CLPR3_ARATH
ID CLPR3_ARATH Reviewed; 330 AA.
AC Q8L770; O04018; Q67XY5; Q680D2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit-related protein 3, chloroplastic {ECO:0000303|PubMed:11299370};
DE Short=ClpR3 {ECO:0000303|PubMed:11299370};
DE AltName: Full=nClpP8;
DE Flags: Precursor;
GN Name=CLPR3 {ECO:0000303|PubMed:11299370}; Synonyms=NCLPP8;
GN OrderedLocusNames=At1g09130 {ECO:0000312|Araport:AT1G09130};
GN ORFNames=F7G19.1 {ECO:0000312|EMBL:AAB70396.1};
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].
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 [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 PROTEIN SEQUENCE OF 174-196 AND 238-252, SUBUNIT, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=11278690; DOI=10.1074/jbc.m010503200;
RA Peltier J.-B., Ytterberg J., Liberles D.A., Roepstorff P., van Wijk K.J.;
RT "Identification of a 350-kDa ClpP protease complex with 10 different Clp
RT isoforms in chloroplasts of Arabidopsis thaliana.";
RL J. Biol. Chem. 276:16318-16327(2001).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11299370; DOI=10.1104/pp.125.4.1912;
RA Adam Z., Adamska I., Nakabayashi K., Ostersetzer O., Haussuhl K.,
RA Manuell A., Zheng B., Vallon O., Rodermel S.R., Shinozaki K., Clarke A.K.;
RT "Chloroplast and mitochondrial proteases in Arabidopsis. A proposed
RT nomenclature.";
RL Plant Physiol. 125:1912-1918(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, AND
RP 3D-STRUCTURE MODELING.
RX PubMed=14593120; DOI=10.1074/jbc.m309212200;
RA Peltier J.-B., Ripoll D.R., Friso G., Rudella A., Cai Y., Ytterberg J.,
RA Giacomelli L., Pillardy J., van Wijk K.J.;
RT "Clp protease complexes from photosynthetic and non-photosynthetic plastids
RT and mitochondria of plants, their predicted three-dimensional structures,
RT and functional implications.";
RL J. Biol. Chem. 279:4768-4781(2004).
RN [8]
RP NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX DOI=10.1111/j.1399-3054.2005.00452.x;
RA Clarke A.K., MacDonald T.M., Sjoegren L.L.;
RT "The ATP-dependent Clp protease in chloroplasts of higher plants.";
RL Physiol. Plantarum 123:406-412(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=16766689; DOI=10.1105/tpc.106.042861;
RA Rudella A., Friso G., Alonso J.M., Ecker J.R., van Wijk K.J.;
RT "Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS
RT protease complex and defects in chloroplast biogenesis in Arabidopsis.";
RL Plant Cell 18:1704-1721(2006).
RN [10]
RP SUBUNIT.
RX PubMed=16980539; DOI=10.1105/tpc.106.044594;
RA Sjoegren L.L.E., Stanne T.M., Zheng B., Sutinen S., Clarke A.K.;
RT "Structural and functional insights into the chloroplast ATP-dependent Clp
RT protease in Arabidopsis.";
RL Plant Cell 18:2635-2649(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=21712416; DOI=10.1105/tpc.111.086454;
RA Olinares P.D., Kim J., Davis J.I., van Wijk K.J.;
RT "Subunit stoichiometry, evolution, and functional implications of an
RT asymmetric plant plastid ClpP/R protease complex in Arabidopsis.";
RL Plant Cell 23:2348-2361(2011).
RN [12]
RP REVIEW.
RX PubMed=22085372; DOI=10.1111/j.1399-3054.2011.01541.x;
RA Clarke A.K.;
RT "The chloroplast ATP-dependent Clp protease in vascular plants - new
RT dimensions and future challenges.";
RL Physiol. Plantarum 145:235-244(2012).
CC -!- SUBUNIT: Component of the chloroplastic Clp protease core complex which
CC consist of at least 16 proteins: CLPP4 (3 copies), CLPP5 (3 copies),
CC CLPR4 (2 copies), ClpP1 (1 copy), CLPP6 (1 copy), CLPR2 (1 copy), CLPT1
CC (1 copy), CLPT2 (1 copy) and 3 copies of CLPP3 and/or CLPR1 and/or
CC CLPR3 (PubMed:11278690, PubMed:14593120, PubMed:16766689,
CC PubMed:16980539). The core complex is organized in two heptameric
CC rings, one containing CLPP3,4,5,6 in a 1:2:3:1 ratio and the other
CC CLPP1 and CLPR1,2,3,4 in a 3:1:1:1:1 ratio (PubMed:21712416).
