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NEF_SIVM1
ID   NEF_SIVM1               Reviewed;         262 AA.
AC   P05862;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 102.
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 Mm142-83) (SIV-mac) (Simian
OS   immunodeficiency virus rhesus monkey).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11733;
OH   NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3649576; DOI=10.1038/328543a0;
RA   Chakrabarti L., Guyader M., Alizon M., Daniel M.D., Desrosiers R.C.,
RA   Tiollais P., Sonigo P.;
RT   "Sequence of simian immunodeficiency virus from macaque and its
RT   relationship to other human and simian retroviruses.";
RL   Nature 328:543-547(1987).
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   EMBL; Y00277; CAA68389.1; -; Genomic_DNA.
DR   SMR; P05862; -.
DR   Proteomes; UP000007220; 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   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..262
FT                   /note="Protein Nef"
FT                   /id="PRO_0000085244"
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   262 AA;  30287 MW;  5A670495737C4553 CRC64;
     MGGAISKKRS KPPRDLRQRL LRARGENYGR LFKGVEDGSS QSLGGLDKGL SSLSCEGQKY
     NQGEYMNTPW RNPAEERKKL PYRKQNIDDI DEEDDDLVGI PVEARVPLRT MSYKLAIDMS
     HFIKEKGGLE GIYYSARRHR ILDIYLEKEE GIIPDWQIHS GPGIRYLKMF GWLWKLIPVN
     VSDEAQEDEE HYLVHPAQTS QWDDPWGEVL AWKFDPTLAY TYEAYIRYPE EFGSKSGLSE
     KEVKRRLAAR GLLEMADRKE TS
 
 
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