RPP29_MOUSE
ID RPP29_MOUSE Reviewed; 221 AA.
AC Q9CR08; Q3U6V7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ribonuclease P protein subunit p29;
GN Name=Pop4; Synonyms=Rpp29;
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=Bone marrow, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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.
CC {ECO:0000250|UniProtKB:O95707}.
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. {ECO:0000250|UniProtKB:O95707}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O95707}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 1 family. {ECO:0000305}.
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DR EMBL; AK002855; BAB22410.1; -; mRNA.
DR EMBL; AK003293; BAB22696.1; -; mRNA.
DR EMBL; AK150459; BAE29579.1; -; mRNA.
DR EMBL; AK152948; BAE31617.1; -; mRNA.
DR EMBL; BC011465; AAH11465.1; -; mRNA.
DR CCDS; CCDS39915.1; -.
DR RefSeq; NP_079666.1; NM_025390.4.
DR AlphaFoldDB; Q9CR08; -.
DR SMR; Q9CR08; -.
DR STRING; 10090.ENSMUSP00000032585; -.
DR iPTMnet; Q9CR08; -.
DR PhosphoSitePlus; Q9CR08; -.
DR EPD; Q9CR08; -.
DR MaxQB; Q9CR08; -.
DR PaxDb; Q9CR08; -.
DR PeptideAtlas; Q9CR08; -.
DR PRIDE; Q9CR08; -.
DR ProteomicsDB; 262704; -.
DR Antibodypedia; 15541; 145 antibodies from 26 providers.
DR DNASU; 66161; -.
DR Ensembl; ENSMUST00000032585; ENSMUSP00000032585; ENSMUSG00000030423.
DR GeneID; 66161; -.
DR KEGG; mmu:66161; -.
DR UCSC; uc009gkv.1; mouse.
DR CTD; 10775; -.
DR MGI; MGI:1913411; Pop4.
DR VEuPathDB; HostDB:ENSMUSG00000030423; -.
DR eggNOG; KOG4046; Eukaryota.
DR GeneTree; ENSGT00390000010067; -.
DR HOGENOM; CLU_078577_2_1_1; -.
DR InParanoid; Q9CR08; -.
DR OMA; IPKSECV; -.
DR OrthoDB; 1362700at2759; -.
DR PhylomeDB; Q9CR08; -.
DR TreeFam; TF313883; -.
DR BioGRID-ORCS; 66161; 27 hits in 71 CRISPR screens.
DR PRO; PR:Q9CR08; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CR08; protein.
DR Bgee; ENSMUSG00000030423; Expressed in floor plate of midbrain and 233 other tissues.
DR ExpressionAtlas; Q9CR08; baseline and differential.
DR Genevisible; Q9CR08; MM.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central.
DR GO; GO:0030677; C:ribonuclease P 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:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; ISS:UniProtKB.
DR Gene3D; 2.30.30.210; -; 1.
DR InterPro; IPR016848; RNase_P/MRP_Rpp29-subunit.
DR InterPro; IPR036980; RNase_P/MRP_Rpp29_sf.
DR InterPro; IPR023534; Rof/RNase_P-like.
DR InterPro; IPR002730; Rpp29/RNP1.
DR PANTHER; PTHR13348; PTHR13348; 1.
DR Pfam; PF01868; RNase_P-MRP_p29; 1.
DR PIRSF; PIRSF027081; RNase_P/MRP_p29_subunit; 1.
DR SMART; SM00538; POP4; 1.
DR SUPFAM; SSF101744; SSF101744; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..221
FT /note="Ribonuclease P protein subunit p29"
FT /id="PRO_0000128419"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95707"
SQ SEQUENCE 221 AA; 25637 MW; 372E834DFC46A086 CRC64;
MKAAIYHAFS HKEAKDHDVQ ELGSQRAEAF VRAFLKQSIP HMSQEDCESH LQRKAVILEY
FTRLKPRPRP KKKSKGLSAK QRRDMRLFDI KPEQQRYSLF LPLHELWKQY IRDLCNGLKP
DTQPQMIQAK LLKADLHGAI ISVTKSKCPS YVGVTGILLQ ETKHVFKIIT REDHLKVIPK
LNCVFTIEID DFISYIYGSK FQLRASERSA KKFKAKGSID L
