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Protein Tax-1 (Protein X-LOR) (Protein PX) (Trans-activating transcriptional regulatory protein of HTLV-1)

 TAX_HTL1C               Reviewed;         353 AA.
P14079; O56231;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
20-JUN-2018, entry version 93.
RecName: Full=Protein Tax-1;
AltName: Full=Protein X-LOR;
Short=Protein PX;
AltName: Full=Trans-activating transcriptional regulatory protein of HTLV-1;
Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A)
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
NCBI_TaxID=9606; Homo sapiens (Human).
PubMed=2899128; DOI=10.1099/0022-1317-69-7-1695;
Malik K.T.A., Even J., Karpas A.;
"Molecular cloning and complete nucleotide sequence of an adult T cell
leukaemia virus/human T cell leukaemia virus type I (ATLV/HTLV-I)
isolate of Caribbean origin: relationship to other members of the
ATLV/HTLV-I subgroup.";
J. Gen. Virol. 69:1695-1710(1988).
Chappey C.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
PubMed=16155604; DOI=10.1038/sj.onc.1208978;
Grassmann R., Aboud M., Jeang K.T.;
"Molecular mechanisms of cellular transformation by HTLV-1 Tax.";
Oncogene 24:5976-5985(2005).
PubMed=14679154; DOI=10.1093/jnci/djg118;
Twizere J.-C., Kruys V., Lefebvre L., Vanderplasschen A., Collete D.,
Debacq C., Lai W.S., Jauniaux J.-C., Bernstein L.R., Semmes J.O.,
Burny A., Blackshear P.J., Kettmann R., Willems L.;
"Interaction of retroviral Tax oncoproteins with tristetraprolin and
regulation of tumor necrosis factor-alpha expression.";
J. Natl. Cancer Inst. 95:1846-1859(2003).
PubMed=16155601; DOI=10.1038/sj.onc.1208973;
Kashanchi F., Brady J.N.;
"Transcriptional and post-transcriptional gene regulation of HTLV-1.";
Oncogene 24:5938-5951(2005).
Garboczi D.N., Utz U., Ghosh P., Seth A., Kim J., VanTienhoven E.A.,
Biddison W.E., Wiley D.C.;
"Assembly, specific binding, and crystallization of a human TCR-
alphabeta with an antigenic Tax peptide from human T lymphotropic
virus type 1 and the class I MHC molecule HLA-A2.";
J. Immunol. 157:5403-5410(1996).
-!- FUNCTION: Transcriptional activator that activates both the viral
long terminal repeat (LTR) and cellular promoters via activation
of CREB, NF-kappa-B, SRF and AP-1 pathways. Binds to three 21 bp
repeat elements located within the LTRs, referred to as Tax-
responsive elements (TRE). Binding to TRE requires the interaction
with CREB1 and CREBBP. Also induces chromatin remodeling of
proviral LTR-mediated gene expression by recruiting the histone
acetyl transferases CREBBP and EP300 to the chromatin, which
results in histone acetylation. Via its interaction with IKK
regulatory subunit IKBKG, Tax-1 persistently stimulates I-kappa-B
kinase (IKK), resulting in constitutive activation of the
transcription factor NF-kappa-B. Induction of the nuclear
expression of members of the NFkB family of transcription factors,
which leads to up-regulated expression of many gene promoters
containing NFkB motifs. These genes include those encoding IL2,
IL15, IL2RA and IL15RA, leading to autocrine IL2/IL2RA and
IL15/IL15RA loops. The resulting T-cell proliferation leads to
malignant transformation and to the development of adult T-cell
leukemia (ATL). IL13, known to be linked to leukemogenesis, is
also up-regulated by Tax-1. Interaction with PDZ domain-containing
proteins induce IL2-independent growth, which may be a factor in
multi-step leukemogenesis. Inhibits the action of at least three
cellular tumor suppressors p53/TP53, RB1 and DLG1, and suppresses
their abilities to dictate apoptosis in primary cells. Required
for viral replication (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with host CREB1, DLG1, IKBKG, KDM4A,
MAGI3 and TAX1BP1. recruits the coactivators CREBBP, EP300 and
PCAF. Interaction with human CARM1 enhances Tax transactivation
and promotes methylation of histone H3. Interacts with host
SUV39H1 protein, leading to abrogate Tax transactivation of HTLV-1
LTR (By similarity). Interacts (via C-terminus) with host ZFP36
(via C-terminus); this interaction inhibits TAX to transactivate
viral long terminal repeat (LTR) promoter (PubMed:14679154).
