RM03_HUMAN
ID RM03_HUMAN Reviewed; 348 AA.
AC P09001; Q6IBT2;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=39S ribosomal protein L3, mitochondrial;
DE Short=L3mt;
DE Short=MRP-L3;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL3m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL3; Synonyms=MRL3, RPML3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2891103; DOI=10.1093/nar/15.21.8919;
RA Ou J.-H., Yen T.S.B., Wang Y.-F., Kam W.K., Rutter W.;
RT "Cloning and characterization of a human ribosomal protein gene with
RT enhanced expression in fetal and neoplastic cells.";
RL Nucleic Acids Res. 15:8919-8934(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-40, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [7] {ECO:0007744|PDB:3J7Y}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25278503; DOI=10.1126/science.1258026;
RA Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G.,
RA Scheres S.H., Ramakrishnan V.;
RT "Structure of the large ribosomal subunit from human mitochondria.";
RL Science 346:718-722(2014).
RN [8] {ECO:0007744|PDB:3J9M}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25838379; DOI=10.1126/science.aaa1193;
RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT "Ribosome. The structure of the human mitochondrial ribosome.";
RL Science 348:95-98(2015).
RN [9] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=28892042; DOI=10.1038/nsmb.3464;
RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA Amunts A., Ramakrishnan V.;
RT "Structures of the human mitochondrial ribosome in native states of
RT assembly.";
RL Nat. Struct. Mol. Biol. 24:866-869(2017).
RN [10]
RP VARIANT COXPD9 ARG-317.
RX PubMed=21786366; DOI=10.1002/humu.21562;
RA Galmiche L., Serre V., Beinat M., Assouline Z., Lebre A.S., Chretien D.,
RA Nietschke P., Benes V., Boddaert N., Sidi D., Brunelle F., Rio M.,
RA Munnich A., Rotig A.;
RT "Exome sequencing identifies MRPL3 mutation in mitochondrial
RT cardiomyopathy.";
RL Hum. Mutat. 32:1225-1231(2011).
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature
CC mammalian 55S mitochondrial ribosomes consist of a small (28S) and a
CC large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA
CC (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains
CC a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA
CC (mt-tRNA(Val)), which plays an integral structural role, and 52
CC different proteins. {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 9 (COXPD9)
CC [MIM:614582]: A mitochondrial disease characterized by failure to
CC thrive, poor feeding, hypertrophic cardiomyopathy, hepatomegaly, and
CC psychomotor retardation. Death in infancy has been observed in some
CC cases. {ECO:0000269|PubMed:21786366}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000305}.
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DR EMBL; X06323; CAA29639.1; -; mRNA.
DR EMBL; CR456720; CAG33001.1; -; mRNA.
DR EMBL; CH471052; EAW79209.1; -; Genomic_DNA.
DR EMBL; BC003375; AAH03375.1; -; mRNA.
DR CCDS; CCDS3071.1; -.
DR PIR; A27294; R5HUL3.
DR RefSeq; NP_009139.1; NM_007208.3.
DR PDB; 3J7Y; EM; 3.40 A; E=1-348.
DR PDB; 3J9M; EM; 3.50 A; E=1-348.
DR PDB; 5OOL; EM; 3.06 A; E=1-348.
DR PDB; 5OOM; EM; 3.03 A; E=1-348.
DR PDB; 6I9R; EM; 3.90 A; E=1-348.
DR PDB; 6NU2; EM; 3.90 A; E=45-348.
DR PDB; 6NU3; EM; 4.40 A; E=1-348.
DR PDB; 6VLZ; EM; 2.97 A; E=1-348.
DR PDB; 6VMI; EM; 2.96 A; E=1-348.
DR PDB; 6ZM5; EM; 2.89 A; E=1-348.
DR PDB; 6ZM6; EM; 2.59 A; E=1-348.
DR PDB; 6ZS9; EM; 4.00 A; XE=1-348.
DR PDB; 6ZSA; EM; 4.00 A; XE=1-348.
DR PDB; 6ZSB; EM; 4.50 A; XE=1-348.
DR PDB; 6ZSC; EM; 3.50 A; XE=1-348.
DR PDB; 6ZSD; EM; 3.70 A; XE=1-348.
DR PDB; 6ZSE; EM; 5.00 A; XE=1-348.
DR PDB; 6ZSG; EM; 4.00 A; XE=1-348.
DR PDB; 7A5F; EM; 4.40 A; E3=1-348.
DR PDB; 7A5G; EM; 4.33 A; E3=1-348.
DR PDB; 7A5H; EM; 3.30 A; E=1-348.
DR PDB; 7A5I; EM; 3.70 A; E3=1-348.
DR PDB; 7A5J; EM; 3.10 A; E=1-348.
DR PDB; 7A5K; EM; 3.70 A; E3=1-348.
DR PDB; 7L08; EM; 3.49 A; E=1-348.
DR PDB; 7L20; EM; 3.15 A; E=1-348.
DR PDB; 7O9K; EM; 3.10 A; E=1-348.
DR PDB; 7O9M; EM; 2.50 A; E=1-348.
DR PDB; 7ODR; EM; 2.90 A; E=1-348.
DR PDB; 7ODS; EM; 3.10 A; E=1-348.
DR PDB; 7ODT; EM; 3.10 A; E=1-348.
DR PDB; 7OF0; EM; 2.20 A; E=1-348.
DR PDB; 7OF2; EM; 2.70 A; E=1-348.
DR PDB; 7OF3; EM; 2.70 A; E=1-348.
DR PDB; 7OF4; EM; 2.70 A; E=1-348.
DR PDB; 7OF5; EM; 2.90 A; E=1-348.
DR PDB; 7OF6; EM; 2.60 A; E=1-348.
DR PDB; 7OF7; EM; 2.50 A; E=1-348.
DR PDB; 7OG4; EM; 3.80 A; XE=1-348.
DR PDB; 7OI6; EM; 5.70 A; E=1-348.
DR PDB; 7OI7; EM; 3.50 A; E=1-348.
DR PDB; 7OI8; EM; 3.50 A; E=1-348.
DR PDB; 7OI9; EM; 3.30 A; E=1-348.
DR PDB; 7OIA; EM; 3.20 A; E=1-348.
DR PDB; 7OIB; EM; 3.30 A; E=1-348.
DR PDB; 7OIC; EM; 3.10 A; E=1-348.
DR PDB; 7OID; EM; 3.70 A; E=1-348.
DR PDB; 7OIE; EM; 3.50 A; E=1-348.
DR PDB; 7PD3; EM; 3.40 A; E=1-348.
DR PDB; 7QH6; EM; 3.08 A; E=1-348.
DR PDBsum; 3J7Y; -.
DR PDBsum; 3J9M; -.
DR PDBsum; 5OOL; -.
DR PDBsum; 5OOM; -.
DR PDBsum; 6I9R; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
DR PDBsum; 6VLZ; -.
DR PDBsum; 6VMI; -.
DR PDBsum; 6ZM5; -.
DR PDBsum; 6ZM6; -.
DR PDBsum; 6ZS9; -.
DR PDBsum; 6ZSA; -.
DR PDBsum; 6ZSB; -.
DR PDBsum; 6ZSC; -.
DR PDBsum; 6ZSD; -.
DR PDBsum; 6ZSE; -.
DR PDBsum; 6ZSG; -.
DR PDBsum; 7A5F; -.
DR PDBsum; 7A5G; -.
DR PDBsum; 7A5H; -.
DR PDBsum; 7A5I; -.
DR PDBsum; 7A5J; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7L20; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF2; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF4; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF6; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OG4; -.
DR PDBsum; 7OI6; -.
DR PDBsum; 7OI7; -.
DR PDBsum; 7OI8; -.
DR PDBsum; 7OI9; -.
DR PDBsum; 7OIA; -.
DR PDBsum; 7OIB; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7OID; -.
DR PDBsum; 7OIE; -.
DR PDBsum; 7PD3; -.
DR PDBsum; 7QH6; -.
DR AlphaFoldDB; P09001; -.
DR SMR; P09001; -.
DR BioGRID; 116390; 176.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; P09001; -.
DR IntAct; P09001; 56.
