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HFA4A_ARATH
ID   HFA4A_ARATH             Reviewed;         401 AA.
AC   O49403; O82078;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Heat stress transcription factor A-4a;
DE            Short=AtHsfA4a;
DE   AltName: Full=AtHsf-15;
DE   AltName: Full=Heat shock factor protein 21;
DE            Short=HSF 21;
DE   AltName: Full=Heat shock transcription factor 21;
DE            Short=HSTF 21;
GN   Name=HSFA4A; Synonyms=HSF15, HSF21; OrderedLocusNames=At4g18880;
GN   ORFNames=F13C5.50;
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=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   [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=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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-401.
RC   STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX   PubMed=9222607; DOI=10.1379/1466-1268(1996)001<0215:thwcap>2.3.co;2;
RA   Nover L., Scharf K.-D., Gagliardi D., Vergne P., Czarnecka-Verner E.,
RA   Gurley W.B.;
RT   "The Hsf world: classification and properties of plant heat stress
RT   transcription factors.";
RL   Cell Stress Chaperones 1:215-223(1996).
RN   [5]
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   [6]
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   -!- INTERACTION:
CC       O49403; Q9C5J9: LIP1; NbExp=4; IntAct=EBI-25511393, EBI-4449491;
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 motifs are transcriptional activator
CC       elements. {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}.
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DR   EMBL; AL021711; CAA16745.1; -; Genomic_DNA.
DR   EMBL; AL161549; CAB78890.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84101.1; -; Genomic_DNA.
DR   EMBL; AY125512; AAM78104.1; -; mRNA.
DR   EMBL; BT001049; AAN46803.1; -; mRNA.
DR   EMBL; U68561; AAC31792.1; -; mRNA.
DR   PIR; T05025; T05025.
DR   RefSeq; NP_193623.1; NM_118004.3.
DR   AlphaFoldDB; O49403; -.
DR   SMR; O49403; -.
DR   BioGRID; 12915; 4.
DR   IntAct; O49403; 1.
DR   STRING; 3702.AT4G18880.1; -.
DR   iPTMnet; O49403; -.
DR   PaxDb; O49403; -.
DR   PRIDE; O49403; -.
DR   ProteomicsDB; 232215; -.
DR   EnsemblPlants; AT4G18880.1; AT4G18880.1; AT4G18880.
DR   GeneID; 827622; -.
DR   Gramene; AT4G18880.1; AT4G18880.1; AT4G18880.
DR   KEGG; ath:AT4G18880; -.
DR   Araport; AT4G18880; -.
DR   TAIR; locus:2117139; AT4G18880.
DR   eggNOG; KOG0627; Eukaryota.
DR   HOGENOM; CLU_030308_0_0_1; -.
DR   InParanoid; O49403; -.
DR   OMA; ERHEQEW; -.
DR   OrthoDB; 1154048at2759; -.
DR   PhylomeDB; O49403; -.
DR   PRO; PR:O49403; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O49403; baseline and differential.
DR   Genevisible; O49403; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEP:TAIR.
DR   GO; GO:0000302; P:response to reactive oxygen species; 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.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Stress response; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..401
FT                   /note="Heat stress transcription factor A-4a"
FT                   /id="PRO_0000270804"
FT   DNA_BIND        13..107
FT                   /evidence="ECO:0000250"
FT   REGION          122..188
FT                   /note="Hydrophobic repeat HR-A/B"
FT   REGION          351..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           207..213
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           256..265
FT                   /note="AHA1"
FT   MOTIF           341..350
FT                   /note="AHA2"
FT   MOTIF           388..395
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        357..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  46245 MW;  B3F7105DC1CBBB87 CRC64;
     MDENNHGVSS SSLPPFLTKT YEMVDDSSSD SIVSWSQSNK SFIVWNPPEF SRDLLPRFFK
     HNNFSSFIRQ LNTYGFRKAD PEQWEFANDD FVRGQPHLMK NIHRRKPVHS HSLPNLQAQL
     NPLTDSERVR MNNQIERLTK EKEGLLEELH KQDEEREVFE MQVKELKERL QHMEKRQKTM
     VSFVSQVLEK PGLALNLSPC VPETNERKRR FPRIEFFPDE PMLEENKTCV VVREEGSTSP
     SSHTREHQVE QLESSIAIWE NLVSDSCESM LQSRSMMTLD VDESSTFPES PPLSCIQLSV
     DSRLKSPPSP RIIDMNCEPD GSKEQNTVAA PPPPPVAGAN DGFWQQFFSE NPGSTEQREV
     QLERKDDKDK AGVRTEKCWW NSRNVNAITE QLGHLTSSER S
 
 
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