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Protein

Heat stress transcription factor A-4a

Gene

HSFA4A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi13 – 10795By similarityAdd
BLAST

GO - Molecular functioni

  • protein homodimerization activity Source: TAIR
  • sequence-specific DNA binding Source: InterPro
  • transcription factor activity, sequence-specific DNA binding Source: TAIR

GO - Biological processi

  • positive regulation of transcription, DNA-templated Source: TAIR
  • regulation of transcription, DNA-templated Source: TAIR
  • response to chitin Source: TAIR
  • response to reactive oxygen species Source: TAIR
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-ATH-3371453. Regulation of HSF1-mediated heat shock response.
R-ATH-3371511. HSF1 activation.
R-ATH-3371568. Attenuation phase.
R-ATH-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat stress transcription factor A-4a
Short name:
AtHsfA4a
Alternative name(s):
AtHsf-15
Heat shock factor protein 21
Short name:
HSF 21
Heat shock transcription factor 21
Short name:
HSTF 21
Gene namesi
Name:HSFA4A
Synonyms:HSF15, HSF21
Ordered Locus Names:At4g18880
ORF Names:F13C5.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G18880.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Heat stress transcription factor A-4aPRO_0000270804Add
BLAST

Post-translational modificationi

Exhibits temperature-dependent phosphorylation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO49403.
PRIDEiO49403.

PTM databases

iPTMnetiO49403.

Expressioni

Gene expression databases

GenevisibleiO49403. AT.

Interactioni

Subunit structurei

Homotrimer.By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi12915. 3 interactions.
STRINGi3702.AT4G18880.1.

Structurei

3D structure databases

ProteinModelPortaliO49403.
SMRiO49403. Positions 14-88.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 18867Hydrophobic repeat HR-A/BAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 2137Nuclear localization signalSequence analysis
Motifi256 – 26510AHA1
Motifi341 – 35010AHA2
Motifi388 – 3958Nuclear export signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi331 – 3355Poly-Pro

Domaini

The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain. AHA motifs are transcriptional activator elements.1 Publication

Sequence similaritiesi

Belongs to the HSF family. Class A subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0627. Eukaryota.
COG5169. LUCA.
HOGENOMiHOG000237979.
InParanoidiO49403.
KOiK09419.
OMAiARTINKP.
PhylomeDBiO49403.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 1 hit.
PfamiPF00447. HSF_DNA-bind. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

O49403-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDENNHGVSS SSLPPFLTKT YEMVDDSSSD SIVSWSQSNK SFIVWNPPEF
60 70 80 90 100
SRDLLPRFFK HNNFSSFIRQ LNTYGFRKAD PEQWEFANDD FVRGQPHLMK
110 120 130 140 150
NIHRRKPVHS HSLPNLQAQL NPLTDSERVR MNNQIERLTK EKEGLLEELH
160 170 180 190 200
KQDEEREVFE MQVKELKERL QHMEKRQKTM VSFVSQVLEK PGLALNLSPC
210 220 230 240 250
VPETNERKRR FPRIEFFPDE PMLEENKTCV VVREEGSTSP SSHTREHQVE
260 270 280 290 300
QLESSIAIWE NLVSDSCESM LQSRSMMTLD VDESSTFPES PPLSCIQLSV
310 320 330 340 350
DSRLKSPPSP RIIDMNCEPD GSKEQNTVAA PPPPPVAGAN DGFWQQFFSE
360 370 380 390 400
NPGSTEQREV QLERKDDKDK AGVRTEKCWW NSRNVNAITE QLGHLTSSER

S
Length:401
Mass (Da):46,245
Last modified:June 1, 1998 - v1
Checksum:iB3F7105DC1CBBB87
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021711 Genomic DNA. Translation: CAA16745.1.
AL161549 Genomic DNA. Translation: CAB78890.1.
CP002687 Genomic DNA. Translation: AEE84101.1.
AY125512 mRNA. Translation: AAM78104.1.
BT001049 mRNA. Translation: AAN46803.1.
U68561 mRNA. Translation: AAC31792.1.
PIRiT05025.
RefSeqiNP_193623.1. NM_118004.2.
UniGeneiAt.1951.

Genome annotation databases

EnsemblPlantsiAT4G18880.1; AT4G18880.1; AT4G18880.
GeneIDi827622.
GrameneiAT4G18880.1; AT4G18880.1; AT4G18880.
KEGGiath:AT4G18880.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021711 Genomic DNA. Translation: CAA16745.1.
AL161549 Genomic DNA. Translation: CAB78890.1.
CP002687 Genomic DNA. Translation: AEE84101.1.
AY125512 mRNA. Translation: AAM78104.1.
BT001049 mRNA. Translation: AAN46803.1.
U68561 mRNA. Translation: AAC31792.1.
PIRiT05025.
RefSeqiNP_193623.1. NM_118004.2.
UniGeneiAt.1951.

3D structure databases

ProteinModelPortaliO49403.
SMRiO49403. Positions 14-88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12915. 3 interactions.
STRINGi3702.AT4G18880.1.

PTM databases

iPTMnetiO49403.

Proteomic databases

PaxDbiO49403.
PRIDEiO49403.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G18880.1; AT4G18880.1; AT4G18880.
GeneIDi827622.
GrameneiAT4G18880.1; AT4G18880.1; AT4G18880.
KEGGiath:AT4G18880.

Organism-specific databases

TAIRiAT4G18880.

Phylogenomic databases

eggNOGiKOG0627. Eukaryota.
COG5169. LUCA.
HOGENOMiHOG000237979.
InParanoidiO49403.
KOiK09419.
OMAiARTINKP.
PhylomeDBiO49403.

Enzyme and pathway databases

ReactomeiR-ATH-3371453. Regulation of HSF1-mediated heat shock response.
R-ATH-3371511. HSF1 activation.
R-ATH-3371568. Attenuation phase.
R-ATH-3371571. HSF1-dependent transactivation.

Miscellaneous databases

PROiO49403.

Gene expression databases

GenevisibleiO49403. AT.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 1 hit.
PfamiPF00447. HSF_DNA-bind. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "The Hsf world: classification and properties of plant heat stress transcription factors."
    Nover L., Scharf K.-D., Gagliardi D., Vergne P., Czarnecka-Verner E., Gurley W.B.
    Cell Stress Chaperones 1:215-223(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-401.
    Strain: cv. Columbia.
    Tissue: Leaf and Stem.
  5. "Arabidopsis and the heat stress transcription factor world: how many heat stress transcription factors do we need?"
    Nover L., Bharti K., Doering P., Mishra S.K., Ganguli A., Scharf K.-D.
    Cell Stress Chaperones 6:177-189(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE, DOMAIN AHA.
  6. "Genome-wide analysis of heat shock transcription factor families in rice and Arabidopsis."
    Guo J., Wu J., Ji Q., Wang C., Luo L., Yuan Y., Wang Y., Wang J.
    J. Genet. Genomics 35:105-118(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiHFA4A_ARATH
AccessioniPrimary (citable) accession number: O49403
Secondary accession number(s): O82078
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 1998
Last modified: February 17, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.