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Heat shock protein 90-5, chloroplastic (AtHSP90.5) (AtHsp90-5) (Heat shock protein 88-1) (Hsp88-1) (Hsp90C) (Protein EMBRYO DEFECTIVE 1956) (Protein chlorate-resistance 88)

 HS905_ARATH             Reviewed;         780 AA.
Q9SIF2; F4IU89; Q0WMQ3; Q0WMV4; Q8LPS0;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
18-JUL-2018, entry version 149.
RecName: Full=Heat shock protein 90-5, chloroplastic {ECO:0000305};
Short=AtHSP90.5 {ECO:0000305};
Short=AtHsp90-5 {ECO:0000303|PubMed:11599565};
AltName: Full=Heat shock protein 88-1 {ECO:0000305};
Short=Hsp88-1 {ECO:0000303|PubMed:11599565};
AltName: Full=Hsp90C {ECO:0000303|PubMed:23382192};
AltName: Full=Protein EMBRYO DEFECTIVE 1956 {ECO:0000303|PubMed:23382192};
AltName: Full=Protein chlorate-resistance 88 {ECO:0000303|PubMed:12943545};
Flags: Precursor;
Name=HSP90-5 {ECO:0000303|PubMed:11599565};
Synonyms=CR88 {ECO:0000303|PubMed:12943545},
EMB1956 {ECO:0000303|PubMed:23382192},
HSP88-1 {ECO:0000303|PubMed:11599565};
OrderedLocusNames=At2g04030 {ECO:0000312|Araport:AT2G04030};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-313 AND 417-777 (ISOFORM
2).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11599565; DOI=10.1379/1466-1268(2001)006<0238:THFOPI>2.0.CO;2;
Krishna P., Gloor G.;
"The Hsp90 family of proteins in Arabidopsis thaliana.";
Cell Stress Chaperones 6:238-246(2001).
[6]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF
GLY-646, AND FUNCTION.
PubMed=12943545; DOI=10.1046/j.1365-313X.2003.016011.x;
Cao D., Froehlich J.E., Zhang H., Cheng C.L.;
"The chlorate-resistant and photomorphogenesis-defective mutant cr88
encodes a chloroplast-targeted HSP90.";
Plant J. 33:107-118(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[9]
INTERACTION WITH P23-1.
PubMed=20493581; DOI=10.1016/j.jplph.2010.03.016;
Song H., Fan P., Shi W., Zhao R., Li Y.;
"Expression of five AtHsp90 genes in Saccharomyces cerevisiae reveals
functional differences of AtHsp90s under abiotic stresses.";
J. Plant Physiol. 167:1172-1178(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
AND DISRUPTION PHENOTYPE.
PubMed=23382192; DOI=10.1073/pnas.1219229110;
Inoue H., Li M., Schnell D.J.;
"An essential role for chloroplast heat shock protein 90 (Hsp90C) in
protein import into chloroplasts.";
Proc. Natl. Acad. Sci. U.S.A. 110:3173-3178(2013).
[11]
FUNCTION, AND HOMODIMERIZATION.
PubMed=25216779; DOI=10.1186/1756-0500-7-643;
Oh S.E., Yeung C., Babaei-Rad R., Zhao R.;
"Cosuppression of the chloroplast localized molecular chaperone
HSP90.5 impairs plant development and chloroplast biogenesis in
Arabidopsis.";
BMC Res. Notes 7:643-643(2014).
[12]
FUNCTION, INTERACTION WITH VIPP1, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=23875936; DOI=10.1111/ppl.12083;
Feng J., Fan P., Jiang P., Lv S., Chen X., Li Y.;
"Chloroplast-targeted Hsp90 plays essential roles in plastid
development and embryogenesis in Arabidopsis possibly linking with
VIPP1.";
Physiol. Plantarum 150:292-307(2014).
-!- FUNCTION: Molecular chaperone required for chloroplast biogenesis
(PubMed:12943545, PubMed:25216779). Essential for chloroplast
biogenesis and maintenance, and thus for embryogenesis
(PubMed:23875936, PubMed:23382192). May be involved in the
disassembly of VIPP1 for thylakoid membrane formation and/or
maintenance (PubMed:23875936). Cooperates with TIC components and
other molecular chaperones to drive transport of preproteins into
chloroplasts and functions in the chloroplast stroma to facilitate
membrane translocation during protein import into the organelle
(PubMed:23382192). {ECO:0000269|PubMed:12943545,
ECO:0000269|PubMed:23382192, ECO:0000269|PubMed:23875936,
ECO:0000269|PubMed:25216779}.
-!- SUBUNIT: Homodimer (PubMed:25216779). Interacts with VIPP1
(PubMed:23875936). Interacts with P23-1 (PubMed:20493581).
