NEF_HV1A2
ID NEF_HV1A2 Reviewed; 210 AA.
AC P03407;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein Nef {ECO:0000255|HAMAP-Rule:MF_04078};
DE AltName: Full=3'ORF {ECO:0000255|HAMAP-Rule:MF_04078};
DE AltName: Full=Negative factor {ECO:0000255|HAMAP-Rule:MF_04078};
DE Short=F-protein {ECO:0000255|HAMAP-Rule:MF_04078};
DE Contains:
DE RecName: Full=C-terminal core protein {ECO:0000255|HAMAP-Rule:MF_04078};
GN Name=nef {ECO:0000255|HAMAP-Rule:MF_04078};
OS Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11685;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2578227; DOI=10.1126/science.2578227;
RA Sanchez-Pescador R., Power M.D., Barr P.J., Steimer K.S., Stempien M.M.,
RA Brown-Shimer S.L., Gee W.W., Renard A., Randolph A., Levy J.A., Dina D.,
RA Luciw P.A.;
RT "Nucleotide sequence and expression of an AIDS-associated retrovirus (ARV-
RT 2).";
RL Science 227:484-492(1985).
RN [2]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-107.
RX PubMed=9032396; DOI=10.1128/jvi.71.3.2535-2539.1997;
RA Luo T., Downing J.R., Garcia J.V.;
RT "Induction of phosphorylation of human immunodeficiency virus type 1 Nef
RT and enhancement of CD4 down-regulation by phorbol myristate acetate.";
RL J. Virol. 71:2535-2539(1997).
RN [3]
RP FUNCTION.
RX PubMed=9218412; DOI=10.1074/jbc.272.29.17899;
RA Briggs S.D., Sharkey M., Stevenson M., Smithgall T.E.;
RT "SH3-mediated Hck tyrosine kinase activation and fibroblast transformation
RT by the Nef protein of HIV-1.";
RL J. Biol. Chem. 272:17899-17902(1997).
RN [4]
RP INTERACTION WITH HUMAN ATP6V1H.
RX PubMed=9620685; DOI=10.1016/s1074-7613(00)80569-5;
RA Lu X., Yu H., Liu S.-H., Brodsky F.M., Peterlin B.M.;
RT "Interactions between HIV1 Nef and vacuolar ATPase facilitate the
RT internalization of CD4.";
RL Immunity 8:647-656(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST TCR-ZETA CHAIN/TCR-ZETA.
RX PubMed=10224289; DOI=10.1084/jem.189.9.1489;
RA Xu X.-N., Laffert B., Screaton G.R., Kraft M., Wolf D., Kolanus W.,
RA Mongkolsapay J., McMichael A.J., Baur A.S.;
RT "Induction of Fas ligand expression by HIV involves the interaction of Nef
RT with the T cell receptor zeta chain.";
RL J. Exp. Med. 189:1489-1496(1999).
RN [6]
RP FUNCTION.
RX PubMed=10208934; DOI=10.1006/viro.1999.9642;
RA Kim Y.-H., Chang S.H., Kwon J.H., Rhee S.S.;
RT "HIV-1 Nef plays an essential role in two independent processes in CD4
RT down-regulation: dissociation of the CD4-p56(lck) complex and targeting of
RT CD4 to lysosomes.";
RL Virology 257:208-219(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH PAK2.
RX PubMed=11070003; DOI=10.1128/jvi.74.23.11081-11087.2000;
RA Arora V.K., Molina R.P., Foster J.L., Blakemore J.L., Chernoff J.,
RA Fredericksen B.L., Garcia J.V.;
RT "Lentivirus Nef specifically activates Pak2.";
RL J. Virol. 74:11081-11087(2000).
RN [8]
RP FUNCTION.
RX PubMed=11420046; DOI=10.1016/s1074-7613(01)00158-3;
RA Simmons A., Aluvihare V., McMichael A.;
RT "Nef triggers a transcriptional program in T cells imitating single-signal
RT T cell activation and inducing HIV virulence mediators.";
RL Immunity 14:763-777(2001).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN A NEF/PI3-KINASE/PAK2 COMPLEX.
