RL37A_MOUSE
ID RL37A_MOUSE Reviewed; 92 AA.
AC P61514; P12751;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=60S ribosomal protein L37a;
GN Name=Rpl37a;
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].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=8415004; DOI=10.1093/nar/21.18.4400;
RA Su Y., Babu N., Raj K., Au W.-C., Pitha P.M.;
RT "Primary sequence of the mouse ribosomal protein L37a.";
RL Nucleic Acids Res. 21:4400-4400(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 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: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000250|UniProtKB:P61513}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P61513}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61513}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL43 family.
CC {ECO:0000305}.
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DR EMBL; X73331; CAA51758.1; -; mRNA.
DR EMBL; AK003501; BAB22825.1; -; mRNA.
DR EMBL; AK011634; BAB27748.1; -; mRNA.
DR EMBL; AK012396; BAB28213.1; -; mRNA.
DR EMBL; AK012439; BAB28239.1; -; mRNA.
DR EMBL; AK012655; BAB28386.1; -; mRNA.
DR EMBL; AK014283; BAB29243.1; -; mRNA.
DR CCDS; CCDS35610.1; -.
DR PIR; S42109; S42109.
DR RefSeq; NP_033110.1; NM_009084.4.
DR PDB; 6SWA; EM; 3.10 A; n=1-92.
DR PDB; 7LS1; EM; 3.30 A; j2=1-92.
DR PDB; 7LS2; EM; 3.10 A; j2=1-92.
DR PDBsum; 6SWA; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P61514; -.
DR SMR; P61514; -.
DR BioGRID; 202984; 8.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR IntAct; P61514; 1.
DR STRING; 10090.ENSMUSP00000058919; -.
DR iPTMnet; P61514; -.
DR PhosphoSitePlus; P61514; -.
DR SwissPalm; P61514; -.
DR EPD; P61514; -.
DR jPOST; P61514; -.
DR PaxDb; P61514; -.
DR PeptideAtlas; P61514; -.
DR PRIDE; P61514; -.
DR ProteomicsDB; 299901; -.
DR TopDownProteomics; P61514; -.
DR DNASU; 19981; -.
DR Ensembl; ENSMUST00000059980; ENSMUSP00000058919; ENSMUSG00000046330.
DR GeneID; 19981; -.
DR KEGG; mmu:19981; -.
DR UCSC; uc007bkv.2; mouse.
DR CTD; 6168; -.
DR MGI; MGI:98068; Rpl37a.
DR VEuPathDB; HostDB:ENSMUSG00000046330; -.
DR eggNOG; KOG0402; Eukaryota.
DR GeneTree; ENSGT00390000016988; -.
DR HOGENOM; CLU_141199_1_0_1; -.
DR InParanoid; P61514; -.
DR OMA; ISTGIWQ; -.
DR OrthoDB; 1621758at2759; -.
DR PhylomeDB; P61514; -.
DR TreeFam; TF313068; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 19981; 27 hits in 53 CRISPR screens.
DR ChiTaRS; Rpl37a; mouse.
DR PRO; PR:P61514; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P61514; protein.
DR Bgee; ENSMUSG00000046330; Expressed in yolk sac and 233 other tissues.
DR ExpressionAtlas; P61514; baseline and differential.
DR Genevisible; P61514; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR Gene3D; 2.20.25.30; -; 1.
DR HAMAP; MF_00327; Ribosomal_L37Ae; 1.
DR InterPro; IPR002674; Ribosomal_L37ae.
DR InterPro; IPR011331; Ribosomal_L37ae/L37e.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR Pfam; PF01780; Ribosomal_L37ae; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR TIGRFAMs; TIGR00280; eL43_euk_arch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Zinc; Zinc-finger.
FT CHAIN 1..92
FT /note="60S ribosomal protein L37a"
FT /id="PRO_0000139818"
FT ZN_FING 39..60
FT /note="C4-type"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
SQ SEQUENCE 92 AA; 10275 MW; 7122AF87B0E24CF6 CRC64;
MAKRTKKVGI VGKYGTRYGA SLRKMVKKIE ISQHAKYTCS FCGKTKMKRR AVGIWHCGSC
MKTVAGGAWT YNTTSAVTVK SAIRRLKELK DQ
