ID   RPP29_RAT               Reviewed;         221 AA.
AC   Q5M882;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Ribonuclease P protein subunit p29;
GN   Name=Pop4; Synonyms=Rpp29;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
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; BC088183; AAH88183.1; -; mRNA.
DR   RefSeq; NP_001009642.1; NM_001009642.1.
DR   AlphaFoldDB; Q5M882; -.
DR   SMR; Q5M882; -.
DR   STRING; 10116.ENSRNOP00000020474; -.
DR   PaxDb; Q5M882; -.
DR   Ensembl; ENSRNOT00000020474; ENSRNOP00000020474; ENSRNOG00000027646.
DR   GeneID; 292831; -.
DR   KEGG; rno:292831; -.
DR   UCSC; RGD:1305955; rat.
DR   CTD; 10775; -.
DR   RGD; 1305955; Pop4.
DR   eggNOG; KOG4046; Eukaryota.
DR   GeneTree; ENSGT00390000010067; -.
DR   HOGENOM; CLU_078577_2_1_1; -.
DR   InParanoid; Q5M882; -.
DR   OMA; IPKSECV; -.
DR   OrthoDB; 1362700at2759; -.
DR   PhylomeDB; Q5M882; -.
DR   TreeFam; TF313883; -.
DR   PRO; PR:Q5M882; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000027646; Expressed in ovary and 20 other tissues.
DR   Genevisible; Q5M882; RN.
DR   GO; GO:0030681; C:multimeric ribonuclease P complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:RGD.
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; IEA:UniProtKB-EC.
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_0000128421"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95707"
SQ   SEQUENCE   221 AA;  25633 MW;  1BC37779DD9B099E CRC64;
     MKAVIYHAFS HKEAKDHDVQ ELGTQRAEAF VRAFLKQSIP HMSQQDCESH LQRKAVILEY
     FTRLKPKPRP KKKSKGLSAK QRRELRLFDI KPEQQRYSLF LPLHELWKQY IRDLCNGLKP
     DTQPQMIQAK LLKADLHGAV ISVTKSKCPS YVGVTGILLQ ETKHVFKIIT KEDHLKVIPK
     QNCVFTIEID DFISYIYGSK FQLRASERSA KKFKAKGTID L