/JVI.00107-08;
Baugh L.L., Garcia J.V., Foster J.L.;
"Functional characterization of the human immunodeficiency virus type
1 Nef acidic domain.";
J. Virol. 82:9657-9667(2008).
[13]
INTERACTION WITH HOST PACS2, INTERACTION WITH HOST PACS1, AND
MUTAGENESIS OF 62-GLU--GLU-65.
PubMed=18296443; DOI=10.1074/jbc.M707572200;
Atkins K.M., Thomas L., Youker R.T., Harriff M.J., Pissani F., You H.,
Thomas G.;
"HIV-1 Nef binds PACS-2 to assemble a multikinase cascade that
triggers major histocompatibility complex class I (MHC-I) down-
regulation: analysis using short interfering RNA and knock-out mice.";
J. Biol. Chem. 283:11772-11784(2008).
[14]
FUNCTION, AND IDENTIFICATION IN A AP1(MU)-NEF-MHC-I COMPLEX.
PubMed=18073204; DOI=10.1074/jbc.M707760200;
Wonderlich E.R., Williams M., Collins K.L.;
"The tyrosine binding pocket in the adaptor protein 1 (AP-1) mu1
subunit is necessary for Nef to recruit AP-1 to the major
histocompatibility complex class I cytoplasmic tail.";
J. Biol. Chem. 283:3011-3022(2008).
[15]
CLEAVAGE BY VIRAL PROTEASE.
PubMed=18987145; DOI=10.1128/JVI.01633-08;
Laguette N., Benichou S., Basmaciogullari S.;
"Human immunodeficiency virus type 1 Nef incorporation into virions
does not increase infectivity.";
J. Virol. 83:1093-1104(2009).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19912576; DOI=10.1111/j.1600-0854.2009.01006.x;
Lenassi M., Cagney G., Liao M., Vaupotic T., Bartholomeeusen K.,
Cheng Y., Krogan N.J., Plemenitas A., Peterlin B.M.;
"HIV Nef is secreted in exosomes and triggers apoptosis in bystander
CD4(+) T cells.";
Traffic 11:110-122(2010).
[17]
FUNCTION, AND IDENTIFICATION IN A AP1(MU)-NEF-MHC-I COMPLEX.
PubMed=20020046; DOI=10.1371/journal.pone.0008364;
Singh R.K., Lau D., Noviello C.M., Ghosh P., Guatelli J.C.;
"An MHC-I cytoplasmic domain/HIV-1 Nef fusion protein binds directly
to the mu subunit of the AP-1 endosomal coat complex.";
PLoS ONE 4:E8364-E8364(2009).
[18] {ECO:0000244|PDB:4NEE}
X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 63-203, INTERACTION WITH
HOST AP2 SUBUNIT ALPHA, AND INTERACTION WITH HOST AP2 SUBUNIT SIGMA2.
PubMed=24473078; DOI=10.7554/eLife.01754;
Ren X., Park S.Y., Bonifacino J.S., Hurley J.H.;
"How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate
CD4.";
Elife 3:E01754-E01754(2014).
-!- FUNCTION: Factor of infectivity and pathogenicity, required for
optimal virus replication. Alters numerous pathways of T-
lymphocytes function and down-regulates immunity surface molecules
in order to evade host defense and increase viral infectivity.
Alters the functionality of other immunity cells, like dendritic
cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-
Rule:MF_04078, ECO:0000269|PubMed:9450757}.
-!- FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the
surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules.
Mediates internalization and degradation of host CD4 through the
interaction of with the cytoplasmic tail of CD4, the recruitment
of AP-2 (clathrin adapter protein complex 2), internalization
through clathrin coated pits, and subsequent transport to
endosomes and lysosomes for degradation. Diverts host MHC-I
molecules to the trans-Golgi network-associated endosomal
compartments by an endocytic pathway to finally target them for
degradation. MHC-I down-regulation may involve AP-1 (clathrin
adapter protein complex 1) or possibly Src family kinase-
ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected
cells are masked for immune recognition by cytotoxic T-
lymphocytes. Decreasing the number of immune receptors also
prevents reinfection by more HIV particles (superinfection). Down-
regulates host SERINC3 and SERINC5 thereby excluding these
proteins from the viral particles. Virion infectivity is
drastically higher when SERINC3 or SERINC5 are excluded from the
viral envelope, because these host antiviral proteins impare the
membrane fusion event necessary for subsequent virion penetration.
{ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:12526811,
ECO:0000269|PubMed:24473078, ECO:0000269|PubMed:8124721}.
-!- FUNCTION: Bypasses host T-cell signaling by inducing a
transcriptional program nearly identical to that of anti-CD3 cell
activation. Interaction with TCR-zeta chain up-regulates the Fas
ligand (FasL). Increasing surface FasL molecules and decreasing
surface MHC-I molecules on infected CD4(+) cells send attacking
cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-
Rule:MF_04078}.
-!- FUNCTION: Plays a role in optimizing the host cell environment for
viral replication without causing cell death by apoptosis.
Protects the infected cells from apoptosis in order to keep them
alive until the next virus generation is ready to strike. Inhibits
the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1.
Decreases the half-life of TP53, protecting the infected cell
against p53-mediated apoptosis. Inhibits the apoptotic signals
regulated by the Bcl-2 family proteins through the formation of a
Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and
induces phosphorylation of Bad. {ECO:0000255|HAMAP-Rule:MF_04078}.
-!- FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes
for apoptosis by interacting with CXCR4 surface receptors.
{ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:19912576}.
-!- SUBUNIT: Monomer; cytosolic form. Homodimer; membrane bound form.
Interacts with Nef associated p21-activated kinase (PAK2); this
interaction activates PAK2. Associates with the Nef-MHC-I-AP1
complex; this complex is required for MHC-I internalization.
Interacts (via C-terminus) with host PI3-kinase. Interacts with
host PACS1; this interaction seems to be weak. Interacts with host
PACS2. Interacts with host LCK and MAPK3; these interactions
inhibit the kinase activity of the latters. Interacts with host
ATP6V1H; this interaction may play a role in CD4 endocytosis.
Associates with the CD4-Nef-AP2 complex; this complex is required
for CD4 internalization. Interacts with host AP2 subunit alpha and
AP2 subunit sigma2. Interacts with TCR-zeta chain; this
interaction up-regulates the Fas ligand (FasL) surface expression.
Interacts with host HCK, LYN, and SRC; these interactions activate
the Src family kinases. Interacts with MAP3K5; this interaction
inhibits the Fas and TNFR-mediated death signals. Interacts with
beta-COP and PTE1. Interacts with human RACK1; this increases Nef
phosphorylation by PKC. Interacts with TP53; this interaction
decreases the half-life of TP53, protecting the infected cell
against p53-mediated apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078,
ECO:0000269|PubMed:10707087, ECO:0000269|PubMed:15569716,
ECO:0000269|PubMed:18073204, ECO:0000269|PubMed:18296443,
ECO:0000269|PubMed:18653452, ECO:0000269|PubMed:20020046,
ECO:0000269|PubMed:24473078}.
-!- INTERACTION:
O14734:ACOT8 (xeno); NbExp=7; IntAct=EBI-6164028, EBI-1237371;
-!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-
Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078};
Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion
{ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-
Rule:MF_04078, ECO:0000269|PubMed:19912576}. Host Golgi apparatus
membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization
requires PACS1. Associates with the inner plasma membrane through
its N-terminal domain. Nef stimulates its own export via the
release of exosomes. Incorporated in virions at a rate of about 10
molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-
Rule:MF_04078, ECO:0000269|PubMed:19912576}.
-!- INDUCTION: Expressed early in the viral replication cycle.
{ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:1707154}.
-!- DOMAIN: The dileucine internalization motif and a diacidic motif
seem to be required for binding to AP-2. {ECO:0000255|HAMAP-
Rule:MF_04078}.
-!- DOMAIN: The acidic region binds to the sorting protein PACS-2,
which targets Nef to the paranuclear region, enabling the PxxP
motif to direct assembly of an SFK/ZAP-70/PI3K complex that
accelerates endocytosis of cell-surface MHC-I. {ECO:0000255|HAMAP-
Rule:MF_04078, ECO:0000269|PubMed:12526811}.
