CPNB3_ARATH
ID CPNB3_ARATH Reviewed; 597 AA.
AC C0Z361; Q0WRG9; Q9FHA9;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chaperonin 60 subunit beta 3, chloroplastic;
DE Short=CPN-60 beta 3;
DE Flags: Precursor;
GN Name=CPN60B3; Synonyms=Cpn60-B(1); OrderedLocusNames=At5g56500;
GN ORFNames=MCD7.27;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, AND IDENTIFICATION IN CPN60 COMPLEX.
RX PubMed=19224397; DOI=10.1007/s12192-009-0104-2;
RA Bonshtien A.L., Parnas A., Sharkia R., Niv A., Mizrahi I., Azem A.,
RA Weiss C.;
RT "Differential effects of co-chaperonin homologs on cpn60 oligomers.";
RL Cell Stress Chaperones 14:509-519(2009).
RN [10]
RP 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: Involved in protein assisted folding.
CC {ECO:0000269|PubMed:19224397, ECO:0000269|Ref.7}.
CC -!- SUBUNIT: Part of the Cpn60 complex composed of 7 alpha and 7 beta
CC subunits. Can also form a complex composed of 14 beta subunits only.
CC Both complexes show ATPase activity. The Cpn60 complex interacts with
CC the Cpn10 complex. {ECO:0000269|PubMed:19224397, ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by light. {ECO:0000269|PubMed:12231961}.
CC -!- MISCELLANEOUS: Assisted protein folding requires ATP hydrolysis, but
CC not K(+) ions.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11583.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019234; BAB11583.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB009049; BAB11583.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED96773.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96774.1; -; Genomic_DNA.
DR EMBL; AK228340; BAF00280.1; -; mRNA.
DR EMBL; AK319025; BAH57140.1; -; mRNA.
DR RefSeq; NP_001032083.1; NM_001037006.4.
DR RefSeq; NP_200461.4; NM_125033.5.
DR AlphaFoldDB; C0Z361; -.
DR SMR; C0Z361; -.
DR BioGRID; 20995; 28.
DR IntAct; C0Z361; 2.
DR STRING; 3702.AT5G56500.2; -.
DR iPTMnet; C0Z361; -.
DR PaxDb; C0Z361; -.
DR PRIDE; C0Z361; -.
DR ProMEX; C0Z361; -.
DR ProteomicsDB; 220438; -.
DR EnsemblPlants; AT5G56500.1; AT5G56500.1; AT5G56500.
DR EnsemblPlants; AT5G56500.2; AT5G56500.2; AT5G56500.
DR GeneID; 835751; -.
DR Gramene; AT5G56500.1; AT5G56500.1; AT5G56500.
DR Gramene; AT5G56500.2; AT5G56500.2; AT5G56500.
DR KEGG; ath:AT5G56500; -.
DR Araport; AT5G56500; -.
DR TAIR; locus:2161048; AT5G56500.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_4_1_1; -.
DR InParanoid; C0Z361; -.
DR OMA; PRICAMA; -.
DR OrthoDB; 415781at2759; -.
DR PhylomeDB; C0Z361; -.
DR PRO; PR:C0Z361; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0Z361; baseline and differential.
DR Genevisible; C0Z361; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
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; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Chloroplast; Coiled coil; Nucleotide-binding;
KW Phosphoprotein; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..29
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 30..597
FT /note="Chaperonin 60 subunit beta 3, chloroplastic"
FT /id="PRO_0000413685"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 387..489
FT /evidence="ECO:0000255"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21238"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21240"
FT CONFLICT 545
FT /note="G -> R (in Ref. 4; BAF00280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 597 AA; 63325 MW; 3B0BDFF3AFFA5F0E CRC64;
MASTFSATSS MGSSLAPPSN RLSSFVSISS SSFGRTQSIA QRKARFPKIY AAKQLHFNKD
GTAIKKLQAG VNKLADLVGV TLGPKGRNVV LESKYGSPRI VNDGVTVARE VELEDPVENI
GAKLVRQAAS KTNDLAGDGT TTSVVLAQGL IAEGVKVVAA GANPVLITRG IEKTTKALVA
ELKKMSKEVE DSELADVAAV SAGNNYEVGN MIAEAMAKVG RKGVVTLEEG KSAENSLYVV
EGMQFDRGYI SPYFVTDSEK MCAEYENCKL FLVDKKITNA RDIISILEDA IKGGYPLLII
AEDIEQEPLA TLVVNKLRGT IKVAALKAPG FGERKSQYLD DIAALTGATV IREEVGLQLE
KVGPEVLGNA GKVVLTKDTT TIVGDGSTEE VVKKRVEQIK NLIEAAEQDY EKEKLNERIA
KLSGGVAVIQ VGAQTETELK EKKLRVEDAL NATKAAVEEG IVVGGGCTLL RLASKVDAIK
ETLANDEEKV GADIVKKALS YPLKLIAKNA GVNGSVVSEK VLSSDNPKHG YNAATGKYED
LMAAGIIDPT KVVRCCLEHA SSVAKTFLMS DCVVVEIKEP ESAAPAGNPM DNSGYGF
