NEF_SIVGB
ID NEF_SIVGB Reviewed; 214 AA.
AC P22378;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 96.
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 GB1) (SIV-mnd) (Simian
OS immunodeficiency virus mandrill).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11732;
OH NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2797181; DOI=10.1038/341539a0;
RA Tsujimoto H., Hasegawa A., Maki N., Fukasawa M., Miura T., Speidel S.,
RA Cooper R.W., Moriyama E.N., Gojobori T., Hayami M.;
RT "Sequence of a novel simian immunodeficiency virus from a wild-caught
RT African mandrill.";
RL Nature 341:539-541(1989).
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 an African mandrill isolate.
CC -!- SIMILARITY: Belongs to the lentivirus primate group Nef protein family.
CC {ECO:0000305}.
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DR EMBL; M27470; AAB49575.1; -; Genomic_RNA.
DR SMR; P22378; -.
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..214
FT /note="Protein Nef"
FT /id="PRO_0000085243"
FT REGION 27..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..86
FT /note="Acidic"
FT REGION 129..145
FT /note="Mediates dimerization"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 214 AA; 24259 MW; 16F9545BEB0028BD CRC64;
MGSSQSKKRS EAWVRYSSAL RQLVGGPVTP DGYKQIESSQ GAEKQSLLRG RAYGTYSEGL
DKVQNDPLTK DEKLDLTQQD PEEEEEVGFP VCRQVSLRVP SYKDLIDFSH FIKEKGGLGG
IYYSRRREEI LDLYAENEWG FEPGWQQYTT GPGTRYPKTF GFLFKLEPVS RAIGDEYAAN
NHLLHSSQLC PQEDPEGETL MWSGTLILPM TLQH