ID   NEF_SIVS4               Reviewed;         263 AA.
AC   P12482;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 109.
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 F236/smH4) (SIV-sm) (Simian
OS   immunodeficiency virus sooty mangabey monkey).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11737;
OH   NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2786147; DOI=10.1038/339389a0;
RA   Hirsch V.M., Olmstead R.A., Murphey-Corb M., Purcell R.H., Johnson P.R.;
RT   "An African primate lentivirus (SIVsm) closely related to HIV-2.";
RL   Nature 339:389-392(1989).
RN   [2]
RP   INTERACTION WITH HOST CD247/TCRZ.
RX   PubMed=9811718; DOI=10.1128/jvi.72.12.9827-9834.1998;
RA   Howe A.Y., Jung J.U., Desrosiers R.C.;
RT   "Zeta chain of the T-cell receptor interacts with nef of simian
RT   immunodeficiency virus and human immunodeficiency virus type 2.";
RL   J. Virol. 72:9827-9834(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=16051847; DOI=10.1128/jvi.79.16.10547-10560.2005;
RA   Munch J., Schindler M., Wildum S., Rucker E., Bailer N., Knoop V.,
RA   Novembre F.J., Kirchhoff F.;
RT   "Primary sooty mangabey simian immunodeficiency virus and human
RT   immunodeficiency virus type 2 nef alleles modulate cell surface expression
RT   of various human receptors and enhance viral infectivity and replication.";
RL   J. Virol. 79:10547-10560(2005).
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:0000305|PubMed:16051847}.
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.
CC       {ECO:0000269|PubMed:16051847}.
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, ECO:0000269|PubMed:9811718}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA32488.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X14307; CAA32488.1; ALT_FRAME; Genomic_DNA.
DR   PIR; S07993; S07993.
DR   PDB; 4ZFZ; X-ray; 1.76 A; C/F/I/L=2-6.
DR   PDBsum; 4ZFZ; -.
DR   SMR; P12482; -.
DR   Proteomes; UP000008173; 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   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   1: Evidence at protein level;
KW   3D-structure; Host cell membrane; Host membrane; Host-virus interaction;
KW   Lipoprotein; Membrane; Myristate; Viral immunoevasion; Virulence.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..263
FT                   /note="Protein Nef"
FT                   /id="PRO_0000085248"
FT   REGION          88..96
FT                   /note="Acidic"
FT   REGION          140..156
FT                   /note="Mediates dimerization"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   263 AA;  30360 MW;  13E8C840F53D1EC9 CRC64;
     MGGAISKKQY KRGGNLRERL LQARGETYGR LWEGLEEGYS QSLGASGKGL SSLSCEPQKY
     SEGQYMNTPW RNPATERAKL GYRQQNMDDV DDEDDDLIGV SVHPRVPLRA MTYKLAIDMS
     HFIKEKGGLE GIYYNERRHR ILDMYLEKEE GIIPDWQNYT SGPGIRYPMH YGWLWKLVPV
     DVSDEAQEDE THCLVHPAQT YQWDDPWGEV LAWKFDPELA YSYKAFIKYP EEFGSKSGLS
     EEEVKRRLTA RGLLKMADKK ETS