TAX_HTL32
ID TAX_HTL32 Reviewed; 350 AA.
AC Q0R5R1;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 02-JUN-2021, entry version 48.
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 2026ND) (HTLV-3).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=402036;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16840323; DOI=10.1128/jvi.00690-06;
RA Switzer W.M., Qari S.H., Wolfe N.D., Burke D.S., Folks T.M., Heneine W.;
RT "Ancient origin and molecular features of the novel human T-lymphotropic
RT virus type 3 revealed by complete genome analysis.";
RL J. Virol. 80:7427-7438(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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with host CREB1, CREBBP and EP300 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}. Note=Shuttles from the nucleus to the cytoplasm. Found
CC predominantly in the nucleus (By similarity). {ECO:0000250}.
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; DQ093792; AAZ77661.1; -; Genomic_DNA.
DR PRIDE; Q0R5R1; -.
DR Proteomes; UP000008029; 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 3: Inferred from homology;
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 Reference proteome; SH3-binding; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..350
FT /note="Protein Tax-3"
FT /id="PRO_0000259952"
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 326..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 /evidence="ECO:0000250"
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"
SQ SEQUENCE 350 AA; 39016 MW; 49CA21BD87179258 CRC64;
MAHFPGFGQS LLYGYPVYVF GDCVQADWCP ISGGLCSARL HRHALLATCP EHQITWDPID
GRVVSSALQY LIPRLPSFPT QRTTRTLKVL TPPTTAATPK IPPSFFHAVK KHTPFRNNCL
ELTLGEQLPA MSFPDPGLRP QNIYTMWGSS VVCLYLYQLS PPMTWPLIPH VIFCHPEQLG
AFLTRVPTKR LEELLYKIFL STGAIIILPE NCFPTTLFQP TRAPAVQAPW HTGLLPCQKE
IATPGLIWTF TDGSPMISGP CPKEGQPSLV VQSSTFIFQQ FQTKASHPAF LLSHKLIHYS
SFHSLHLLFE EYTTIPFSLL FNEKGANVDD DEPRDGSQPP ARGQIAESPV
