Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

20 kDa chaperonin, chloroplastic

Gene

CPN21

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Seems to function only as a co-chaperone, along with cpn60, and in certain cases is essential for the discharge of biologically active proteins from cpn60. Required to activate the iron superoxide dismutases (FeSOD).1 Publication

GO - Molecular functioni

  • ATP binding Source: InterPro
  • chaperone binding Source: GO_Central
  • copper ion binding Source: TAIR
  • unfolded protein binding Source: GO_Central

GO - Biological processi

  • chaperone mediated protein folding requiring cofactor Source: GO_Central
  • positive regulation of superoxide dismutase activity Source: TAIR
  • response to cadmium ion Source: TAIR
  • response to cold Source: TAIR
  • response to unfolded protein Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
20 kDa chaperonin, chloroplastic
Alternative name(s):
Chaperonin 10
Short name:
Ch-CPN10
Short name:
Cpn10
Chaperonin 20
Protein Cpn21
Gene namesi
Name:CPN21
Synonyms:CHCPN10, CPN20
Ordered Locus Names:At5g20720
ORF Names:T1M15.120
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G20720.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • chloroplast thylakoid membrane Source: TAIR
  • mitochondrial matrix Source: GO_Central
  • mitochondrion Source: TAIR
  • plastid Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5151ChloroplastBy similarityAdd
BLAST
Chaini52 – 25320220 kDa chaperonin, chloroplasticPRO_0000005045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei212 – 2121PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO65282.
PRIDEiO65282.

2D gel databases

SWISS-2DPAGEO65282.

PTM databases

iPTMnetiO65282.

Expressioni

Tissue specificityi

Ubiquitous. Most abundant in leaves and inflorescence. Low levels found in roots.

Inductioni

Increased by heat treatment.

Gene expression databases

GenevisibleiO65282. AT.

Interactioni

Subunit structurei

Forms stable complexes with cpn60 in the presence of ATP. Homotetramer. Interacts with FSD1 (PubMed:23057508). Interacts with CLPT1 and CLPT2 (PubMed:25921872).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FSD1P212762EBI-4435709,EBI-4466816

GO - Molecular functioni

Protein-protein interaction databases

BioGridi17470. 3 interactions.
IntActiO65282. 5 interactions.
STRINGi3702.AT5G20720.1.

Structurei

3D structure databases

ProteinModelPortaliO65282.
SMRiO65282. Positions 61-152, 159-253.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 154103Cpn-10 domain 1Add
BLAST
Regioni155 – 25399Cpn-10 domain 2Add
BLAST

Sequence similaritiesi

Belongs to the GroES chaperonin family.Curated

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG1641. Eukaryota.
COG0234. LUCA.
HOGENOMiHOG000133897.
InParanoidiO65282.
KOiK04078.
OMAiGEGHSIG.
PhylomeDBiO65282.

Family and domain databases

Gene3Di2.30.33.40. 2 hits.
HAMAPiMF_00580. CH10. 2 domains.
InterProiIPR020818. Chaperonin_GroES.
IPR018369. Chaprnonin_Cpn10_CS.
IPR017416. Cpn20.
IPR011032. GroES-like.
[Graphical view]
PANTHERiPTHR10772. PTHR10772. 1 hit.
PfamiPF00166. Cpn10. 2 hits.
[Graphical view]
PIRSFiPIRSF038157. Chaperonin_21_chloroplast. 1 hit.
PRINTSiPR00297. CHAPERONIN10.
SMARTiSM00883. Cpn10. 2 hits.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
PROSITEiPS00681. CHAPERONINS_CPN10. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O65282-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATQLTASP VTMSARSLAS LDGLRASSVK FSSLKPGTLR QSQFRRLVVK
60 70 80 90 100
AASVVAPKYT SIKPLGDRVL VKIKEAEEKT LGGILLPSTA QSKPQGGEVV
110 120 130 140 150
AVGEGRTIGK NKIDITVPTG AQIIYSKYAG TEVEFNDVKH LILKEDDIVG
160 170 180 190 200
ILETEDIKDL KPLNDRVFIK VAEAEEKTAG GLLLTETTKE KPSIGTVIAV
210 220 230 240 250
GPGSLDEEGK ITPLPVSTGS TVLYSKYAGN DFKGKDGSNY IALRASDVMA

ILS
Length:253
Mass (Da):26,802
Last modified:December 8, 2000 - v2
Checksum:i43A8CD78E7C95BCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311F → V in AAC14026 (Ref. 3) Curated
Sequence conflicti86 – 872LP → TFH in AAC14026 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010818 mRNA. Translation: CAA09368.1.
AF268068 mRNA. Translation: AAG13931.1.
AF059037 mRNA. Translation: AAC14026.1.
AB007130 mRNA. Translation: BAB61619.1.
AF296832 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92881.1.
CP002688 Genomic DNA. Translation: AED92882.1.
CP002688 Genomic DNA. Translation: AED92883.1.
AY062971 mRNA. Translation: AAL33817.1.
AY034979 mRNA. Translation: AAK59484.1.
AF428366 mRNA. Translation: AAL16296.1.
AF428339 mRNA. Translation: AAL16269.1.
PIRiT52122.
T52613.
RefSeqiNP_001190350.1. NM_001203421.1.
NP_197572.1. NM_122079.4.
NP_851045.1. NM_180714.3.
UniGeneiAt.49045.
At.59645.

