CER7_ARATH
ID CER7_ARATH Reviewed; 438 AA.
AC Q9M209;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Exosome complex component RRP45B {ECO:0000305};
DE AltName: Full=Protein ECERIFERUM 7 {ECO:0000303|PubMed:17351114};
DE AltName: Full=RNA-processing protein CER7;
DE AltName: Full=RRP45 homolog B {ECO:0000305};
DE AltName: Full=Ribosomal RNA-processing protein 45B {ECO:0000305};
GN Name=RRP45B {ECO:0000305}; Synonyms=CER7 {ECO:0000303|PubMed:17351114};
GN OrderedLocusNames=At3g60500; ORFNames=T8B10.160;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17351114; DOI=10.1105/tpc.106.049304;
RA Hooker T.S., Lam P., Zheng H., Kunst L.;
RT "A core subunit of the RNA-processing/degrading exosome specifically
RT influences cuticular wax biosynthesis in Arabidopsis.";
RL Plant Cell 19:904-913(2007).
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=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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22689894; DOI=10.1104/pp.112.199646;
RA Lam P., Zhao L., McFarlane H.E., Aiga M., Lam V., Hooker T.S., Kunst L.;
RT "RDR1 and SGS3, components of RNA-mediated gene silencing, are required for
RT the regulation of cuticular wax biosynthesis in developing inflorescence
RT stems of Arabidopsis.";
RL Plant Physiol. 159:1385-1395(2012).
CC -!- FUNCTION: Probable 3'->5' exoribonuclease involved in the regulation of
CC cuticular wax biosynthesis by controlling the expression of CER3. May
CC act by degrading a specific mRNA species encoding a negative regulator
CC of CER3 transcription. Can perform exosomal functions and complement
CC the yeast rrp45 null mutant. {ECO:0000269|PubMed:17351114,
CC ECO:0000269|PubMed:22689894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17351114}. Nucleus
CC {ECO:0000269|PubMed:17351114}. Note=Excluded from the nucleolus.
CC -!- DISRUPTION PHENOTYPE: Bright green glossy stems and siliques due to
CC reduced cuticular wax accumulation. {ECO:0000269|PubMed:17351114,
CC ECO:0000269|PubMed:22689894}.
CC -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
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DR EMBL; DQ869270; ABI31441.1; -; Genomic_DNA.
DR EMBL; AL138646; CAB81836.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80068.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80069.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80070.1; -; Genomic_DNA.
DR EMBL; BT004196; AAO42214.1; -; mRNA.
DR EMBL; BT005701; AAO64121.1; -; mRNA.
DR PIR; T47861; T47861.
DR RefSeq; NP_001190143.1; NM_001203214.1.
DR RefSeq; NP_191609.1; NM_115914.4.
DR RefSeq; NP_974466.1; NM_202737.3.
DR AlphaFoldDB; Q9M209; -.
DR SMR; Q9M209; -.
DR BioGRID; 10535; 14.
DR IntAct; Q9M209; 2.
DR STRING; 3702.AT3G60500.3; -.
DR PaxDb; Q9M209; -.
DR PRIDE; Q9M209; -.
DR ProteomicsDB; 224458; -.
DR EnsemblPlants; AT3G60500.1; AT3G60500.1; AT3G60500.
DR EnsemblPlants; AT3G60500.2; AT3G60500.2; AT3G60500.
DR EnsemblPlants; AT3G60500.3; AT3G60500.3; AT3G60500.
DR GeneID; 825221; -.
DR Gramene; AT3G60500.1; AT3G60500.1; AT3G60500.
DR Gramene; AT3G60500.2; AT3G60500.2; AT3G60500.
DR Gramene; AT3G60500.3; AT3G60500.3; AT3G60500.
DR KEGG; ath:AT3G60500; -.
DR Araport; AT3G60500; -.
DR TAIR; locus:2103316; AT3G60500.
DR eggNOG; KOG1614; Eukaryota.
DR HOGENOM; CLU_038194_1_1_1; -.
DR OrthoDB; 996662at2759; -.
DR PhylomeDB; Q9M209; -.
DR PRO; PR:Q9M209; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M209; baseline and differential.
DR Genevisible; Q9M209; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:TAIR.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central.
DR 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.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0034473; P:U1 snRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0034476; P:U5 snRNA 3'-end processing; IBA:GO_Central.
DR CDD; cd11368; RNase_PH_RRP45; 1.
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 InterPro; IPR033100; Rrp45.
DR Pfam; PF01138; RNase_PH; 1.
DR Pfam; PF03725; RNase_PH_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55666; SSF55666; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..438
FT /note="Exosome complex component RRP45B"
FT /id="PRO_0000424435"
FT REGION 293..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ 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
