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Exosome complex component RRP45B (Protein ECERIFERUM 7) (RNA-processing protein CER7) (RRP45 homolog B) (Ribosomal RNA-processing protein 45B)

 CER7_ARATH              Reviewed;         438 AA.
Q9M209;
13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
23-MAY-2018, entry version 108.
RecName: Full=Exosome complex component RRP45B {ECO:0000305};
AltName: Full=Protein ECERIFERUM 7 {ECO:0000303|PubMed:17351114};
AltName: Full=RNA-processing protein CER7;
AltName: Full=RRP45 homolog B {ECO:0000305};
AltName: Full=Ribosomal RNA-processing protein 45B {ECO:0000305};
Name=RRP45B {ECO:0000305};
Synonyms=CER7 {ECO:0000303|PubMed:17351114};
OrderedLocusNames=At3g60500; ORFNames=T8B10.160;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
DISRUPTION PHENOTYPE.
STRAIN=cv. Landsberg erecta;
PubMed=17351114; DOI=10.1105/tpc.106.049304;
Hooker T.S., Lam P., Zheng H., Kunst L.;
"A core subunit of the RNA-processing/degrading exosome specifically
influences cuticular wax biosynthesis in Arabidopsis.";
Plant Cell 19:904-913(2007).
[2]
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).
[3]
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).
[4]
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).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22689894; DOI=10.1104/pp.112.199646;
Lam P., Zhao L., McFarlane H.E., Aiga M., Lam V., Hooker T.S.,
Kunst L.;
"RDR1 and SGS3, components of RNA-mediated gene silencing, are
required for the regulation of cuticular wax biosynthesis in
developing inflorescence stems of Arabidopsis.";
Plant Physiol. 159:1385-1395(2012).
-!- FUNCTION: Probable 3'->5' exoribonuclease involved in the
regulation of cuticular wax biosynthesis by controlling the
expression of CER3. May act by degrading a specific mRNA species
encoding a negative regulator of CER3 transcription. Can perform
exosomal functions and complement the yeast rrp45 null mutant.
{ECO:0000269|PubMed:17351114, ECO:0000269|PubMed:22689894}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17351114}.
Nucleus {ECO:0000269|PubMed:17351114}. Note=Excluded from the
nucleolus.
-!- DISRUPTION PHENOTYPE: Bright green glossy stems and siliques due
to reduced cuticular wax accumulation.
{ECO:0000269|PubMed:17351114, ECO:0000269|PubMed:22689894}.
-!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
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EMBL; DQ869270; ABI31441.1; -; Genomic_DNA.
EMBL; AL138646; CAB81836.1; -; Genomic_DNA.
EMBL; CP002686; AEE80068.1; -; Genomic_DNA.
EMBL; CP002686; AEE80069.1; -; Genomic_DNA.
EMBL; CP002686; AEE80070.1; -; Genomic_DNA.
EMBL; BT004196; AAO42214.1; -; mRNA.
EMBL; BT005701; AAO64121.1; -; mRNA.
PIR; T47861; T47861.
RefSeq; NP_001190143.1; NM_001203214.1.
RefSeq; NP_191609.1; NM_115914.4.
RefSeq; NP_974466.1; NM_202737.3.
UniGene; At.34436; -.
ProteinModelPortal; Q9M209; -.
SMR; Q9M209; -.
BioGrid; 10535; 2.
IntAct; Q9M209; 2.
STRING; 3702.AT3G60500.1; -.
PaxDb; Q9M209; -.
EnsemblPlants; AT3G60500.1; AT3G60500.1; AT3G60500.
EnsemblPlants; AT3G60500.2; AT3G60500.2; AT3G60500.
EnsemblPlants; AT3G60500.3; AT3G60500.3; AT3G60500.
GeneID; 825221; -.
Gramene; AT3G60500.1; AT3G60500.1; AT3G60500.
Gramene; AT3G60500.2; AT3G60500.2; AT3G60500.
Gramene; AT3G60500.3; AT3G60500.3; AT3G60500.
KEGG; ath:AT3G60500; -.
Araport; AT3G60500; -.
TAIR; locus:2103316; AT3G60500.
eggNOG; KOG1614; Eukaryota.
eggNOG; COG2123; LUCA.
HOGENOM; HOG000229504; -.
KO; K03678; -.
OMA; FDFRRLK; -.
OrthoDB; EOG09360FNA; -.
PhylomeDB; Q9M209; -.
Reactome; R-ATH-429958; mRNA decay by 3' to 5' exoribonuclease.
Reactome; R-ATH-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-ATH-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
PRO; PR:Q9M209; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9M209; baseline and differential.
Genevisible; Q9M209; AT.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:TAIR.
GO; GO:0017091; F:AU-rich element binding; IBA:GO_Central.
GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; IBA:GO_Central.
GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IBA:GO_Central.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
GO; GO:0034473; P:U1 snRNA 3'-end processing; IBA:GO_Central.
GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
GO; GO:0034476; P:U5 snRNA 3'-end processing; IBA:GO_Central.
CDD; cd11368; RNase_PH_RRP45; 1.
Gene3D; 3.30.230.70; -; 1.
InterPro; IPR001247; ExoRNase_PH_dom1.
InterPro; IPR015847; ExoRNase_PH_dom2.
InterPro; IPR036345; ExoRNase_PH_dom2_sf.
InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR033100; Rrp45.
Pfam; PF01138; RNase_PH; 1.
Pfam; PF03725; RNase_PH_C; 1.
SUPFAM; SSF54211; SSF54211; 2.
SUPFAM; SSF55666; SSF55666; 1.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; Nucleus; Reference proteome;
RNA-binding.
CHAIN 1 438 Exosome complex component RRP45B.
/FTId=PRO_0000424435.
SEQUENCE 438 AA; 48296 MW; D5FFB004BE1370F2 CRC64;
MEGRLANMWR LTVNESKFVE TALQSELRVD GRGLYDYRKL TIKFGKEYGS SEVQLGQTHV
MGFVTAQLVQ PYKDRPNEGS LSIFTEFSPM ADPSFEPGRP GESAVELGRI IDRGLRESRA
VDTESLCVLA GKMVWSVRID LHILDNGGNL VDAANIAALA ALMTFRRPDC TVGGENGQEV
IIHPLEEREP LPLIIHHLPI AFTFGFFNKG NIVVMDPTYV EEAVMCGRMT VTVNANGDIC
AIQKPGEEGV NQSVILHCLR LASSRAAATT KIIREEVEAY NCERSLQKVK RHPTLAKSEV
SGPTVAVKEE HRKSSDQERA AEISREHVER LKLSTEEVRS SKEEEAANFK GGPSNWDPYS
EAMDVDSLKV SLASRGDPVT KSSSTKKMNG SGNAQKVGVE ISVEEVTGEL GKKDTKHKDG
EMTLKDAVKP KKKRKNKS


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