CP41B_ARATH
ID CP41B_ARATH Reviewed; 378 AA.
AC Q9SA52; O49260; Q8LAU2; Q8W4G5; Q9T0N9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Chloroplast stem-loop binding protein of 41 kDa b, chloroplastic;
DE Short=CSP41-b;
DE AltName: Full=Heteroglycan-interacting protein 1.3;
DE AltName: Full=Protein CHLOROPLAST RNA BINDING;
DE AltName: Full=Protein Gb5f;
DE Flags: Precursor;
GN Name=CSP41B; Synonyms=CRB, HIP1.3; OrderedLocusNames=At1g09340;
GN ORFNames=T31J12.6;
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 [MRNA].
RA Koncz C., Nuotio S., Eckstein L.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Fulgosi H., Alcaraz J.-P., Herrmann R., Lerbs-Mache S.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=16633814; DOI=10.1007/s00425-006-0282-4;
RA Raab S., Toth Z., de Groot C., Stamminger T., Hoth S.;
RT "ABA-responsive RNA-binding proteins are involved in chloroplast and
RT stromule function in Arabidopsis seedlings.";
RL Planta 224:900-914(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17617174; DOI=10.1111/j.1365-313x.2007.03160.x;
RA Hassidim M., Yakir E., Fradkin D., Hilman D., Kron I., Keren N., Harir Y.,
RA Yerushalmi S., Green R.M.;
RT "Mutations in CHLOROPLAST RNA BINDING provide evidence for the involvement
RT of the chloroplast in the regulation of the circadian clock in
RT Arabidopsis.";
RL Plant J. 51:551-562(2007).
RN [11]
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 [12]
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 [13]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
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 [14]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21087810; DOI=10.1016/j.jplph.2010.09.008;
RA Fettke J., Nunes-Nesi A., Fernie A.R., Steup M.;
RT "Identification of a novel heteroglycan-interacting protein, HIP 1.3, from
RT Arabidopsis thaliana.";
RL J. Plant Physiol. 168:1415-1425(2011).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH PRIN2.
RC STRAIN=cv. Columbia;
RX PubMed=25161659; DOI=10.3389/fpls.2014.00385;
RA Kremnev D., Strand A.;
RT "Plastid encoded RNA polymerase activity and expression of photosynthesis
RT genes required for embryo and seed development in Arabidopsis.";
RL Front. Plant Sci. 5:385-385(2014).
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. Involved in the
CC regulation of heteroglycans and monosaccharide mobilization. Required
CC for full expression of genes transcribed by the plastid-encoded RNA
CC polymerase (PEP). Essential for embryo development (PubMed:25161659).
CC {ECO:0000269|PubMed:16633814, ECO:0000269|PubMed:17617174,
CC ECO:0000269|PubMed:18398686, ECO:0000269|PubMed:19067181,
CC ECO:0000269|PubMed:21087810, ECO:0000269|PubMed:25161659}.
CC -!- SUBUNIT: Component of a complex made of CSP41A, CSP41B, ribosomes, and
CC the plastid-encoded RNA polymerase. Interacts with CSP41A. Binds DNA
CC when in complex with PRIN2 (PubMed:25161659).
CC {ECO:0000269|PubMed:19067181, ECO:0000269|PubMed:25161659}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:16461379}. Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481}. Cytoplasm. Note=Present in stromules
CC (PubMed:16633814). In the cytoplasm, accumulates around chloroplasts
CC (PubMed:21087810). {ECO:0000269|PubMed:16633814,
CC ECO:0000269|PubMed:21087810}.
CC -!- TISSUE SPECIFICITY: Highly expressed in seedlings, particularly in
CC photosynthetically active organs. Mostly expressed in young and mature
CC leaves, and, to a lower extent, in flowers. Low expression in etiolated
CC seedlings compared to green seedlings. {ECO:0000269|PubMed:16633814,
CC ECO:0000269|PubMed:21087810}.
CC -!- DEVELOPMENTAL STAGE: In young seedlings, expressed in hypocotyls and
CC cotyledons. In older seedlings, limited to the outer epidermal cell
CC layer of leaves and petioles (including guard cells). Present in
CC trichomes and hydathodes. In flowers, detected in sepals and siliques.
CC {ECO:0000269|PubMed:16633814}.
CC -!- INDUCTION: Expressed with a circadian rhythm showing a peak during the
CC end of the day (under long day conditions). Repressed during senescence
CC and upon water stress. Accumulates at wounding sites. Altered
CC expression of both oscillator and output genes.
CC {ECO:0000269|PubMed:16633814}.
