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TAX_HTL3P
ID   TAX_HTL3P               Reviewed;         350 AA.
AC   Q4U0X7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Protein Tax-3;
DE   AltName: Full=Trans-activating transcriptional regulatory protein of HTLV-3;
GN   Name=tax;
OS   Human T-cell leukemia virus 3 (strain Pyl43) (HTLV-3).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX   NCBI_TaxID=406769;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, SUBCELLULAR LOCATION,
RP   PDZ-BINDING MOTIF, AND MUTAGENESIS OF MET-131 AND 319-LEU-LEU-320.
RX   PubMed=16973592; DOI=10.1128/jvi.00799-06;
RA   Calattini S., Chevalier S.A., Duprez R., Afonso P., Froment A., Gessain A.,
RA   Mahieux R.;
RT   "Human T-cell lymphotropic virus type 3: complete nucleotide sequence and
RT   characterization of the human tax3 protein.";
RL   J. Virol. 80:9876-9888(2006).
CC   -!- FUNCTION: Transcriptional activator that activates both the viral long
CC       terminal repeat (LTR) and cellular promoters via activation of CREB,
CC       NF-kappa-B, SRF and AP-1 pathways. Binds to two 21 bp repeat elements
CC       located within the LTRs, referred to as Tax-responsive element (TRE).
CC       Binding to TRE requires the interaction with CREB1 and CREBBP.
CC       Activation of NF-kappa-B leads to up-regulation of the expression of
CC       gene promoters containing NFkB motifs like IL8 or BCL2L1. Inhibits the
CC       action of p53/TP53 and MYCB. All these functions could lead to the
CC       possible occurrence of lymphoproliferative disorders. Required for
CC       viral replication.
CC   -!- SUBUNIT: Homodimer. Interacts with host CREB1, CREBBP and EP300 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16973592}. Host
CC       cytoplasm {ECO:0000269|PubMed:16973592}. Note=Shuttles from the nucleus
CC       to the cytoplasm. Found predominantly in the nucleus, with some
CC       cytoplasmic speckles.
CC   -!- DOMAIN: The 48 N-terminal residues contain a non-canonical functional
CC       nuclear localization signal (NLS). {ECO:0000250}.
CC   -!- DOMAIN: The PDZ-binding domain may mediate binding to PDZ-containing
CC       proteins and could be a factor of pathogenicity.
CC   -!- PTM: Phosphorylation at Thr-48 results in the loss of NF-kappa-B
CC       activation function. Phosphorylation at Thr-215 results in loss of CREB
CC       and NF-B responsive promoters activation. Phosphorylation at Thr-184
CC       has no effect on these functions. Phosphorylation of either Ser-300 or
CC       Ser-301 is necessary for localization to nuclear bodies. Thr-48, Thr-
CC       184 and Thr-215 are highly phosphorylated, whereas Ser-300 or Ser-301
CC       are only rarely phosphorylated (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the deltaretrovirus Tax protein family.
CC       {ECO:0000305}.
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DR   EMBL; DQ462191; AAY34568.2; -; Genomic_DNA.
DR   Proteomes; UP000007684; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0039646; P:modulation by virus of host G0/G1 transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR004120; Tax.
DR   Pfam; PF02959; Tax; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding;
KW   G0/G1 host cell cycle checkpoint dysregulation by virus; Host cytoplasm;
KW   Host nucleus; Host-virus interaction; Metal-binding;
KW   Modulation of host cell cycle by virus; Oncogene; Phosphoprotein;
KW   SH3-binding; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..350
FT                   /note="Protein Tax-3"
FT                   /id="PRO_0000260490"
FT   ZN_FING         23..49
FT                   /evidence="ECO:0000255"
FT   REGION          1..58
FT                   /note="Interaction with CREB1"
FT                   /evidence="ECO:0000250"
FT   REGION          81..95
FT                   /note="Interaction with CREBBP/P300"
FT                   /evidence="ECO:0000250"
FT   REGION          106..111
FT                   /note="Interaction with IKBKG"
FT                   /evidence="ECO:0000250"
FT   REGION          116..145
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          213..248
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          289..322
FT                   /note="Transactivation"
FT                   /evidence="ECO:0000250"
FT   REGION          312..319
FT                   /note="Interaction with CREBBP C-terminus"
FT                   /evidence="ECO:0000250"
FT   REGION          327..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           73..80
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           188..202
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           347..350
FT                   /note="PDZ-binding"
FT   MOD_RES         48
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         184
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         215
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         300
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         301
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         131
FT                   /note="M->S: Nuclear localization, with fewer cytoplasmic
FT                   speckles than wild-type."
FT                   /evidence="ECO:0000269|PubMed:16973592"
FT   MUTAGEN         319..320
FT                   /note="LL->RS: Nuclear localization, with fewer cytoplasmic
FT                   speckles than wild-type."
FT                   /evidence="ECO:0000269|PubMed:16973592"
SQ   SEQUENCE   350 AA;  38866 MW;  4E120DF493D6D868 CRC64;
     MAHFPGFGQS LLYGYPVYVF GDCVQADWCP ISGGLCSARL HRHALLATCP EHQITWDPID
     GRVVSSALQY LIPRLPSFPT QRTTRTLKVL TPPTTATTPK VPPSFFHAVK KHTPFRNNCL
     ELTLGEQLPA MSFPDPGLRP QNVYTIWGCS VVCLYLYQLS PPMTWPLIPH VIFCHPEQLG
     AFLTRVPTKR LEELLYKIFL STGAIIILPE NCFPTTLFQP TRAPAIQAPW HTGLLPCQKE
     IVTPGLIWTF TDGSPMISGP CPKEGQPSLV VQSSTFIFQQ FQTKASHPAF LLSHKLIQYS
     SFHSLHLLFE EYSTVPFSLL FNEKGANVSD DEPRGGPQPP TGGQIAESSV
 
 
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