RX PubMed=11689886; DOI=10.1038/nm1101-1217;
RA Wolf D., Witte V., Laffert B., Blume K., Stromer E., Trapp S., d'Aloja P.,
RA Schuermann A., Baur A.S.;
RT "HIV-1 Nef associated PAK and PI3-kinases stimulate Akt-independent Bad-
RT phosphorylation to induce anti-apoptotic signals.";
RL Nat. Med. 7:1217-1224(2001).
RN [10]
RP MUTAGENESIS OF ARG-75.
RX PubMed=11525746; DOI=10.1016/s0960-9822(01)00373-6;
RA Fackler O.T., Wolf D., Weber H.O., Laffert B., D'Aloja P.,
RA Schuler-Thurner B., Geffin R., Saksela K., Geyer M., Peterlin B.M.,
RA Schuler G., Baur A.S.;
RT "A natural variability in the proline-rich motif of Nef modulates HIV-1
RT replication in primary T cells.";
RL Curr. Biol. 11:1294-1299(2001).
RN [11]
RP INTERACTION WITH HUMAN PI3-KINASE.
RX PubMed=12009866; DOI=10.1006/viro.2002.1365;
RA Linnemann T., Zheng Y.-H., Mandic R., Peterlin B.M.;
RT "Interaction between Nef and phosphatidylinositol-3-kinase leads to
RT activation of p21-activated kinase and increased production of HIV.";
RL Virology 294:246-255(2002).
RN [12]
RP INTERACTION WITH HUMAN ATP6V1H, AND MUTAGENESIS OF 168-LEU-LEU-169 AND
RP 178-GLU-ASP-179.
RX PubMed=12058068; DOI=10.1091/mbc.02-02-0026;
RA Geyer M., Fackler O.T., Peterlin B.M.;
RT "Subunit H of the V-ATPase involved in endocytosis shows homology to beta-
RT adaptins.";
RL Mol. Biol. Cell 13:2045-2056(2002).
RN [13]
RP INTERACTION WITH HUMAN ATP6V1H.
RX PubMed=12032142; DOI=10.1074/jbc.m200522200;
RA Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.-H., Fackler O.T.,
RA Peterlin B.M.;
RT "Subunit H of the V-ATPase binds to the medium chain of adaptor protein
RT complex 2 and connects Nef to the endocytic machinery.";
RL J. Biol. Chem. 277:28521-28529(2002).
RN [14]
RP SH3-BINDING MOTIF, FUNCTION, INTERACTION WITH HOST HCK, INTERACTION WITH
RP HOST LYN, AND INTERACTION WITH HOST SRC.
RX PubMed=16849330; DOI=10.1074/jbc.m601128200;
RA Trible R.P., Emert-Sedlak L., Smithgall T.E.;
RT "HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src
RT through direct SH3 domain interaction.";
RL J. Biol. Chem. 281:27029-27038(2006).
RN [15]
RP SUBUNIT.
RX PubMed=16475823; DOI=10.1021/bi052052c;
RA Breuer S., Gerlach H., Kolaric B., Urbanke C., Opitz N., Geyer M.;
RT "Biochemical indication for myristoylation-dependent conformational changes
RT in HIV-1 Nef.";
RL Biochemistry 45:2339-2349(2006).
RN [16]
RP PHOSPHORYLATION AT SER-6.
RX PubMed=17904606; DOI=10.1016/j.virol.2007.08.015;
RA Wolf D., Giese S.I., Witte V., Krautkraemer E., Trapp S., Sass G.,
RA Haller C., Blume K., Fackler O.T., Baur A.S.;
RT "Novel (n)PKC kinases phosphorylate Nef for increased HIV transcription,
RT replication and perinuclear targeting.";
RL Virology 370:45-54(2008).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 45-210, AND DILEUCINE MOTIF.
RX PubMed=21477083; DOI=10.1111/j.1600-0854.2011.01205.x;
RA Horenkamp F.A., Breuer S., Schulte A., Lulf S., Weyand M., Saksela K.,
RA Geyer M.;
RT "Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by
RT intermolecular domain assembly.";
RL Traffic 12:867-877(2011).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 62-209, AND INTERACTION WITH HOST
RP HCK.
