HS905_ARATH
ID HS905_ARATH Reviewed; 780 AA.
AC Q9SIF2; F4IU89; Q0WMQ3; Q0WMV4; Q8LPS0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Heat shock protein 90-5, chloroplastic {ECO:0000305};
DE Short=AtHSP90.5 {ECO:0000305};
DE Short=AtHsp90-5 {ECO:0000303|PubMed:11599565};
DE AltName: Full=Heat shock protein 88-1 {ECO:0000305};
DE Short=Hsp88-1 {ECO:0000303|PubMed:11599565};
DE AltName: Full=Hsp90C {ECO:0000303|PubMed:23382192};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1956 {ECO:0000303|PubMed:23382192};
DE AltName: Full=Protein chlorate-resistance 88 {ECO:0000303|PubMed:12943545};
DE Flags: Precursor;
GN Name=HSP90-5 {ECO:0000303|PubMed:11599565};
GN Synonyms=CR88 {ECO:0000303|PubMed:12943545},
GN EMB1956 {ECO:0000303|PubMed:23382192},
GN HSP88-1 {ECO:0000303|PubMed:11599565};
GN OrderedLocusNames=At2g04030 {ECO:0000312|Araport:AT2G04030};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] (ISOFORM 1).
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 [LARGE SCALE MRNA] OF 1-313 AND 417-777 (ISOFORM 2).
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 [5]
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 [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF
RP GLY-646, AND FUNCTION.
RX PubMed=12943545; DOI=10.1046/j.1365-313x.2003.016011.x;
RA Cao D., Froehlich J.E., Zhang H., Cheng C.L.;
RT "The chlorate-resistant and photomorphogenesis-defective mutant cr88
RT encodes a chloroplast-targeted HSP90.";
RL Plant J. 33:107-118(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23382192; DOI=10.1073/pnas.1219229110;
RA Inoue H., Li M., Schnell D.J.;
RT "An essential role for chloroplast heat shock protein 90 (Hsp90C) in
RT protein import into chloroplasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3173-3178(2013).
RN [11]
RP FUNCTION, AND HOMODIMERIZATION.
RX PubMed=25216779; DOI=10.1186/1756-0500-7-643;
RA Oh S.E., Yeung C., Babaei-Rad R., Zhao R.;
RT "Cosuppression of the chloroplast localized molecular chaperone HSP90.5
RT impairs plant development and chloroplast biogenesis in Arabidopsis.";
RL BMC Res. Notes 7:643-643(2014).
RN [12]
RP FUNCTION, INTERACTION WITH VIPP1, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23875936; DOI=10.1111/ppl.12083;
RA Feng J., Fan P., Jiang P., Lv S., Chen X., Li Y.;
RT "Chloroplast-targeted Hsp90 plays essential roles in plastid development
RT and embryogenesis in Arabidopsis possibly linking with VIPP1.";
RL Physiol. Plantarum 150:292-307(2014).
CC -!- FUNCTION: Molecular chaperone required for chloroplast biogenesis
CC (PubMed:12943545, PubMed:25216779). Essential for chloroplast
CC biogenesis and maintenance, and thus for embryogenesis
CC (PubMed:23875936, PubMed:23382192). May be involved in the disassembly
CC of VIPP1 for thylakoid membrane formation and/or maintenance
CC (PubMed:23875936). Cooperates with TIC components and other molecular
CC chaperones to drive transport of preproteins into chloroplasts and
CC functions in the chloroplast stroma to facilitate membrane
CC translocation during protein import into the organelle
CC (PubMed:23382192). {ECO:0000269|PubMed:12943545,
CC ECO:0000269|PubMed:23382192, ECO:0000269|PubMed:23875936,
CC ECO:0000269|PubMed:25216779}.
CC -!- SUBUNIT: Homodimer (PubMed:25216779). Interacts with VIPP1
CC (PubMed:23875936). Interacts with P23-1 (PubMed:20493581).
CC {ECO:0000269|PubMed:20493581, ECO:0000269|PubMed:23875936,
CC ECO:0000269|PubMed:25216779}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:12943545, ECO:0000269|PubMed:23382192}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SIF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SIF2-2; Sequence=VSP_057880;
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, young leaves,
CC mature leaves, stems, flowers, petals and siliques.
CC {ECO:0000269|PubMed:12943545}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, highly expressed at 4 days
CC post anthesis. {ECO:0000269|PubMed:23875936}.
CC -!- INDUCTION: By heat shock and light. {ECO:0000269|PubMed:12943545}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality due to embryo development
CC arrest at the heart stage. {ECO:0000269|PubMed:23382192,
CC ECO:0000269|PubMed:23875936}.
CC -!- MISCELLANEOUS: Plants over-expressing HSP90.7 show albino and stunted
CC leaves. {ECO:0000269|PubMed:23875936}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; AC007167; AAD32922.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05778.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05779.1; -; Genomic_DNA.
