REX_HTLV2
ID REX_HTLV2 Reviewed; 170 AA.
AC Q85601;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 69.
DE RecName: Full=Protein Rex;
DE AltName: Full=Rev homolog;
DE AltName: Full=Rex-2;
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].
RA Glaser J.B., Dube S., Poiesz B.J.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP RNA-BINDING.
RX PubMed=2016758; DOI=10.1128/jvi.65.5.2261-2272.1991;
RA Yip M.T., Dynan W.S., Green P.L., Black A.C., Arrigo S.J., Torbati A.,
RA Heaphy S., Ruland C., Rosenblatt J.D., Chen I.S.Y.;
RT "Human T-cell leukemia virus (HTLV) type II Rex protein binds specifically
RT to RNA sequences of the HTLV long terminal repeat but poorly to the human
RT immunodeficiency virus type 1 Rev-responsive element.";
RL J. Virol. 65:2261-2272(1991).
RN [4]
RP FUNCTION.
RX PubMed=10482560; DOI=10.1128/jvi.73.10.8112-8119.1999;
RA Kusuhara K., Anderson M., Pettiford S.M., Green P.L.;
RT "Human T-cell leukemia virus type 2 Rex protein increases stability and
RT promotes nuclear to cytoplasmic transport of gag/pol and env RNAs.";
RL J. Virol. 73:8112-8119(1999).
RN [5]
RP PHOSPHORYLATION AT SER-151 AND SER-153, AND MUTAGENESIS OF THR-4; THR-9;
RP THR-19; SER-24; SER-31; THR-35; SER-37; SER-51; SER-65; SER-71; THR-72;
RP SER-74; THR-77; SER-79; SER-84; 88-SER--THR-90; SER-92; SER-95; SER-98;
RP SER-107; SER-109; SER-117; SER-125; SER-131; THR-132; THR-135;
RP 144-SER--SER-148; 151-SER--SER-153; SER-158; THR-162; SER-163 AND THR-164.
RX PubMed=11507189; DOI=10.1128/jvi.75.18.8440-8448.2001;
RA Narayan M., Kusuhara K., Green P.L.;
RT "Phosphorylation of two serine residues regulates human T-cell leukemia
RT virus type 2 Rex function.";
RL J. Virol. 75:8440-8448(2001).
RN [6]
RP DOMAIN, AND MUTAGENESIS OF THR-4; THR-9; SER-65; SER-71; SER-92; SER-95;
RP SER-125; SER-131; THR-132; 144-SER--SER-148; 151-SER--SER-153; SER-158;
RP THR-162; SER-163 AND THR-164.
RX PubMed=14610204; DOI=10.1128/jvi.77.23.12829-12840.2003;
RA Narayan M., Younis I., D'Agostino D.M., Green P.L.;
RT "Functional domain structure of human T-cell leukemia virus type 2 rex.";
RL J. Virol. 77:12829-12840(2003).
RN [7]
RP REVIEW.
RX PubMed=15574380; DOI=10.2741/1539;
RA Younis I., Green P.L.;
RT "The human T-cell leukemia virus Rex protein.";
RL Front. Biosci. 10:431-445(2005).
CC -!- FUNCTION: Rex escorts unspliced gag-pro-pol and singly spliced env
CC mRNAs out of the nucleus of infected cells. These mRNAs carry a
CC recognition sequence called Rex responsive element (RxRE or XRE)
CC located at the 3' region of the long terminal repeat (LTR). This
CC function is essential since most HTLV proteins are translated from
CC unspliced or partially spliced pre-mRNAs that cannot exit the nucleus
CC by the pathway used by fully processed cellular mRNAs (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:10482560}.
CC -!- SUBUNIT: Homomultimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q85601; Q96FJ2: DYNLL2; Xeno; NbExp=3; IntAct=EBI-9676175, EBI-742371;
CC Q85601; Q8N448: LNX2; Xeno; NbExp=4; IntAct=EBI-9676175, EBI-2340947;
CC Q85601; Q9GZT8: NIF3L1; Xeno; NbExp=3; IntAct=EBI-9676175, EBI-740897;
CC -!- SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000250}. Host
CC cytoplasm {ECO:0000250}. Note=The presence of both nuclear import (NLS)
CC and nuclear export (NES) signals leads to continuous shuttling between
CC the nucleus and cytoplasm. {ECO:0000250}.
