CPNA1_ARATH
ID CPNA1_ARATH Reviewed; 586 AA.
AC P21238; Q42554; Q56WB8; Q8L5U4;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Chaperonin 60 subunit alpha 1, chloroplastic;
DE Short=CPN-60 alpha 1;
DE AltName: Full=Protein SCHLEPPERLESS;
DE AltName: Full=RuBisCO large subunit-binding protein subunit alpha 1;
DE Flags: Precursor;
GN Name=CPN60A1; Synonyms=Cpn60-A(2), SLP; OrderedLocusNames=At2g28000;
GN ORFNames=T1E2.8;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11402200; DOI=10.1104/pp.126.2.717;
RA Apuya N.R., Yadegari R., Fischer R.L., Harada J.J., Zimmerman J.L.,
RA Goldberg R.B.;
RT "The Arabidopsis embryo mutant schlepperless has a defect in the
RT chaperonin-60alpha gene.";
RL Plant Physiol. 126:717-730(2001).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-311.
RC STRAIN=cv. Columbia;
RX PubMed=1979547; DOI=10.1016/0378-1119(90)90385-5;
RA Martel R., Cloney L.P., Pelcher L.E., Hemmingsen S.M.;
RT "Unique composition of plastid chaperonin-60: alpha and beta polypeptide-
RT encoding genes are highly divergent.";
RL Gene 94:181-187(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-586.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INDUCTION BY LIGHT.
RX PubMed=12231961; DOI=10.1104/pp.103.2.553;
RA Pilgrim M.L., McClung C.R.;
RT "Differential involvement of the circadian clock in the expression of genes
RT required for ribulose-1,5-bisphosphate carboxylase/oxygenase synthesis,
RT assembly, and activation in Arabidopsis thaliana.";
RL Plant Physiol. 103:553-564(1993).
RN [9]
RP FUNCTION, AND INTERACTION.
RX DOI=10.1074/jbc.270.30.18158;
RA Viitanen P.V., Schmidt M., Buchner J., Suzuki T., Vierling E., Dickson R.,
RA Lorimer G.H., Gatenby A., Soll J.;
RT "Functional characterization of the higher plant chloroplast chaperonins.";
RL J. Biol. Chem. 270:18158-18164(1995).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599560; DOI=10.1379/1466-1268(2001)006<0190:attiai>2.0.co;2;
RA Hill J.E., Hemmingsen S.M.;
RT "Arabidopsis thaliana type I and II chaperonins.";
RL Cell Stress Chaperones 6:190-200(2001).
RN [11]
RP FUNCTION, MUTAGENESIS OF ALA-342, AND DISRUPTION PHENOTYPE.
RX PubMed=19344532; DOI=10.1186/1471-2229-9-38;
RA Suzuki K., Nakanishi H., Bower J., Yoder D.W., Osteryoung K.W.,
RA Miyagishima S.Y.;
RT "Plastid chaperonin proteins Cpn60 alpha and Cpn60 beta are required for
RT plastid division in Arabidopsis thaliana.";
RL BMC Plant Biol. 9:38-38(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [14]
RP MUTAGENESIS OF ASP-335, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21483722; DOI=10.1371/journal.pbio.1001040;
RA Peng L., Fukao Y., Myouga F., Motohashi R., Shinozaki K., Shikanai T.;
RT "A chaperonin subunit with unique structures is essential for folding of a
RT specific substrate.";
RL PLoS Biol. 9:E1001040-E1001040(2011).
CC -!- FUNCTION: Binds RuBisCO small and large subunits and is implicated in
CC the assembly of the enzyme oligomer. Involved in protein assisted
CC folding. Required for proper chloroplast development.
CC {ECO:0000269|PubMed:19344532, ECO:0000269|Ref.9}.
CC -!- SUBUNIT: Part of the Cpn60 complex composed of 7 alpha and 7 beta
CC subunits. This complex shows ATPase activity. The Cpn60 complex
CC interacts with the Cpn10 complex. {ECO:0000269|Ref.9}.
CC -!- INTERACTION:
CC P21238; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-1253243, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, siliques and flowers.
CC {ECO:0000269|PubMed:11402200}.
CC -!- INDUCTION: Up-regulated by light. {ECO:0000269|PubMed:12231961}.
