ID   NEF_SIVV1               Reviewed;         230 AA.
AC   P27970;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 93.
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 agm.vervet (isolate AGM155) (SIV-agm.ver)
OS   (Simian immunodeficiency virus African green monkey vervet).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11727;
OH   NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2304139; DOI=10.1128/jvi.64.3.1086-1092.1990;
RA   Johnson P.R., Fomsgaard A., Allan J.S., Gravell M., London W.T.,
RA   Olmstead R.A., Hirsch V.M.;
RT   "Simian immunodeficiency viruses from African green monkeys display unusual
RT   genetic diversity.";
RL   J. Virol. 64:1086-1092(1990).
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: The 155 isolate is from a monkey imported from Kenya.
CC   -!- SIMILARITY: Belongs to the lentivirus primate group Nef protein family.
CC       {ECO:0000305}.
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DR   EMBL; M29975; AAA91912.1; -; Genomic_RNA.
DR   SMR; P27970; -.
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   3: Inferred from homology;
KW   Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW   Membrane; Myristate; Viral immunoevasion; Virulence.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..230
FT                   /note="Protein Nef"
FT                   /id="PRO_0000085239"
FT   REGION          76..84
FT                   /note="Acidic"
FT   REGION          127..143
FT                   /note="Mediates dimerization"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   230 AA;  26528 MW;  4C8A376DF7522CAB CRC64;
     MGLGSSKPQH KKQLTIWRAL HATRHTRYGL LADPLIGQSS TLQEECDKGL RKSLIRKRNG
     NMTPEGRRLQ DGDQWDEWSD EEDEVGFPVR PRVPLRQITY KLAVDFSHFL KEKGGLDGIY
     YSDRRNKILN LYALNEWGII DDWNAWSKGP GIRYPRCFGF CFKLVPVALH EEAETCERHC
     LVHPAQLHED PDGINHGEIL AWKFDPMLAV QYDPSREYFT DLYSTVGTGN