HBZ_HTL1A
ID HBZ_HTL1A Reviewed; 209 AA.
AC P0C746;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 23-FEB-2022, entry version 33.
DE RecName: Full=HTLV-1 basic zipper factor;
DE Short=HBZ;
GN Name=HBZ;
OS Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=11926;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6304725; DOI=10.1073/pnas.80.12.3618;
RA Seiki M., Hattori S., Hirayama Y., Yoshida M.C.;
RT "Human adult T-cell leukemia virus: complete nucleotide sequence of the
RT provirus genome integrated in leukemia cell DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3618-3622(1983).
RN [2]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH HOST ATF4.
RX PubMed=12438606; DOI=10.1128/jvi.76.24.12813-12822.2002;
RA Gaudray G., Gachon F., Basbous J., Biard-Piechaczyk M., Devaux C.,
RA Mesnard J.M.;
RT "The complementary strand of the human T-cell leukemia virus type 1 RNA
RT genome encodes a bZIP transcription factor that down-regulates viral
RT transcription.";
RL J. Virol. 76:12813-12822(2002).
RN [3]
RP INTERACTION WITH HOST JUN AND JUNB.
RX PubMed=12937177; DOI=10.1074/jbc.m307275200;
RA Basbous J., Arpin C., Gaudray G., Piechaczyk M., Devaux C., Mesnard J.M.;
RT "The HBZ factor of human T-cell leukemia virus type I dimerizes with
RT transcription factors JunB and c-Jun and modulates their transcriptional
RT activity.";
RL J. Biol. Chem. 278:43620-43627(2003).
RN [4]
RP ISOFORM HBZ-SI.
RX PubMed=16474156; DOI=10.1128/jvi.80.5.2495-2505.2006;
RA Murata K., Hayashibara T., Sugahara K., Uemura A., Yamaguchi T.,
RA Harasawa H., Hasegawa H., Tsuruda K., Okazaki T., Koji T., Miyanishi T.,
RA Yamada Y., Kamihira S.;
RT "A novel alternative splicing isoform of human T-cell leukemia virus type 1
RT bZIP factor (HBZ-SI) targets distinct subnuclear localization.";
RL J. Virol. 80:2495-2505(2006).
RN [5]
RP INTERACTION WITH HOST CREB1.
RX PubMed=17151132; DOI=10.1128/jvi.00480-06;
RA Lemasson I., Lewis M.R., Polakowski N., Hivin P., Cavanagh M.H.,
RA Thebault S., Barbeau B., Nyborg J.K., Mesnard J.M.;
RT "Human T-cell leukemia virus type 1 (HTLV-1) bZIP protein interacts with
RT the cellular transcription factor CREB to inhibit HTLV-1 transcription.";
RL J. Virol. 81:1543-1553(2007).
RN [6]
RP INTERACTION WITH HOST JUND.
RX PubMed=18078517; DOI=10.1186/1742-4690-4-92;
RA Kuhlmann A.S., Villaudy J., Gazzolo L., Castellazzi M., Mesnard J.M.,
RA Duc Dodon M.;
RT "HTLV-1 HBZ cooperates with JunD to enhance transcription of the human
RT telomerase reverse transcriptase gene (hTERT).";
RL Retrovirology 4:92-92(2007).
RN [7]
RP INTERACTION WITH HOST EP300.
RX PubMed=18599479; DOI=10.1074/jbc.m803116200;
RA Clerc I., Polakowski N., Andre-Arpin C., Cook P., Barbeau B., Mesnard J.M.,
RA Lemasson I.;
RT "An interaction between the human T cell leukemia virus type 1 basic
RT leucine zipper factor (HBZ) and the KIX domain of p300/CBP contributes to
RT the down-regulation of tax-dependent viral transcription by HBZ.";
RL J. Biol. Chem. 283:23903-23913(2008).
RN [8]
RP FUNCTION.
RX PubMed=19064727; DOI=10.1182/blood-2008-06-161729;
RA Zhao T., Yasunaga J., Satou Y., Nakao M., Takahashi M., Fujii M.,
RA Matsuoka M.;
RT "Human T-cell leukemia virus type 1 bZIP factor selectively suppresses the
RT classical pathway of NF-kappaB.";
RL Blood 113:2755-2764(2009).
CC -!- FUNCTION: Contributes to the regulation of viral RNA transcription by
CC interacting with host proteins involved in transcriptional activation
CC such as ATF4, or CREB1, and by inhibiting their activity. Additionally,
CC HBZ suppresses host NF-kappa-B-driven transcription mediated by host
CC RELA as well as transcription of some classical NF-kappa-B target
CC genes, including IL8, IL2RA, IRF4, VCAM1, and VEGFA.
CC {ECO:0000269|PubMed:19064727}.