-!- DOMAIN: The N-terminal domain is composed of the N-myristoyl
glycine and of a cluster of positively charged amino acids. It is
required for inner plasma membrane targeting of Nef and virion
incorporation, and thereby for infectivity. This domain is also
involved in binding to TP53. {ECO:0000255|HAMAP-Rule:MF_04078}.
-!- DOMAIN: The SH3-binding domain constituted of PxxP motifs mediates
binding to several Src family proteins thereby regulating their
tyrosine kinase activity. The same motifs also mediates the
association with MAPK3, PI3-kinase and TCR-zeta.
{ECO:0000255|HAMAP-Rule:MF_04078}.
-!- PTM: Phosphorylated on serine residues, probably by host PKCdelta
and theta. {ECO:0000255|HAMAP-Rule:MF_04078}.
-!- PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.
-!- PTM: The virion-associated Nef proteins are cleaved by the viral
protease to release the soluble C-terminal core protein. Nef is
probably cleaved concomitantly with viral structural proteins on
maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.
-!- 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:0000255|HAMAP-Rule:MF_04078}.
-!- SIMILARITY: Belongs to the lentivirus primate group Nef protein
family. {ECO:0000255|HAMAP-Rule:MF_04078}.
-!- SEQUENCE CAUTION:
Sequence=AAB50263.1; Type=Miscellaneous discrepancy; Note=Readthrough of a premature stop codon in position 123 that truncates the Nef protein. The sequence displayed is that of wild-type full-length HXB2-R7 clone.; Evidence={ECO:0000305};
Sequence=AAC82597.1; Type=Miscellaneous discrepancy; Note=Readthrough of a premature stop codon in position 123 that truncates the Nef protein. The sequence displayed is that of wild-type full-length HXB2-R7 clone.; Evidence={ECO:0000305};
Sequence=CAA26946.1; Type=Miscellaneous discrepancy; Note=Readthrough of a premature stop codon in position 123 that truncates the Nef protein. The sequence displayed is that of wild-type full-length HXB2-R7 clone.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=Nef
entry;
URL="http://www.bioafrica.net/proteomics/NEFprot.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X03187; CAA26946.1; ALT_SEQ; Genomic_RNA.
EMBL; K03455; AAB50263.1; ALT_SEQ; Genomic_RNA.
EMBL; AF033819; AAC82597.1; ALT_SEQ; Genomic_RNA.
RefSeq; NP_057857.2; NC_001802.1.
PDB; 3RL2; X-ray; 2.39 A; C=73-82.
PDB; 4NEE; X-ray; 2.88 A; C/E/H/K=63-203.
PDB; 4WU5; X-ray; 2.40 A; C/F=134-141.
PDB; 4WU7; X-ray; 2.30 A; C/F=136-141.
PDB; 5HGA; X-ray; 2.20 A; C/F=136-141.
PDB; 5HGB; X-ray; 2.40 A; C/F/I/L=134-141.
PDB; 5HGD; X-ray; 2.07 A; C/F=136-142.
PDB; 5HGH; X-ray; 2.39 A; C=134-142.
PDBsum; 3RL2; -.
PDBsum; 4NEE; -.
PDBsum; 4WU5; -.
PDBsum; 4WU7; -.
PDBsum; 5HGA; -.
PDBsum; 5HGB; -.
PDBsum; 5HGD; -.
PDBsum; 5HGH; -.
SMR; P04601; -.
BioGrid; 1205545; 70.
DIP; DIP-61724N; -.
ELM; P04601; -.
IntAct; P04601; 9.
GeneID; 156110; -.
KEGG; vg:156110; -.
OrthoDB; VOG090000RB; -.
Reactome; R-HSA-162585; Uncoating of the HIV Virion.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-162599; Late Phase of HIV Life Cycle.
Reactome; R-HSA-164939; Nef mediated downregulation of CD28 cell surface expression.
Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
Reactome; R-HSA-164944; Nef and signal transduction.
Reactome; R-HSA-167590; Nef Mediated CD4 Down-regulation.
Reactome; R-HSA-173107; Binding and entry of HIV virion.
Reactome; R-HSA-175474; Assembly Of The HIV Virion.
Reactome; R-HSA-182218; Nef Mediated CD8 Down-regulation.
Proteomes; UP000002241; Genome.
