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HFA1D_ARATH
ID   HFA1D_ARATH             Reviewed;         485 AA.
AC   Q9LQM7; Q8GXS5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 144.
DE   RecName: Full=Heat stress transcription factor A-1d;
DE            Short=AtHsfA1d;
DE   AltName: Full=AtHsf-01;
DE   AltName: Full=Heat shock factor protein 8;
DE            Short=HSF 8;
DE   AltName: Full=Heat shock transcription factor 8;
DE            Short=HSTF 8;
GN   Name=HSFA1D; Synonyms=HSF01, HSF8; OrderedLocusNames=At1g32330;
GN   ORFNames=F27G20.6, F5D14.8;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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] OF 347-485.
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, AND NOMENCLATURE.
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   INTERACTION WITH HSP90-2.
RX   PubMed=17965410; DOI=10.1074/jbc.m707168200;
RA   Yamada K., Fukao Y., Hayashi M., Fukazawa M., Suzuki I., Nishimura M.;
RT   "Cytosolic HSP90 regulates the heat shock response that is responsible for
RT   heat acclimation in Arabidopsis thaliana.";
RL   J. Biol. Chem. 282:37794-37804(2007).
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 regulator that specifically binds DNA
CC       sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
CC   -!- SUBUNIT: Homotrimer (By similarity). Interacts with HSP90-2
CC       (PubMed:17965410). {ECO:0000250, ECO:0000269|PubMed:17965410}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC   -!- DOMAIN: The hydrophobic-rich region (HR-A/B) corresponds to the
CC       oligomerization domain.
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=AAF81328.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG60176.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007767; AAF81328.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC084110; AAG60176.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31464.1; -; Genomic_DNA.
DR   EMBL; AK118066; BAC42697.1; -; mRNA.
DR   PIR; H86447; H86447.
DR   RefSeq; NP_001321152.1; NM_001333004.1.
DR   RefSeq; NP_174511.2; NM_102966.4.
DR   AlphaFoldDB; Q9LQM7; -.
DR   SMR; Q9LQM7; -.
DR   BioGRID; 25359; 6.
DR   IntAct; Q9LQM7; 6.
DR   STRING; 3702.AT1G32330.1; -.
DR   PaxDb; Q9LQM7; -.
DR   ProteomicsDB; 230343; -.
DR   EnsemblPlants; AT1G32330.1; AT1G32330.1; AT1G32330.
DR   GeneID; 840125; -.
DR   Gramene; AT1G32330.1; AT1G32330.1; AT1G32330.
DR   KEGG; ath:AT1G32330; -.
DR   Araport; AT1G32330; -.
DR   TAIR; locus:2028326; AT1G32330.
DR   eggNOG; KOG0627; Eukaryota.
DR   HOGENOM; CLU_030308_0_6_1; -.
DR   InParanoid; Q9LQM7; -.
DR   OrthoDB; 1154048at2759; -.
DR   PhylomeDB; Q9LQM7; -.
DR   PRO; PR:Q9LQM7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LQM7; baseline and differential.
DR   Genevisible; Q9LQM7; 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   GO; GO:0009408; P:response to heat; IEP: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   Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Stress response; Transcription; Transcription regulation.
FT   CHAIN           1..485
FT                   /note="Heat stress transcription factor A-1d"
FT                   /id="PRO_0000270801"
FT   DNA_BIND        35..129
FT                   /evidence="ECO:0000250"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..218
FT                   /note="Hydrophobic repeat HR-A/B"
FT   REGION          229..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           238..252
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           472..480
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  54524 MW;  2B8AF0C29BFA3B39 CRC64;
     MDVSKVTTSD GGGDSMETKP SPQPQPAAIL SSNAPPPFLS KTYDMVDDHN TDSIVSWSAN
     NNSFIVWKPP EFARDLLPKN FKHNNFSSFV RQLNTYGFRK VDPDRWEFAN EGFLRGQKHL
     LQSITRRKPA HGQGQGHQRS QHSNGQNSSV SACVEVGKFG LEEEVERLKR DKNVLMQELV
     RLRQQQQSTD NQLQTMVQRL QGMENRQQQL MSFLAKAVQS PHFLSQFLQQ QNQQNESNRR
     ISDTSKKRRF KRDGIVRNND SATPDGQIVK YQPPMHEQAK AMFKQLMKME PYKTGDDGFL
     LGNGTSTTEG TEMETSSNQV SGITLKEMPT ASEIQSSSPI ETTPENVSAA SEATENCIPS
     PDDLTLPDFT HMLPENNSEK PPESFMEPNL GGSSPLLDPD LLIDDSLSFD IDDFPMDSDI
     DPVDYGLLER LLMSSPVPDN MDSTPVDNET EQEQNGWDKT KHMDNLTQQM GLLSPETLDL
     SRQNP
 
 
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