{ECO:0000250, ECO:0000269|PubMed:14679154}.
Q53HC0:CCDC92 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-719994;
Q96MT8:CEP63 (xeno); NbExp=5; IntAct=EBI-9675698, EBI-741977;
P78560:CRADD (xeno); NbExp=3; IntAct=EBI-9675698, EBI-520375;
O14595:CTDSP2 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-2802973;
Q9BY27:DGCR6L (xeno); NbExp=3; IntAct=EBI-9675698, EBI-742953;
P43268:ETV4 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-6447147;
O15287:FANCG (xeno); NbExp=3; IntAct=EBI-9675698, EBI-81610;
Q969F0:FATE1 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-743099;
Q5T8I9:HENMT1 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-9675710;
O14964:HGS (xeno); NbExp=4; IntAct=EBI-9675698, EBI-740220;
P19012:KRT15 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-739566;
P19013:KRT4 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-2371606;
P05787:KRT8 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-297852;
Q8N448:LNX2 (xeno); NbExp=4; IntAct=EBI-9675698, EBI-2340947;
P82932:MRPS6 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-716172;
P07196:NEFL (xeno); NbExp=4; IntAct=EBI-9675698, EBI-475646;
Q9GZT8:NIF3L1 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-740897;
P29474:NOS3 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-1391623;
Q6ZVK8:NUDT18 (xeno); NbExp=5; IntAct=EBI-9675698, EBI-740486;
Q9NP87:POLM (xeno); NbExp=3; IntAct=EBI-9675698, EBI-9675790;
Q969H6:POP5 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-366525;
Q33E94:RFX4 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-9675925;
Q92546:RGP1 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-2823702;
Q9H4K1:RIBC2 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-740128;
Q6PF05:TTC23L (xeno); NbExp=3; IntAct=EBI-9675698, EBI-8656864;
Q8IZQ1:WDFY3 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-1569256;
Q8N883:ZNF614 (xeno); NbExp=3; IntAct=EBI-9675698, EBI-9675993;
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:14679154}.
Host cytoplasm {ECO:0000269|PubMed:14679154}. Note=Shuttles from
the nucleus to the cytoplasm. Found predominantly in the nucleus,
where it is equally distributed between the nucleoplasm and the
nuclear matrix (By similarity). Colocalizes with host ZFP36 in the
nucleus and the cytoplasm in a region surrounding the nucleus
(PubMed:14679154). {ECO:0000250, ECO:0000269|PubMed:14679154}.
-!- INDUCTION: Down-regulated by P30II.
-!- DOMAIN: The 48 N-terminal residues contain a non-canonical
functional nuclear localization signal (NLS). {ECO:0000250}.
-!- DOMAIN: The PDZ-binding domain mediates binding to human DLG1 and
MAGI3. Interaction with other PDZ domain-containing protein
induces IL2-independent growth (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylation at Thr-48 results in the loss of NF-kappa-B
activation function. Phosphorylation at Thr-215 results in loss of
CREB and NF-B responsive promoters activation. Phosphorylation at
Thr-184 and Ser-336 have no effect on these Tax functions.