{ECO:0000269|PubMed:20493581, ECO:0000269|PubMed:23875936,
ECO:0000269|PubMed:25216779}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:12943545, ECO:0000269|PubMed:23382192}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9SIF2-1; Sequence=Displayed;
Name=2;
IsoId=Q9SIF2-2; Sequence=VSP_057880;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, young leaves,
mature leaves, stems, flowers, petals and siliques.
{ECO:0000269|PubMed:12943545}.
-!- DEVELOPMENTAL STAGE: During embryogenesis, highly expressed at 4
days post anthesis. {ECO:0000269|PubMed:23875936}.
-!- INDUCTION: By heat shock and light. {ECO:0000269|PubMed:12943545}.
-!- DISRUPTION PHENOTYPE: Embyronic lethality due to embryo
development arrest at the heart stage.
{ECO:0000269|PubMed:23382192, ECO:0000269|PubMed:23875936}.
-!- MISCELLANEOUS: Plants over-expressing HSP90.7 show albino and
stunted leaves. {ECO:0000269|PubMed:23875936}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AC007167; AAD32922.1; -; Genomic_DNA.
EMBL; CP002685; AEC05778.1; -; Genomic_DNA.
EMBL; CP002685; AEC05779.1; -; Genomic_DNA.
EMBL; AF436826; AAL32008.1; -; mRNA.
EMBL; AY053403; AAK96633.1; -; mRNA.
EMBL; AY094422; AAM19795.1; -; mRNA.
EMBL; BT002234; AAN72245.1; -; mRNA.
EMBL; AK229707; BAF01546.1; -; mRNA.
EMBL; AK229761; BAF01597.1; -; mRNA.
PIR; H84453; H84453.
RefSeq; NP_178487.1; NM_126439.4. [Q9SIF2-1]
RefSeq; NP_849932.1; NM_179601.1. [Q9SIF2-2]
UniGene; At.1835; -.
ProteinModelPortal; Q9SIF2; -.
SMR; Q9SIF2; -.
IntAct; Q9SIF2; 2.
STRING; 3702.AT2G04030.1; -.
SwissPalm; Q9SIF2; -.
PaxDb; Q9SIF2; -.
PRIDE; Q9SIF2; -.
ProMEX; Q9SIF2; -.
EnsemblPlants; AT2G04030.1; AT2G04030.1; AT2G04030. [Q9SIF2-1]
EnsemblPlants; AT2G04030.2; AT2G04030.2; AT2G04030. [Q9SIF2-2]
GeneID; 814930; -.
Gramene; AT2G04030.1; AT2G04030.1; AT2G04030. [Q9SIF2-1]
Gramene; AT2G04030.2; AT2G04030.2; AT2G04030. [Q9SIF2-2]
KEGG; ath:AT2G04030; -.
Araport; AT2G04030; -.
TAIR; locus:2049651; AT2G04030.
eggNOG; KOG0019; Eukaryota.
eggNOG; COG0326; LUCA.
KO; K09487; -.
OMA; NTQKAIW; -.
OrthoDB; EOG093603ZM; -.
PhylomeDB; Q9SIF2; -.
PRO; PR:Q9SIF2; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9SIF2; baseline and differential.
Genevisible; Q9SIF2; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IDA:TAIR.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0009704; P:de-etiolation; IMP:TAIR.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
GO; GO:0010157; P:response to chlorate; IMP:TAIR.
GO; GO:0009408; P:response to heat; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
CDD; cd00075; HATPase_c; 1.
Gene3D; 1.20.120.790; -; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Chaperone; Chloroplast;
Complete proteome; Nucleotide-binding; Plastid; Protein transport;
Reference proteome; Stress response; Transit peptide; Transport.
TRANSIT 1 60 Chloroplast. {ECO:0000255}.
CHAIN 61 780 Heat shock protein 90-5, chloroplastic.
{ECO:0000255}.
/FTId=PRO_0000434018.
NP_BIND 172 173 ATP. {ECO:0000250|UniProtKB:P02829}.
NP_BIND 196 201 ATP. {ECO:0000250|UniProtKB:P02829}.
COMPBIAS 313 316 Poly-Lys. {ECO:0000255}.
COMPBIAS 745 749 Poly-Glu. {ECO:0000255}.
BINDING 106 106 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 110 110 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 152 152 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 157 157 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 251 251 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 441 441 ATP. {ECO:0000250|UniProtKB:P02829}.
VAR_SEQ 476 478 Missing (in isoform 2).
/FTId=VSP_057880.
MUTAGEN 646 646 G->R: In cr88; delay in greening of young
rosette leaves. Reduced nitrate reductase
activity in response to nitrate.
{ECO:0000269|PubMed:12943545}.
CONFLICT 224 224 Y -> N (in Ref. 3; AAM19795).
{ECO:0000305}.
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


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