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Protein

Chaperonin 60 subunit alpha 1, chloroplastic

Gene

CPN60A1

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

Functioni

Binds RuBisCO small and large subunits and is implicated in the assembly of the enzyme oligomer. Involved in protein assisted folding. Required for proper chloroplast development.2 Publications

GO - Molecular functioni

GO - Biological processi

  • chloroplast organization Source: TAIR
  • embryo development ending in seed dormancy Source: TAIR
  • protein folding Source: TAIR
  • protein refolding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperonin 60 subunit alpha 1, chloroplastic
Short name:
CPN-60 alpha 1
Alternative name(s):
Protein SCHLEPPERLESS
RuBisCO large subunit-binding protein subunit alpha 1
Gene namesi
Name:CPN60A1
Synonyms:Cpn60-A(2), SLP
Ordered Locus Names:At2g28000
ORF Names:T1E2.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G28000.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosolic ribosome Source: TAIR
  • membrane Source: TAIR
  • mitochondrion Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Embryos are albino, can germinate but are unable to produce viable seedlings.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi335 – 3351D → A: Retarded growth and pale-green leaves. 1 Publication
Mutagenesisi342 – 3421A → V in arc2; fewer, but larger chloroplasts. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646ChloroplastBy similarityAdd
BLAST
Chaini47 – 586540Chaperonin 60 subunit alpha 1, chloroplasticPRO_0000005016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP21238.
PRIDEiP21238.

2D gel databases

SWISS-2DPAGEP21238.

PTM databases

iPTMnetiP21238.
SwissPalmiP21238.

Expressioni

Tissue specificityi

Expressed in leaves, stems, siliques and flowers.1 Publication

Inductioni

Up-regulated by light.1 Publication

Gene expression databases

GenevisibleiP21238. AT.

Interactioni

Subunit structurei

Part of the Cpn60 complex composed of 7 alpha and 7 beta subunits. This complex shows ATPase activity. The Cpn60 complex interacts with the Cpn10 complex.1 Publication

Protein-protein interaction databases

BioGridi2694. 5 interactions.
IntActiP21238. 2 interactions.
STRINGi3702.AT2G28000.1.

Structurei

3D structure databases

ProteinModelPortaliP21238.
SMRiP21238. Positions 49-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.
HOGENOMiHOG000076290.
InParanoidiP21238.
OMAiRCPLFIV.
PhylomeDBiP21238.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21238-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASANALSSA SVLCSSRQSK LGGGNQQQGQ RVSYNKRTIR RFSVRANVKE
60 70 80 90 100
IAFDQHSRAA LQAGIDKLAD CVGLTLGPRG RNVVLDEFGS PKVVNDGVTI
110 120 130 140 150
ARAIELPNAM ENAGAALIRE VASKTNDSAG DGTTTASILA REIIKHGLLS
160 170 180 190 200
VTSGANPVSL KRGIDKTVQG LIEELQKKAR PVKGRDDIRA VASISAGNDD
210 220 230 240 250
LIGSMIADAI DKVGPDGVLS IESSSSFETT VEVEEGMEID RGYISPQFVT
260 270 280 290 300
NPEKLLAEFE NARVLITDQK ITAIKDIIPI LEKTTQLRAP LLIIAEDVTG
310 320 330 340 350
EALATLVVNK LRGVLNVVAV KAPGFGERRK AMLQDIAILT GAEYLAMDMS
360 370 380 390 400
LLVENATIDQ LGIARKVTIS KDSTTLIADA ASKDELQARI AQLKKELFET
410 420 430 440 450
DSVYDSEKLA ERIAKLSGGV AVIKVGAATE TELEDRKLRI EDAKNATFAA
460 470 480 490 500
IEEGIVPGGG AALVHLSTVI PAIKETFEDA DERLGADIVQ KALLSPAALI
510 520 530 540 550
AQNAGVEGEV VVEKIMFSDW ENGYNAMTDT YENLFEAGVI DPAKVTRCAL
560 570 580
QNAASVAGMV LTTQAIVVDK PKPKAPAAAA PEGLMV
Length:586
Mass (Da):62,072
Last modified:November 1, 1997 - v2
Checksum:i71BCBDC81C7905B3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841G → D in AAM63618 (Ref. 5) Curated
Sequence conflicti186 – 1861D → V in AAA32724 (PubMed:1979547).Curated
Sequence conflicti188 – 1881I → Y in AAA32724 (PubMed:1979547).Curated
Sequence conflicti569 – 5691D → G in BAD95121 (Ref. 7) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49357 Genomic DNA. Translation: AAA92061.1.
AC006929 Genomic DNA. Translation: AAD21502.1.
CP002685 Genomic DNA. Translation: AEC08068.1.
BT002441 mRNA. Translation: AAO00801.1.
BT008784 mRNA. Translation: AAP68223.1.
AY086555 mRNA. Translation: AAM63618.1.
M35597 mRNA. Translation: AAA32724.1.
AK222126 mRNA. Translation: BAD95121.1.
PIRiS71235.
RefSeqiNP_180367.1. NM_128359.4.
UniGeneiAt.24154.
At.67332.