RX PubMed=25122770; DOI=10.1074/jbc.m114.600031;
RA Alvarado J.J., Tarafdar S., Yeh J.I., Smithgall T.E.;
RT "Interaction with the Src homology (SH3-SH2) region of the Src-family
RT kinase Hck structures the HIV-1 Nef dimer for kinase activation and
RT effector recruitment.";
RL J. Biol. Chem. 289:28539-28553(2014).
CC -!- FUNCTION: Factor of infectivity and pathogenicity, required for optimal
CC virus replication. Alters numerous pathways of T-lymphocyte function
CC and down-regulates immunity surface molecules in order to evade host
CC defense and increase viral infectivity. Alters the functionality of
CC other immunity cells, like dendritic cells, monocytes/macrophages and
CC NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface
CC MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates
CC internalization and degradation of host CD4 through the interaction of
CC with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin
CC adapter protein complex 2), internalization through clathrin coated
CC pits, and subsequent transport to endosomes and lysosomes for
CC degradation. Diverts host MHC-I molecules to the trans-Golgi network-
CC associated endosomal compartments by an endocytic pathway to finally
CC target them for degradation. MHC-I down-regulation may involve AP-1
CC (clathrin adapter protein complex 1) or possibly Src family kinase-
CC ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected
CC cells are masked for immune recognition by cytotoxic T-lymphocytes.
CC Decreasing the number of immune receptors also prevents reinfection by
CC more HIV particles (superinfection). Down-regulates host SERINC3 and
CC SERINC5 thereby excluding these proteins from the viral particles.
CC Virion infectivity is drastically higher when SERINC3 or SERINC5 are
CC excluded from the viral envelope, because these host antiviral proteins
CC impair the membrane fusion event necessary for subsequent virion
CC penetration. {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional
CC program nearly identical to that of anti-CD3 cell activation.
CC Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL).
CC Increasing surface FasL molecules and decreasing surface MHC-I
CC molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-
CC lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078,
CC ECO:0000269|PubMed:10224289}.
CC -!- FUNCTION: Plays a role in optimizing the host cell environment for
CC viral replication without causing cell death by apoptosis. Protects the
CC infected cells from apoptosis in order to keep them alive until the
CC next virus generation is ready to strike. Inhibits the Fas and TNFR-
CC mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life
CC of TP53, protecting the infected cell against p53-mediated apoptosis.
CC Inhibits the apoptotic signals regulated by the Bcl-2 family proteins
CC through the formation of a Nef/PI3-kinase/PAK2 complex that leads to
CC activation of PAK2 and induces phosphorylation of host BAD.
CC {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:11689886}.
CC -!- FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for
CC apoptosis by interacting with CXCR4 surface receptors.
CC {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- SUBUNIT: Monomer; cytosolic form. Homodimer; membrane bound form.
CC Interacts with Nef associated p21-activated kinase (PAK2); this
CC interaction activates PAK2. Associates with the Nef-MHC-I-AP1 complex;
CC this complex is required for MHC-I internalization. Interacts (via C-
CC terminus) with host PI3-kinase. Interacts with host PACS1; this
CC interaction seems to be weak. Interacts with host PACS2. Interacts with
CC host LCK and MAPK3; these interactions inhibit the kinase activity of
CC the latter. Interacts with host ATP6V1H; this interaction may play a
CC role in CD4 endocytosis. Associates with the CD4-Nef-AP2 complex; this
CC complex is required for CD4 internalization. Interacts with host AP2
CC subunit alpha and AP2 subunit sigma2. Interacts with TCR-zeta chain;
CC this interaction up-regulates the Fas ligand (FasL) surface expression.
CC Interacts with host HCK, LYN, and SRC; these interactions activate the
CC Src family kinases. Interacts with MAP3K5; this interaction inhibits
CC the Fas and TNFR-mediated death signals. Interacts with beta-COP and
CC PTE1. Interacts with human RACK1; this increases Nef phosphorylation by
CC PKC. Interacts with TP53; this interaction decreases the half-life of
CC TP53, protecting the infected cell against p53-mediated apoptosis.
