RM18_MOUSE
ID RM18_MOUSE Reviewed; 180 AA.
AC Q9CQL5; Q9D6N7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=39S ribosomal protein L18, mitochondrial;
DE Short=L18mt;
DE Short=MRP-L18;
DE Flags: Precursor;
GN Name=Mrpl18;
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=Heart, Stomach, and Tongue;
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].
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=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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: Together with thiosulfate sulfurtransferase (TST), acts as a
CC mitochondrial import factor for the cytosolic 5S rRNA. The precursor
CC form shows RNA chaperone activity; is able to fold the 5S rRNA into an
CC import-competent conformation that is recognized by rhodanese (TST).
CC Both the cytoplasmic and mitochondrial forms are able to bind to the
CC helix IV-loop D in the gamma domain of the 5S rRNA (By similarity).
CC {ECO:0000250|UniProtKB:Q9H0U6}.
CC -!- SUBUNIT: Component of the mitochondrial ribosome large subunit (39S)
CC which comprises a 16S rRNA and about 50 distinct proteins.
CC {ECO:0000250|UniProtKB:Q9H0U6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H0U6}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK003104; BAB22567.1; -; mRNA.
DR EMBL; AK008680; BAB25828.1; -; mRNA.
DR EMBL; AK010150; BAB26735.1; -; mRNA.
DR EMBL; BC011425; AAH11425.1; -; mRNA.
DR CCDS; CCDS28396.1; -.
DR RefSeq; NP_080586.1; NM_026310.3.
DR AlphaFoldDB; Q9CQL5; -.
DR SMR; Q9CQL5; -.
DR BioGRID; 212363; 21.
DR ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR STRING; 10090.ENSMUSP00000078123; -.
DR PhosphoSitePlus; Q9CQL5; -.
DR EPD; Q9CQL5; -.
DR MaxQB; Q9CQL5; -.
DR PaxDb; Q9CQL5; -.
DR PeptideAtlas; Q9CQL5; -.
DR PRIDE; Q9CQL5; -.
DR ProteomicsDB; 299908; -.
DR Antibodypedia; 33462; 126 antibodies from 21 providers.
DR DNASU; 67681; -.
DR Ensembl; ENSMUST00000079121; ENSMUSP00000078123; ENSMUSG00000057388.
DR GeneID; 67681; -.
DR KEGG; mmu:67681; -.
DR UCSC; uc008alj.1; mouse.
DR CTD; 29074; -.
DR MGI; MGI:1914931; Mrpl18.
DR VEuPathDB; HostDB:ENSMUSG00000057388; -.
DR eggNOG; KOG3333; Eukaryota.
DR GeneTree; ENSGT00390000006394; -.
DR HOGENOM; CLU_108540_0_0_1; -.
DR InParanoid; Q9CQL5; -.
DR OMA; TSEWAIK; -.
DR OrthoDB; 1336080at2759; -.
DR PhylomeDB; Q9CQL5; -.
DR TreeFam; TF313292; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 67681; 19 hits in 71 CRISPR screens.
DR ChiTaRS; Mrpl18; mouse.
DR PRO; PR:Q9CQL5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CQL5; protein.
DR Bgee; ENSMUSG00000057388; Expressed in primary oocyte and 63 other tissues.
DR Genevisible; Q9CQL5; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008097; F:5S rRNA binding; ISS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0035928; P:rRNA import into mitochondrion; ISS:UniProtKB.
DR Gene3D; 3.30.420.80; -; 1.
DR InterPro; IPR005484; Ribosomal_L18.
DR InterPro; IPR036967; Ribosomal_S11_sf.
DR PANTHER; PTHR12899; PTHR12899; 1.
DR Pfam; PF00861; Ribosomal_L18p; 1.
PE 1: Evidence at protein level;
KW Chaperone; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..180
FT /note="39S ribosomal protein L18, mitochondrial"
FT /id="PRO_0000030557"
FT CONFLICT 29
FT /note="V -> A (in Ref. 1; BAB26735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20677 MW; 7B7759EF8A5315DD CRC64;
MALRPRFWKC LSVCRKLECG FAALSTSSVP AVQPDVESKE NEAVAPEFTN RNPRNLELLG
VARKERGWAT VWPNREFWHR LRVVKTQHHV EAFVEHLNGQ VVVSASTREW AIKKHLYSTR
NVVACESIGR VLAQRCLEAG INFMVYQPTP WEASSDSIKR LQNAMTESGV MLREPRRIYE