CC -!- SUBUNIT: Interacts with host ATF4; this interaction inhibits viral RNA
CC transcriptional activation by preventing ATF4 binding to Tax-responsive
CC elements. Interacts with host CREB1; this interaction inhibits host
CC CREB1 transcriptional activity. Interacts with host JUN, JUNB and JUND.
CC Interacts with host EP300. {ECO:0000269|PubMed:12438606,
CC ECO:0000269|PubMed:12937177, ECO:0000269|PubMed:17151132,
CC ECO:0000269|PubMed:18078517, ECO:0000269|PubMed:18599479}.
CC -!- INTERACTION:
CC P0C746; P18846: ATF1; Xeno; NbExp=2; IntAct=EBI-10890294, EBI-852794;
CC P0C746; P15336: ATF2; Xeno; NbExp=3; IntAct=EBI-10890294, EBI-1170906;
CC P0C746; P17544: ATF7; Xeno; NbExp=2; IntAct=EBI-10890294, EBI-765623;
CC P0C746; P53567: CEBPG; Xeno; NbExp=2; IntAct=EBI-10890294, EBI-740209;
CC P0C746; P16220: CREB1; Xeno; NbExp=2; IntAct=EBI-10890294, EBI-711855;
CC P0C746; Q9NS37: CREBZF; Xeno; NbExp=3; IntAct=EBI-10890294, EBI-632965;
CC P0C746; P05412: JUN; Xeno; NbExp=3; IntAct=EBI-10890294, EBI-852823;
CC P0C746; P17275: JUNB; Xeno; NbExp=2; IntAct=EBI-10890294, EBI-748062;
CC P0C746; P17535: JUND; Xeno; NbExp=2; IntAct=EBI-10890294, EBI-2682803;
CC P0C746; O75444: MAF; Xeno; NbExp=2; IntAct=EBI-10890294, EBI-2805091;
CC P0C746; Q9Y5Q3: MAFB; Xeno; NbExp=3; IntAct=EBI-10890294, EBI-3649340;
CC P0C746; O15525: MAFG; Xeno; NbExp=3; IntAct=EBI-10890294, EBI-713514;
CC P0C746; Q9DGW5: MDV005; Xeno; NbExp=2; IntAct=EBI-10890294, EBI-10889526;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:12438606}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=HBZ;
CC IsoId=P0C746-1; Sequence=Displayed;
CC Name=HBZ-SI;
CC IsoId=P0C746-2; Sequence=VSP_037726;
CC -!- DOMAIN: Contains three nuclear localization signals NLS-1 and NLS-2,
CC corresponding to two regions rich in basic amino acids, and NLS-3
CC corresponding to its DNA-binding domain.
CC -!- MISCELLANEOUS: Expressed from antisense transcripts. While mRNA
CC expression levels of HBZ-SI were similar to those of HBZ, HBZ-SI seems
CC slightly more expressed at the protein level ex vivo.
CC -!- SIMILARITY: Belongs to the HTLV-1 HBZ protein family. {ECO:0000305}.
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DR EMBL; J02029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6DMX; X-ray; 2.80 A; E/J=6-59.
DR PDBsum; 6DMX; -.
DR SMR; P0C746; -.
DR IntAct; P0C746; 15.
DR Proteomes; UP000007683; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR InterPro; IPR026220; HTLV1ZIPPER.
DR PRINTS; PR02097; HTLV1ZIPPER.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Host nucleus;
KW Host-virus interaction; Reference proteome.
FT CHAIN 1..209
FT /note="HTLV-1 basic zipper factor"
FT /id="PRO_0000379886"
FT REGION 48..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 87..92
FT /note="Nuclear localization signal 1"
FT MOTIF 116..120
FT /note="Nuclear localization signal 2"
FT MOTIF 137..141
FT /note="Nuclear localization signal 3"
FT VAR_SEQ 1..7
FT /note="MVNFVSA -> MAAS (in isoform HBZ-SI)"
FT /evidence="ECO:0000305"
FT /id="VSP_037726"
FT HELIX 19..58
FT /evidence="ECO:0007829|PDB:6DMX"
SQ SEQUENCE 209 AA; 24893 MW; B47598ABCE66EE71 CRC64;
MVNFVSAGLF RCLPVSCPED LLVEELVDGL LSLEEELKDK EEEEAVLDGL LSLEEESRGR
LRRGPPGEKA PPRGETHRDR QRRAEEKRKR KKEREKEEEK QTAEYLKRKE EEKARRRRRA
EKKAADVARR KQEEQERRER KWRQGAEKAK QHSARKEKMQ ELGIDGYTRQ LEGEVESLEA
ERRKLLQEKE DLMGEVNYWQ GRLEAMWLQ
