HSFA2_ARATH
ID HSFA2_ARATH Reviewed; 345 AA.
AC O80982;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Heat stress transcription factor A-2 {ECO:0000303|PubMed:16649111, ECO:0000303|PubMed:17059409, ECO:0000303|PubMed:17085506};
DE Short=AtHsfA2 {ECO:0000303|PubMed:16649111, ECO:0000303|PubMed:17059409, ECO:0000303|PubMed:17085506};
DE AltName: Full=AtHsf-04 {ECO:0000303|PubMed:18407058};
GN Name=HSFA2 {ECO:0000303|PubMed:16649111, ECO:0000303|PubMed:17059409,
GN ECO:0000303|PubMed:17085506}; Synonyms=HSF04 {ECO:0000303|PubMed:18407058};
GN OrderedLocusNames=At2g26150 {ECO:0000312|Araport:AT2G26150};
GN ORFNames=T19L18.4 {ECO:0000312|EMBL:AAC31222.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [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 FUNCTION, AND INDUCTION.
RX PubMed=17059409; DOI=10.1111/j.1365-313x.2006.02889.x;
RA Nishizawa A., Yabuta Y., Yoshida E., Maruta T., Yoshimura K., Shigeoka S.;
RT "Arabidopsis heat shock transcription factor A2 as a key regulator in
RT response to several types of environmental stress.";
RL Plant J. 48:535-547(2006).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=16649111; DOI=10.1007/s11103-005-5750-x;
RA Schramm F., Ganguli A., Kiehlmann E., Englich G., Walch D.,
RA von Koskull-Doering P.;
RT "The heat stress transcription factor HsfA2 serves as a regulatory
RT amplifier of a subset of genes in the heat stress response in
RT Arabidopsis.";
RL Plant Mol. Biol. 60:759-772(2006).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=17085506; DOI=10.1104/pp.106.091322;
RA Charng Y.-Y., Liu H.-C., Liu N.-Y., Chi W.-T., Wang C.-N., Chang S.-H.,
RA Wang T.-T.;
RT "A heat-inducible transcription factor, HsfA2, is required for extension of
RT acquired thermotolerance in Arabidopsis.";
RL Plant Physiol. 143:251-262(2007).
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 SUMO1, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-315,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-5; LYS-167; LYS-269 AND
RP LYS-315.
RX PubMed=20521085; DOI=10.1007/s11103-010-9652-1;
RA Cohen-Peer R., Schuster S., Meiri D., Breiman A., Avni A.;
RT "Sumoylation of Arabidopsis heat shock factor A2 (HsfA2) modifies its
RT activity during acquired thermotholerance.";
RL Plant Mol. Biol. 74:33-45(2010).
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 FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY HEAT.
RC STRAIN=cv. Columbia;
RX PubMed=30778176; DOI=10.1038/s41422-019-0145-8;
RA Liu J., Feng L., Gu X., Deng X., Qiu Q., Li Q., Zhang Y., Wang M., Deng Y.,
RA Wang E., He Y., Baeurle I., Li J., Cao X., He Z.;
RT "An H3K27me3 demethylase-HSFA2 regulatory loop orchestrates
RT transgenerational thermomemory in Arabidopsis.";
RL Cell Res. 29:379-390(2019).
CC -!- FUNCTION: Transcriptional activator that specifically binds DNA
CC sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
CC Seems to be involved in other environmental stress responses. Activates
CC ascorbate peroxidase 2 (APX2) in addition to several heat shock protein
CC (HSPs). Binds to the promoter of SGIP1 and activates its expression in
CC heat acclimated plants (PubMed:30778176). Involved in the mechanisms
CC necessary for quick response to heat and subsequent heritable
CC transgenerational memory of heat acclimation (global warming) such as
CC early flowering and attenuated immunity; this process includes
CC epigenetic regulation as well as post-transcriptional gene silencing
CC (PTGS) (PubMed:30778176). In response to heat, HSFA2 is activated and
CC promotes the expression of REF6 which in turn derepresses HSFA2, thus
CC establishing an heritable feedback loop able to trigger SGIP1 and
CC subsequent SGIP1-mediated SGS3 degradation; this prevents the
CC biosynthesis of trans-acting siRNA (tasiRNA) and leads to the release
CC of HTT5, which drives early flowering but attenuates immunity
CC (PubMed:30778176). {ECO:0000269|PubMed:16649111,
CC ECO:0000269|PubMed:17059409, ECO:0000269|PubMed:17085506,
CC ECO:0000269|PubMed:30778176}.
CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with SUMO1
CC (PubMed:20521085). Binds to HSBP (PubMed:20388662). {ECO:0000250,
CC ECO:0000269|PubMed:20388662, ECO:0000269|PubMed:20521085}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:20521085}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:20521085}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O80982-1; Sequence=Displayed;
CC -!- INDUCTION: By high light and hydrogen peroxide (H(2)O(2))
CC (PubMed:16649111, PubMed:17059409, PubMed:17085506, PubMed:30778176).
CC Up-regulated by heat stress (at 30 degrees Celsius) and remains up-
CC regulated transgenerationally in the unstressed progeny (at 22 degrees
CC Celsius) via heat-induced REF6-dependent depletion of H3K27me3 marks
CC within its coding regions (PubMed:16649111, PubMed:17059409,
CC PubMed:17085506, PubMed:30778176). {ECO:0000269|PubMed:16649111,
CC ECO:0000269|PubMed:17059409, ECO:0000269|PubMed:17085506,
CC ECO:0000269|PubMed:30778176}.
