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Chloroplast stem-loop binding protein of 41 kDa b, chloroplastic (CSP41-b) (Heteroglycan-interacting protein 1.3) (Protein CHLOROPLAST RNA BINDING) (Protein Gb5f)

 CP41B_ARATH             Reviewed;         378 AA.
Q9SA52; O49260; Q8LAU2; Q8W4G5; Q9T0N9;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-MAR-2018, entry version 119.
RecName: Full=Chloroplast stem-loop binding protein of 41 kDa b, chloroplastic;
Short=CSP41-b;
AltName: Full=Heteroglycan-interacting protein 1.3;
AltName: Full=Protein CHLOROPLAST RNA BINDING;
AltName: Full=Protein Gb5f;
Flags: Precursor;
Name=CSP41B; Synonyms=CRB, HIP1.3; OrderedLocusNames=At1g09340;
ORFNames=T31J12.6;
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 [MRNA].
Koncz C., Nuotio S., Eckstein L.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Fulgosi H., Alcaraz J.-P., Herrmann R., Lerbs-Mache S.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
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).
[8]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR
LOCATION, AND INDUCTION.
STRAIN=cv. Columbia;
PubMed=16633814; DOI=10.1007/s00425-006-0282-4;
Raab S., Toth Z., de Groot C., Stamminger T., Hoth S.;
"ABA-responsive RNA-binding proteins are involved in chloroplast and
stromule function in Arabidopsis seedlings.";
Planta 224:900-914(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=17617174; DOI=10.1111/j.1365-313X.2007.03160.x;
Hassidim M., Yakir E., Fradkin D., Hilman D., Kron I., Keren N.,
Harir Y., Yerushalmi S., Green R.M.;
"Mutations in CHLOROPLAST RNA BINDING provide evidence for the
involvement of the chloroplast in the regulation of the circadian
clock in Arabidopsis.";
Plant J. 51:551-562(2007).
[11]
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).
[12]
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).
[13]
FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
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).
[14]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
STRAIN=cv. Columbia;
PubMed=21087810; DOI=10.1016/j.jplph.2010.09.008;
Fettke J., Nunes-Nesi A., Fernie A.R., Steup M.;
"Identification of a novel heteroglycan-interacting protein, HIP 1.3,
from Arabidopsis thaliana.";
J. Plant Physiol. 168:1415-1425(2011).
[15]
FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH PRIN2.
STRAIN=cv. Columbia;
PubMed=25161659; DOI=10.3389/fpls.2014.00385;
Kremnev D., Strand A.;
"Plastid encoded RNA polymerase activity and expression of
photosynthesis genes required for embryo and seed development in
Arabidopsis.";
Front. Plant Sci. 5:385-385(2014).
-!- 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. Involved in the regulation of heteroglycans
and monosaccharide mobilization. Required for full expression of
genes transcribed by the plastid-encoded RNA polymerase (PEP).
Essential for embryo development (PubMed:25161659).
{ECO:0000269|PubMed:16633814, ECO:0000269|PubMed:17617174,
ECO:0000269|PubMed:18398686, ECO:0000269|PubMed:19067181,
ECO:0000269|PubMed:21087810, ECO:0000269|PubMed:25161659}.
-!- SUBUNIT: Component of a complex made of CSP41A, CSP41B, ribosomes,
and the plastid-encoded RNA polymerase. Interacts with CSP41A.
Binds DNA when in complex with PRIN2 (PubMed:25161659).
{ECO:0000269|PubMed:19067181, ECO:0000269|PubMed:25161659}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
{ECO:0000269|PubMed:16461379}. Plastid, chloroplast
{ECO:0000269|PubMed:18431481}. Cytoplasm. Note=Present in
stromules (PubMed:16633814). In the cytoplasm, accumulates around
chloroplasts (PubMed:21087810). {ECO:0000269|PubMed:16633814,
ECO:0000269|PubMed:21087810}.
-!- TISSUE SPECIFICITY: Highly expressed in seedlings, particularly in
photosynthetically active organs. Mostly expressed in young and
mature leaves, and, to a lower extent, in flowers. Low expression
in etiolated seedlings compared to green seedlings.
{ECO:0000269|PubMed:16633814, ECO:0000269|PubMed:21087810}.
-!- DEVELOPMENTAL STAGE: In young seedlings, expressed in hypocotyls
and cotyledons. In older seedlings, limited to the outer epidermal
cell layer of leaves and petioles (including guard cells). Present
in trichomes and hydathodes. In flowers, detected in sepals and
siliques. {ECO:0000269|PubMed:16633814}.