Proteomes; UP000105453; Genome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:InterPro.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0030260; P:entry into host cell; TAS:Reactome.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0006499; P:N-terminal protein myristoylation; TAS:Reactome.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:0039504; P:suppression by virus of host adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0046776; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
GO; GO:0039505; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class II; IEA:UniProtKB-KW.
GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
Gene3D; 3.30.62.10; -; 1.
Gene3D; 4.10.890.10; -; 1.
HAMAP; MF_04078; NEF_HIV; 1.
InterPro; IPR027480; HIV-1_Nef_anchor.
InterPro; IPR027481; HIV-1_Nef_core.
InterPro; IPR001558; HIV_Nef.
Pfam; PF00469; F-protein; 1.
SUPFAM; SSF55671; SSF55671; 1.
1: Evidence at protein level;
3D-structure; AIDS; Apoptosis; Complete proteome; Early protein;
Host cell membrane; Host Golgi apparatus; Host membrane;
Host-virus interaction;
Inhibition of host adaptive immune response by virus;
Inhibition of host autophagy by virus;
Inhibition of host MHC class I molecule presentation by virus;
Inhibition of host MHC class II molecule presentation by virus;
Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome;
Secreted; SH3-binding; Viral immunoevasion; Virion; Virulence.
INIT_MET 1 1 Removed; by host. {ECO:0000255|HAMAP-
Rule:MF_04078}.
CHAIN 2 206 Protein Nef. {ECO:0000255|HAMAP-
Rule:MF_04078}.
/FTId=PRO_0000038365.
CHAIN 58 206 C-terminal core protein.
{ECO:0000255|HAMAP-Rule:MF_04078}.
/FTId=PRO_0000038366.
REGION 62 65 Acidic; interacts with host PACS1 and
PACS2; stabilizes the interaction of
NEF/MHC-I with host AP1M1; necessary for
MHC-I internalization.
{ECO:0000255|HAMAP-Rule:MF_04078,
ECO:0000269|PubMed:10707087,
ECO:0000269|PubMed:12526811}.
REGION 69 78 SH3-binding; interaction with Src family
tyrosine kinases. {ECO:0000255|HAMAP-
Rule:MF_04078}.
REGION 108 124 Mediates dimerization, Nef-PTE1
interaction. {ECO:0000255|HAMAP-
Rule:MF_04078}.
REGION 148 180 Binding to ATP6V1H. {ECO:0000255|HAMAP-
Rule:MF_04078}.
MOTIF 72 75 PxxP; stabilizes the interaction of
NEF/MHC-I with host AP1M1; necessary for
MHC-I internalization.
{ECO:0000255|HAMAP-Rule:MF_04078,
ECO:0000269|PubMed:12526811}.
MOTIF 164 165 Dileucine internalization motif;
necessary for CD4 internalization.
{ECO:0000255|HAMAP-Rule:MF_04078,
ECO:0000269|PubMed:8124721}.
MOTIF 174 175 Diacidic; necessary for CD4
internalization. {ECO:0000255|HAMAP-
Rule:MF_04078}.
SITE 20 20 Might play a role in AP-1 recruitment to
the Nef-MHC-I complex.
{ECO:0000255|HAMAP-Rule:MF_04078,
ECO:0000269|PubMed:18073204}.
SITE 57 58 Cleavage; by viral protease.
{ECO:0000255|HAMAP-Rule:MF_04078}.
MOD_RES 6 6 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04078}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255|HAMAP-Rule:MF_04078}.
MUTAGEN 20 20 M->A: Complete loss of Nef-induced MHC-I
down-regulation, MHC-I is internalized
but not sequestred in TGN.
{ECO:0000269|PubMed:12526811}.
MUTAGEN 62 65 EEEE->AAAA: Complete loss of Nef-induced
MHC-I down-regulation, MHC-I is not
internalized. Reduced interaction with
host PACS1 and PACS2.
{ECO:0000269|PubMed:18296443,
ECO:0000269|PubMed:18653452}.
MUTAGEN 62 65 EEEE->AAEA: About 50% loss of Nef-induced
MHC-I down-regulation.
{ECO:0000269|PubMed:18296443,
ECO:0000269|PubMed:18653452}.
MUTAGEN 62 65 EEEE->AEAA: About 50% loss of Nef-induced
MHC-I down-regulation.
