RPP25_MOUSE
ID RPP25_MOUSE Reviewed; 199 AA.
AC Q91WE3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Ribonuclease P protein subunit p25;
DE Short=RNase P protein subunit p25;
GN Name=Rpp25;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
CC -!- FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that
CC generates mature tRNA molecules by cleaving their 5'-ends. Also a
CC component of the MRP ribonuclease complex, which cleaves pre-rRNA
CC sequences. {ECO:0000250|UniProtKB:Q9BUL9}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins.
CC RNase P consists of a catalytic RNA moiety and 10 different protein
CC chains; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and
CC RPP40. Within the RNase P complex, POP1, POP7 and RPP25 form the
CC 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form the
CC '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. Several subunits of RNase P are also part of the RNase
CC MRP complex. RNase MRP consists of a catalytic RNA moiety and about 8
CC protein subunits; POP1, POP7, RPP25, RPP30, RPP38, RPP40 and possibly
CC also POP4 and POP5. POP7 forms a heterodimer with RPP25 that binds to
CC the P3 stem loop of the catalytic RNA. {ECO:0000250|UniProtKB:Q9BUL9}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9BUL9}.
CC -!- SIMILARITY: Belongs to the histone-like Alba family. {ECO:0000305}.
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DR EMBL; AK082822; BAC38636.1; -; mRNA.
DR EMBL; BC016085; AAH16085.1; -; mRNA.
DR EMBL; BC083064; AAH83064.1; -; mRNA.
DR CCDS; CCDS23222.1; -.
DR RefSeq; NP_598743.1; NM_133982.1.
DR AlphaFoldDB; Q91WE3; -.
DR SMR; Q91WE3; -.
DR BioGRID; 221908; 1.
DR STRING; 10090.ENSMUSP00000079358; -.
DR iPTMnet; Q91WE3; -.
DR PhosphoSitePlus; Q91WE3; -.
DR MaxQB; Q91WE3; -.
DR PaxDb; Q91WE3; -.
DR PeptideAtlas; Q91WE3; -.
DR PRIDE; Q91WE3; -.
DR ProteomicsDB; 299928; -.
DR Antibodypedia; 50450; 94 antibodies from 23 providers.
DR DNASU; 102614; -.
DR Ensembl; ENSMUST00000080514; ENSMUSP00000079358; ENSMUSG00000062309.
DR GeneID; 102614; -.
DR KEGG; mmu:102614; -.
DR UCSC; uc009puy.1; mouse.
DR CTD; 54913; -.
DR MGI; MGI:2143151; Rpp25.
DR VEuPathDB; HostDB:ENSMUSG00000062309; -.
DR eggNOG; KOG2567; Eukaryota.
DR GeneTree; ENSGT00390000002564; -.
DR HOGENOM; CLU_096311_0_0_1; -.
DR InParanoid; Q91WE3; -.
DR OMA; CGRAVTK; -.
DR OrthoDB; 1075123at2759; -.
DR PhylomeDB; Q91WE3; -.
DR TreeFam; TF325688; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 102614; 0 hits in 74 CRISPR screens.
DR PRO; PR:Q91WE3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q91WE3; protein.
DR Bgee; ENSMUSG00000062309; Expressed in epithelium of stomach and 114 other tissues.
DR Genevisible; Q91WE3; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000172; C:ribonuclease MRP complex; ISO:MGI.
DR GO; GO:0004526; F:ribonuclease P activity; ISO:MGI.
DR GO; GO:0033204; F:ribonuclease P RNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0001682; P:tRNA 5'-leader removal; ISS:UniProtKB.
DR Gene3D; 3.30.110.20; -; 1.
DR InterPro; IPR036882; Alba-like_dom_sf.
DR InterPro; IPR002775; DNA/RNA-bd_Alba-like.
DR InterPro; IPR040207; Rpp25.
DR PANTHER; PTHR13516:SF5; PTHR13516:SF5; 1.
DR Pfam; PF01918; Alba; 1.
DR SUPFAM; SSF82704; SSF82704; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; rRNA processing;
KW tRNA processing.
FT CHAIN 1..199
FT /note="Ribonuclease P protein subunit p25"
FT /id="PRO_0000237583"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL9"
SQ SEQUENCE 199 AA; 21038 MW; B9DE105BE3293D64 CRC64;
MENFRKVRSE EAPAGDGDEG GSPNSGPFAD LAPGAVHMRV KEGSKIRNLL AFATASMAQP
ATRAIVFSGC GRATTKTVTC AEILKRRLAG LHQVTRLRYR SVREVWQSLP PGPTPGQTPS
DPAASLSVLK NVPSLAILLS KDALDPRQLG YQPPNLSPGP SSPPTVSTSK RSLGESAAEE
GTAKRSQPEP EAENEDRTA
