CPNB1_ARATH
ID CPNB1_ARATH Reviewed; 600 AA.
AC P21240; B9DFS9; B9DHQ8; Q9SAV2;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Chaperonin 60 subunit beta 1, chloroplastic;
DE Short=CPN-60 beta 1;
DE AltName: Full=60 kDa chaperonin subunit beta 1;
DE AltName: Full=RuBisCO large subunit-binding protein subunit beta, chloroplastic;
DE Flags: Precursor;
GN Name=CPN60B1; Synonyms=Cpn60-B(3), LEN1; OrderedLocusNames=At1g55490;
GN ORFNames=T5A14.11;
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 / MRNA].
RX PubMed=1347275; DOI=10.1016/0378-1119(92)90685-i;
RA Zabaleta E., Oropeza A., Jimenez B., Salerno G., Crespi M.,
RA Herrera-Estrella L.;
RT "Isolation and characterization of genes encoding chaperonin 60 beta from
RT Arabidopsis thaliana.";
RL Gene 111:175-181(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 127-312.
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 FUNCTION, PROTEIN SEQUENCE OF 55-68, AND INTERACTION WITH RAB.
RX PubMed=18353762; DOI=10.1093/jxb/erm343;
RA Salvucci M.E.;
RT "Association of Rubisco activase with chaperonin-60beta: a possible
RT mechanism for protecting photosynthesis during heat stress.";
RL J. Exp. Bot. 59:1923-1933(2008).
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 TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING AND HEAT.
RX PubMed=7906560; DOI=10.1007/bf00040585;
RA Zabaleta E., Assad N., Oropeza A., Salerno G., Herrera-Estrella L.;
RT "Expression of one of the members of the Arabidopsis chaperonin 60 beta
RT gene family is developmentally regulated and wound-repressible.";
RL Plant Mol. Biol. 24:195-202(1994).
RN [10]
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 [11]
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 [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12668771; DOI=10.1093/pcp/pcg031;
RA Ishikawa A., Tanaka H., Nakai M., Asahi T.;
RT "Deletion of a chaperonin 60 beta gene leads to cell death in the
RT Arabidopsis lesion initiation 1 mutant.";
RL Plant Cell Physiol. 44:255-261(2003).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, 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 [16]
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: 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 plastid division.
CC {ECO:0000269|PubMed:12668771, ECO:0000269|PubMed:18353762,
CC ECO:0000269|PubMed:19224397, ECO:0000269|PubMed:19344532,
CC ECO:0000269|Ref.10}.
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. Interacts with RAB during heat stress.
CC {ECO:0000269|PubMed:18353762, ECO:0000269|PubMed:19224397,
CC ECO:0000269|Ref.10}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19344532}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, petioles and flowers.
CC {ECO:0000269|PubMed:7906560}.
CC -!- INDUCTION: Up-regulated by light. Down-regulated by wounding. Not
CC induced by heat. {ECO:0000269|PubMed:12231961,
CC ECO:0000269|PubMed:7906560}.
CC -!- DISRUPTION PHENOTYPE: Normal germination, but chloroplast-division
CC defect and late dwarf phenotype. Lesion formation on leaves when grown
CC under short-day conditions. Cpn60B1 and cpn60B2 double mutant produces
CC small albino seedlings. {ECO:0000269|PubMed:12668771,
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; AC005223; AAD10647.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33251.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33252.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58183.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58184.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58185.1; -; Genomic_DNA.
DR EMBL; AF386945; AAK62390.1; -; mRNA.
DR EMBL; AY081501; AAM10063.1; -; mRNA.
DR EMBL; AK316889; BAH19596.1; -; mRNA.
DR EMBL; AK317612; BAH20275.1; -; mRNA.
DR EMBL; M35598; AAA32725.1; -; mRNA.
DR PIR; B96597; B96597.
DR PIR; JT0901; JT0901.
DR PIR; PW0008; PW0008.
DR RefSeq; NP_001320637.1; NM_001333712.1.
