ID   RPP25_RAT               Reviewed;         199 AA.
AC   Q5PPN2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Ribonuclease P protein subunit p25;
DE            Short=RNase P protein subunit p25;
GN   Name=Rpp25;
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=Ovary;
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; BC087592; AAH87592.1; -; mRNA.
DR   RefSeq; NP_001012124.1; NM_001012124.1.
DR   AlphaFoldDB; Q5PPN2; -.
DR   SMR; Q5PPN2; -.
DR   STRING; 10116.ENSRNOP00000025408; -.
DR   iPTMnet; Q5PPN2; -.
DR   PhosphoSitePlus; Q5PPN2; -.
DR   jPOST; Q5PPN2; -.
DR   PaxDb; Q5PPN2; -.
DR   Ensembl; ENSRNOT00000025410; ENSRNOP00000025408; ENSRNOG00000018812.
DR   GeneID; 315705; -.
DR   KEGG; rno:315705; -.
DR   UCSC; RGD:1305290; rat.
DR   CTD; 54913; -.
DR   RGD; 1305290; Rpp25.
DR   eggNOG; KOG2567; Eukaryota.
DR   GeneTree; ENSGT00390000002564; -.
DR   HOGENOM; CLU_096311_0_0_1; -.
DR   InParanoid; Q5PPN2; -.
DR   OMA; CGRAVTK; -.
DR   OrthoDB; 1075123at2759; -.
DR   PhylomeDB; Q5PPN2; -.
DR   TreeFam; TF325688; -.
DR   Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q5PPN2; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000018812; Expressed in ovary and 16 other tissues.
DR   Genevisible; Q5PPN2; RN.
DR   GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0000172; C:ribonuclease MRP complex; ISO:RGD.
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: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_0000237584"
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   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUL9"
SQ   SEQUENCE   199 AA;  20939 MW;  FF0CF2AD99BB5BB0 CRC64;
     MENFRKVRSE EAPAGDGDEG GSPSSGPFAD LAPGAVHMRV KEGSKIRNLL AFATASMAQP
     ATRAIVFSGC GRATTKTVTC AEILKRRLAG LHQVTRLRYR SVREVWQSLP PGPTPGQTPS
     DPAASLSVLK NVPSLAILLS KDALDPRQLG YQPPNLSPGP SSPPTVSTSK RSLGESAAGE
     GTAKRSQPEP EAENEDRTA