CC -!- DOMAIN: The hydrophobic-rich region (HR-A/B) corresponds to the
CC oligomerization domain. AHA motifs are transcriptional activator
CC elements. {ECO:0000269|PubMed:11599559}.
CC -!- PTM: Exhibits temperature-dependent phosphorylation. {ECO:0000250}.
CC -!- PTM: Sumoylated at Lys-315. Sumoylation represses its function.
CC {ECO:0000269|PubMed:20521085}.
CC -!- DISRUPTION PHENOTYPE: Heat-sensitive phenotype (PubMed:20521085).
CC Reduced expression of SGIP1 (PubMed:30778176).
CC {ECO:0000269|PubMed:20521085, ECO:0000269|PubMed:30778176}.
CC -!- MISCELLANEOUS: Plants overexpressing HSFA2 show increased tolerance to
CC combined environmental stresses.
CC -!- SIMILARITY: Belongs to the HSF family. Class A subfamily.
CC {ECO:0000305}.
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DR EMBL; AC004747; AAC31222.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07800.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62674.1; -; Genomic_DNA.
DR EMBL; AK118744; BAC43337.1; -; mRNA.
DR PIR; T02609; T02609.
DR RefSeq; NP_001324815.1; NM_001336039.1. [O80982-1]
DR RefSeq; NP_180184.1; NM_128173.3. [O80982-1]
DR AlphaFoldDB; O80982; -.
DR SMR; O80982; -.
DR BioGRID; 2507; 6.
DR IntAct; O80982; 2.
DR MINT; O80982; -.
DR STRING; 3702.AT2G26150.1; -.
DR iPTMnet; O80982; -.
DR PaxDb; O80982; -.
DR PRIDE; O80982; -.
DR ProteomicsDB; 230150; -. [O80982-1]
DR EnsemblPlants; AT2G26150.1; AT2G26150.1; AT2G26150. [O80982-1]
DR EnsemblPlants; AT2G26150.4; AT2G26150.4; AT2G26150. [O80982-1]
DR GeneID; 817155; -.
DR Gramene; AT2G26150.1; AT2G26150.1; AT2G26150. [O80982-1]
DR Gramene; AT2G26150.4; AT2G26150.4; AT2G26150. [O80982-1]
DR KEGG; ath:AT2G26150; -.
DR Araport; AT2G26150; -.
DR TAIR; locus:2057371; AT2G26150.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_030308_1_1_1; -.
DR InParanoid; O80982; -.
DR OMA; RNVGQSM; -.
DR OrthoDB; 1154048at2759; -.
DR PhylomeDB; O80982; -.
DR PRO; PR:O80982; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80982; baseline and differential.
DR Genevisible; O80982; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IEP:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
DR GO; GO:0034620; P:cellular response to unfolded protein; IMP:TAIR.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0001666; P:response to hypoxia; 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; Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Stress response;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..345
FT /note="Heat stress transcription factor A-2"
FT /id="PRO_0000270802"
FT DNA_BIND 42..136
FT /evidence="ECO:0000250|UniProtKB:P10961"
FT REGION 17..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..216
FT /note="Hydrophobic repeat HR-A/B"
FT /evidence="ECO:0000255"
FT MOTIF 231..238
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 273..282
FT /note="AHA1"
FT /evidence="ECO:0000255"
FT MOTIF 324..333
FT /note="AHA2"
FT /evidence="ECO:0000255"
FT MOTIF 334..341
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 17..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:20521085"
FT MUTAGEN 5
FT /note="K->R: No effect on SUMO1 binding."
FT /evidence="ECO:0000269|PubMed:20521085"
FT MUTAGEN 167
FT /note="K->R: Reduces SUMO1 binding efficiency."
FT /evidence="ECO:0000269|PubMed:20521085"
FT MUTAGEN 269
FT /note="K->R: Increases SUMO1 binding efficiency."
FT /evidence="ECO:0000269|PubMed:20521085"
FT MUTAGEN 315
FT /note="K->R: Loss of sumoylation. Loss of SUMO1 binding."
FT /evidence="ECO:0000269|PubMed:20521085"
SQ SEQUENCE 345 AA; 39114 MW; 455FAB34582D7150 CRC64;
MEELKVEMEE ETVTFTGSVA ASSSVGSSSS PRPMEGLNET GPPPFLTKTY EMVEDPATDT
VVSWSNGRNS FVVWDSHKFS TTLLPRYFKH SNFSSFIRQL NTYGFRKIDP DRWEFANEGF
LAGQKHLLKN IKRRRNMGLQ NVNQQGSGMS CVEVGQYGFD GEVERLKRDH GVLVAEVVRL
RQQQHSSKSQ VAAMEQRLLV TEKRQQQMMT FLAKALNNPN FVQQFAVMSK EKKSLFGLDV
GRKRRLTSTP SLGTMEENLL HDQEFDRMKD DMEMLFAAAI DDEANNSMPT KEEQCLEAMN
VMMRDGNLEA ALDVKVEDLV GSPLDWDSQD LHDMVDQMGF LGSEP