{ECO:0000269|PubMed:18296443,
ECO:0000269|PubMed:18653452}.
MUTAGEN 62 65 EEEE->DDDD: No effect on Nef-induced MHC-
I down-regulation.
{ECO:0000269|PubMed:18296443,
ECO:0000269|PubMed:18653452}.
MUTAGEN 62 64 EEE->AAA: About 50% loss of Nef-induced
MHC-I down-regulation.
MUTAGEN 62 63 EE->AA: Almost no effect on Nef-induced
MHC-I down-regulation.
MUTAGEN 63 65 EEE->AAA: About 50% loss of Nef-induced
MHC-I down-regulation.
{ECO:0000269|PubMed:12526811}.
MUTAGEN 63 64 EE->AA: Almost no effect on Nef-induced
MHC-I down-regulation.
MUTAGEN 64 65 EE->AA: Almost no effect on Nef-induced
MHC-I down-regulation.
MUTAGEN 72 72 P->A: Complete loss of Nef-induced MHC-I
down-regulation, MHC-I is not
internalized; when associated with A-75.
{ECO:0000269|PubMed:12526811}.
MUTAGEN 75 75 P->A: Complete loss of Nef-induced MHC-I
down-regulation, MHC-I is not
internalized; when associated with A-72.
{ECO:0000269|PubMed:12526811}.
MUTAGEN 123 123 D->E: Complete loss of Nef-induced MHC-I
down-regulation, CD4 down-regulation, and
enhancement of infectivity. Activates
PAK2 twofold over wild-type levels.
CONFLICT 29 29 R -> G (in Ref. 1; CAA26946).
{ECO:0000305}.
HELIX 81 94 {ECO:0000244|PDB:4NEE}.
HELIX 104 118 {ECO:0000244|PDB:4NEE}.
STRAND 130 132 {ECO:0000244|PDB:4NEE}.
STRAND 136 138 {ECO:0000244|PDB:4NEE}.
STRAND 143 147 {ECO:0000244|PDB:4NEE}.
HELIX 150 157 {ECO:0000244|PDB:4NEE}.
HELIX 167 170 {ECO:0000244|PDB:4NEE}.
STRAND 172 175 {ECO:0000244|PDB:4NEE}.
STRAND 181 185 {ECO:0000244|PDB:4NEE}.
HELIX 188 191 {ECO:0000244|PDB:4NEE}.
HELIX 194 198 {ECO:0000244|PDB:4NEE}.
HELIX 200 202 {ECO:0000244|PDB:4NEE}.
SEQUENCE 206 AA; 23469 MW; 5A26976E95483E9C CRC64;
MGGKWSKSSV IGWPTVRERM RRAEPAADRV GAASRDLEKH GAITSSNTAA TNAACAWLEA
QEEEEVGFPV TPQVPLRPMT YKAAVDLSHF LKEKGGLEGL IHSQRRQDIL DLWIYHTQGY
FPDWQNYTPG PGVRYPLTFG WCYKLVPVEP DKIEEANKGE NTSLLHPVSL HGMDDPEREV
LEWRFDSRLA FHHVARELHP EYFKNC


Related products :

Catalog number Product name Quantity
EIAAB39885 Chondroitin sulfate proteoglycan core protein,Cytolytic granule proteoglycan core protein,PG19 core protein,Pgsg,Prg,Prg1,Proteoglycan 10K core protein,Rat,Rattus norvegicus,Secretory granule proteogl
orb81568 Hepatitis Virus Nucleocapsid (core) 24 protein The HCV Core 24 genotype-1b, E.coli derived recombinant protein, contains the HCV core nucleocapsid immunodominant regions. The protein is fused with b-g 100
EIAAB39887 Hematopoetic proteoglycan core protein,Homo sapiens,Human,P.PG,Platelet proteoglycan core protein,PRG,PRG1,Secretory granule proteoglycan core protein,Serglycin,SRGN
18-003-43322 Krueppel-like factor 6 - Core promoter element-binding protein; B-cell-derived protein 1; Proto-oncogene BCD1; Transcription factor Zf9; GC-rich sites-binding factor GBF Polyclonal 0.05 mg Aff Pur
orb82544 West Nile Virus Core (CT) protein West Nile Virus Core Protein, C-terminal is an infectious disease antigen_toxin. For research use only. 50
orb81558 Hepatitis Virus Nucleocapsid (core) Genotype-2b protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81559 Hepatitis Virus Nucleocapsid (core) Genotype-3a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81557 Hepatitis Virus Nucleocapsid (core) Genotype-2a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81561 Hepatitis Virus Nucleocapsid (core) Genotype-4 protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81556 Hepatitis Virus Nucleocapsid (core) Genotype-1b protein The E.coli derived recombinant multimer protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fus 100
