TAX_HTLV2
ID TAX_HTLV2 Reviewed; 331 AA.
AC P03410; P03411; Q85602;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 23-FEB-2022, entry version 87.
DE RecName: Full=Protein Tax-2;
DE AltName: Full=Trans-activating transcriptional regulatory protein of HTLV-2;
GN Name=tax;
OS Human T-cell leukemia virus 2 (HTLV-2).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=11909;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2582407; DOI=10.1073/pnas.82.10.3101;
RA Shimotohno K., Takahashi Y., Shimizu N., Gojobori T., Golde D.W.,
RA Chen I.S.Y., Miwa M., Sugimura T.;
RT "Complete nucleotide sequence of an infectious clone of human T-cell
RT leukemia virus type II: an open reading frame for the protease gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3101-3105(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6330894; DOI=10.1126/science.6330894;
RA Haseltine W.A., Sodroski J., Patarca R., Briggs D., Perkins D.,
RA Wong-Staal F.;
RT "Structure of 3' terminal region of type II human T lymphotropic virus:
RT evidence for new coding region.";
RL Science 225:419-421(1984).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=15269214; DOI=10.1074/jbc.m400497200;
RA Meertens L., Chevalier S., Weil R., Gessain A., Mahieux R.;
RT "A 10-amino acid domain within human T-cell leukemia virus type 1 and type
RT 2 tax protein sequences is responsible for their divergent subcellular
RT distribution.";
RL J. Biol. Chem. 279:43307-43320(2004).
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 three 21 bp repeat elements
CC located within the LTRs, referred to as Tax-responsive elements (TRE).
CC Binding to TRE requires the interaction with CREB1 and CREBBP. Induces
CC T-cell transformation, although much less efficiently than HTLV-1.
CC Required for viral replication (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with host CREB1, CREBBP and EP300 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P03410; Q96MT8: CEP63; Xeno; NbExp=4; IntAct=EBI-9676218, EBI-741977;
CC P03410; O43186: CRX; Xeno; NbExp=3; IntAct=EBI-9676218, EBI-748171;
CC P03410; O14964: HGS; Xeno; NbExp=4; IntAct=EBI-9676218, EBI-740220;
CC P03410; Q6PEX3: KRTAP26-1; Xeno; NbExp=3; IntAct=EBI-9676218, EBI-3957672;
CC P03410; Q8N448: LNX2; Xeno; NbExp=4; IntAct=EBI-9676218, EBI-2340947;
CC P03410; Q9BRK4: LZTS2; Xeno; NbExp=5; IntAct=EBI-9676218, EBI-741037;
CC P03410; P82932: MRPS6; Xeno; NbExp=3; IntAct=EBI-9676218, EBI-716172;
CC P03410; Q6ZVK8: NUDT18; Xeno; NbExp=4; IntAct=EBI-9676218, EBI-740486;
CC P03410; P35711: SOX5; Xeno; NbExp=3; IntAct=EBI-9676218, EBI-3505701;
CC P03410; Q9NZD8: SPG21; Xeno; NbExp=3; IntAct=EBI-9676218, EBI-742688;
CC P03410; Q9Y2D8: SSX2IP; Xeno; NbExp=3; IntAct=EBI-9676218, EBI-2212028;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:15269214}.
CC Host nucleus {ECO:0000269|PubMed:15269214}. Note=Tax-2 is mainly found
CC in the cytoplasm.
CC -!- DOMAIN: The 48 N-terminal residues contain a non-canonical functional
CC nuclear localization signal (NLS). {ECO:0000250}.
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 Tax functions. Phosphorylation of either Ser-300
CC or Ser-301 is necessary for localization to nuclear bodies. Thr-48,
CC Thr-184 and Thr-215 are highly phosphorylated, whereas Ser-300 or Ser-
CC 301 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; M10060; AAB59888.1; -; Genomic_DNA.
DR EMBL; K02532; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PIR; A04012; TNLJH2.
DR PIR; A04013; TNLJT2.
DR PIR; A48751; A48751.
DR RefSeq; NP_041005.1; NC_001488.1.
DR IntAct; P03410; 48.
DR MINT; P03410; -.
DR PRIDE; P03410; -.
DR GeneID; 1491946; -.
DR KEGG; vg:1491946; -.
DR Proteomes; UP000009254; 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:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
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; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR004120; Tax.
DR Pfam; PF02959; Tax; 1.
DR SUPFAM; SSF50022; SSF50022; 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 Reference proteome; SH3-binding; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..331
FT /note="Protein Tax-2"
FT /id="PRO_0000085496"
FT ZN_FING 23..49
FT /evidence="ECO:0000255"
FT REGION 2..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 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 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 CONFLICT 5
FT /note="P -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="D -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="T -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="Y -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="E -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 37318 MW; A13F590EB6075101 CRC64;
MAHFPGFGQS LLYGYPVYVF GDCVQADWCP VSGGLCSTRL HRHALLATCP EHQLTWDPID
GRVVSSPLQY LIPRLPSFPT QRTSRTLKVL TPPTTPVSPK VPPAFFQSMR KHTPYRNGCL
EPTLGDQLPS LAFPEPGLRP QNIYTTWGKT VVCLYLYQLS PPMTWPLIPH VIFCHPRQLG
AFLTKVPLKR LEELLYKMFL HTGTVIVLPE DDLPTTMFQP VRAPCIQTAW CTGLLPYHSI
LTTPGLIWTF NDGSPMISGP YPKAGQPSLV VQSSLLIFEK FETKAFHPSY LLSHQLIQYS
SFHNLHLLFD EYTNIPVSIL FNKEEADDNG D
