CH20_ARATH
ID CH20_ARATH Reviewed; 253 AA.
AC O65282; Q9TNN2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=20 kDa chaperonin, chloroplastic;
DE AltName: Full=Chaperonin 10;
DE Short=Ch-CPN10;
DE Short=Cpn10;
DE AltName: Full=Chaperonin 20;
DE AltName: Full=Protein Cpn21;
DE Flags: Precursor;
GN Name=CPN20; Synonyms=CHCPN10, CPN21; OrderedLocusNames=At5g20720;
GN ORFNames=T1M15.120;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9989238; DOI=10.1016/s0167-4838(98)00268-4;
RA Hirohashi T., Nishio K., Nakai M.;
RT "cDNA sequence and overexpression of chloroplast chaperonin 21 from
RT Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1429:512-515(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seedling;
RX PubMed=10964710; DOI=10.1006/bbrc.2000.3335;
RA Yang T., Poovaiah B.W.;
RT "Arabidopsis chloroplast chaperonin 10 is a calmodulin-binding protein.";
RL Biochem. Biophys. Res. Commun. 275:601-607(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Yi H., Lee J., Shin B., Choi G.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION BY HEAT SHOCK.
RC STRAIN=cv. Landsberg erecta; TISSUE=Seedling;
RX PubMed=10205903; DOI=10.1046/j.1365-313x.1999.00388.x;
RA Koumoto Y., Shimada T., Kondo M., Takao T., Shimonishi Y.,
RA Hara-Nishimura I., Nishimura M.;
RT "Chloroplast Cpn20 forms a tetrameric structure in Arabidopsis thaliana.";
RL Plant J. 17:467-477(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [6]
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 [7]
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 [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-83; LEU-86; GLY-181 AND LEU-184.
RX PubMed=17178727; DOI=10.1074/jbc.m606433200;
RA Bonshtien A.L., Weiss C., Vitlin A., Niv A., Lorimer G.H., Azem A.;
RT "Significance of the N-terminal domain for the function of chloroplast
RT cpn20 chaperonin.";
RL J. Biol. Chem. 282:4463-4469(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [10]
RP INTERACTION WITH FSD1, AND FUNCTION.
RX PubMed=23057508; DOI=10.1111/j.1469-8137.2012.04369.x;
RA Kuo W.Y., Huang C.H., Liu A.C., Cheng C.P., Li S.H., Chang W.C., Weiss C.,
RA Azem A., Jinn T.L.;
RT "CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity
RT independent of its co-chaperonin role in Arabidopsis chloroplasts.";
RL New Phytol. 197:99-110(2013).
RN [11]
RP FUNCTION, AND INTERACTION WITH CHLH.
RX PubMed=23783410; DOI=10.1007/s11103-013-0082-8;
RA Zhang X.F., Jiang T., Wu Z., Du S.Y., Yu Y.T., Jiang S.C., Lu K.,
RA Feng X.J., Wang X.F., Zhang D.P.;
RT "Cochaperonin CPN20 negatively regulates abscisic acid signaling in
RT Arabidopsis.";
RL Plant Mol. Biol. 83:205-218(2013).
RN [12]
RP INTERACTION WITH CLPT1 AND CLPT2.
RX PubMed=25921872; DOI=10.1105/tpc.15.00106;
RA Kim J., Kimber M.S., Nishimura K., Friso G., Schultz L., Ponnala L.,
RA van Wijk K.J.;
RT "Structures, functions, and interactions of ClpT1 and ClpT2 in the Clp
RT protease system of Arabidopsis chloroplasts.";
RL Plant Cell 27:1477-1496(2015).
RN [13]
RP INTERACTION WITH SPY.
RX PubMed=34712252; DOI=10.3389/fpls.2021.724144;
RA Liang L., Wang Q., Song Z., Wu Y., Liang Q., Wang Q., Yang J., Bi Y.,
RA Zhou W., Fan L.M.;
RT "O-fucosylation of CPN20 by SPINDLY derepresses abscisic acid signaling
RT during seed germination and seedling development.";
RL Front. Plant Sci. 12:724144-724144(2021).
CC -!- FUNCTION: Seems to function only as a co-chaperone, along with CPN60,
CC and in certain cases is essential for the discharge of biologically
CC active proteins from CPN60 (PubMed:17178727, PubMed:23057508). Required
CC to activate the iron superoxide dismutases (FeSOD) (PubMed:23057508).
CC {ECO:0000269|PubMed:17178727, ECO:0000269|PubMed:23057508}.
CC -!- FUNCTION: Involved in abscisic acid (ABA) signaling, independently of
CC its co-chaperone role. Acts as negative regulator of the CHLH-WRKY40
CC coupled ABA signaling pathway, downstream of CHLH and upstream of
CC WRKY40. {ECO:0000269|PubMed:23783410}.
CC -!- SUBUNIT: Homotetramer. Forms stable complexes with CPN60 in the
CC presence of ATP (PubMed:10205903). Interacts with FSD1
CC (PubMed:23057508). Interacts with CLPT1 and CLPT2 (PubMed:25921872).
CC Interacts with CHLH (PubMed:23783410, PubMed:10205903, PubMed:23057508,
CC PubMed:25921872). Interacts with SPY (PubMed:34712252).
CC {ECO:0000269|PubMed:10205903, ECO:0000269|PubMed:23057508,
CC ECO:0000269|PubMed:23783410, ECO:0000269|PubMed:25921872,
CC ECO:0000269|PubMed:34712252}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10205903}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in leaves and
CC inflorescence. Low levels found in roots.
CC {ECO:0000269|PubMed:10205903}.
