HFA1B_ARATH
ID HFA1B_ARATH Reviewed; 481 AA.
AC O81821; Q9LFD6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Heat stress transcription factor A-1b;
DE Short=AtHsfA1b;
DE AltName: Full=AtHsf-18;
DE AltName: Full=Heat shock factor protein 3;
DE Short=HSF 3;
DE AltName: Full=Heat shock transcription factor 3;
DE Short=HSTF 3;
GN Name=HSFA1B; Synonyms=HSF18, HSF3; OrderedLocusNames=At5g16820;
GN ORFNames=F5E19.160;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=9645433; DOI=10.1007/s004380050731;
RA Praendl R., Hinderhofer K., Eggers-Schumacher G., Schoeffl F.;
RT "HSF3, a new heat shock factor from Arabidopsis thaliana, derepresses the
RT heat shock response and confers thermotolerance when overexpressed in
RT transgenic plants.";
RL Mol. Gen. Genet. 258:269-278(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 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 [5]
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 [6]
RP INTERACTION WITH HSBP, AND REPRESSION BY 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 [7]
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 (By similarity). Binds to HSBP (PubMed:20388662,
CC PubMed:20657173). {ECO:0000250|UniProtKB:P41151,
CC ECO:0000269|PubMed:20388662, ECO:0000269|PubMed:20657173}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- INDUCTION: DNA-binding capacity is reduced by HSBP in vitro.
CC {ECO:0000269|PubMed:20388662}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HSF family. Class A subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01846.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y14068; CAA74397.1; -; mRNA.
DR EMBL; AL391147; CAC01846.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED92343.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92344.1; -; Genomic_DNA.
DR PIR; T51514; T51514.
DR PIR; T51945; T51945.
DR RefSeq; NP_197184.2; NM_121688.4.
DR RefSeq; NP_850832.1; NM_180501.3.
DR AlphaFoldDB; O81821; -.
DR SMR; O81821; -.
DR BioGRID; 16821; 5.
DR IntAct; O81821; 1.
DR STRING; 3702.AT5G16820.2; -.
DR iPTMnet; O81821; -.
DR PaxDb; O81821; -.
DR PRIDE; O81821; -.
DR ProteomicsDB; 230131; -.
DR EnsemblPlants; AT5G16820.1; AT5G16820.1; AT5G16820.
DR EnsemblPlants; AT5G16820.2; AT5G16820.2; AT5G16820.
DR GeneID; 831545; -.
DR Gramene; AT5G16820.1; AT5G16820.1; AT5G16820.
DR Gramene; AT5G16820.2; AT5G16820.2; AT5G16820.
DR KEGG; ath:AT5G16820; -.
DR Araport; AT5G16820; -.
DR TAIR; locus:2149050; AT5G16820.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_030308_0_0_1; -.
DR InParanoid; O81821; -.
DR OMA; PRYESVS; -.
DR OrthoDB; 1154048at2759; -.
DR PhylomeDB; O81821; -.
DR PRO; PR:O81821; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O81821; baseline and differential.
DR Genevisible; O81821; 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; IMP: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; IMP: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..481
FT /note="Heat stress transcription factor A-1b"
FT /id="PRO_0000124584"
FT DNA_BIND 25..119
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..204
FT /note="Hydrophobic repeat HR-A/B"
FT REGION 213..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 229..233
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 418..427
FT /note="AHA"
FT MOTIF 467..474
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 226..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 53576 MW; B0BEAD9E184358C1 CRC64;
MESVPESVPS PNSNTPSIPP PVNSVPPFLS KTYDMVDDPL TNEVVSWSSG NNSFVVWSAP
EFSKVLLPKY FKHNNFSSFV RQLNTYGFRK VDPDRWEFAN EGFLRGRKQL LKSIVRRKPS
HVQQNQQQTQ VQSSSVGACV EVGKFGIEEE VERLKRDKNV LMQELVRLRQ QQQATENQLQ
NVGQKVQVME QRQQQMMSFL AKAVQSPGFL NQLVQQNNND GNRQIPGSNK KRRLPVDEQE
NRGDNVANGL NRQIVRYQPS INEAAQNMLR QFLNTSTSPR YESVSNNPDS FLLGDVPSST
SVDNGNPSSR VSGVTLAEFS PNTVQSATNQ VPEASLAHHP QAGLVQPNIG QSPAQGAAPA
DSWSPEFDLV GCETDSGECF DPIMAVLDES EGDAISPEGE GKMNELLEGV PKLPGIQDPF
WEQFFSVELP AIADTDDILS GSVENNDLVL EQEPNEWTRN EQQMKYLTEQ MGLLSSEAQR
K