DR RefSeq; NP_001320638.1; NM_001333711.1.
DR RefSeq; NP_001320639.1; NM_001333710.1.
DR RefSeq; NP_175945.1; NM_104424.2.
DR RefSeq; NP_849811.1; NM_179480.3.
DR AlphaFoldDB; P21240; -.
DR SMR; P21240; -.
DR BioGRID; 27221; 35.
DR IntAct; P21240; 3.
DR MINT; P21240; -.
DR STRING; 3702.AT1G55490.2; -.
DR iPTMnet; P21240; -.
DR MetOSite; P21240; -.
DR PaxDb; P21240; -.
DR PRIDE; P21240; -.
DR ProteomicsDB; 224487; -.
DR EnsemblPlants; AT1G55490.1; AT1G55490.1; AT1G55490.
DR EnsemblPlants; AT1G55490.2; AT1G55490.2; AT1G55490.
DR EnsemblPlants; AT1G55490.3; AT1G55490.3; AT1G55490.
DR EnsemblPlants; AT1G55490.4; AT1G55490.4; AT1G55490.
DR EnsemblPlants; AT1G55490.5; AT1G55490.5; AT1G55490.
DR GeneID; 841996; -.
DR Gramene; AT1G55490.1; AT1G55490.1; AT1G55490.
DR Gramene; AT1G55490.2; AT1G55490.2; AT1G55490.
DR Gramene; AT1G55490.3; AT1G55490.3; AT1G55490.
DR Gramene; AT1G55490.4; AT1G55490.4; AT1G55490.
DR Gramene; AT1G55490.5; AT1G55490.5; AT1G55490.
DR KEGG; ath:AT1G55490; -.
DR Araport; AT1G55490; -.
DR TAIR; locus:2193839; AT1G55490.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_4_1_1; -.
DR InParanoid; P21240; -.
DR OMA; TGAQLMR; -.
DR OrthoDB; 415781at2759; -.
DR PhylomeDB; P21240; -.
DR PRO; PR:P21240; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P21240; baseline and differential.
DR Genevisible; P21240; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA: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:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA: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:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; 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; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Chloroplast; Direct protein sequencing;
KW Nucleotide-binding; Phosphoprotein; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:18353762"
FT CHAIN 55..600
FT /note="Chaperonin 60 subunit beta 1, chloroplastic"
FT /id="PRO_0000005022"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21238"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 242
FT /note="Y -> H (in Ref. 2; AAA32725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 63809 MW; 78B10E9B2EE19859 CRC64;
MASTFTATSS IGSMVAPNGH KSDKKLISKL SSSSFGRRQS VCPRPRRSSS AIVCAAKELH
FNKDGTTIRR LQAGVNKLAD LVGVTLGPKG RNVVLESKYG SPRIVNDGVT VAREVELEDP
VENIGAKLVR QAAAKTNDLA GDGTTTSVVL AQGFIAEGVK VVAAGANPVL ITRGIEKTAK
ALVTELKKMS KEVEDSELAD VAAVSAGNND EIGNMIAEAM SKVGRKGVVT LEEGKSAENN
LYVVEGMQFD RGYISPYFVT DSEKMSVEFD NCKLLLVDKK ITNARDLVGV LEDAIRGGYP
ILIIAEDIEQ EALATLVVNK LRGTLKIAAL RAPGFGERKS QYLDDIAILT GATVIREEVG
LSLDKAGKEV LGNASKVVLT KETSTIVGDG STQDAVKKRV TQIKNLIEQA EQDYEKEKLN
ERIAKLSGGV AVIQVGAQTE TELKEKKLRV EDALNATKAA VEEGIVVGGG CTLLRLASKV
DAIKATLDND EEKVGADIVK RALSYPLKLI AKNAGVNGSV VSEKVLSNDN VKFGYNAATG
KYEDLMAAGI IDPTKVVRCC LEHAASVAKT FLMSDCVVVE IKEPEPVPVG NPMDNSGYGY