-!- INDUCTION: Expressed with a circadian rhythm showing a peak during
the end of the day (under long day conditions). Repressed during
senescence and upon water stress. Accumulates at wounding sites.
Altered expression of both oscillator and output genes.
{ECO:0000269|PubMed:16633814}.
-!- DISRUPTION PHENOTYPE: Small and pale plants, with altered
chloroplast morphology (anarchic membrane organization) and
reduced photosynthetic performance associated with a reduction in
CSP41A levels. Altered monosaccharide pattern of heteroglycans.
Lethal when associated with CSP41A disruption. Reduced transcript
levels of photosynthesis genes. Defects in embryo development. The
csp41b-2 prin2-2 double mutant is embryo lethal (PubMed:25161659).
{ECO:0000269|PubMed:17617174, ECO:0000269|PubMed:18398686,
ECO:0000269|PubMed:19067181, ECO:0000269|PubMed:21087810,
ECO:0000269|PubMed:25161659}.
-!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y10557; CAA71589.1; -; mRNA.
EMBL; Y15382; CAA75602.1; -; mRNA.
EMBL; AC006416; AAD18098.1; -; Genomic_DNA.
EMBL; CP002684; AEE28431.1; -; Genomic_DNA.
EMBL; AY070022; AAL47493.1; -; mRNA.
EMBL; AF428282; AAL16114.1; -; mRNA.
EMBL; AY035050; AAK59555.1; -; mRNA.
EMBL; AF325043; AAG40395.1; -; mRNA.
EMBL; AY062570; AAL32648.1; -; mRNA.
EMBL; AY087609; AAM65150.1; -; mRNA.
PIR; E86226; E86226.
PIR; T51863; T51863.
PIR; T52072; T52072.
RefSeq; NP_172405.1; NM_100804.4.
UniGene; At.21708; -.
UniGene; At.50307; -.
ProteinModelPortal; Q9SA52; -.
SMR; Q9SA52; -.
BioGrid; 22696; 8.
STRING; 3702.AT1G09340.1; -.
iPTMnet; Q9SA52; -.
PaxDb; Q9SA52; -.
PRIDE; Q9SA52; -.
EnsemblPlants; AT1G09340.1; AT1G09340.1; AT1G09340.
GeneID; 837455; -.
Gramene; AT1G09340.1; AT1G09340.1; AT1G09340.
KEGG; ath:AT1G09340; -.
Araport; AT1G09340; -.
TAIR; locus:2203028; AT1G09340.
eggNOG; ENOG410IKAZ; Eukaryota.
eggNOG; ENOG410XQQI; LUCA.
HOGENOM; HOG000232785; -.
InParanoid; Q9SA52; -.
OMA; FDNNGRE; -.
OrthoDB; EOG09360CDH; -.
PhylomeDB; Q9SA52; -.
PRO; PR:Q9SA52; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9SA52; baseline and differential.
Genevisible; Q9SA52; 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:0016020; C:membrane; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0000427; C:plastid-encoded plastid RNA polymerase complex; IMP:UniProtKB.
GO; GO:0010287; C:plastoglobule; IDA:TAIR.
GO; GO:0005840; C:ribosome; IDA:TAIR.
GO; GO:0010319; C:stromule; IDA:UniProtKB.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0003824; F:catalytic activity; IEA:InterPro.
GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0010297; F:heteropolysaccharide binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
GO; GO:0042631; P:cellular response to water deprivation; IEP:UniProtKB.
GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
GO; GO:0007623; P:circadian rhythm; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0005996; P:monosaccharide metabolic process; IMP:UniProtKB.
GO; GO:0032544; P:plastid translation; IMP:UniProtKB.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
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;
Carbohydrate metabolism; Chloroplast; Complete proteome; Cytoplasm;
DNA-binding; Phosphoprotein; Plastid; Polysaccharide degradation;
Reference proteome; RNA-binding; rRNA processing; rRNA-binding;
Transit peptide.
TRANSIT 1 50 Chloroplast. {ECO:0000305}.
CHAIN 51 378 Chloroplast stem-loop binding protein of
41 kDa b, chloroplastic.
/FTId=PRO_0000286529.
MOD_RES 240 240 Phosphoserine.
{ECO:0000250|UniProtKB:Q9LYA9}.
CONFLICT 1 4 Missing (in Ref. 2; CAA75602).
{ECO:0000305}.
CONFLICT 170 170 S -> F (in Ref. 1; CAA71589).
{ECO:0000305}.
CONFLICT 223 223 E -> K (in Ref. 5; AAL32648).
{ECO:0000305}.
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


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