ID   POP5_MOUSE              Reviewed;         169 AA.
AC   Q9DB28; Q9CSC3; Q9CSL4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Ribonuclease P/MRP protein subunit POP5;
GN   Name=Pop5;
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, and Embryo;
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=Colon;
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).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-159, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Liver, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Component of ribonuclease P, a protein complex that generates
CC       mature tRNA molecules by cleaving their 5'-ends. Also a component of
CC       the MRP ribonuclease complex, which cleaves pre-rRNA sequences.
CC       {ECO:0000250|UniProtKB:Q969H6}.
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:Q969H6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q969H6}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB28294.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK005290; BAB23935.1; -; mRNA.
DR   EMBL; AK012523; BAB28294.1; ALT_FRAME; mRNA.
DR   EMBL; AK013257; BAB28751.1; -; mRNA.
DR   EMBL; BC022670; AAH22670.1; -; mRNA.
DR   CCDS; CCDS19583.1; -.
DR   RefSeq; NP_080674.1; NM_026398.4.
DR   AlphaFoldDB; Q9DB28; -.
DR   SMR; Q9DB28; -.
DR   IntAct; Q9DB28; 1.
DR   STRING; 10090.ENSMUSP00000080215; -.
DR   iPTMnet; Q9DB28; -.
DR   PhosphoSitePlus; Q9DB28; -.
DR   EPD; Q9DB28; -.
DR   MaxQB; Q9DB28; -.
DR   PaxDb; 10090-ENSMUSP00000080215; -.
DR   PeptideAtlas; Q9DB28; -.
DR   ProteomicsDB; 291639; -.
DR   Pumba; Q9DB28; -.
DR   Antibodypedia; 45552; 59 antibodies from 18 providers.
DR   Ensembl; ENSMUST00000081497.13; ENSMUSP00000080215.7; ENSMUSG00000060152.15.
DR   Ensembl; ENSMUST00000135455.2; ENSMUSP00000118408.2; ENSMUSG00000060152.15.
DR   GeneID; 117109; -.
DR   KEGG; mmu:117109; -.
DR   UCSC; uc008zdi.1; mouse.
DR   AGR; MGI:2151221; -.
DR   CTD; 51367; -.
DR   MGI; MGI:2151221; Pop5.
DR   VEuPathDB; HostDB:ENSMUSG00000060152; -.
DR   eggNOG; KOG4639; Eukaryota.
DR   GeneTree; ENSGT00390000012331; -.
DR   HOGENOM; CLU_086710_2_0_1; -.
DR   InParanoid; Q9DB28; -.
DR   OMA; MQNYLDK; -.
DR   OrthoDB; 2787248at2759; -.
DR   PhylomeDB; Q9DB28; -.
DR   TreeFam; TF317496; -.
DR   BioGRID-ORCS; 117109; 25 hits in 112 CRISPR screens.
DR   ChiTaRS; Pop5; mouse.
DR   PRO; PR:Q9DB28; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9DB28; Protein.
DR   Bgee; ENSMUSG00000060152; Expressed in dentate gyrus of hippocampal formation granule cell and 273 other cell types or tissues.
DR   GO; GO:0030681; C:multimeric ribonuclease P complex; ISO:MGI.
DR   GO; GO:0005655; C:nucleolar ribonuclease P complex; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0000172; C:ribonuclease MRP complex; ISA:MGI.
DR   GO; GO:0000171; F:ribonuclease MRP activity; ISA:MGI.
DR   GO; GO:0004526; F:ribonuclease P activity; IDA:MGI.
DR   GO; GO:0033204; F:ribonuclease P RNA binding; ISS:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; ISA:MGI.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; ISS:UniProtKB.
DR   GO; GO:0008033; P:tRNA processing; IDA:MGI.
DR   Gene3D; 3.30.70.3250; Ribonuclease P, Pop5 subunit; 1.
DR   InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR   InterPro; IPR016819; RNase_P/MRP_POP5.
DR   InterPro; IPR038085; Rnp2-like_sf.
DR   PANTHER; PTHR48326; RIBONUCLEASE P_MRP PROTEIN SUBUNIT POP5; 1.
DR   PANTHER; PTHR48326:SF1; RIBONUCLEASE P_MRP PROTEIN SUBUNIT POP5; 1.
DR   Pfam; PF01900; RNase_P_Rpp14; 1.
DR   PIRSF; PIRSF023803; Ribonuclease_P_prd; 1.
DR   SUPFAM; SSF160350; Rnp2-like; 1.
DR   Genevisible; Q9DB28; MM.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; rRNA processing;
KW   tRNA processing.
FT   CHAIN           1..169
FT                   /note="Ribonuclease P/MRP protein subunit POP5"
FT                   /id="PRO_0000239008"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        2
FT                   /note="V -> R (in Ref. 1; BAB28751)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   169 AA;  19285 MW;  8334DECD7665A48D CRC64;
     MVRFKHRYLL CELVSEDARC RLSLDDRVLG GLVRDTIARV HGAFGAAACS VGFAVRYLNA
     YTGVVLLRCR KDFYQLVWSA LPFITYLENK GHRYPCFFNT LHVGGTIRTC QKFLIQYNRR
     QLLILLQNCT DEGEREAIKK SVSRSCLLDR EPVEELSDSA GEEVAEAME
//