CC {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:10224289,
CC ECO:0000269|PubMed:11070003, ECO:0000269|PubMed:11689886,
CC ECO:0000269|PubMed:12009866, ECO:0000269|PubMed:16475823,
CC ECO:0000269|PubMed:16849330, ECO:0000269|PubMed:25122770}.
CC -!- INTERACTION:
CC P03407; Q14457: BECN1; Xeno; NbExp=2; IntAct=EBI-7355020, EBI-949378;
CC P03407; P01730: CD4; Xeno; NbExp=2; IntAct=EBI-7355020, EBI-353826;
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-
CC Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion
CC {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-
CC Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with
CC the inner plasma membrane through its N-terminal domain. Nef stimulates
CC its own export via the release of exosomes. Incorporated in virions at
CC a rate of about 10 molecules per virion, where it is cleaved.
CC {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- INDUCTION: Expressed early in the viral replication cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- DOMAIN: The N-terminal domain is composed of the N-myristoyl glycine
CC and of a cluster of positively charged amino acids. It is required for
CC inner plasma membrane targeting of Nef and virion incorporation, and
CC thereby for infectivity. This domain is also involved in binding to
CC TP53. {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- DOMAIN: The SH3-binding domain constituted of PxxP motifs mediates
CC binding to several Src family proteins thereby regulating their
CC tyrosine kinase activity. The same motifs also mediates the association
CC with MAPK3, PI3-kinase and TCR-zeta. {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- DOMAIN: The dileucine internalization motif and a diacidic motif seem
CC to be required for binding to AP-2. {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- DOMAIN: The acidic region binds to the sorting protein PACS-2, which
CC targets Nef to the paranuclear region, enabling the PxxP motif to
CC direct assembly of an SFK/ZAP-70/PI3K complex that accelerates
CC endocytosis of cell-surface MHC-I. {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- PTM: The virion-associated Nef proteins are cleaved by the viral
CC protease to release the soluble C-terminal core protein. Nef is
CC probably cleaved concomitantly with viral structural proteins on
CC maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.
CC -!- PTM: Phosphorylated on serine residues, probably by host PKCdelta and
CC theta. {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:17904606,
CC ECO:0000269|PubMed:9032396}.
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:0000255|HAMAP-Rule:MF_04078}.
CC -!- SIMILARITY: Belongs to the lentivirus primate group Nef protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04078}.
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DR EMBL; K02007; AAB59883.1; -; Genomic_RNA.
DR PIR; A04009; ASLJO2.
DR PDB; 3RBB; X-ray; 2.35 A; A/C=45-210.
DR PDB; 3REA; X-ray; 2.00 A; A/C=45-210.
DR PDB; 3REB; X-ray; 3.45 A; A/C=45-210.
DR PDB; 4ORZ; X-ray; 2.00 A; B=45-209.
DR PDB; 4U1K; X-ray; 2.09 A; C/F=75-83.
DR PDB; 4U1L; X-ray; 2.06 A; C/F=75-83.
DR PDB; 4U1M; X-ray; 1.18 A; C=75-83.
DR PDB; 4U1N; X-ray; 1.77 A; C=75-83.
DR PDB; 4U5W; X-ray; 1.86 A; A/C=62-209.
DR PDB; 5XOV; X-ray; 2.68 A; C/F=138-147.
DR PDB; 6B72; X-ray; 3.20 A; A/B/C/D/E/F=57-207.
DR PDB; 7D7S; X-ray; 3.32 A; A/B=1-209.
DR PDBsum; 3RBB; -.
DR PDBsum; 3REA; -.
DR PDBsum; 3REB; -.
DR PDBsum; 4ORZ; -.
DR PDBsum; 4U1K; -.
DR PDBsum; 4U1L; -.
DR PDBsum; 4U1M; -.
DR PDBsum; 4U1N; -.
DR PDBsum; 4U5W; -.
DR PDBsum; 5XOV; -.
DR PDBsum; 6B72; -.
DR PDBsum; 7D7S; -.
DR SMR; P03407; -.
DR DIP; DIP-29212N; -.
DR IntAct; P03407; 7.
DR MINT; P03407; -.
DR iPTMnet; P03407; -.
DR ABCD; P03407; 2 sequenced antibodies.
DR EvolutionaryTrace; P03407; -.