CC -!- DISRUPTION PHENOTYPE: Small and pale plants, with altered chloroplast
CC morphology (anarchic membrane organization) and reduced photosynthetic
CC performance associated with a reduction in CSP41A levels. Altered
CC monosaccharide pattern of heteroglycans. Lethal when associated with
CC CSP41A disruption. Reduced transcript levels of photosynthesis genes.
CC Defects in embryo development. The csp41b-2 prin2-2 double mutant is
CC embryo lethal (PubMed:25161659). {ECO:0000269|PubMed:17617174,
CC ECO:0000269|PubMed:18398686, ECO:0000269|PubMed:19067181,
CC ECO:0000269|PubMed:21087810, ECO:0000269|PubMed:25161659}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; Y10557; CAA71589.1; -; mRNA.
DR EMBL; Y15382; CAA75602.1; -; mRNA.
DR EMBL; AC006416; AAD18098.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28431.1; -; Genomic_DNA.
DR EMBL; AY070022; AAL47493.1; -; mRNA.
DR EMBL; AF428282; AAL16114.1; -; mRNA.
DR EMBL; AY035050; AAK59555.1; -; mRNA.
DR EMBL; AF325043; AAG40395.1; -; mRNA.
DR EMBL; AY062570; AAL32648.1; -; mRNA.
DR EMBL; AY087609; AAM65150.1; -; mRNA.
DR PIR; E86226; E86226.
DR PIR; T51863; T51863.
DR PIR; T52072; T52072.
DR RefSeq; NP_172405.1; NM_100804.4.
DR AlphaFoldDB; Q9SA52; -.
DR SMR; Q9SA52; -.
DR BioGRID; 22696; 11.
DR STRING; 3702.AT1G09340.1; -.
DR iPTMnet; Q9SA52; -.
DR MetOSite; Q9SA52; -.
DR PaxDb; Q9SA52; -.
DR PRIDE; Q9SA52; -.
DR EnsemblPlants; AT1G09340.1; AT1G09340.1; AT1G09340.
DR GeneID; 837455; -.
DR Gramene; AT1G09340.1; AT1G09340.1; AT1G09340.
DR KEGG; ath:AT1G09340; -.
DR Araport; AT1G09340; -.
DR TAIR; locus:2203028; AT1G09340.
DR eggNOG; ENOG502QPZ0; Eukaryota.
DR HOGENOM; CLU_050934_0_1_1; -.
DR InParanoid; Q9SA52; -.
DR OMA; SRHKGKF; -.
DR PhylomeDB; Q9SA52; -.
DR PRO; PR:Q9SA52; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA52; baseline and differential.
DR Genevisible; Q9SA52; 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:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0000427; C:plastid-encoded plastid RNA polymerase complex; IMP:UniProtKB.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0005840; C:ribosome; IDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0010297; F:heteropolysaccharide binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IMP:TAIR.
DR GO; GO:0005996; P:monosaccharide metabolic process; IMP:UniProtKB.
DR GO; GO:0032544; P:plastid translation; IMP:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP: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 Carbohydrate metabolism; Chloroplast; Cytoplasm; DNA-binding;
KW Phosphoprotein; Plastid; Polysaccharide degradation; Reference proteome;
KW RNA-binding; rRNA processing; rRNA-binding; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 51..378
FT /note="Chloroplast stem-loop binding protein of 41 kDa b,
FT chloroplastic"
FT /id="PRO_0000286529"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LYA9"
FT CONFLICT 1..4
FT /note="Missing (in Ref. 2; CAA75602)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="S -> F (in Ref. 1; CAA71589)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="E -> K (in Ref. 5; AAL32648)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42620 MW; 9607E7B093F52518 CRC64;
MAKMMMLQQH QPSFSLLTSS LSDFNGAKLH LQVQYKRKVH QPKGALYVSA SSEKKILIMG
GTRFIGLFLS RILVKEGHQV TLFTRGKSPI AKQLPGESDQ DFADFSSKIL HLKGDRKDYD
FVKSSLSAEG FDVVYDINGR EAEEVEPILE ALPKLEQYIY CSSAGVYLKS DILPHCEEDA
VDPKSRHKGK LETESLLQSK GVNWTSIRPV YIYGPLNYNP VEEWFFHRLK AGRPIPVPNS
GIQISQLGHV KDLATAFLNV LGNEKASREI FNISGEKYVT FDGLAKACAK AGGFPEPEIV
HYNPKEFDFG KKKAFPFRDQ HFFASVEKAK HVLGWKPEFD LVEGLTDSYN LDFGRGTFRK
EADFTTDDMI LSKKLVLQ
