RT02_MOUSE
ID RT02_MOUSE Reviewed; 291 AA.
AC Q924T2; A2AK29; Q3TMF8;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=28S ribosomal protein S2, mitochondrial;
DE Short=MRP-S2;
DE Short=S2mt;
GN Name=Mrps2;
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 [MRNA].
RX PubMed=11402041; DOI=10.1074/jbc.m103236200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Proteomic analysis of the mammalian mitochondrial ribosome. Identification
RT of protein components in the 28S small subunit.";
RL J. Biol. Chem. 276:33181-33195(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Required for mitoribosome formation and stability, and
CC mitochondrial translation. {ECO:0000250|UniProtKB:Q9Y399}.
CC -!- SUBUNIT: Component of the mitochondrial ribosome small subunit (28S)
CC which comprises a 12S rRNA and about 30 distinct proteins.
CC {ECO:0000250|UniProtKB:Q9Y399}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y399}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000305}.
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DR EMBL; AB055389; BAB62530.1; -; mRNA.
DR EMBL; AK077219; BAC36691.1; -; mRNA.
DR EMBL; AK154131; BAE32396.1; -; mRNA.
DR EMBL; AK165956; BAE38484.1; -; mRNA.
DR EMBL; AL772249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060503; AAH60503.1; -; mRNA.
DR CCDS; CCDS15838.1; -.
DR RefSeq; NP_001159503.2; NM_001166031.2.
DR RefSeq; NP_536700.3; NM_080452.3.
DR AlphaFoldDB; Q924T2; -.
DR SMR; Q924T2; -.
DR BioGRID; 228246; 24.
DR ComplexPortal; CPX-5301; 28S mitochondrial small ribosomal subunit.
DR STRING; 10090.ENSMUSP00000036725; -.
DR iPTMnet; Q924T2; -.
DR PhosphoSitePlus; Q924T2; -.
DR SwissPalm; Q924T2; -.
DR EPD; Q924T2; -.
DR MaxQB; Q924T2; -.
DR PaxDb; Q924T2; -.
DR PeptideAtlas; Q924T2; -.
DR PRIDE; Q924T2; -.
DR ProteomicsDB; 261000; -.
DR Antibodypedia; 32046; 240 antibodies from 25 providers.
DR DNASU; 118451; -.
DR Ensembl; ENSMUST00000038600; ENSMUSP00000036725; ENSMUSG00000035772.
DR GeneID; 118451; -.
DR KEGG; mmu:118451; -.
DR UCSC; uc008iyg.1; mouse.
DR CTD; 51116; -.
DR MGI; MGI:2153089; Mrps2.
DR VEuPathDB; HostDB:ENSMUSG00000035772; -.
DR eggNOG; KOG0832; Eukaryota.
DR GeneTree; ENSGT00390000017382; -.
DR HOGENOM; CLU_040318_3_0_1; -.
DR InParanoid; Q924T2; -.
DR OMA; SYIDRAY; -.
DR OrthoDB; 573006at2759; -.
DR PhylomeDB; Q924T2; -.
DR TreeFam; TF313480; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 118451; 22 hits in 73 CRISPR screens.
DR ChiTaRS; Mrps2; mouse.
DR PRO; PR:Q924T2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q924T2; protein.
DR Bgee; ENSMUSG00000035772; Expressed in primitive streak and 258 other tissues.
DR Genevisible; Q924T2; MM.
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:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0061668; P:mitochondrial ribosome assembly; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_00291_B; Ribosomal_S2_B; 1.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR005706; Ribosomal_S2_bac/mit/plastid.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR12534; PTHR12534; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..291
FT /note="28S ribosomal protein S2, mitochondrial"
FT /id="PRO_0000134344"
FT REGION 27..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 32313 MW; 33CFE4731BCEBADD CRC64;
MAPAPAVLTR LLCAGVRRWP GFLQKAIPGP AEQNGRKVTG APVPAVSEPQ DGDDFQSRIL
DTPLQHSDFF NVKELFSVKS LFEARVHLGH KAGCRHRFME PYIFGNRLGQ DIIDLDQTAL
NLQLALNFTA HVAYRKGIIL FVSRNRQFSH LIETTAQACG EYAHTRYFKG GLLTNAQLLF
GPSVRLPDLI IFLHTLNNVF EPHVAVRDAA KMNIPTVGIV DTNCNPCLIT YPIPGNDDSP
QAIQLFCKLF RTTINRAKEK RRQMEALHRL QSPKGSEGSG TSPVPDKSHS P
