RT27_MOUSE
ID RT27_MOUSE Reviewed; 415 AA.
AC Q8BK72; E9QKZ5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=28S ribosomal protein S27, mitochondrial {ECO:0000305};
DE Short=MRP-S27;
DE Short=S27mt;
DE AltName: Full=Mitochondrial ribosomal protein S27 {ECO:0000312|MGI:MGI:1919064};
DE Flags: Precursor;
GN Name=Mrps27 {ECO:0000312|MGI:MGI:1919064};
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] {ECO:0000312|EMBL:BAC36116.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36116.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAC36116.1};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC 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).
RN [4]
RP INTERACTION WITH METTL17.
RX PubMed=31487196; DOI=10.1096/fj.201901331r;
RA Shi Z., Xu S., Xing S., Yao K., Zhang L., Xue L., Zhou P., Wang M., Yan G.,
RA Yang P., Liu J., Hu Z., Lan F.;
RT "Mettl17, a regulator of mitochondrial ribosomal RNA modifications, is
RT required for the translation of mitochondrial coding genes.";
RL FASEB J. 33:13040-13050(2019).
CC -!- FUNCTION: RNA-binding component of the mitochondrial small ribosomal
CC subunit (mt-SSU) that plays a role in mitochondrial protein synthesis.
CC Stimulates mitochondrial mRNA translation of subunit components of the
CC mitochondrial electron transport chain. Binds to the mitochondrial 12S
CC rRNA (12S mt-rRNA) and tRNA(Glu). Overexpressed in hepatocellular
CC carcinoma tissues compared with adjacent non-tumoral liver tissues.
CC {ECO:0000250|UniProtKB:Q92552}.
CC -!- SUBUNIT: Component of the mitochondrial ribosome small subunit (28S)
CC which comprises a 12S rRNA and about 30 distinct proteins (By
CC similarity). Interacts with NOA1 (By similarity). Interacts with MIEF1
CC upstream open reading frame protein (By similarity). Interacts with
CC METTL17 (PubMed:31487196). {ECO:0000250|UniProtKB:Q92552,
CC ECO:0000269|PubMed:31487196}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92552}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q92552}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS27 family. {ECO:0000305}.
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DR EMBL; AK076008; BAC36116.1; -; mRNA.
DR EMBL; AC132347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS26722.1; -.
DR RefSeq; NP_776118.2; NM_173757.3.
DR AlphaFoldDB; Q8BK72; -.
DR SMR; Q8BK72; -.
DR BioGRID; 230042; 13.
DR ComplexPortal; CPX-5301; 28S mitochondrial small ribosomal subunit.
DR STRING; 10090.ENSMUSP00000062326; -.
DR iPTMnet; Q8BK72; -.
DR PhosphoSitePlus; Q8BK72; -.
DR EPD; Q8BK72; -.
DR jPOST; Q8BK72; -.
DR MaxQB; Q8BK72; -.
DR PaxDb; Q8BK72; -.
DR PeptideAtlas; Q8BK72; -.
DR PRIDE; Q8BK72; -.
DR ProteomicsDB; 260860; -.
DR Antibodypedia; 24192; 406 antibodies from 28 providers.
DR DNASU; 218506; -.
DR Ensembl; ENSMUST00000052249; ENSMUSP00000062326; ENSMUSG00000041632.
DR GeneID; 218506; -.
DR KEGG; mmu:218506; -.
DR UCSC; uc007rpn.1; mouse.
DR CTD; 23107; -.
DR MGI; MGI:1919064; Mrps27.
DR VEuPathDB; HostDB:ENSMUSG00000041632; -.
DR eggNOG; KOG4570; Eukaryota.
DR GeneTree; ENSGT00390000007246; -.
DR HOGENOM; CLU_065381_0_0_1; -.
DR InParanoid; Q8BK72; -.
DR OMA; ANLMDRT; -.
DR OrthoDB; 793417at2759; -.
DR PhylomeDB; Q8BK72; -.
DR TreeFam; TF316446; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 218506; 23 hits in 72 CRISPR screens.
DR ChiTaRS; Mrps27; mouse.
DR PRO; PR:Q8BK72; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BK72; protein.
DR Bgee; ENSMUSG00000041632; Expressed in ear vesicle and 247 other tissues.
DR ExpressionAtlas; Q8BK72; baseline and differential.
DR Genevisible; Q8BK72; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0097177; F:mitochondrial ribosome binding; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR019266; MRPS27.
DR InterPro; IPR034913; MRPS27/PTCD2.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR21393; PTHR21393; 1.
DR Pfam; PF10037; MRP-S27; 1.
DR PROSITE; PS51375; PPR; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Mitochondrion; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Transit peptide; Translation regulation; tRNA-binding.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..415
FT /note="28S ribosomal protein S27, mitochondrial"
FT /id="PRO_0000261586"
FT REPEAT 105..139
FT /note="PPR 1"
FT REPEAT 140..175
FT /note="PPR 2"
FT COILED 369..415
FT /evidence="ECO:0000255"
FT CONFLICT 81
FT /note="S -> C (in Ref. 1; BAC36116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47779 MW; 188A19628C12CA26 CRC64;
MAAPMVRCGM LLARRLDASR LCLAGKRCLL SAAYVDSHQW EAREKEEYHL ADLASLMDKA
YERKLPVSSL SISRFVDNIA SREDLDSAEY YLYKFRHSPN CWYLRDWTIH SWIRQCLKYG
AQDKALYTLV NKVQYGIFPD NFTFNLLMDY FIKKGNYKDA LSVVFEIMMQ EAFDVPSTQF
LSLYVLYRCL AEKTELTWEE ERDFGASLLL SGLKQRNTVG LSSQLYGYAL LGKVELQRGV
RAVYHGMPLM WTPGYLDRAL QVMERVASSP EDLKLGREVL DVLDGVLKVV TSPDVQTSEA
QPQEGEDGLG SANLVEQLDT EEPEQSKLPR YLERFQASRS KLQELNRVES ESLLTLTTQL
VKEKLPACEA EDLATYEQKL REWHLERVQL IQREQEQREK AKQEYQALSA AEKAA
