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HS906_ARATH
ID   HS906_ARATH             Reviewed;         799 AA.
AC   F4JFN3; A0A1I9LN11; Q0WRS4; Q9S7E7;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Heat shock protein 90-6, mitochondrial {ECO:0000305};
DE            Short=AtHSP90.6 {ECO:0000305};
DE            Short=AtHsp90-6 {ECO:0000303|PubMed:11599565};
DE   AltName: Full=Heat shock protein 89-1 {ECO:0000305};
DE            Short=Hsp89-1 {ECO:0000303|PubMed:11599565};
DE   Flags: Precursor;
GN   Name=HSP90-6 {ECO:0000303|PubMed:11599565};
GN   Synonyms=HSP89-1 {ECO:0000303|PubMed:11599565};
GN   OrderedLocusNames=At3g07770 {ECO:0000312|Araport:AT3G07770};
GN   ORFNames=F17A17.11 {ECO:0000312|EMBL:AAF21187.1},
GN   MLP3.22 {ECO:0000312|EMBL:AAF13098.1};
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11599565; DOI=10.1379/1466-1268(2001)006<0238:thfopi>2.0.co;2;
RA   Krishna P., Gloor G.;
RT   "The Hsp90 family of proteins in Arabidopsis thaliana.";
RL   Cell Stress Chaperones 6:238-246(2001).
RN   [5]
RP   INTERACTION WITH P23-1.
RX   PubMed=20493581; DOI=10.1016/j.jplph.2010.03.016;
RA   Song H., Fan P., Shi W., Zhao R., Li Y.;
RT   "Expression of five AtHsp90 genes in Saccharomyces cerevisiae reveals
RT   functional differences of AtHsp90s under abiotic stresses.";
RL   J. Plant Physiol. 167:1172-1178(2010).
CC   -!- FUNCTION: Molecular chaperone which stabilizes unfolding protein
CC       intermediates and functions as a folding molecular chaperone that
CC       assists the non-covalent folding of proteins in an ATP-dependent
CC       manner. {ECO:0000250|UniProtKB:P27323}.
CC   -!- SUBUNIT: Interacts with P23-1. {ECO:0000269|PubMed:20493581}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF13098.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF21187.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC009176; AAF13098.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC013483; AAF21187.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE74602.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM63969.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM63970.1; -; Genomic_DNA.
DR   EMBL; AK228225; BAF00175.1; -; mRNA.
DR   RefSeq; NP_001319498.1; NM_001337742.1.
DR   RefSeq; NP_001326027.1; NM_001337743.1.
DR   RefSeq; NP_187434.2; NM_111656.4.
DR   AlphaFoldDB; F4JFN3; -.
DR   SMR; F4JFN3; -.
DR   STRING; 3702.AT3G07770.1; -.
DR   iPTMnet; F4JFN3; -.
DR   MetOSite; F4JFN3; -.
DR   PaxDb; F4JFN3; -.
DR   PRIDE; F4JFN3; -.
DR   ProteomicsDB; 228809; -.
DR   EnsemblPlants; AT3G07770.1; AT3G07770.1; AT3G07770.
DR   EnsemblPlants; AT3G07770.2; AT3G07770.2; AT3G07770.
DR   EnsemblPlants; AT3G07770.3; AT3G07770.3; AT3G07770.
DR   GeneID; 819968; -.
DR   Gramene; AT3G07770.1; AT3G07770.1; AT3G07770.
DR   Gramene; AT3G07770.2; AT3G07770.2; AT3G07770.
DR   Gramene; AT3G07770.3; AT3G07770.3; AT3G07770.
DR   KEGG; ath:AT3G07770; -.
DR   Araport; AT3G07770; -.
DR   TAIR; locus:2077352; AT3G07770.
DR   eggNOG; KOG0019; Eukaryota.
DR   HOGENOM; CLU_006684_1_3_1; -.
DR   InParanoid; F4JFN3; -.
DR   OMA; EINPNHY; -.
DR   OrthoDB; 924636at2759; -.
DR   PRO; PR:F4JFN3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; F4JFN3; baseline and differential.
DR   Genevisible; F4JFN3; AT.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Stress response; Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..799
FT                   /note="Heat shock protein 90-6, mitochondrial"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434019"
FT   REGION          23..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..799
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P02829"
FT   BINDING         128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P02829"
FT   BINDING         170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P02829"
FT   BINDING         175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P02829"
FT   BINDING         190..191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P02829"
FT   BINDING         214..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P02829"
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P02829"
FT   BINDING         464
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P02829"
FT   CONFLICT        250
FT                   /note="S -> L (in Ref. 3; BAF00175)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   799 AA;  90567 MW;  2B3E70F97FE9BC14 CRC64;
     MIRLSKRSVS TLLRSGNQSF RIAAAASTSR SSPSATDVKR SDTESRWYSS LTNGQSKNSG
     SFAQLNMKTN WFMGYRNESS AAASDSSSQA PPPAEKFEYQ AEVSRLMDLI VNSLYSNKEV
     FLRELISNAS DALDKLRYLS VTNPELSKDA PDLDIRIYAD KENGIITLTD SGIGMTRQEL
     VDCLGTIAQS GTAKFMKALK DSKDAGGDNN LIGQFGVGFY SAFLVADRVI VSTKSPKSDK
     QYVWEGEANS SSFTIQEDTD PQSLIPRGTR ITLHLKQEAK NFADPERIQK LVKNYSQFVS
     FPIYTWQEKG YTKEVEVEDD PTETKKDDQD DQTEKKKKTK KVVERYWDWE LTNETQPIWL
     RNPKEVTTAE YNEFYRKAFN EYLDPLASSH FTTEGEVEFR SILYVPPVSP SGKDDIVNQK
     TKNIRLYVKR VFISDDFDGE LFPRYLSFVK GVVDSHDLPL NVSREILQES RIVRIMKKRL
     VRKAFDMILG ISLSENREDY EKFWDNFGKH LKLGCIEDRE NHKRIAPLLR FFSSQSENDM
     ISLDEYVENM KPEQKAIYFI ASDSITSAKN APFLEKMLEK GLEVLYLVEP IDEVAVQSLK
     AYKEKDFVDI SKEDLDLGDK NEEKEAAVKK EFGQTCDWIK KRLGDKVASV QISNRLSSSP
     CVLVSGKFGW SANMERLMKA QSTGDTISLD YMKGRRVFEI NPDHSIIKNI NAAYNSNPND
     EDAMRAIDLM YDAALVSSGF TPDNPAELGG KIYEMMDVAL SGKWSSPEVQ PQQQQMAHSH
     DAETFEAEVV EPVEVDGKK
 
 
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