Genome annotation databases

EnsemblPlantsiAT5G20720.1; AT5G20720.1; AT5G20720.
AT5G20720.2; AT5G20720.2; AT5G20720.
AT5G20720.3; AT5G20720.3; AT5G20720.
GeneIDi832195.
GrameneiAT5G20720.1; AT5G20720.1; AT5G20720.
AT5G20720.2; AT5G20720.2; AT5G20720.
AT5G20720.3; AT5G20720.3; AT5G20720.
KEGGiath:AT5G20720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010818 mRNA. Translation: CAA09368.1.
AF268068 mRNA. Translation: AAG13931.1.
AF059037 mRNA. Translation: AAC14026.1.
AB007130 mRNA. Translation: BAB61619.1.
AF296832 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92881.1.
CP002688 Genomic DNA. Translation: AED92882.1.
CP002688 Genomic DNA. Translation: AED92883.1.
AY062971 mRNA. Translation: AAL33817.1.
AY034979 mRNA. Translation: AAK59484.1.
AF428366 mRNA. Translation: AAL16296.1.
AF428339 mRNA. Translation: AAL16269.1.
PIRiT52122.
T52613.
RefSeqiNP_001190350.1. NM_001203421.1.
NP_197572.1. NM_122079.4.
NP_851045.1. NM_180714.3.
UniGeneiAt.49045.
At.59645.

3D structure databases

ProteinModelPortaliO65282.
SMRiO65282. Positions 61-152, 159-253.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17470. 3 interactions.
IntActiO65282. 5 interactions.
STRINGi3702.AT5G20720.1.

PTM databases

iPTMnetiO65282.

2D gel databases

SWISS-2DPAGEO65282.

Proteomic databases

PaxDbiO65282.
PRIDEiO65282.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G20720.1; AT5G20720.1; AT5G20720.
AT5G20720.2; AT5G20720.2; AT5G20720.
AT5G20720.3; AT5G20720.3; AT5G20720.
GeneIDi832195.
GrameneiAT5G20720.1; AT5G20720.1; AT5G20720.
AT5G20720.2; AT5G20720.2; AT5G20720.
AT5G20720.3; AT5G20720.3; AT5G20720.
KEGGiath:AT5G20720.

Organism-specific databases

TAIRiAT5G20720.

Phylogenomic databases

eggNOGiKOG1641. Eukaryota.
COG0234. LUCA.
HOGENOMiHOG000133897.
InParanoidiO65282.
KOiK04078.
OMAiGEGHSIG.
PhylomeDBiO65282.

Miscellaneous databases

PROiO65282.

Gene expression databases

GenevisibleiO65282. AT.

Family and domain databases

Gene3Di2.30.33.40. 2 hits.
HAMAPiMF_00580. CH10. 2 domains.
InterProiIPR020818. Chaperonin_GroES.
IPR018369. Chaprnonin_Cpn10_CS.
IPR017416. Cpn20.
IPR011032. GroES-like.
[Graphical view]
PANTHERiPTHR10772. PTHR10772. 1 hit.
PfamiPF00166. Cpn10. 2 hits.
[Graphical view]
PIRSFiPIRSF038157. Chaperonin_21_chloroplast. 1 hit.
PRINTSiPR00297. CHAPERONIN10.
SMARTiSM00883. Cpn10. 2 hits.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
PROSITEiPS00681. CHAPERONINS_CPN10. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence and overexpression of chloroplast chaperonin 21 from Arabidopsis thaliana."
    Hirohashi T., Nishio K., Nakai M.
    Biochim. Biophys. Acta 1429:512-515(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Arabidopsis chloroplast chaperonin 10 is a calmodulin-binding protein."
    Yang T., Poovaiah B.W.
    Biochem. Biophys. Res. Commun. 275:601-607(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Seedling.
  3. Yi H., Lee J., Shin B., Choi G.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  4. "Chloroplast Cpn20 forms a tetrameric structure in Arabidopsis thaliana."
    Koumoto Y., Shimada T., Kondo M., Takao T., Shimonishi Y., Hara-Nishimura I., Nishimura M.
    Plant J. 17:467-477(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Landsberg erecta.
    Tissue: Seedling.
  5. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  6. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  7. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  8. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
    Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
    Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Wassilewskija.
  9. "Identification of phosphoproteins in Arabidopsis thaliana leaves using polyethylene glycol fractionation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry."
    Aryal U.K., Krochko J.E., Ross A.R.
    J. Proteome Res. 11:425-437(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co-chaperonin role in Arabidopsis chloroplasts."
    Kuo W.Y., Huang C.H., Liu A.C., Cheng C.P., Li S.H., Chang W.C., Weiss C., Azem A., Jinn T.L.
    New Phytol. 197:99-110(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FSD1, FUNCTION.
  11. "Structures, functions, and interactions of ClpT1 and ClpT2 in the Clp protease system of Arabidopsis chloroplasts."
    Kim J., Kimber M.S., Nishimura K., Friso G., Schultz L., Ponnala L., van Wijk K.J.
    Plant Cell 27:1477-1496(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLPT1 AND CLPT2.

Entry informationi

Entry nameiCH10C_ARATH
AccessioniPrimary (citable) accession number: O65282
Secondary accession number(s): Q9TNN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: December 8, 2000
Last modified: June 8, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.