DR EMBL; AF436826; AAL32008.1; -; mRNA.
DR EMBL; AY053403; AAK96633.1; -; mRNA.
DR EMBL; AY094422; AAM19795.1; -; mRNA.
DR EMBL; BT002234; AAN72245.1; -; mRNA.
DR EMBL; AK229707; BAF01546.1; -; mRNA.
DR EMBL; AK229761; BAF01597.1; -; mRNA.
DR PIR; H84453; H84453.
DR RefSeq; NP_178487.1; NM_126439.4. [Q9SIF2-1]
DR RefSeq; NP_849932.1; NM_179601.1. [Q9SIF2-2]
DR AlphaFoldDB; Q9SIF2; -.
DR SMR; Q9SIF2; -.
DR IntAct; Q9SIF2; 2.
DR STRING; 3702.AT2G04030.1; -.
DR SwissPalm; Q9SIF2; -.
DR PaxDb; Q9SIF2; -.
DR PRIDE; Q9SIF2; -.
DR ProMEX; Q9SIF2; -.
DR ProteomicsDB; 230250; -. [Q9SIF2-1]
DR EnsemblPlants; AT2G04030.1; AT2G04030.1; AT2G04030. [Q9SIF2-1]
DR EnsemblPlants; AT2G04030.2; AT2G04030.2; AT2G04030. [Q9SIF2-2]
DR GeneID; 814930; -.
DR Gramene; AT2G04030.1; AT2G04030.1; AT2G04030. [Q9SIF2-1]
DR Gramene; AT2G04030.2; AT2G04030.2; AT2G04030. [Q9SIF2-2]
DR KEGG; ath:AT2G04030; -.
DR Araport; AT2G04030; -.
DR TAIR; locus:2049651; AT2G04030.
DR eggNOG; KOG0019; Eukaryota.
DR InParanoid; Q9SIF2; -.
DR OMA; RKFWENF; -.
DR PhylomeDB; Q9SIF2; -.
DR PRO; PR:Q9SIF2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIF2; baseline and differential.
DR Genevisible; Q9SIF2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0009704; P:de-etiolation; IMP:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
DR GO; GO:0010157; P:response to chlorate; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
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 SMART; SM00387; HATPase_c; 1.
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 Alternative splicing; ATP-binding; Chaperone; Chloroplast;
KW Nucleotide-binding; Plastid; Protein transport; Reference proteome;
KW Stress response; Transit peptide; Transport.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..780
FT /note="Heat shock protein 90-5, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434018"
FT REGION 742..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 172..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 196..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT VAR_SEQ 476..478
FT /note="Missing (in isoform 2)"
FT /id="VSP_057880"
FT MUTAGEN 646
FT /note="G->R: In cr88; delay in greening of young rosette
FT leaves. Reduced nitrate reductase activity in response to
FT nitrate."
FT /evidence="ECO:0000269|PubMed:12943545"
FT CONFLICT 224
FT /note="Y -> N (in Ref. 3; AAM19795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 780 AA; 88663 MW; 6838772716E75924 CRC64;
MAPALSRSLY TSPLTSVPIT PVSSRLSHLR SSFLPHGGAL RTGVSCSWNL EKRCNRFAVK
CDAAVAEKET TEEGSGEKFE YQAEVSRLLD LIVHSLYSHK EVFLRELVSN ASDALDKLRF
LSVTEPSLLG DGGDLEIRIK PDPDNGTITI TDTGIGMTKE ELIDCLGTIA QSGTSKFLKA
LKENKDLGAD NGLIGQFGVG FYSAFLVAEK VVVSTKSPKS DKQYVWESVA DSSSYLIREE
TDPDNILRRG TQITLYLRED DKYEFAESTR IKNLVKNYSQ FVGFPIYTWQ EKSRTIEVEE
DEPVKEGEEG EPKKKKTTKT EKYWDWELAN ETKPLWMRNS KEVEKGEYNE FYKKAFNEFL
DPLAHTHFTT EGEVEFRSIL YIPGMGPLNN EDVTNPKTKN IRLYVKRVFI SDDFDGELFP
RYLSFVKGVV DSDDLPLNVS REILQESRIV RIMRKRLIRK TFDMIQEISE SENKEDYKKF
WENFGRFLKL GCIEDTGNHK RITPLLRFFS SKNEEELTSL DDYIENMGEN QKAIYYLATD
SLKSAKSAPF LEKLIQKDIE VLYLVEPIDE VAIQNLQTYK EKKFVDISKE DLELGDEDEV
KDREAKQEFN LLCDWIKQQL GDKVAKVQVS NRLSSSPCVL VSGKFGWSAN MERLMKAQAL
GDTSSLEFMR GRRILEINPD HPIIKDLNAA CKNAPESTEA TRVVDLLYDT AIISSGFTPD
SPAELGNKIY EMMAMAVGGR WGRVEEEEES STVNEGDDKS GETEVVEPSE VRAESDPWQD
