ID   RPP40_MOUSE             Reviewed;         363 AA.
AC   Q8R1F9; Q8BX66;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Ribonuclease P protein subunit p40;
DE            Short=RNaseP protein p40;
GN   Name=Rpp40;
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; TISSUE=Cerebellum;
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 GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-363.
RC   STRAIN=FVB/N; TISSUE=Kidney;
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:O75818}.
CC   -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins.
CC       RNase P consists of a catalytic RNA moiety and about 10 protein
CC       subunits; 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. {ECO:0000250|UniProtKB:O75818}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24607.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC33465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=EDL40907.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK048810; BAC33465.1; ALT_INIT; mRNA.
DR   EMBL; CH466546; EDL40907.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC024607; AAH24607.1; ALT_INIT; mRNA.
DR   CCDS; CCDS26451.2; -.
DR   RefSeq; NP_666050.3; NM_145938.4.
DR   RefSeq; XP_011242604.1; XM_011244302.1.
DR   AlphaFoldDB; Q8R1F9; -.
DR   SMR; Q8R1F9; -.
DR   BioGRID; 228975; 1.
DR   STRING; 10090.ENSMUSP00000130290; -.
DR   iPTMnet; Q8R1F9; -.
DR   PhosphoSitePlus; Q8R1F9; -.
DR   EPD; Q8R1F9; -.
DR   MaxQB; Q8R1F9; -.
DR   PaxDb; Q8R1F9; -.
DR   PRIDE; Q8R1F9; -.
DR   ProteomicsDB; 262705; -.
DR   Antibodypedia; 24532; 77 antibodies from 20 providers.
DR   DNASU; 208366; -.
DR   Ensembl; ENSMUST00000171686; ENSMUSP00000130290; ENSMUSG00000021418.
DR   GeneID; 208366; -.
DR   KEGG; mmu:208366; -.
DR   UCSC; uc011yyj.1; mouse.
DR   CTD; 10799; -.
DR   MGI; MGI:1346084; Rpp40.
DR   VEuPathDB; HostDB:ENSMUSG00000021418; -.
DR   eggNOG; ENOG502QSAV; Eukaryota.
DR   GeneTree; ENSGT00390000014167; -.
DR   HOGENOM; CLU_065211_0_0_1; -.
DR   InParanoid; Q8R1F9; -.
DR   OMA; LQWETGF; -.
DR   OrthoDB; 1273379at2759; -.
DR   PhylomeDB; Q8R1F9; -.
DR   TreeFam; TF330967; -.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 208366; 23 hits in 72 CRISPR screens.
DR   PRO; PR:Q8R1F9; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q8R1F9; protein.
DR   Bgee; ENSMUSG00000021418; Expressed in morula and 196 other tissues.
DR   ExpressionAtlas; Q8R1F9; baseline and differential.
DR   Genevisible; Q8R1F9; MM.
DR   GO; GO:0030681; C:multimeric ribonuclease P complex; ISS:UniProtKB.
DR   GO; GO:0005655; C:nucleolar ribonuclease P complex; ISO:MGI.
DR   GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central.
DR   GO; GO:0004526; F:ribonuclease P activity; ISO:MGI.
DR   GO; GO:0033204; F:ribonuclease P RNA binding; ISS:UniProtKB.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:1905267; P:endonucleolytic cleavage involved in tRNA processing; IBA:GO_Central.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; ISS:UniProtKB.
DR   InterPro; IPR013893; RNase_P_Rpp40.
DR   PANTHER; PTHR15396; PTHR15396; 1.
DR   Pfam; PF08584; Ribonuc_P_40; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Reference proteome; rRNA processing; tRNA processing.
FT   CHAIN           1..363
FT                   /note="Ribonuclease P protein subunit p40"
FT                   /id="PRO_0000354076"
FT   CONFLICT        75
FT                   /note="H -> Y (in Ref. 1; BAC33465)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   363 AA;  41547 MW;  B62F8025633C2B8E CRC64;
     MATLRRLQEA PRHLLVCEKS NFGHDKSRHK HLVETHYHNY RVSFLIPECG LLSKELKSLV
     MDIGPYYSVK NLPLHELITH EFINTFVKKG SFSALTYNTS IDEDNTVALL PNGKLILSLD
     KDTYEETGLQ GRPSRYSGRK SMKFVISIDL MDLSLNLDSK KYRRISWSFK EKKPLKFDFL
     LAWHPTGTEE STMMSYFSKY QIQEHQPKVA LSTVRELQCP VLRSSGLAGE PEEACSALEF
     FDWLGAVFCS ADLNNEPYNF ISTYCCPQPS AVVAQAFLCT ITGFILPEKI HVLLEQLCHY
     FDEPKLAPWV TLTVQGFADS PVAWREKEHG FHKGGEHLYN FVVFNNQDYW LQMAVGANDD
     CPP