RPP21_MOUSE
ID RPP21_MOUSE Reviewed; 150 AA.
AC Q8R040; Q80XY3; Q811B7; Q9CPX1;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ribonuclease P protein subunit p21;
DE Short=RNaseP protein p21;
DE AltName: Full=Ribonucleoprotein V;
GN Name=Rpp21; Synonyms=Cat60;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ; TISSUE=Testis;
RX PubMed=12671000; DOI=10.1101/gr.975303;
RA Takada T., Kumanovics A., Amadou C., Yoshino M., Jones E.P., Athanasiou M.,
RA Evans G.A., Lindahl K.F.;
RT "Species-specific class I gene expansions formed the telomeric 1 mb of the
RT mouse major histocompatibility complex.";
RL Genome Res. 13:589-600(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RA Raha-Chowdhury R., Andrews S.R., Gruen J.R., Weissman S.M.;
RT "Genes from major histocompatibility complex (MHC) class I region from HLA-
RT C to HLA-A.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that
CC generates mature tRNA molecules by cleaving their 5'-ends.
CC {ECO:0000250|UniProtKB:Q9H633}.
CC -!- SUBUNIT: RNase P consists of a catalytic RNA moiety and about 10
CC protein subunits; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30,
CC RPP38 and RPP40. Within the RNase P complex, POP1, POP7 and RPP25 form
CC the 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form
CC the 'palm' subcomplex, and RPP21, POP4 and RPP38 form the 'wrist'
CC subcomplex. All subunits of the RNase P complex interact with the
CC catalytic RNA. {ECO:0000250|UniProtKB:Q9H633}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9H633}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 4 family. {ECO:0000305}.
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DR EMBL; AY251016; AAP03887.1; -; mRNA.
DR EMBL; AJ504717; CAD44293.1; -; mRNA.
DR EMBL; AK002780; BAB22353.1; -; mRNA.
DR EMBL; AK003455; BAB22800.1; -; mRNA.
DR EMBL; BC028491; AAH28491.1; -; mRNA.
DR CCDS; CCDS28719.1; -.
DR RefSeq; NP_080584.1; NM_026308.2.
DR AlphaFoldDB; Q8R040; -.
DR SMR; Q8R040; -.
DR BioGRID; 212359; 1.
DR STRING; 10090.ENSMUSP00000025319; -.
DR iPTMnet; Q8R040; -.
DR PhosphoSitePlus; Q8R040; -.
DR EPD; Q8R040; -.
DR MaxQB; Q8R040; -.
DR PaxDb; Q8R040; -.
DR PeptideAtlas; Q8R040; -.
DR PRIDE; Q8R040; -.
DR ProteomicsDB; 262703; -.
DR Antibodypedia; 34965; 57 antibodies from 14 providers.
DR DNASU; 67676; -.
DR Ensembl; ENSMUST00000025319; ENSMUSP00000025319; ENSMUSG00000024446.
DR GeneID; 67676; -.
DR KEGG; mmu:67676; -.
DR UCSC; uc008ckq.1; mouse.
DR CTD; 79897; -.
DR MGI; MGI:1914926; Rpp21.
DR VEuPathDB; HostDB:ENSMUSG00000024446; -.
DR eggNOG; KOG4394; Eukaryota.
DR GeneTree; ENSGT00390000003020; -.
DR HOGENOM; CLU_079140_2_1_1; -.
DR InParanoid; Q8R040; -.
DR OMA; DPKHLLW; -.
DR OrthoDB; 1560813at2759; -.
DR PhylomeDB; Q8R040; -.
DR TreeFam; TF323865; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 67676; 30 hits in 76 CRISPR screens.
DR ChiTaRS; Rpp21; mouse.
DR PRO; PR:Q8R040; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8R040; protein.
DR Bgee; ENSMUSG00000024446; Expressed in morula and 194 other tissues.
DR ExpressionAtlas; Q8R040; baseline and differential.
DR Genevisible; Q8R040; MM.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; ISO:MGI.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004526; F:ribonuclease P activity; ISO:MGI.
DR GO; GO:0033204; F:ribonuclease P RNA binding; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0001682; P:tRNA 5'-leader removal; ISO:MGI.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR Pfam; PF04032; Rpr2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Metal-binding; Nucleus; Reference proteome; tRNA processing;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H633"
FT CHAIN 2..150
FT /note="Ribonuclease P protein subunit p21"
FT /id="PRO_0000153846"
FT REGION 121..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H633"
FT CONFLICT 18
FT /note="Y -> C (in Ref. 1; AAP03887)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..53
FT /note="KRLVLRQ -> NAGPPA (in Ref. 2; CAD44293)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="I -> M (in Ref. 4; AAH28491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 150 AA; 17243 MW; EDB5C52A6F2FF519 CRC64;
MAGPVKDREA FQRLSFLYQA AHCVLSQNPE NQALARFYCH TEKTIAKRLV LRQDPSVKRT
LCRSCSSLLI PGLTCTQRQR RRKGQRWTVQ TCLTCQRSQR FLNDPKHLLW GDRPEAQLEN
QADINPSEPL PNIADLPKEN IQTQALNTSE