CC -!- DOMAIN: The RNA-binding motif binds to the RxRE, a complex secondary
CC structure consisting of four stem loops and a long stretch of stem
CC structure, present in incompletely spliced viral pre-mRNAs. This region
CC also contains the NLS which mediates nuclear localization. These
CC overlapping functions prevent Rex bound to RxRE from undesirable return
CC to the nucleus. When Rex binds the RxRE, the NLS becomes masked while
CC the NES remains accessible (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation is essential for RNA-binding and function.
CC {ECO:0000269|PubMed:11507189}.
CC -!- SIMILARITY: Belongs to the deltaretrovirus Rex protein family.
CC {ECO:0000305}.
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DR EMBL; M10060; AAB59886.1; -; Genomic_DNA.
DR EMBL; AF412314; AAL30505.1; -; Genomic_DNA.
DR RefSeq; NP_041004.1; NC_001488.1.
DR IntAct; Q85601; 7.
DR MINT; Q85601; -.
DR iPTMnet; Q85601; -.
DR PRIDE; Q85601; -.
DR GeneID; 1491945; -.
DR KEGG; vg:1491945; -.
DR Proteomes; UP000009254; Genome.
DR Proteomes; UP000174344; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host nucleus; mRNA transport; Phosphoprotein;
KW Reference proteome; RNA-binding; Transport.
FT CHAIN 1..170
FT /note="Protein Rex"
FT /id="PRO_0000259786"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..71
FT /note="Homomultimerization"
FT REGION 69..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..132
FT /note="Homomultimerization"
FT MOTIF 2..19
FT /note="Nuclear localization signal, and RNA-binding (RxRE)"
FT /evidence="ECO:0000250"
FT MOTIF 83..94
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:11507189"
FT MOD_RES 153
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 4
FT /note="T->A: 50% loss of function, no effect on Rex's
FT phosphorylation and RNA-binding; when associated with A-9."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 9
FT /note="T->A: 50% loss of function, no effect on Rex's
FT phosphorylation and RNA-binding; when associated with A-4."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 19
FT /note="T->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 24
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 31
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 35
FT /note="T->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 37
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 51
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 65
FT /note="S->A: 80% loss of function, no effect on Rex's
FT phosphorylation and RNA-binding; when associated with A-
FT 71."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 71
FT /note="S->A: 80% loss of function, no effect on Rex's
FT phosphorylation and RNA-binding; when associated with A-
FT 65."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 72
FT /note="T->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 74
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 77
FT /note="T->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 79
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 84
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 88..90
FT /note="SNT->ANA: Almost complete loss of function, no
FT effect on Rex's phosphorylation."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 92
FT /note="S->A: Almost complete loss of function, no effect on
FT Rex's phosphorylation and RNA-binding; when associated with
FT A-95."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 95
FT /note="S->A: Almost complete loss of function, no effect on
FT Rex's phosphorylation and RNA-binding; when associated with
FT A-92."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 98
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 107
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 109
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 117
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 125
FT /note="S->A: 70% loss of function, no effect on Rex's
FT phosphorylation and RNA-binding; when associated with A-131
FT and A-132."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 131
FT /note="S->A: 70% loss of function, no effect on Rex's
FT phosphorylation and RNA-binding; when associated with A-125
FT and A-132."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 132
FT /note="T->A: 70% loss of function, no effect on Rex's
FT phosphorylation and RNA-binding; when associated with A-125
FT and A-131."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 135
FT /note="T->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189"
FT MUTAGEN 144..148
FT /note="SGISS->AGIAA: No effect on function and RNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 151..153
FT /note="SPS->APA: Loss of Rex's phosphorylation, function
FT and RNA-binding."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 151..153
FT /note="SPS->DPD: Increase in Rex's function and RNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 151..153
FT /note="SPS->TPT: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 158
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 162
FT /note="T->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 163
FT /note="S->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
FT MUTAGEN 164
FT /note="T->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:11507189,
FT ECO:0000269|PubMed:14610204"
SQ SEQUENCE 170 AA; 18463 MW; E2B2AE24E2BC4D47 CRC64;
MPKTRRQRTR RARRNRPPTP WPISQDLDRA SYMDTPSTCL AIVYRPIGVP SQVVYVPPAY
IDMPSWPPVQ STNSPGTPSM DALSALLSNT LSLASPPSPP REPQGPSRSL PLPPLLSPPR
FHLPSFNQCE STPPTEMDAW NQPSGISSPP SPSPNLASVP KTSTPPGEKP