orb81567 Hepatitis Virus Nucleocapsid (core) (105-302) protein The E.coli derived recombinant protein from E1 region contains the HCV core nucleocapsid immunodominant regions, amino acids 105-302. The protein 100
U1908h CLIA ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,Chondroitin sulfate proteoglycan 1,Chondroitin sulfate proteoglycan core protein 1,CSPCP,CSPG1,Homo sapiens,Human,MSK1 96T
EIAAB28014 Homo sapiens,Human,NTAN1,PNAA,PNAD,Protein NH2-terminal asparagine amidohydrolase,Protein NH2-terminal asparagine deamidase,Protein N-terminal Asn amidase,Protein N-terminal asparagine amidohydrolase,
E1908h ELISA ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,Chondroitin sulfate proteoglycan 1,Chondroitin sulfate proteoglycan core protein 1,CSPCP,CSPG1,Homo sapiens,Human,MSK 96T
E1908h ELISA kit ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,Chondroitin sulfate proteoglycan 1,Chondroitin sulfate proteoglycan core protein 1,CSPCP,CSPG1,Homo sapiens,Huma 96T
U1908h CLIA kit ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,Chondroitin sulfate proteoglycan 1,Chondroitin sulfate proteoglycan core protein 1,CSPCP,CSPG1,Homo sapiens,Human 96T
EIAAB28016 NTAN1,Pig,PNAA,PNAD,Protein NH2-terminal asparagine amidohydrolase,Protein NH2-terminal asparagine deamidase,Protein N-terminal Asn amidase,Protein N-terminal asparagine amidohydrolase,Protein NTN-ami
EIAAB28015 Mouse,Mus musculus,Ntan1,PNAA,PNAD,Protein NH2-terminal asparagine amidohydrolase,Protein NH2-terminal asparagine deamidase,Protein N-terminal Asn amidase,Protein N-terminal asparagine amidohydrolase,
EIAAB32501 Androgen receptor N-terminal domain-transactivating protein 1,ANT-1,C20orf14,Homo sapiens,Human,Pre-mRNA-processing factor 6,PRP6 homolog,PRPF6,U5 snRNP-associated 102 kDa protein,U5-102 kDa protein
10-663-45365 Hepatitis B Virus HBe - Precore_core protein; Core protein; PreC_C protein; Precore protein; Core and e antigen; HBe antigen; Precore_core antigen; PreC+C; Core antigen; Precore_core ORF N_A 0.1 mg
10-663-45365 Hepatitis B Virus HBe - Precore_core protein; Core protein; PreC_C protein; Precore protein; Core and e antigen; HBe antigen; Precore_core antigen; PreC+C; Core antigen; Precore_core ORF N_A 1 mg
10-663-45365 Hepatitis B Virus HBe - Precore_core protein; Core protein; PreC_C protein; Precore protein; Core and e antigen; HBe antigen; Precore_core antigen; PreC+C; Core antigen; Precore_core ORF N_A 0.5 mg
EIAAB46308 Elafin-like protein II,Mouse,Mus musculus,Single WAP motif protein 2,Swam2,WAP four-disulfide core domain protein 12,Wfdc12,Whey acidic protein 2
orb81570 Hepatitis Virus Nucleocapsid (core) 22kDa protein The E.coli derived recombinant protein contains the HCV core nucleocapsid genotype 1b, immunodominant regions, amino acids 2-192, 22kDa.The protein is 100
AS06 172 Antibody: PsaA | PSI-A core protein of photosystem I, Immunogen: N-terminal part of recombinanat PsaA protein from Chlamydomonas reinhardtii P12154, Host: rabbit, polyclonal, Confirmed reactivity: Ara 200


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur