POP5_MOUSE
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 03-AUG-2022, entry version 127.
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; Q9DB28; -.
DR PeptideAtlas; Q9DB28; -.
DR PRIDE; Q9DB28; -.
DR ProteomicsDB; 291639; -.
DR Antibodypedia; 45552; 51 antibodies from 17 providers.
DR Ensembl; ENSMUST00000081497; ENSMUSP00000080215; ENSMUSG00000060152.
DR Ensembl; ENSMUST00000135455; ENSMUSP00000118408; ENSMUSG00000060152.
DR GeneID; 117109; -.
DR KEGG; mmu:117109; -.
DR UCSC; uc008zdi.1; mouse.
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; FLDRAMG; -.
DR OrthoDB; 1492689at2759; -.
DR PhylomeDB; Q9DB28; -.
DR TreeFam; TF317496; -.
DR BioGRID-ORCS; 117109; 25 hits in 107 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 270 other tissues.
DR Genevisible; Q9DB28; MM.
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; -; 1.
DR InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR InterPro; IPR016819; RNase_P/MRP_POP5.
DR InterPro; IPR038085; Rnp2-like_sf.
DR Pfam; PF01900; RNase_P_Rpp14; 1.
DR PIRSF; PIRSF023803; Ribonuclease_P_prd; 1.
DR SUPFAM; SSF160350; SSF160350; 1.
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
