HSFA5_ARATH
ID HSFA5_ARATH Reviewed; 466 AA.
AC Q94BZ5; O23259; Q56X02;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Heat stress transcription factor A-5;
DE Short=AtHsfA5;
DE AltName: Full=AtHsf-12;
GN Name=HSFA5; Synonyms=HSF12; OrderedLocusNames=At4g13980;
GN ORFNames=dl3030c, FCAALL.27;
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-466.
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 (MAR-2005) 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 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).
CC -!- FUNCTION: Transcriptional activator that specifically binds DNA
CC sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
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=CAB10177.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g13980 has been split into 2 genes: At4g13980 and At4g13985.; Evidence={ECO:0000305};
CC Sequence=CAB78440.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g13980 has been split into 2 genes: At4g13980 and At4g13985.; Evidence={ECO:0000305};
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DR EMBL; Z97335; CAB10177.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161537; CAB78440.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83355.1; -; Genomic_DNA.
DR EMBL; AY039528; AAK62584.1; -; mRNA.
DR EMBL; BT001056; AAN46810.1; -; mRNA.
DR EMBL; AK221877; BAD94194.1; -; mRNA.
DR PIR; G71400; G71400.
DR RefSeq; NP_567415.1; NM_117472.4.
DR AlphaFoldDB; Q94BZ5; -.
DR SMR; Q94BZ5; -.
DR BioGRID; 12330; 4.
DR IntAct; Q94BZ5; 3.
DR STRING; 3702.AT4G13980.1; -.
DR iPTMnet; Q94BZ5; -.
DR PaxDb; Q94BZ5; -.
DR PRIDE; Q94BZ5; -.
DR ProteomicsDB; 230151; -.
DR EnsemblPlants; AT4G13980.1; AT4G13980.1; AT4G13980.
DR GeneID; 827033; -.
DR Gramene; AT4G13980.1; AT4G13980.1; AT4G13980.
DR KEGG; ath:AT4G13980; -.
DR Araport; AT4G13980; -.
DR TAIR; locus:2129276; AT4G13980.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_030308_0_0_1; -.
DR InParanoid; Q94BZ5; -.
DR OMA; ISCHLNL; -.
DR OrthoDB; 1154048at2759; -.
DR PhylomeDB; Q94BZ5; -.
DR PRO; PR:Q94BZ5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94BZ5; baseline and differential.
DR Genevisible; Q94BZ5; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 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 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..466
FT /note="Heat stress transcription factor A-5"
FT /id="PRO_0000270806"
FT DNA_BIND 21..115
FT /evidence="ECO:0000250"
FT REGION 125..191
FT /note="Hydrophobic repeat HR-A/B"
FT REGION 215..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 198..217
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 414..423
FT /note="AHA"
FT MOTIF 461..466
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 215..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 52355 MW; 570F6D0C95639223 CRC64;
MNGALGNSSA SVSGGEGAGG PAPFLVKTYE MVDDSSTDQI VSWSANNNSF IVWNHAEFSR
LLLPTYFKHN NFSSFIRQLN TYGFRKIDPE RWEFLNDDFI KDQKHLLKNI HRRKPIHSHS
HPPASSTDQE RAVLQEQMDK LSREKAAIEA KLLKFKQQKV VAKHQFEEMT EHVDDMENRQ
KKLLNFLETA IRNPTFVKNF GKKVEQLDIS AYNKKRRLPE VEQSKPPSED SHLDNSSGSS
RRESGNIFHQ NFSNKLRLEL SPADSDMNMV SHSIQSSNEE GASPKGILSG GDPNTTLTKR
EGLPFAPEAL ELADTGTCPR RLLLNDNTRV ETLQQRLTSS EETDGSFSCH LNLTLASAPL
PDKTASQIAK TTLKSQELNF NSIETSASEK NRGRQEIAVG GSQANAAPPA RVNDVFWEQF
LTERPGSSDN EEASSTYRGN PYEEQEEKRN GSMMLRNTKN IEQLTL
