HFA1A_ARATH
ID HFA1A_ARATH Reviewed; 495 AA.
AC P41151; O23615; Q0WNT9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Heat stress transcription factor A-1a;
DE Short=AtHsfA1a;
DE AltName: Full=AtHsf-13;
DE AltName: Full=Heat shock factor protein 1;
DE Short=HSF 1;
DE AltName: Full=Heat shock transcription factor 1;
DE Short=HSTF 1;
GN Name=HSFA1A; Synonyms=HSF1, HSF13; OrderedLocusNames=At4g17750;
GN ORFNames=dl4910c, FCAALL.107;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=7948881; DOI=10.1007/bf00039545;
RA Huebel A., Schoeffl F.;
RT "Arabidopsis heat shock factor: isolation and characterization of the gene
RT and the recombinant protein.";
RL Plant Mol. Biol. 26:353-362(1994).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-495.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND DOMAIN AHA.
RX PubMed=11599559; DOI=10.1379/1466-1268(2001)006<0177:aathst>2.0.co;2;
RA Nover L., Bharti K., Doering P., Mishra S.K., Ganguli A., Scharf K.-D.;
RT "Arabidopsis and the heat stress transcription factor world: how many heat
RT stress transcription factors do we need?";
RL Cell Stress Chaperones 6:177-189(2001).
RN [7]
RP INTERACTION WITH HSP70-1 AND HSP70-4.
RX PubMed=11807141; DOI=10.1093/jexbot/53.367.371;
RA Kim B.H., Schoeffl F.;
RT "Interaction between Arabidopsis heat shock transcription factor 1 and 70
RT kDa heat shock proteins.";
RL J. Exp. Bot. 53:371-375(2002).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18407058; DOI=10.1016/s1673-8527(08)60016-8;
RA Guo J., Wu J., Ji Q., Wang C., Luo L., Yuan Y., Wang Y., Wang J.;
RT "Genome-wide analysis of heat shock transcription factor families in rice
RT and Arabidopsis.";
RL J. Genet. Genomics 35:105-118(2008).
RN [9]
RP INTERACTION WITH CRK1, AND PHOSPHORYLATION BY CRK1.
RX PubMed=18466301; DOI=10.1111/j.1365-313x.2008.03544.x;
RA Liu H.-T., Gao F., Li G.-L., Han J.-L., Liu D.-L., Sun D.-Y., Zhou R.-G.;
RT "The calmodulin-binding protein kinase 3 is part of heat-shock signal
RT transduction in Arabidopsis thaliana.";
RL Plant J. 55:760-773(2008).
RN [10]
RP INTERACTION WITH HSBP.
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 [11]
RP INTERACTION WITH HSBP.
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: Transcriptional activator that specifically binds DNA
CC sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
CC -!- SUBUNIT: Homotrimer (PubMed:11807141). Interacts with HSP70-1 and
CC HSP70-4 (PubMed:11807141). Binds to CRK1 (PubMed:18466301). Binds to
CC HSBP (PubMed:20388662, PubMed:20657173). {ECO:0000269|PubMed:11807141,
CC ECO:0000269|PubMed:18466301, ECO:0000269|PubMed:20388662,
CC ECO:0000269|PubMed:20657173}.
CC -!- INTERACTION:
CC P41151; O80673: CRK1; NbExp=3; IntAct=EBI-1544927, EBI-1804894;
CC P41151; P28147: TBP1; NbExp=3; IntAct=EBI-1544927, EBI-1247453;
CC P41151; P28148: TBP2; NbExp=2; IntAct=EBI-1544927, EBI-1247465;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus.
CC -!- TISSUE SPECIFICITY: Constitutively expressed.
CC {ECO:0000269|PubMed:7948881}.
CC -!- INDUCTION: By heat stress. {ECO:0000269|PubMed:7948881}.
