MASU1_MOUSE
ID MASU1_MOUSE Reviewed; 228 AA.
AC Q9CWV0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Mitochondrial assembly of ribosomal large subunit protein 1;
GN Name=Malsu1;
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=Medulla oblongata;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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: Required for normal mitochondrial ribosome function and
CC mitochondrial translation. May play a role in ribosome biogenesis by
CC preventing premature association of the 28S and 39S ribosomal subunits.
CC Interacts with mitochondrial ribosomal protein L14 (MRPL14), probably
CC blocking formation of intersubunit bridge B8, preventing association of
CC the 28S and 39S ribosomal subunits. Addition to isolated mitochondrial
CC ribosomal subunits partially inhibits translation, probably by
CC interfering with the association of the 28S and 39S ribosomal subunits
CC and the formation of functional ribosomes. May also participate in the
CC assembly and/or regulation of the stability of the large subunit of the
CC mitochondrial ribosome. May function as a ribosomal silencing factor.
CC {ECO:0000250|UniProtKB:Q96EH3}.
CC -!- SUBUNIT: Associates with the mitochondrial ribosome large subunit (39S)
CC via interaction with MRPL12 and/or MRPL14. The interaction generates
CC steric hindrance that is expected to prevent premature association of
CC the 28S and 39S ribosomal subunits. Identified in a complex composed of
CC MALSU1, MIEF1 upstream open reading frame protein and NDUFAB1; within
CC the trimeric complex, MIEF1 upstream open reading frame protein
CC functions as a bridging scaffold that interacts with MALSU1 on one
CC side, and with NDUFAB1 on the other side. Interacts with MRPL12 and
CC MRPL14. {ECO:0000250|UniProtKB:Q96EH3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q96EH3}. Note=Colocalizes with MRPL12 and/or
CC MRPL14. {ECO:0000250|UniProtKB:Q96EH3}.
CC -!- SIMILARITY: Belongs to the Iojap/RsfS family. {ECO:0000305}.
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DR EMBL; AK010366; BAB26886.1; -; mRNA.
DR EMBL; AK031878; BAC27589.1; -; mRNA.
DR CCDS; CCDS51768.1; -.
DR RefSeq; NP_083629.1; NM_029353.1.
DR AlphaFoldDB; Q9CWV0; -.
DR SMR; Q9CWV0; -.
DR BioGRID; 217601; 2.
DR STRING; 10090.ENSMUSP00000122941; -.
DR iPTMnet; Q9CWV0; -.
DR PhosphoSitePlus; Q9CWV0; -.
DR EPD; Q9CWV0; -.
DR MaxQB; Q9CWV0; -.
DR PaxDb; Q9CWV0; -.
DR PRIDE; Q9CWV0; -.
DR ProteomicsDB; 287314; -.
DR Antibodypedia; 12100; 55 antibodies from 15 providers.
DR Ensembl; ENSMUST00000128616; ENSMUSP00000122941; ENSMUSG00000029815.
DR GeneID; 75593; -.
DR KEGG; mmu:75593; -.
DR UCSC; uc009bwg.2; mouse.
DR CTD; 115416; -.
DR MGI; MGI:1922843; Malsu1.
DR VEuPathDB; HostDB:ENSMUSG00000029815; -.
DR eggNOG; KOG3212; Eukaryota.
DR GeneTree; ENSGT00390000015035; -.
DR InParanoid; Q9CWV0; -.
DR OMA; HLKCKHD; -.
DR OrthoDB; 1590818at2759; -.
DR PhylomeDB; Q9CWV0; -.
DR BioGRID-ORCS; 75593; 9 hits in 72 CRISPR screens.
DR ChiTaRS; Malsu1; mouse.
DR PRO; PR:Q9CWV0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CWV0; protein.
DR Bgee; ENSMUSG00000029815; Expressed in gastrocnemius medialis and 217 other tissues.
DR ExpressionAtlas; Q9CWV0; baseline and differential.
DR Genevisible; Q9CWV0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0070130; P:negative regulation of mitochondrial translation; ISO:MGI.
DR GO; GO:0090071; P:negative regulation of ribosome biogenesis; IBA:GO_Central.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR HAMAP; MF_01477; Iojap_RsfS; 1.
DR InterPro; IPR004394; Iojap/RsfS/C7orf30.
DR InterPro; IPR043519; NT_sf.
DR PANTHER; PTHR21043; PTHR21043; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00090; rsfS_iojap_ybeB; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..228
FT /note="Mitochondrial assembly of ribosomal large subunit
FT protein 1"
FT /id="PRO_0000228109"
FT REGION 53..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 228 AA; 26020 MW; F4DAEE582D1A0288 CRC64;
MGPGWSPARR LWPLLWRRAV FQRAGPAMAS VPWLPRLAER WLPARPATCL TPSLTRGLHH
GPQPEERTAG DARLQPGPAD HIGAKFDIDM LVSLLRQENA RDICVIQVPP EMRYTDYFVI
GSGTSTRHLH AMVHYLVKMY KHLKCRSDPY VKIEGKDADD WLCVDFGSMV IHLMLPETRE
TYELEKLWTL RSFDDQLAQI AAETLPEDFI LGLEDDTSSL TPVEFKCK
