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RP41L_ARATH
ID   RP41L_ARATH             Reviewed;         256 AA.
AC   A2RVK7; Q8GWJ0; Q9SZS4;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Exosome complex component RRP41-like {ECO:0000305};
DE   AltName: Full=Protein SLOWER GROWTH {ECO:0000303|PubMed:23132787};
DE   AltName: Full=Ribosomal RNA-processing protein 41-like {ECO:0000305};
GN   Name=RRP41L {ECO:0000303|PubMed:23132787};
GN   Synonyms=SLG {ECO:0000303|PubMed:23132787};
GN   OrderedLocusNames=At4g27490 {ECO:0000312|Araport:AT4G27490};
GN   ORFNames=F27G19.90 {ECO:0000312|EMBL:CAB43881.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=23132787; DOI=10.1104/pp.112.206706;
RA   Yang M., Zhang B., Jia J., Yan C., Habaike A., Han Y.;
RT   "RRP41L, a putative core subunit of the exosome, plays an important role in
RT   seed germination and early seedling growth in Arabidopsis.";
RL   Plant Physiol. 161:165-178(2013).
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 (By
CC       similarity). Plays an important role in seed germination and early
CC       seedling growth by mediating specific cytoplasmic mRNA decay of
CC       transcripts coding for the abscisic acid (ABA) biosynthetic enzymes
CC       NCED5 and NCED6, and the ABA signaling transcription factors ABI3 and
CC       ABI4 (PubMed:23132787). {ECO:0000250|UniProtKB:Q9SP08,
CC       ECO:0000269|PubMed:23132787}.
CC   -!- SUBUNIT: Probable component of the RNA exosome complex.
CC       {ECO:0000250|UniProtKB:Q9SP08}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23132787}. Nucleus
CC       {ECO:0000269|PubMed:23132787}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in imbibed seeds and young
CC       seedlings. {ECO:0000269|PubMed:23132787}.
CC   -!- DISRUPTION PHENOTYPE: Extremely slow growth, especially during the
CC       early stage of development. {ECO:0000269|PubMed:23132787}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC43402.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB43881.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB81399.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL078467; CAB43881.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161571; CAB81399.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85349.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66335.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66338.1; -; Genomic_DNA.
DR   EMBL; AK118812; BAC43402.1; ALT_FRAME; mRNA.
DR   EMBL; BT029998; ABN04736.1; -; mRNA.
DR   EMBL; BT030054; ABN04792.1; -; mRNA.
DR   PIR; T08941; T08941.
DR   RefSeq; NP_001320075.1; NM_001341852.1.
DR   RefSeq; NP_001328238.1; NM_001341854.1.
DR   RefSeq; NP_001328241.1; NM_001341855.1.
DR   AlphaFoldDB; A2RVK7; -.
DR   SMR; A2RVK7; -.
DR   IntAct; A2RVK7; 2.
DR   STRING; 3702.AT4G27490.1; -.
DR   iPTMnet; A2RVK7; -.
DR   PaxDb; A2RVK7; -.
DR   PRIDE; A2RVK7; -.
DR   ProteomicsDB; 227986; -.
DR   EnsemblPlants; AT4G27490.1; AT4G27490.1; AT4G27490.
DR   EnsemblPlants; AT4G27490.3; AT4G27490.3; AT4G27490.
DR   EnsemblPlants; AT4G27490.4; AT4G27490.4; AT4G27490.
DR   GeneID; 828858; -.
DR   Gramene; AT4G27490.1; AT4G27490.1; AT4G27490.
DR   Gramene; AT4G27490.3; AT4G27490.3; AT4G27490.
DR   Gramene; AT4G27490.4; AT4G27490.4; AT4G27490.
DR   KEGG; ath:AT4G27490; -.
DR   Araport; AT4G27490; -.
DR   TAIR; locus:2124024; AT4G27490.
DR   eggNOG; ENOG502QWHI; Eukaryota.
DR   HOGENOM; CLU_063514_1_1_1; -.
DR   OMA; RCGLVSQ; -.
DR   OrthoDB; 1101132at2759; -.
DR   PhylomeDB; A2RVK7; -.
DR   PRO; PR:A2RVK7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; A2RVK7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
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:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IMP:TAIR.
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:0009845; P:seed germination; IMP:TAIR.
DR   GO; GO:0090351; P:seedling development; IMP:TAIR.
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   2: Evidence at transcript level;
KW   Cytoplasm; Exosome; Nucleus; Reference proteome; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..256
FT                   /note="Exosome complex component RRP41-like"
FT                   /id="PRO_0000435319"
SQ   SEQUENCE   256 AA;  27448 MW;  CD1D16E9D1971771 CRC64;
     MAAKPGAATP TYSPKIVGRS RLPIFKDSDL DWSRPDGRGF HQCRPALLQT GAVSSASGSA
     YAEFGNTKVI VSVFGPRESK KAMVYSDVGR LNCNVSYTNF ASPTLGQGTD HKEYSSMLHK
     ALEGVIMMET FPKTTVDVFA LVLESGGSDL SVLISCASLA LADAGIMMYD LITAVSVSCI
     GKSLMIDPVT EEEGCEDGSF MMTCMPSRYE ITQLTITGEW TTPNINEAMQ LCLDASSKLG
     EIMRDCLKQS ASASDE
 
 
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