CP41A_ARATH
ID CP41A_ARATH Reviewed; 406 AA.
AC Q9LYA9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Chloroplast stem-loop binding protein of 41 kDa a, chloroplastic;
DE Short=CSP41-a;
DE Flags: Precursor;
GN Name=CSP41A; OrderedLocusNames=At3g63140; ORFNames=T20O10.240;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=16461379; DOI=10.1104/pp.105.076083;
RA Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT surprising site for differential accumulation of metabolic enzymes.";
RL Plant Physiol. 140:984-997(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18398686; DOI=10.1007/s11103-008-9328-2;
RA Beligni M.V., Mayfield S.P.;
RT "Arabidopsis thaliana mutants reveal a role for CSP41a and CSP41b, two
RT ribosome-associated endonucleases, in chloroplast ribosomal RNA
RT metabolism.";
RL Plant Mol. Biol. 67:389-401(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [7]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=19067181; DOI=10.1007/s11103-008-9436-z;
RA Bollenbach T.J., Sharwood R.E., Gutierrez R., Lerbs-Mache S., Stern D.B.;
RT "The RNA-binding proteins CSP41a and CSP41b may regulate transcription and
RT translation of chloroplast-encoded RNAs in Arabidopsis.";
RL Plant Mol. Biol. 69:541-552(2009).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
CC -!- FUNCTION: Binds and cleaves RNA, particularly in stem-loops. Associates
CC with pre-ribosomal particles in chloroplasts, and participates in
CC chloroplast ribosomal RNA metabolism, probably during the final steps
CC of 23S rRNA maturation. May enhance transcription by the plastid-
CC encoded polymerase and translation in plastid via the stabilization of
CC ribosome assembly intermediates. Required for chloroplast integrity.
CC Involved in the regulation of the circadian system.
CC {ECO:0000269|PubMed:18398686, ECO:0000269|PubMed:19067181}.
CC -!- SUBUNIT: Component of a complex made of CSP41A, CSP41B, ribosomes, and
CC the plastid-encoded RNA polymerase. Interacts with CSP41B.
CC {ECO:0000269|PubMed:19067181}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:18431481}.
CC Note=Present in stromules. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Lethal when associated with CSP41B disruption.
CC {ECO:0000269|PubMed:18398686}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AL163816; CAB87759.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80440.1; -; Genomic_DNA.
DR EMBL; AF428269; AAL16101.1; -; mRNA.
DR EMBL; AY059887; AAL24369.1; -; mRNA.
DR EMBL; AY128804; AAM91204.1; -; mRNA.
DR PIR; T48103; T48103.
DR RefSeq; NP_191873.1; NM_116179.5.
DR AlphaFoldDB; Q9LYA9; -.
DR SMR; Q9LYA9; -.
DR BioGRID; 10803; 3.
DR STRING; 3702.AT3G63140.1; -.
DR iPTMnet; Q9LYA9; -.
DR PaxDb; Q9LYA9; -.
DR PRIDE; Q9LYA9; -.
DR ProteomicsDB; 224376; -.
DR EnsemblPlants; AT3G63140.1; AT3G63140.1; AT3G63140.
DR GeneID; 825489; -.
DR Gramene; AT3G63140.1; AT3G63140.1; AT3G63140.
DR KEGG; ath:AT3G63140; -.
DR Araport; AT3G63140; -.
DR TAIR; locus:2099222; AT3G63140.
DR eggNOG; ENOG502QUUA; Eukaryota.
DR HOGENOM; CLU_050934_0_1_1; -.
DR InParanoid; Q9LYA9; -.
DR OMA; VHFYAEP; -.
DR OrthoDB; 930591at2759; -.
DR PhylomeDB; Q9LYA9; -.
DR PRO; PR:Q9LYA9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYA9; baseline and differential.
DR Genevisible; Q9LYA9; 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:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0005840; C:ribosome; ISS:UniProtKB.
DR GO; GO:0010319; C:stromule; ISS:UniProtKB.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009658; P:chloroplast organization; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
DR GO; GO:0032544; P:plastid translation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IGI:TAIR.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Phosphoprotein; Plastid; Reference proteome; RNA-binding;
KW rRNA processing; rRNA-binding; Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 73..406
FT /note="Chloroplast stem-loop binding protein of 41 kDa a,
FT chloroplastic"
FT /id="PRO_0000286531"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
SQ SEQUENCE 406 AA; 43930 MW; B8CCBAE33FDBDDC8 CRC64;
MAALSSSSLF FSSKTTSPIS NLLIPPSLHR FSLPSSSSSF SSLSSSSSSS SSLLTFSLRT
SRRLSPQKFT VKASSVGEKK NVLIVNTNSG GHAVIGFYFA KELLSAGHAV TILTVGDESS
EKMKKPPFNR FSEIVSGGGK TVWGNPANVA NVVGGETFDV VLDNNGKDLD TVRPVVDWAK
SSGVKQFLFI SSAGIYKSTE QPPHVEGDAV KADAGHVVVE KYLAETFGNW ASFRPQYMIG
SGNNKDCEEW FFDRIVRDRA VPIPGSGLQL TNISHVRDLS SMLTSAVANP EAASGNIFNC
VSDRAVTLDG MAKLCAAAAG KTVEIVHYDP KAIGVDAKKA FLFRNMHFYA EPRAAKDLLG
WESKTNLPED LKERFEEYVK IGRDKKEIKF ELDDKILEAL KTPVAA