DR Proteomes; UP000007688; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IDA:CACAO.
DR GO; GO:0046776; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-UniRule.
DR GO; GO:0039505; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class II; IEA:UniProtKB-UniRule.
DR GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-UniRule.
DR DisProt; DP02889; -.
DR Gene3D; 3.30.62.10; -; 1.
DR Gene3D; 4.10.890.10; -; 1.
DR HAMAP; MF_04078; NEF_HIV; 1.
DR InterPro; IPR027480; HIV-1_Nef_anchor_sf.
DR InterPro; IPR027481; HIV-1_Nef_core_sf.
DR InterPro; IPR001558; HIV_Nef.
DR Pfam; PF00469; F-protein; 1.
DR SUPFAM; SSF55671; SSF55671; 1.
PE 1: Evidence at protein level;
KW 3D-structure; AIDS; Apoptosis; Early protein; Host cell membrane;
KW Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Inhibition of host adaptive immune response by virus;
KW Inhibition of host autophagy by virus;
KW Inhibition of host MHC class I molecule presentation by virus;
KW Inhibition of host MHC class II molecule presentation by virus;
KW Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome;
KW Secreted; SH3-binding; Viral immunoevasion; Virion; Virulence.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT CHAIN 2..210
FT /note="Protein Nef"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT /id="PRO_0000038333"
FT CHAIN 62..210
FT /note="C-terminal core protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT /id="PRO_0000038334"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..69
FT /note="Acidic; interacts with host PACS1 and PACS2;
FT stabilizes the interaction of NEF/MHC-I with host AP1M1;
FT necessary for MHC-I internalization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT REGION 73..82
FT /note="SH3-binding; interaction with Src family tyrosine
FT kinases"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT REGION 112..128
FT /note="Mediates dimerization, Nef-PTE1 interaction"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT REGION 152..184
FT /note="Binding to ATP6V1H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078,
FT ECO:0000269|PubMed:9620685"
FT MOTIF 76..79
FT /note="PxxP; stabilizes the interaction of NEF/MHC-I with
FT host AP1M1; necessary for MHC-I internalization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT MOTIF 168..169
FT /note="Dileucine internalization motif; necessary for CD4
FT internalization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078,
FT ECO:0000269|PubMed:21477083"
FT MOTIF 178..179
FT /note="Diacidic; necessary for CD4 internalization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT COMPBIAS 14..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 20
FT /note="Might play a role in AP-1 recruitment to the Nef-
FT MHC-I complex"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT SITE 61..62
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT MOD_RES 6
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078,
FT ECO:0000269|PubMed:17904606"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04078"
FT MUTAGEN 75
FT /note="R->T: Complete loss of viral replication. Incapacity
FT to trigger cellular activation, probably due to reduced
FT interaction with the TCR environment."
FT /evidence="ECO:0000269|PubMed:11525746"
FT MUTAGEN 107
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:9032396"
FT MUTAGEN 168..169
FT /note="LL->AA: Partial loss of binding to NBP1."
FT /evidence="ECO:0000269|PubMed:12058068"
FT MUTAGEN 178..179
FT /note="ED->AA: Partial loss of binding to NBP1."
FT /evidence="ECO:0000269|PubMed:12058068"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:3REA"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6B72"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:4U5W"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:7D7S"
FT HELIX 108..122
FT /evidence="ECO:0007829|PDB:4U5W"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4U5W"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:4U5W"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:4U5W"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:3RBB"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3RBB"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:4ORZ"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:4U5W"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:4U5W"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:4U5W"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4U5W"
SQ SEQUENCE 210 AA; 24042 MW; ED255233F8A17DAB CRC64;
MGGKWSKRSM GGWSAIRERM RRAEPRAEPA ADGVGAVSRD LEKHGAITSS NTAATNADCA
WLEAQEEEEV GFPVRPQVPL RPMTYKAALD ISHFLKEKGG LEGLIWSQRR QEILDLWIYH
TQGYFPDWQN YTPGPGIRYP LTFGWCFKLV PVEPEKVEEA NEGENNSLLH PMSLHGMEDA
EKEVLVWRFD SKLAFHHMAR ELHPEYYKDC