CC -!- DISRUPTION PHENOTYPE: Embryos are albino, can germinate but are unable
CC to produce viable seedlings. {ECO:0000269|PubMed:11402200,
CC ECO:0000269|PubMed:19344532}.
CC -!- MISCELLANEOUS: Assisted protein folding requires ATP hydrolysis, but
CC not K(+) ions.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; U49357; AAA92061.1; -; Genomic_DNA.
DR EMBL; AC006929; AAD21502.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08068.1; -; Genomic_DNA.
DR EMBL; BT002441; AAO00801.1; -; mRNA.
DR EMBL; BT008784; AAP68223.1; -; mRNA.
DR EMBL; AY086555; AAM63618.1; -; mRNA.
DR EMBL; M35597; AAA32724.1; -; mRNA.
DR EMBL; AK222126; BAD95121.1; -; mRNA.
DR PIR; S71235; S71235.
DR RefSeq; NP_180367.1; NM_128359.5.
DR AlphaFoldDB; P21238; -.
DR SMR; P21238; -.
DR BioGRID; 2694; 32.
DR IntAct; P21238; 4.
DR STRING; 3702.AT2G28000.1; -.
DR iPTMnet; P21238; -.
DR MetOSite; P21238; -.
DR SwissPalm; P21238; -.
DR SWISS-2DPAGE; P21238; -.
DR PaxDb; P21238; -.
DR PRIDE; P21238; -.
DR ProteomicsDB; 220437; -.
DR EnsemblPlants; AT2G28000.1; AT2G28000.1; AT2G28000.
DR GeneID; 817344; -.
DR Gramene; AT2G28000.1; AT2G28000.1; AT2G28000.
DR KEGG; ath:AT2G28000; -.
DR Araport; AT2G28000; -.
DR TAIR; locus:2057841; AT2G28000.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_1_1_1; -.
DR InParanoid; P21238; -.
DR OMA; WILICIT; -.
DR OrthoDB; 415781at2759; -.
DR PhylomeDB; P21238; -.
DR PRO; PR:P21238; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P21238; baseline and differential.
DR Genevisible; P21238; 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:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0050821; P:protein stabilization; IMP:TAIR.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 2.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Phosphoprotein;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 47..586
FT /note="Chaperonin 60 subunit alpha 1, chloroplastic"
FT /id="PRO_0000005016"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MUTAGEN 335
FT /note="D->A: Retarded growth and pale-green leaves."
FT /evidence="ECO:0000269|PubMed:21483722"
FT MUTAGEN 342
FT /note="A->V: In arc2; fewer, but larger chloroplasts."
FT /evidence="ECO:0000269|PubMed:19344532"
FT CONFLICT 184
FT /note="G -> D (in Ref. 5; AAM63618)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="D -> V (in Ref. 6; AAA32724)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="I -> Y (in Ref. 6; AAA32724)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="D -> G (in Ref. 7; BAD95121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 62072 MW; 71BCBDC81C7905B3 CRC64;
MASANALSSA SVLCSSRQSK LGGGNQQQGQ RVSYNKRTIR RFSVRANVKE IAFDQHSRAA
LQAGIDKLAD CVGLTLGPRG RNVVLDEFGS PKVVNDGVTI ARAIELPNAM ENAGAALIRE
VASKTNDSAG DGTTTASILA REIIKHGLLS VTSGANPVSL KRGIDKTVQG LIEELQKKAR
PVKGRDDIRA VASISAGNDD LIGSMIADAI DKVGPDGVLS IESSSSFETT VEVEEGMEID
RGYISPQFVT NPEKLLAEFE NARVLITDQK ITAIKDIIPI LEKTTQLRAP LLIIAEDVTG
EALATLVVNK LRGVLNVVAV KAPGFGERRK AMLQDIAILT GAEYLAMDMS LLVENATIDQ
LGIARKVTIS KDSTTLIADA ASKDELQARI AQLKKELFET DSVYDSEKLA ERIAKLSGGV
AVIKVGAATE TELEDRKLRI EDAKNATFAA IEEGIVPGGG AALVHLSTVI PAIKETFEDA
DERLGADIVQ KALLSPAALI AQNAGVEGEV VVEKIMFSDW ENGYNAMTDT YENLFEAGVI
DPAKVTRCAL QNAASVAGMV LTTQAIVVDK PKPKAPAAAA PEGLMV