Genome annotation databases

EnsemblPlantsiAT2G28000.1; AT2G28000.1; AT2G28000.
GeneIDi817344.
GrameneiAT2G28000.1; AT2G28000.1; AT2G28000.
KEGGiath:AT2G28000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49357 Genomic DNA. Translation: AAA92061.1.
AC006929 Genomic DNA. Translation: AAD21502.1.
CP002685 Genomic DNA. Translation: AEC08068.1.
BT002441 mRNA. Translation: AAO00801.1.
BT008784 mRNA. Translation: AAP68223.1.
AY086555 mRNA. Translation: AAM63618.1.
M35597 mRNA. Translation: AAA32724.1.
AK222126 mRNA. Translation: BAD95121.1.
PIRiS71235.
RefSeqiNP_180367.1. NM_128359.4.
UniGeneiAt.24154.
At.67332.

3D structure databases

ProteinModelPortaliP21238.
SMRiP21238. Positions 49-572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi2694. 5 interactions.
IntActiP21238. 2 interactions.
STRINGi3702.AT2G28000.1.

PTM databases

iPTMnetiP21238.
SwissPalmiP21238.

2D gel databases

SWISS-2DPAGEP21238.

Proteomic databases

PaxDbiP21238.
PRIDEiP21238.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G28000.1; AT2G28000.1; AT2G28000.
GeneIDi817344.
GrameneiAT2G28000.1; AT2G28000.1; AT2G28000.
KEGGiath:AT2G28000.

Organism-specific databases

TAIRiAT2G28000.

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.
HOGENOMiHOG000076290.
InParanoidiP21238.
OMAiRCPLFIV.
PhylomeDBiP21238.

Miscellaneous databases

PROiP21238.

Gene expression databases

GenevisibleiP21238. AT.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Arabidopsis embryo mutant schlepperless has a defect in the chaperonin-60alpha gene."
    Apuya N.R., Yadegari R., Fischer R.L., Harada J.J., Zimmerman J.L., Goldberg R.B.
    Plant Physiol. 126:717-730(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    Strain: cv. Wassilewskija.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Unique composition of plastid chaperonin-60: alpha and beta polypeptide-encoding genes are highly divergent."
    Martel R., Cloney L.P., Pelcher L.E., Hemmingsen S.M.
    Gene 94:181-187(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 67-311.
    Strain: cv. Columbia.
  7. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    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.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-586.
  8. "Differential involvement of the circadian clock in the expression of genes required for ribulose-1,5-bisphosphate carboxylase/oxygenase synthesis, assembly, and activation in Arabidopsis thaliana."
    Pilgrim M.L., McClung C.R.
    Plant Physiol. 103:553-564(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY LIGHT.
  9. "Functional characterization of the higher plant chloroplast chaperonins."
    Viitanen P.V., Schmidt M., Buchner J., Suzuki T., Vierling E., Dickson R., Lorimer G.H., Gatenby A., Soll J.
    J. Biol. Chem. 270:18158-18164(1995)
    Cited for: FUNCTION, INTERACTION.
  10. "Arabidopsis thaliana type I and II chaperonins."
    Hill J.E., Hemmingsen S.M.
    Cell Stress Chaperones 6:190-200(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  11. "Plastid chaperonin proteins Cpn60 alpha and Cpn60 beta are required for plastid division in Arabidopsis thaliana."
    Suzuki K., Nakanishi H., Bower J., Yoder D.W., Osteryoung K.W., Miyagishima S.Y.
    BMC Plant Biol. 9:38-38(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ALA-342, DISRUPTION PHENOTYPE.
  12. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  13. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "A chaperonin subunit with unique structures is essential for folding of a specific substrate."
    Peng L., Fukao Y., Myouga F., Motohashi R., Shinozaki K., Shikanai T.
    PLoS Biol. 9:E1001040-E1001040(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-335, GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiCPNA1_ARATH
AccessioniPrimary (citable) accession number: P21238
Secondary accession number(s): Q42554, Q56WB8, Q8L5U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: November 1, 1997
Last modified: February 17, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Assisted protein folding requires ATP hydrolysis, but not K+ ions.

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.