CC {ECO:0000269|PubMed:11278690, ECO:0000269|PubMed:14593120,
CC ECO:0000269|PubMed:16766689, ECO:0000269|PubMed:16980539,
CC ECO:0000269|PubMed:21712416}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:14593120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8L770-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Embryo lethal. {ECO:0000303|Ref.8}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70396.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC000106; AAB70396.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28397.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28398.1; -; Genomic_DNA.
DR EMBL; AY136442; AAM97107.1; -; mRNA.
DR EMBL; BT002132; AAN72143.1; -; mRNA.
DR EMBL; AK175123; BAD42886.1; -; mRNA.
DR EMBL; AK175317; BAD43080.1; -; mRNA.
DR EMBL; AK175337; BAD43100.1; -; mRNA.
DR EMBL; AK175767; BAD43530.1; -; mRNA.
DR EMBL; AK175857; BAD43620.1; -; mRNA.
DR EMBL; AK175858; BAD43621.1; -; mRNA.
DR EMBL; AK175935; BAD43698.1; -; mRNA.
DR EMBL; AK176445; BAD44208.1; -; mRNA.
DR EMBL; AK176591; BAD44354.1; -; mRNA.
DR EMBL; AK176592; BAD44355.1; -; mRNA.
DR EMBL; AK176683; BAD44446.1; -; mRNA.
DR EMBL; AK176714; BAD44477.1; -; mRNA.
DR EMBL; AK176771; BAD44534.1; -; mRNA.
DR EMBL; AK227271; BAE99296.1; -; mRNA.
DR PIR; D86223; D86223.
DR RefSeq; NP_001031008.1; NM_001035931.2. [Q8L770-1]
DR RefSeq; NP_563836.1; NM_100782.5. [Q8L770-1]
DR AlphaFoldDB; Q8L770; -.
DR SMR; Q8L770; -.
DR BioGRID; 22673; 10.
DR IntAct; Q8L770; 1.
DR STRING; 3702.AT1G09130.3; -.
DR iPTMnet; Q8L770; -.
DR PaxDb; Q8L770; -.
DR PRIDE; Q8L770; -.
DR EnsemblPlants; AT1G09130.1; AT1G09130.1; AT1G09130. [Q8L770-1]
DR EnsemblPlants; AT1G09130.2; AT1G09130.2; AT1G09130. [Q8L770-1]
DR GeneID; 837432; -.
DR Gramene; AT1G09130.1; AT1G09130.1; AT1G09130. [Q8L770-1]
DR Gramene; AT1G09130.2; AT1G09130.2; AT1G09130. [Q8L770-1]
DR KEGG; ath:AT1G09130; -.
DR Araport; AT1G09130; -.
DR eggNOG; KOG0840; Eukaryota.
DR HOGENOM; CLU_058707_5_0_1; -.
DR InParanoid; Q8L770; -.
DR OMA; FCSINAK; -.
DR PhylomeDB; Q8L770; -.
DR PRO; PR:Q8L770; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L770; baseline and differential.
DR Genevisible; Q8L770; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR GO; GO:0009532; C:plastid stroma; IEA:UniProt.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR CDD; cd07017; S14_ClpP_2; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR023562; ClpP/TepA.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..330
FT /note="ATP-dependent Clp protease proteolytic subunit-
FT related protein 3, chloroplastic"
FT /id="PRO_0000308984"
FT REGION 7..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 235
FT /note="Q -> R (in Ref. 4; BAD44446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 36307 MW; 363C4ECE368523D6 CRC64;
MASCLQASMN SLLPRSSSFS PHPPLSSNSS GRRNLKTFRY AFRAKASAKI PMPPINPKDP
FLSTLASIAA NSPEKLLNRP VNADVPPYLD IFDSPQLMSS PAQVERSVAY NEHRPRTPPP
DLPSMLLDGR IVYIGMPLVP AVTELVVAEL MYLQWLDPKE PIYIYINSTG TTRDDGETVG
MESEGFAIYD SLMQLKNEVH TVCVGAAIGQ ACLLLSAGTK GKRFMMPHAK AMIQQPRVPS
SGLMPASDVL IRAKEVITNR DILVELLSKH TGNSVETVAN VMRRPYYMDA PKAKEFGVID
RILWRGQEKI IADVVPSEEF DKNAGIKSVV
