RPP14_MOUSE
ID RPP14_MOUSE Reviewed; 122 AA.
AC Q9CQH8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ribonuclease P protein subunit p14;
GN Name=Rpp14;
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=Embryo, and Testis;
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=C57BL/6J; TISSUE=Brain, and Eye;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 ribonucleoprotein complex that
CC generates mature tRNA molecules by cleaving their 5'-ends.
CC {ECO:0000250|UniProtKB:O95059}.
CC -!- SUBUNIT: RNase P consists of a catalytic RNA moiety and about 10
CC protein subunits; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30,
CC RPP38 and RPP40. Within the RNase P complex, POP1, POP7 and RPP25 form
CC the 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form
CC the '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. {ECO:0000250|UniProtKB:O95059}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O95059}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 2 family. {ECO:0000305}.
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DR EMBL; AK012105; BAB28036.1; -; mRNA.
DR EMBL; AK016631; BAB30347.1; -; mRNA.
DR EMBL; BC026988; AAH26988.1; -; mRNA.
DR EMBL; BC046803; AAH46803.1; -; mRNA.
DR CCDS; CCDS26809.1; -.
DR RefSeq; NP_080214.1; NM_025938.4.
DR RefSeq; XP_006518153.1; XM_006518090.2.
DR RefSeq; XP_006518154.1; XM_006518091.2.
DR AlphaFoldDB; Q9CQH8; -.
DR SMR; Q9CQH8; -.
DR IntAct; Q9CQH8; 2.
DR MINT; Q9CQH8; -.
DR STRING; 10090.ENSMUSP00000023924; -.
DR iPTMnet; Q9CQH8; -.
DR PhosphoSitePlus; Q9CQH8; -.
DR EPD; Q9CQH8; -.
DR MaxQB; Q9CQH8; -.
DR PaxDb; Q9CQH8; -.
DR PeptideAtlas; Q9CQH8; -.
DR PRIDE; Q9CQH8; -.
DR ProteomicsDB; 299946; -.
DR Antibodypedia; 69913; 17 antibodies from 4 providers.
DR DNASU; 67053; -.
DR Ensembl; ENSMUST00000023924; ENSMUSP00000023924; ENSMUSG00000023156.
DR GeneID; 67053; -.
DR KEGG; mmu:67053; -.
DR UCSC; uc007seq.2; mouse.
DR CTD; 11102; -.
DR MGI; MGI:1914303; Rpp14.
DR VEuPathDB; HostDB:ENSMUSG00000023156; -.
DR eggNOG; ENOG502S10S; Eukaryota.
DR GeneTree; ENSGT00530000065109; -.
DR HOGENOM; CLU_157358_0_0_1; -.
DR InParanoid; Q9CQH8; -.
DR OrthoDB; 1492689at2759; -.
DR PhylomeDB; Q9CQH8; -.
DR TreeFam; TF324711; -.
DR BioGRID-ORCS; 67053; 23 hits in 74 CRISPR screens.
DR PRO; PR:Q9CQH8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CQH8; protein.
DR Bgee; ENSMUSG00000023156; Expressed in ectoplacental cone and 278 other tissues.
DR ExpressionAtlas; Q9CQH8; baseline and differential.
DR Genevisible; Q9CQH8; MM.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0004526; F:ribonuclease P activity; ISO:MGI.
DR GO; GO:0033204; F:ribonuclease P RNA binding; ISS:UniProtKB.
DR GO; GO:0001682; P:tRNA 5'-leader removal; ISS:UniProtKB.
DR Gene3D; 3.30.70.3250; -; 1.
DR InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR InterPro; IPR038085; Rnp2-like_sf.
DR Pfam; PF01900; RNase_P_Rpp14; 1.
DR SUPFAM; SSF160350; SSF160350; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; tRNA processing.
FT CHAIN 1..122
FT /note="Ribonuclease P protein subunit p14"
FT /id="PRO_0000140011"
SQ SEQUENCE 122 AA; 13565 MW; 8B66600CB7AB6239 CRC64;
MPATAYERVV YKSPSEYHYM KVCLEFQEHG VGLNVAQFKQ LLVSALRDLF GEVGAALPVD
VLTYDEKTLS AILRICSSGL VKLWSSLTLF GAYKSKKCAF RVIQVSPFLL ALSGNSREQV
LD