CC -!- DOMAIN: The hydrophobic-rich region (HR-A/B) corresponds to the
CC oligomerization domain. AHA motif is a transcriptional activator
CC element. {ECO:0000269|PubMed:11599559}.
CC -!- PTM: Exhibits temperature-dependent phosphorylation (By similarity).
CC Phosphorylated by CRK1. {ECO:0000250, ECO:0000269|PubMed:18466301}.
CC -!- SIMILARITY: Belongs to the HSF family. Class A subfamily.
CC {ECO:0000305}.
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DR EMBL; X76167; CAA53761.1; -; Genomic_DNA.
DR EMBL; Z97344; CAB10555.1; -; Genomic_DNA.
DR EMBL; AL161547; CAB78778.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83945.1; -; Genomic_DNA.
DR EMBL; AK229347; BAF01210.1; -; mRNA.
DR PIR; F71447; S52641.
DR RefSeq; NP_193510.1; NM_117884.3.
DR AlphaFoldDB; P41151; -.
DR SMR; P41151; -.
DR BioGRID; 12789; 17.
DR IntAct; P41151; 6.
DR STRING; 3702.AT4G17750.1; -.
DR iPTMnet; P41151; -.
DR PaxDb; P41151; -.
DR PRIDE; P41151; -.
DR ProteomicsDB; 230342; -.
DR EnsemblPlants; AT4G17750.1; AT4G17750.1; AT4G17750.
DR GeneID; 827496; -.
DR Gramene; AT4G17750.1; AT4G17750.1; AT4G17750.
DR KEGG; ath:AT4G17750; -.
DR Araport; AT4G17750; -.
DR TAIR; locus:2005495; AT4G17750.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_030308_0_6_1; -.
DR InParanoid; P41151; -.
DR OMA; HVTEANK; -.
DR OrthoDB; 1154048at2759; -.
DR PhylomeDB; P41151; -.
DR PRO; PR:P41151; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P41151; baseline and differential.
DR Genevisible; P41151; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..495
FT /note="Heat stress transcription factor A-1a"
FT /id="PRO_0000124582"
FT DNA_BIND 50..144
FT /evidence="ECO:0000250"
FT REGION 140..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..238
FT /note="Hydrophobic repeat HR-A/B"
FT REGION 255..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 262..268
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 433..442
FT /note="AHA"
FT MOTIF 482..489
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 145..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 216
FT /note="L -> M (in Ref. 1; CAA53761)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="E -> D (in Ref. 1; CAA53761)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="I -> T (in Ref. 1; CAA53761)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="F -> Y (in Ref. 1; CAA53761)"
FT /evidence="ECO:0000305"
FT CONFLICT 462..473
FT /note="Missing (in Ref. 1; CAA53761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 55744 MW; 2F0DE55252B5682A CRC64;
MFVNFKYFSF FIRTKMDGVT GGGTNIGEAV TAPPPRNPHP ATLLNANSLP PPFLSKTYDM
VEDPATDAIV SWSPTNNSFI VWDPPEFSRD LLPKYFKHNN FSSFVRQLNT YGFRKVDPDR
WEFANEGFLR GQKHLLKKIS RRKSVQGHGS SSSNPQSQQL SQGQGSMAAL SSCVEVGKFG
LEEEVEQLKR DKNVLMQELV KLRQQQQTTD NKLQVLVKHL QVMEQRQQQI MSFLAKAVQN
PTFLSQFIQK QTDSNMHVTE ANKKRRLRED STAATESNSH SHSLEASDGQ IVKYQPLRND
SMMWNMMKTD DKYPFLDGFS SPNQVSGVTL QEVLPITSGQ SQAYASVPSG QPLSYLPSTS
TSLPDTIMPE TSQIPQLTRE SINDFPTENF MDTEKNVPEA FISPSPFLDG GSVPIQLEGI
PEDPEIDELM SNFEFLEEYM PESPVFGDAT TLENNNNNNN NNNNNNNNNN NNNTNGRHMD
KLIEELGLLT SETEH