Phosphorylation of either Ser-300 or Ser-301 is necessary for
localization to nuclear bodies. Thr-48, Thr-184, Thr-215 and Ser-
336 are highly phosphorylated, whereas Ser-300 or Ser-301 are only
rarely phosphorylated (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: HTLV-1 lineages are divided in four clades, A
(Cosmopolitan), B (Central African group), C (Melanesian group)
and D (New Central African group).
-!- SIMILARITY: Belongs to the deltaretrovirus Tax protein family.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; D13784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF033817; AAC82583.1; -; Genomic_DNA.
PIR; E28136; TNLJCN.
RefSeq; NP_057864.1; NC_001436.1.
PDB; 1AO7; X-ray; 2.60 A; C=11-19.
PDB; 1BD2; X-ray; 2.50 A; C=11-19.
PDB; 1HHK; X-ray; 2.50 A; C/F=11-19.
PDB; 1IM3; X-ray; 2.20 A; C/G/K/O=11-19.
PDB; 2AV1; X-ray; 1.95 A; C/F=11-19.
PDB; 2AV7; X-ray; 2.05 A; C/F=11-19.
PDB; 5IRO; X-ray; 2.64 A; B/F/J/N/R/V=11-19.
PDBsum; 1AO7; -.
PDBsum; 1BD2; -.
PDBsum; 1HHK; -.
PDBsum; 1IM3; -.
PDBsum; 2AV1; -.
PDBsum; 2AV7; -.
PDBsum; 5IRO; -.
SMR; P14079; -.
IntAct; P14079; 56.
MINT; P14079; -.
GeneID; 1491938; -.
KEGG; vg:1491938; -.
KO; K21857; -.
OrthoDB; VOG090000CJ; -.
EvolutionaryTrace; P14079; -.
Proteomes; UP000001061; Genome.
Proteomes; UP000110593; Genome.
GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0039652; P:activation by virus of host NF-kappaB transcription factor activity; IEA:UniProtKB-KW.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0039646; P:modulation by virus of host G0/G1 transition checkpoint; IEA:UniProtKB-KW.
GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
GO; GO:0039593; P:suppression by virus of host exit from mitosis; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004120; Tax.
Pfam; PF02959; Tax; 1.
1: Evidence at protein level;
3D-structure; Activation of host NF-kappa-B by virus; Activator;
Complete proteome; DNA-binding;
G0/G1 host cell cycle checkpoint dysregulation by virus;
G1/S host cell cycle checkpoint dysregulation by virus;
Host cytoplasm; Host nucleus; Host-virus interaction;
Inhibition of host mitotic exit by virus; Metal-binding;
Modulation of host cell cycle by virus; Oncogene; Phosphoprotein;
Reference proteome; SH3-binding; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 353 Protein Tax-1.
ZN_FING 23 49 {ECO:0000255}.
REGION 2 58 Interaction with CREB1. {ECO:0000250}.
REGION 81 95 Interaction with CREBBP/P300.
REGION 106 111 Interaction with IKBKG. {ECO:0000250}.
REGION 116 145 Homodimerization. {ECO:0000250}.
REGION 213 248 Homodimerization. {ECO:0000250}.
REGION 289 322 Transactivation. {ECO:0000250}.
REGION 312 319 Interaction with CREBBP C-terminus.
MOTIF 73 80 SH3-binding. {ECO:0000255}.
MOTIF 188 202 Nuclear export signal. {ECO:0000250}.
MOTIF 350 353 PDZ-binding. {ECO:0000250}.
MOD_RES 48 48 Phosphothreonine; by host. {ECO:0000250}.
MOD_RES 184 184 Phosphothreonine; by host. {ECO:0000250}.
MOD_RES 215 215 Phosphothreonine; by host. {ECO:0000250}.
MOD_RES 300 300 Phosphoserine; by host. {ECO:0000250}.
MOD_RES 301 301 Phosphoserine; by host. {ECO:0000250}.
MOD_RES 336 336 Phosphoserine; by host. {ECO:0000250}.
SEQUENCE 353 AA; 39513 MW; 60DF69BFD58265F4 CRC64;

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