Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-11707-00206
Entry Name
UniProt Accession
Theoretical PI
6.31
Molecular Weight
23419.43
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
C-terminal core protein
Protein Synonyms/Alias
3'ORF; Negative factor; F-protein;
Gene Name
nef
Gene Synonyms/Alias
Created Date
01-NOV-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGGKWSKSS
[1][2]
N-Myristoylation
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate HXB3 (HIV-1)
NCBI Taxa ID
11707
Reference
[1] Yu G, Felsted RL. Effect of myristoylation on p27 nef subcellular distributionand suppression of HIV-LTR transcription. Virology. 1992 Mar;187(1):46-55. PubMedPMID: 1736544.[PMID:1736544]
[2] Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR. Structure of theanchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein. J MolBiol. 1999 May 28;289(1):123-38.[PMID:10339411]
Functional Description
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. One of the earliest and most abundantly expressed viral proteins (By similarity).
Sequence Annotation
Region: 2 57 N-terminal; associates with the hostplasma membrane.
Region: 7 26 Necessary for MHC-I internalization.
Region: 62 65 Acidic; stabilizes the interaction ofNEF/MHC-I with host AP1M1; necessary forMHC-I internalization and interactionwith host PACS1 and PACS2.
Region: 69 78 SH3-binding; interaction with Src familytyrosine kinases.
Region: 108 124 Mediates dimerization, Nef-PTE1interaction, Nef-induced CD4 and MHC-Idown-regulation and enhancement ofinfectivity.
Region: 148 180 Binding to ATP6V1H.
Motif: 72 75 PxxP; stabilizes the interaction ofNEF/MHC-I with host AP1M1; necessary forMHC-I internalization.
Motif: 164 165 Di-leucine internalization motif;necessary for CD4 internalization.
Motif: 174 175 Diacidic; necessary for CD4internalization.
Functional site: 20 20 Might play a role in AP-1 recruitment tothe Nef-MHC-I complex.
Functional site: 57 58 Cleavage; by viral protease.
Protein Length
206 AA.
Protein Sequence
(Canonical)
MGGKWSKSSV VGWPAVRERM RRAEPAADGV GAASRDLEKH GAITSSNTAA NNAACAWLEA  60
QEEEKVGFPV TPQVPLRPMT YKAAVDLSHF LKEKGGLEGL IHSQRRQDIL DLWIYHTQGY  120
FPDWQNYTPG PGIRYPLTFG WRYKLVPVEP EKLEEANKGE NTSLLHPVSL HGMDDPEREV  180
LEWRFDSRLA FHHVARELHP EYFKNC                                       206
FASTA
(Canonical)
>LipidDB-11707-00206|P05854
MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAWLEA
QEEEKVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGY
FPDWQNYTPGPGIRYPLTFGWRYKLVPVEPEKLEEANKGENTSLLHPVSLHGMDDPEREV
LEWRFDSRLAFHHVARELHPEYFKNC
Gene Ontology
GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0019012; C:virion; IEA:UniProtKB-KW
GO:0005525; F:GTP binding; IEA:InterPro
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW
GO:0009405; P:pathogenesis; IEA:UniProtKB-KW
GO:0039504; P:suppression by virus of host adaptive immune response; IEA:UniProtKB-KW
GO:0046776; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW
GO:0039505; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class II; IEA:UniProtKB-KW
GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-KW
Interpro
InterPro; IPR027480; HIV-1_Nef_anchor
InterPro; IPR027481; HIV-1_Nef_core
InterPro; IPR001558; HIV_Nef
Pfam
Pfam; PF00469; F-protein;
SMART
PROSITE
PRINTS