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Database: UniProt
Entry: NEF_SIVSP
LinkDB: NEF_SIVSP
Original site: NEF_SIVSP 
ID   NEF_SIVSP               Reviewed;         261 AA.
AC   P19501;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   22-APR-2020, entry version 97.
DE   RecName: Full=Protein Nef;
DE   AltName: Full=3'ORF;
DE   AltName: Full=Negative factor;
DE            Short=F-protein;
GN   Name=nef;
OS   Simian immunodeficiency virus (isolate PBj14/BCL-3) (SIV-sm) (Simian
OS   immunodeficiency virus sooty mangabey monkey).
OC   Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11738;
OH   NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1971917; DOI=10.1038/345636a0;
RA   Dewhurst S., Embretson J.E., Anderson D.C., Mullins J.I., Fultz P.N.;
RT   "Sequence analysis and acute pathogenicity of molecularly cloned SIVSMM-
RT   PBj14.";
RL   Nature 345:636-640(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1503826; DOI=10.1089/aid.1992.8.1179;
RA   Dewhurst S., Embretson J.E., Fultz P.N., Mullins J.I.;
RT   "Molecular clones from a non-acutely pathogenic derivative of SIVsmmPBj14:
RT   characterization and comparison to acutely pathogenic clones.";
RL   AIDS Res. Hum. Retroviruses 8:1179-1187(1992).
CC   -!- FUNCTION: Seems to play a role in optimizing the host cell environment
CC       for viral replication without causing cell death by apoptosis. Enhances
CC       virus infectivity and pathogenicity. Probably involved in viral immune
CC       evasion mechanisms (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates cell surface
CC       expression of CD4, CD28, CD3, and MHC-I or MHC-II molecules.
CC       {ECO:0000250}.
CC   -!- FUNCTION: Interferes with TCR signaling from the cell membrane.
CC       Interacts with CD247/TCRZ (TCR zeta chain) and exert potent down-
CC       regulation of cell surface TCR/CD3 complexes (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with host CD247/TCRZ;
CC       this interaction induces down-regulation of cell surface TCR/CD3
CC       complexes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associates with the
CC       inner plasma membrane through its N-terminal domain. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lentivirus primate group Nef protein family.
CC       {ECO:0000305}.
DR   EMBL; L03298; AAA47782.1; -; Genomic_RNA.
DR   EMBL; M31325; AAA47758.1; -; Genomic_RNA.
DR   SMR; P19501; -.
DR   Proteomes; UP000007221; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0030683; P:mitigation of host immune response by virus; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.62.10; -; 1.
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   3: Inferred from homology;
KW   Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW   Membrane; Myristate; Reference proteome; Viral immunoevasion; Virulence.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..261
FT                   /note="Protein Nef"
FT                   /id="PRO_0000085249"
FT   REGION          88..94
FT                   /note="Acidic"
FT   REGION          138..154
FT                   /note="Mediates dimerization"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   261 AA;  30088 MW;  AAD7A0BECD9C4847 CRC64;
     MGGVTSKKQR RRGGNLYERL LQARGETYGR LWEGLEGEYS QSQDASGKGL SSLSCEPQKY
     CEGQFMNTPW RNPATERAKL DYRQQNMDDV DSADLVGCPV SPRVPVRIMT YKLAIDMSHF
     IKEKGGLEGI YYSDRRHKIL DLYLEKEEGI IPDWQNYTAG PGIRYPMFFG WLWKLVPVNV
     SDEAQEDETH YLMHPAQTSQ WDDPWGEVLA WKFDPKLAYN YKAFVEHPEE FGSQSGLSKE
     EVQRRLTARG LLKMADKKKT S
//
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