RRP41_ARATH
ID RRP41_ARATH Reviewed; 241 AA.
AC Q9SP08;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Exosome complex component RRP41 homolog {ECO:0000305};
DE AltName: Full=Ribosomal RNA-processing protein 41 {ECO:0000305};
DE Short=AtRRP41 {ECO:0000303|PubMed:10930416};
DE Short=AtRrp41p {ECO:0000303|PubMed:10930416};
GN Name=RRP41 {ECO:0000305};
GN OrderedLocusNames=At3g61620 {ECO:0000312|Araport:AT3G61620};
GN ORFNames=F15G16.10 {ECO:0000312|EMBL:CAB71092.1};
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 [MRNA], FUNCTION, AND SUBUNIT.
RC STRAIN=cv. Columbia; TISSUE=Immature flower {ECO:0000312|EMBL:AAF04590.1};
RX PubMed=10930416; DOI=10.1074/jbc.m005493200;
RA Chekanova J.A., Shaw R.J., Wills M.A., Belostotsky D.A.;
RT "Poly(A) tail-dependent exonuclease AtRrp41p from Arabidopsis thaliana
RT rescues 5.8 S rRNA processing and mRNA decay defects of the yeast ski6
RT mutant and is found in an exosome-sized complex in plant and yeast cells.";
RL J. Biol. Chem. 275:33158-33166(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 INTERACTION WITH RPP4.
RX PubMed=11809881; DOI=10.1093/nar/30.3.695;
RA Chekanova J.A., Dutko J.A., Mian I.S., Belostotsky D.A.;
RT "Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3'-->5'
RT exonuclease containing S1 and KH RNA-binding domains.";
RL Nucleic Acids Res. 30:695-700(2002).
RN [7]
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=18160042; DOI=10.1016/j.cell.2007.10.056;
RA Chekanova J.A., Gregory B.D., Reverdatto S.V., Chen H., Kumar R.,
RA Hooker T., Yazaki J., Li P., Skiba N., Peng Q., Alonso J., Brukhin V.,
RA Grossniklaus U., Ecker J.R., Belostotsky D.A.;
RT "Genome-wide high-resolution mapping of exosome substrates reveals hidden
RT features in the Arabidopsis transcriptome.";
RL Cell 131:1340-1353(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Non-catalytic component of the RNA exosome complex which has
CC 3'->5' exoribonuclease activity and participates in a multitude of
CC cellular RNA processing, maturation and degradation events. In vitro,
CC is a processive phosphorolytic exonuclease and requires a single-
CC stranded poly(A) tail on the substrate RNA for its activity. Can
CC complement the growth defect of a yeast mutant lacking RRP41
CC exonuclease (PubMed:10930416). Required for normal development of
CC female gametophytes (PubMed:18160042). {ECO:0000269|PubMed:10930416,
CC ECO:0000269|PubMed:18160042}.
CC -!- SUBUNIT: Component of the RNA exosome complex (PubMed:10930416,
CC PubMed:18160042). Interacts with RPP4 (PubMed:11809881).
CC {ECO:0000269|PubMed:10930416, ECO:0000269|PubMed:11809881,
CC ECO:0000269|PubMed:18160042}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NPD3}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NPD3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NPD3}.
CC -!- DISRUPTION PHENOTYPE: Aborted ovule development after the first
CC mitosis. {ECO:0000269|PubMed:18160042}.
CC -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
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DR EMBL; AF191741; AAF04590.1; -; mRNA.
DR EMBL; AL132959; CAB71092.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80232.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80233.1; -; Genomic_DNA.
DR EMBL; AK118846; BAC43435.1; -; mRNA.
DR EMBL; BT005485; AAO63905.1; -; mRNA.
DR PIR; T47954; T47954.
DR RefSeq; NP_001118878.1; NM_001125406.1.
DR RefSeq; NP_191721.1; NM_116027.5.
DR AlphaFoldDB; Q9SP08; -.
DR SMR; Q9SP08; -.
DR IntAct; Q9SP08; 8.
DR STRING; 3702.AT3G61620.2; -.
DR iPTMnet; Q9SP08; -.
DR PaxDb; Q9SP08; -.
DR PRIDE; Q9SP08; -.
DR ProteomicsDB; 228255; -.
DR DNASU; 825335; -.
DR EnsemblPlants; AT3G61620.1; AT3G61620.1; AT3G61620.
DR EnsemblPlants; AT3G61620.2; AT3G61620.2; AT3G61620.
DR GeneID; 825335; -.
DR Gramene; AT3G61620.1; AT3G61620.1; AT3G61620.
DR Gramene; AT3G61620.2; AT3G61620.2; AT3G61620.
DR KEGG; ath:AT3G61620; -.
DR Araport; AT3G61620; -.
DR TAIR; locus:2076710; AT3G61620.
DR eggNOG; KOG1068; Eukaryota.
DR HOGENOM; CLU_063514_0_0_1; -.
DR InParanoid; Q9SP08; -.
DR OMA; KGKGQGW; -.
DR OrthoDB; 1394468at2759; -.
DR PhylomeDB; Q9SP08; -.
DR PRO; PR:Q9SP08; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SP08; baseline and differential.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 3.30.230.70; -; 1.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR Pfam; PF01138; RNase_PH; 1.
DR Pfam; PF03725; RNase_PH_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55666; SSF55666; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Exosome; Nucleus; Reference proteome; RNA-binding;
KW rRNA processing.
FT CHAIN 1..241
FT /note="Exosome complex component RRP41 homolog"
FT /id="PRO_0000435318"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 241 AA; 26551 MW; 7E1955A09C4585E5 CRC64;
MEYVNPEGLR LDGRRFNEMR QIVAEVGVVS KADGSAVFEM GNTKVIAAVY GPREIQNKSQ
QKKNDHAVVL CEYSMAQFST GDRRRQKFDR RSTELSLVIR QTMEACILTE LMPHSQIDIF
LQVLQADGGT RSACINAATL ALADAGIPMR DLAVSCSAGY LNSTPLLDLN YVEDSAGGAD
VTVGILPKLD KVSLLQMDAK LPMETFETVF ALASEGCKAI AERIREVLQE NTKQLEYRRA
A
