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Chloroplast stem-loop binding protein of 41 kDa a, chloroplastic (CSP41-a)

 CP41A_ARATH             Reviewed;         406 AA.
Q9LYA9;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 110.
RecName: Full=Chloroplast stem-loop binding protein of 41 kDa a, chloroplastic;
Short=CSP41-a;
Flags: Precursor;
Name=CSP41A; OrderedLocusNames=At3g63140; ORFNames=T20O10.240;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=16461379; DOI=10.1104/pp.105.076083;
Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
"Protein profiling of plastoglobules in chloroplasts and chromoplasts.
A surprising site for differential accumulation of metabolic
enzymes.";
Plant Physiol. 140:984-997(2006).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=18398686; DOI=10.1007/s11103-008-9328-2;
Beligni M.V., Mayfield S.P.;
"Arabidopsis thaliana mutants reveal a role for CSP41a and CSP41b, two
ribosome-associated endonucleases, in chloroplast ribosomal RNA
metabolism.";
Plant Mol. Biol. 67:389-401(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=18431481; DOI=10.1371/journal.pone.0001994;
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,
Sun Q., van Wijk K.J.;
"Sorting signals, N-terminal modifications and abundance of the
chloroplast proteome.";
PLoS ONE 3:E1994-E1994(2008).
[7]
FUNCTION, AND SUBUNIT.
STRAIN=cv. Columbia;
PubMed=19067181; DOI=10.1007/s11103-008-9436-z;
Bollenbach T.J., Sharwood R.E., Gutierrez R., Lerbs-Mache S.,
Stern D.B.;
"The RNA-binding proteins CSP41a and CSP41b may regulate transcription
and translation of chloroplast-encoded RNAs in Arabidopsis.";
Plant Mol. Biol. 69:541-552(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
-!- FUNCTION: Binds and cleaves RNA, particularly in stem-loops.
Associates with pre-ribosomal particles in chloroplasts, and
participates in chloroplast ribosomal RNA metabolism, probably
during the final steps of 23S rRNA maturation. May enhance
transcription by the plastid-encoded polymerase and translation in
plastid via the stabilization of ribosome assembly intermediates.
Required for chloroplast integrity. Involved in the regulation of
the circadian system. {ECO:0000269|PubMed:18398686,
ECO:0000269|PubMed:19067181}.
-!- SUBUNIT: Component of a complex made of CSP41A, CSP41B, ribosomes,
and the plastid-encoded RNA polymerase. Interacts with CSP41B.
{ECO:0000269|PubMed:19067181}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
{ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:18431481}.
Note=Present in stromules. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Lethal when associated with CSP41B
disruption. {ECO:0000269|PubMed:18398686}.
-!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
family. {ECO:0000305}.
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EMBL; AL163816; CAB87759.1; -; Genomic_DNA.
EMBL; CP002686; AEE80440.1; -; Genomic_DNA.
EMBL; AF428269; AAL16101.1; -; mRNA.
EMBL; AY059887; AAL24369.1; -; mRNA.
EMBL; AY128804; AAM91204.1; -; mRNA.
PIR; T48103; T48103.
RefSeq; NP_191873.1; NM_116179.5.
UniGene; At.48804; -.
UniGene; At.5159; -.
ProteinModelPortal; Q9LYA9; -.
BioGrid; 10803; 2.
STRING; 3702.AT3G63140.1; -.
iPTMnet; Q9LYA9; -.
PaxDb; Q9LYA9; -.
PRIDE; Q9LYA9; -.
EnsemblPlants; AT3G63140.1; AT3G63140.1; AT3G63140.
GeneID; 825489; -.
Gramene; AT3G63140.1; AT3G63140.1; AT3G63140.
KEGG; ath:AT3G63140; -.
Araport; AT3G63140; -.
TAIR; locus:2099222; AT3G63140.
eggNOG; ENOG410IEM4; Eukaryota.
eggNOG; ENOG410ZXC4; LUCA.
HOGENOM; HOG000232785; -.
InParanoid; Q9LYA9; -.
OMA; FRPQYIY; -.
OrthoDB; EOG09360F9Y; -.
PhylomeDB; Q9LYA9; -.
PRO; PR:Q9LYA9; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LYA9; baseline and differential.
Genevisible; Q9LYA9; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
GO; GO:0010287; C:plastoglobule; IDA:TAIR.
GO; GO:0005840; C:ribosome; ISS:UniProtKB.
GO; GO:0010319; C:stromule; ISS:UniProtKB.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0003824; F:catalytic activity; IEA:InterPro.
GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
GO; GO:0008266; F:poly(U) RNA binding; IDA:TAIR.
GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
GO; GO:0009658; P:chloroplast organization; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
GO; GO:0032544; P:plastid translation; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0006364; P:rRNA processing; IGI:TAIR.
InterPro; IPR001509; Epimerase_deHydtase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF01370; Epimerase; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Chloroplast; Complete proteome; Phosphoprotein; Plastid;
Reference proteome; RNA-binding; rRNA processing; rRNA-binding;
Transit peptide.
TRANSIT 1 72 Chloroplast. {ECO:0000255}.
CHAIN 73 406 Chloroplast stem-loop binding protein of
41 kDa a, chloroplastic.
/FTId=PRO_0000286531.
COMPBIAS 316 319 Poly-Ala.
MOD_RES 266 266 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
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


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