HSBP_ARATH
ID HSBP_ARATH Reviewed; 86 AA.
AC Q8GW48; O23431;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Heat shock factor-binding protein {ECO:0000303|PubMed:20388662};
DE Short=AtHSBP {ECO:0000303|PubMed:20388662};
GN Name=HSBP {ECO:0000312|EMBL:AEE83654.1};
GN OrderedLocusNames=At4g15802 {ECO:0000312|Araport:AT4G15802};
GN ORFNames=dl3940c {ECO:0000312|EMBL:CAB10358.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-35, INDUCTION BY HEAT
RP SHOCK, SUBCELLULAR LOCATION, INTERACTION WITH HSFA1A; HSFA1B AND HSFA2, AND
RP SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=20388662; DOI=10.1104/pp.109.151225;
RA Hsu S.-F., Lai H.-C., Jinn T.-L.;
RT "Cytosol-localized heat shock factor-binding protein, AtHSBP, functions as
RT a negative regulator of heat shock response by translocation to the nucleus
RT and is required for seed development in Arabidopsis.";
RL Plant Physiol. 153:773-784(2010).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-35; ILE-42; MET-45;
RP ILE-49 AND LEU-52, AND INTERACTION WITH HSFA1A AND HSFA1B.
RC STRAIN=cv. Columbia;
RX PubMed=20657173; DOI=10.4161/psb.5.8.12404;
RA Hsu S.-F., Jinn T.-L.;
RT "AtHSBP functions in seed development and the motif is required for
RT subcellular localization and interaction with AtHSFs.";
RL Plant Signal. Behav. 5:1042-1044(2010).
CC -!- FUNCTION: Negative regulator of the heat shock (HS) response. Affects
CC negatively HSFA1B DNA-binding capacity in vitro (PubMed:20388662).
CC Involved in acquired thermotolerance but not basal thermotolerance
CC (PubMed:20388662). Crucial for seed development, after fertilization
CC and during embryogenesis (PubMed:20388662, PubMed:20657173).
CC {ECO:0000269|PubMed:20388662, ECO:0000269|PubMed:20657173}.
CC -!- SUBUNIT: Homohexamer (PubMed:20388662). Interacts with HSFA1A, HSFA1B
CC and HSFA2 (PubMed:20388662). {ECO:0000269|PubMed:20388662}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20388662}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:20388662}. Note=Translocates from the
CC cytosol to the nucleus upon heat shock (HS).
CC {ECO:0000269|PubMed:20388662}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in siliques and flowers, and, to a
CC lower extent, in roots, stems and leaves.
CC {ECO:0000269|PubMed:20388662}.
CC -!- INDUCTION: Reversibly induced by heat shock (HS).
CC {ECO:0000269|PubMed:20388662}.
CC -!- DISRUPTION PHENOTYPE: Early flowering, short siliques and seed abortion
CC (PubMed:20388662). The seed abortion occurs after fertilization and
CC during embryogenesis (PubMed:20657173). Differential HSP expression,
CC mainly during the recovery from heat shock (HS). Increased seedling
CC survival rates during acquired thermotolerance (AT) tests, but not in
CC response to basal thermotolerance (BT) tests (PubMed:20388662).
CC {ECO:0000269|PubMed:20388662, ECO:0000269|PubMed:20657173}.
CC -!- SIMILARITY: Belongs to the HSBP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78622.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97339; CAB10358.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161542; CAB78622.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83654.1; -; Genomic_DNA.
DR EMBL; AK119086; BAC43661.1; -; mRNA.
DR EMBL; BT004664; AAO42910.1; -; mRNA.
DR PIR; D71423; D71423.
DR RefSeq; NP_849392.4; NM_179061.5.
DR AlphaFoldDB; Q8GW48; -.
DR SMR; Q8GW48; -.
DR IntAct; Q8GW48; 1.
DR STRING; 3702.AT4G15802.1; -.
DR iPTMnet; Q8GW48; -.
DR MetOSite; Q8GW48; -.
DR PaxDb; Q8GW48; -.
DR PRIDE; Q8GW48; -.
DR ProMEX; Q8GW48; -.
DR ProteomicsDB; 230145; -.
DR DNASU; 827261; -.
DR EnsemblPlants; AT4G15802.1; AT4G15802.1; AT4G15802.
DR GeneID; 827261; -.
DR Gramene; AT4G15802.1; AT4G15802.1; AT4G15802.
DR KEGG; ath:AT4G15802; -.
DR Araport; AT4G15802; -.
DR TAIR; locus:1005716315; AT4G15802.
DR eggNOG; KOG4117; Eukaryota.
DR HOGENOM; CLU_149552_1_2_1; -.
DR InParanoid; Q8GW48; -.
DR OMA; VDPKNMQ; -.
DR OrthoDB; 1576489at2759; -.
DR PhylomeDB; Q8GW48; -.
DR PRO; PR:Q8GW48; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GW48; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IPI:TAIR.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:UniProtKB.
DR InterPro; IPR009643; HS1-bd.
DR PANTHER; PTHR19424; PTHR19424; 1.
DR Pfam; PF06825; HSBP1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..86
FT /note="Heat shock factor-binding protein"
FT /id="PRO_0000444378"
FT REGION 42..52
FT /note="Required for interactions with heat shock factors
FT (HSFs)"
FT /evidence="ECO:0000269|PubMed:20657173"
FT REGION 59..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..63
FT /evidence="ECO:0000255"
FT SITE 35
FT /note="Required for nucleus localization after heat shock
FT (HS)"
FT /evidence="ECO:0000269|PubMed:20388662,
FT ECO:0000269|PubMed:20657173"
FT MUTAGEN 35
FT /note="S->A: Dominantly expressed in the cytoplasm in
FT normal conditions. Impaired translocation from the cytosol
FT to the nucleus upon heat shock (HS)."
FT /evidence="ECO:0000269|PubMed:20388662,
FT ECO:0000269|PubMed:20657173"
FT MUTAGEN 42
FT /note="I->M: Expressed both in the cytoplasm and nucleus in
FT normal conditions, but strongly reduced interaction with
FT HSFA1A and HSFA1B; when associated with K-45."
FT /evidence="ECO:0000269|PubMed:20657173"
FT MUTAGEN 45
FT /note="M->K: Expressed both in the cytoplasm and nucleus in
FT normal conditions, but strongly reduced interaction with
FT HSFA1A and HSFA1B; when associated with M-42."
FT /evidence="ECO:0000269|PubMed:20657173"
FT MUTAGEN 49
FT /note="I->K: Expressed both in the cytoplasm and nucleus in
FT normal conditions, but strongly reduced interaction with
FT HSFA1A and HSFA1B; when associated with K-52."
FT /evidence="ECO:0000269|PubMed:20657173"
FT MUTAGEN 52
FT /note="L->K: Expressed both in the cytoplasm and nucleus in
FT normal conditions, but strongly reduced interaction with
FT HSFA1A and HSFA1B; when associated with K-49."
FT /evidence="ECO:0000269|PubMed:20657173"
SQ SEQUENCE 86 AA; 9347 MW; 1694AD6B4F1D07E4 CRC64;
MDGHDSEDTK QSTADMTAFV QNLLQQMQTR FQTMSDSIIT KIDDMGGRIN ELEQSINDLR
AEMGVEGTPP PASKSGDEPK TPASSS
