CPNB4_ARATH
ID CPNB4_ARATH Reviewed; 611 AA.
AC Q9C667; F4IE47; Q56XN6;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Chaperonin 60 subunit beta 4, chloroplastic;
DE Short=CPN-60 beta 4;
DE Flags: Precursor;
GN Name=CPN60B4; Synonyms=Cpn60-B(4); OrderedLocusNames=At1g26230;
GN ORFNames=F28B23.11;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, 3D-STRUCTURE MODELING, 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 specifically in the folding of NDHH, a subunit of
CC the chloroplast NADH dehydrogenase-like complex (NDH).
CC {ECO:0000269|PubMed:19224397, ECO:0000269|PubMed:21483722,
CC ECO:0000269|Ref.5}.
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 NDHH. {ECO:0000269|PubMed:19224397,
CC ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:21483722}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C667-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C667-2; Sequence=VSP_041957;
CC -!- INDUCTION: Up-regulated by light. {ECO:0000269|PubMed:12231961}.
CC -!- DOMAIN: The C-terminus (568-611) is required for efficient NDHH
CC folding, but not for the formation of the chaperonin complex.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype besides impaired NDH
CC activity. {ECO:0000269|PubMed:21483722}.
CC -!- MISCELLANEOUS: CPN60B1, CPN60B2 or CPN60B3 cannot complement the
CC function of CPN60B4.
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; AC079829; AAG50688.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30663.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59894.1; -; Genomic_DNA.
DR EMBL; AK221637; BAD95277.1; -; mRNA.
DR PIR; E86388; E86388.
DR RefSeq; NP_001185097.1; NM_001198168.2. [Q9C667-2]
DR RefSeq; NP_173947.1; NM_102387.3. [Q9C667-1]
DR AlphaFoldDB; Q9C667; -.
DR SMR; Q9C667; -.
DR BioGRID; 24401; 1.
DR STRING; 3702.AT1G26230.1; -.
DR PaxDb; Q9C667; -.
DR PRIDE; Q9C667; -.
DR EnsemblPlants; AT1G26230.1; AT1G26230.1; AT1G26230. [Q9C667-1]
DR EnsemblPlants; AT1G26230.4; AT1G26230.4; AT1G26230. [Q9C667-2]
DR GeneID; 839164; -.
DR Gramene; AT1G26230.1; AT1G26230.1; AT1G26230. [Q9C667-1]
DR Gramene; AT1G26230.4; AT1G26230.4; AT1G26230. [Q9C667-2]
DR KEGG; ath:AT1G26230; -.
DR Araport; AT1G26230; -.
DR TAIR; locus:2028751; AT1G26230.
DR eggNOG; KOG0356; Eukaryota.
DR InParanoid; Q9C667; -.
DR OMA; SAEFTDC; -.
DR PhylomeDB; Q9C667; -.
DR PRO; PR:Q9C667; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C667; baseline and differential.
DR Genevisible; Q9C667; AT.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IMP:TAIR.
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 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.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chaperone; Chloroplast; Coiled coil;
KW Nucleotide-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 38..611
FT /note="Chaperonin 60 subunit beta 4, chloroplastic"
FT /id="PRO_0000413686"
FT REGION 574..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 377..480
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..56
FT /note="MAFSQAALSALPLSDRTFRKKPSSSSSSSPNFVLRVRAAAKEVHFNRDGSVT
FT KKLQ -> MVVK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041957"
FT CONFLICT 394
FT /note="T -> N (in Ref. 3; BAD95277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 66796 MW; D7CA90E3F5632CBE CRC64;
MAFSQAALSA LPLSDRTFRK KPSSSSSSSP NFVLRVRAAA KEVHFNRDGS VTKKLQAGAD
MVAKLLGVTL GPKGRNVVLQ NKYGPPRIVN DGETVLKEIE LEDPLENVGV KLVRQAGAKT
NDLAGDGSTT SIILAHGLIT EGIKVISAGT NPIQVARGIE KTTKALVLEL KSMSREIEDH
ELAHVAAVSA GNDYEVGNMI SNAFQQVGRT GVVTIEKGKY LVNNLEIVEG MQFNRGYLSP
YFVTDRRKRE AEFHDCKLLL VDKKITNPKD MFKILDSAVK EEFPVLIVAE DIEQDALAPV
IRNKLKGNLK VAAIKAPAFG ERKSHCLDDL AIFTGATVIR DEMGLSLEKA GKEVLGTAKR
VLVTKDSTLI VTNGFTQKAV DERVSQIKNL IENTEENFQK KILNERVARL SGGIAIIQVG
ALTQVELKDK QLKVEDALNA TKSAIEEGIV VGGGCALLRL ATKVDRIKET LDNTEQKIGA
EIFKKALSYP IRLIAKNADT NGNIVIEKVL SNKNTMYGYN AAKNQYEDLM LAGIIDPTKV
VRCCLEHASS VAQTFLTSDC VVVEIKEIKP RPIINPPLPT SSPATSSMFP DRKLPRFPQI
MPRTRSHFPR K