CC -!- INDUCTION: Induced by heat treatment. {ECO:0000269|PubMed:10205903}.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
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DR EMBL; AJ010818; CAA09368.1; -; mRNA.
DR EMBL; AF268068; AAG13931.1; -; mRNA.
DR EMBL; AF059037; AAC14026.1; -; mRNA.
DR EMBL; AB007130; BAB61619.1; -; mRNA.
DR EMBL; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92881.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92882.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92883.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70274.1; -; Genomic_DNA.
DR EMBL; AY062971; AAL33817.1; -; mRNA.
DR EMBL; AY034979; AAK59484.1; -; mRNA.
DR EMBL; AF428366; AAL16296.1; -; mRNA.
DR EMBL; AF428339; AAL16269.1; -; mRNA.
DR PIR; T52122; T52122.
DR PIR; T52613; T52613.
DR RefSeq; NP_001318614.1; NM_001343684.1.
DR RefSeq; NP_001331898.1; NM_001343685.1.
DR RefSeq; NP_197572.1; NM_122079.4.
DR RefSeq; NP_851045.1; NM_180714.4.
DR AlphaFoldDB; O65282; -.
DR SMR; O65282; -.
DR BioGRID; 17470; 21.
DR IntAct; O65282; 5.
DR STRING; 3702.AT5G20720.3; -.
DR iPTMnet; O65282; -.
DR SWISS-2DPAGE; O65282; -.
DR PaxDb; O65282; -.
DR PRIDE; O65282; -.
DR ProteomicsDB; 224486; -.
DR EnsemblPlants; AT5G20720.1; AT5G20720.1; AT5G20720.
DR EnsemblPlants; AT5G20720.2; AT5G20720.2; AT5G20720.
DR EnsemblPlants; AT5G20720.3; AT5G20720.3; AT5G20720.
DR EnsemblPlants; AT5G20720.4; AT5G20720.4; AT5G20720.
DR GeneID; 832195; -.
DR Gramene; AT5G20720.1; AT5G20720.1; AT5G20720.
DR Gramene; AT5G20720.2; AT5G20720.2; AT5G20720.
DR Gramene; AT5G20720.3; AT5G20720.3; AT5G20720.
DR Gramene; AT5G20720.4; AT5G20720.4; AT5G20720.
DR KEGG; ath:AT5G20720; -.
DR Araport; AT5G20720; -.
DR TAIR; locus:2180454; AT5G20720.
DR eggNOG; KOG1641; Eukaryota.
DR HOGENOM; CLU_073980_0_0_1; -.
DR InParanoid; O65282; -.
DR OMA; VIMPESK; -.
DR OrthoDB; 1368363at2759; -.
DR PhylomeDB; O65282; -.
DR PRO; PR:O65282; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65282; baseline and differential.
DR Genevisible; O65282; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IDA:TAIR.
DR GO; GO:0051290; P:protein heterotetramerization; IPI:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR CDD; cd00320; cpn10; 2.
DR Gene3D; 2.30.33.40; -; 2.
DR HAMAP; MF_00580; CH10; 2.
DR InterPro; IPR020818; Chaperonin_GroES.
DR InterPro; IPR037124; Chaperonin_GroES_sf.
DR InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR InterPro; IPR017416; Cpn20.
DR InterPro; IPR011032; GroES-like_sf.
DR PANTHER; PTHR10772; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 2.
DR PIRSF; PIRSF038157; Chaperonin_21_chloroplast; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 2.
DR SUPFAM; SSF50129; SSF50129; 2.
DR PROSITE; PS00681; CHAPERONINS_CPN10; 2.
PE 1: Evidence at protein level;
KW Chaperone; Chloroplast; Phosphoprotein; Plastid; Reference proteome;
KW Repeat; Stress response; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..253
FT /note="20 kDa chaperonin, chloroplastic"
FT /id="PRO_0000005045"
FT REGION 60..153
FT /note="Cpn-10 domain 1"
FT /evidence="ECO:0000305"
FT REGION 159..252
FT /note="Cpn-10 domain 2"
FT /evidence="ECO:0000305"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MUTAGEN 83
FT /note="G->A: Reduces co-chaperone activity more than 20-
FT fold."
FT /evidence="ECO:0000269|PubMed:17178727"
FT MUTAGEN 86
FT /note="L->A: Reduces co-chaperone activity more than 20-
FT fold."
FT /evidence="ECO:0000269|PubMed:17178727"
FT MUTAGEN 181
FT /note="G->A: Reduces co-chaperone activity more than 3-
FT fold."
FT /evidence="ECO:0000269|PubMed:17178727"
FT MUTAGEN 184
FT /note="L->A: Reduces co-chaperone activity more than 20-
FT fold."
FT /evidence="ECO:0000269|PubMed:17178727"
FT CONFLICT 31
FT /note="F -> V (in Ref. 3; AAC14026)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..87
FT /note="LP -> TFH (in Ref. 3; AAC14026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 26802 MW; 43A8CD78E7C95BCC CRC64;
MAATQLTASP VTMSARSLAS LDGLRASSVK FSSLKPGTLR QSQFRRLVVK AASVVAPKYT
SIKPLGDRVL VKIKEAEEKT LGGILLPSTA QSKPQGGEVV AVGEGRTIGK NKIDITVPTG
AQIIYSKYAG TEVEFNDVKH LILKEDDIVG ILETEDIKDL KPLNDRVFIK VAEAEEKTAG
GLLLTETTKE KPSIGTVIAV GPGSLDEEGK ITPLPVSTGS TVLYSKYAGN DFKGKDGSNY
IALRASDVMA ILS
