ID   NEF_SIVMA               Reviewed;         263 AA.
AC   P31818;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 92.
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 1A11) (SIV-mac) (Simian
OS   immunodeficiency virus rhesus monkey).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=31682;
OH   NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=1501282; DOI=10.1128/jvi.66.9.5432-5442.1992;
RA   Unger R.E., Marthas M.L., Pratt-Lowe E., Padrid P.A., Luciw P.A.;
RT   "The nef gene of simian immunodeficiency virus SIVmac1A11.";
RL   J. Virol. 66:5432-5442(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. Interacts with host CD247/TCRZ; this interaction
CC       induces down-regulation of cell surface TCR/CD3 complexes.
CC       {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   -!- MISCELLANEOUS: This is a macaque isolate.
CC   -!- SIMILARITY: Belongs to the lentivirus primate group Nef protein family.
CC       {ECO:0000305}.
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DR   PIR; A42747; ASLJMA.
DR   PDB; 3IK5; X-ray; 2.05 A; A/C=95-235.
DR   PDBsum; 3IK5; -.
DR   SMR; P31818; -.
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   IDEAL; IID90022; -.
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_0000085245"
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"
FT   HELIX           113..125
FT                   /evidence="ECO:0007829|PDB:3IK5"
FT   HELIX           136..148
FT                   /evidence="ECO:0007829|PDB:3IK5"
FT   STRAND          163..166
FT                   /evidence="ECO:0007829|PDB:3IK5"
FT   STRAND          168..170
FT                   /evidence="ECO:0007829|PDB:3IK5"
FT   STRAND          175..179
FT                   /evidence="ECO:0007829|PDB:3IK5"
FT   STRAND          211..215
FT                   /evidence="ECO:0007829|PDB:3IK5"
FT   HELIX           217..220
FT                   /evidence="ECO:0007829|PDB:3IK5"
FT   HELIX           224..228
FT                   /evidence="ECO:0007829|PDB:3IK5"
FT   HELIX           230..232
FT                   /evidence="ECO:0007829|PDB:3IK5"
SQ   SEQUENCE   263 AA;  30620 MW;  A46FAA79A47B0077 CRC64;
     MGGTISMRRS RSTGDLRQRL LRARGETYER LLGEVEDGSS QSLGELDKGL SSLSCEGQKY
     NQEQYMNTPW RNPAEEREKL AYRKQNMDDI DEEDDDLVGD TVRPKVPLRT MSYKLAIDMS
     HFIKEKGGLE GIYYSARRHR ILDIYLEKEE GIIPDWQDYT SGPGIRYPKT FGWLWKLVPV
     NVSDEAQEDE EHYLMHPAQT SQWDDPWGEV PAWKFDPTLA YTYEAYVRYP EEFGSKSGLS
     EEEVRRRLTA RGLLNMADKK ETR