DR MINT; P09001; -.
DR STRING; 9606.ENSP00000264995; -.
DR GlyGen; P09001; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09001; -.
DR PhosphoSitePlus; P09001; -.
DR SwissPalm; P09001; -.
DR BioMuta; MRPL3; -.
DR EPD; P09001; -.
DR jPOST; P09001; -.
DR MassIVE; P09001; -.
DR MaxQB; P09001; -.
DR PaxDb; P09001; -.
DR PeptideAtlas; P09001; -.
DR PRIDE; P09001; -.
DR ProteomicsDB; 52183; -.
DR Antibodypedia; 33349; 200 antibodies from 33 providers.
DR DNASU; 11222; -.
DR Ensembl; ENST00000264995.8; ENSP00000264995.2; ENSG00000114686.9.
DR GeneID; 11222; -.
DR KEGG; hsa:11222; -.
DR MANE-Select; ENST00000264995.8; ENSP00000264995.2; NM_007208.4; NP_009139.1.
DR UCSC; uc003eoh.4; human.
DR CTD; 11222; -.
DR DisGeNET; 11222; -.
DR GeneCards; MRPL3; -.
DR HGNC; HGNC:10379; MRPL3.
DR HPA; ENSG00000114686; Low tissue specificity.
DR MalaCards; MRPL3; -.
DR MIM; 607118; gene.
DR MIM; 614582; phenotype.
DR neXtProt; NX_P09001; -.
DR OpenTargets; ENSG00000114686; -.
DR Orphanet; 319509; Combined oxidative phosphorylation defect type 9.
DR PharmGKB; PA30960; -.
DR VEuPathDB; HostDB:ENSG00000114686; -.
DR eggNOG; KOG3141; Eukaryota.
DR GeneTree; ENSGT00390000011422; -.
DR HOGENOM; CLU_044142_1_1_1; -.
DR InParanoid; P09001; -.
DR OMA; FRDSGVM; -.
DR OrthoDB; 1269775at2759; -.
DR PhylomeDB; P09001; -.
DR TreeFam; TF105634; -.
DR PathwayCommons; P09001; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; P09001; -.
DR SIGNOR; P09001; -.
DR BioGRID-ORCS; 11222; 291 hits in 1085 CRISPR screens.
DR ChiTaRS; MRPL3; human.
DR GeneWiki; MRPL3; -.
DR GenomeRNAi; 11222; -.
DR Pharos; P09001; Tbio.
DR PRO; PR:P09001; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P09001; protein.
DR Bgee; ENSG00000114686; Expressed in secondary oocyte and 212 other tissues.
DR ExpressionAtlas; P09001; baseline and differential.
DR Genevisible; P09001; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR11229; PTHR11229; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR TIGRFAMs; TIGR03625; L3_bact; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Mitochondrion;
KW Primary mitochondrial disease; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 41..348
FT /note="39S ribosomal protein L3, mitochondrial"
FT /id="PRO_0000077253"
FT VARIANT 261
FT /note="M -> T (in dbSNP:rs2291381)"
FT /id="VAR_020108"
FT VARIANT 317
FT /note="P -> R (in COXPD9; dbSNP:rs387906962)"
FT /evidence="ECO:0000269|PubMed:21786366"
FT /id="VAR_066676"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 99..111
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 140..151
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:7OIA"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:5OOL"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 264..277
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:7OI9"
SQ SEQUENCE 348 AA; 38633 MW; 6DE6B5BD6BD72E32 CRC64;
MPGWRLLTQV GAQVLGRLGD GLGAALGPGN RTHIWLFVRG LHGKSGTWWD EHLSEENVPF
IKQLVSDEDK AQLASKLCPL KDEPWPIHPW EPGSFRVGLI ALKLGMMPLW TKDGQKHVVT
LLQVQDCHVL KYTSKENCNG KMATLSVGGK TVSRFRKATS ILEFYRELGL PPKQTVKIFN
ITDNAAIKPG TPLYAAHFRP GQYVDVTAKT IGKGFQGVMK RWGFKGQPAT HGQTKTHRRP
GAVATGDIGR VWPGTKMPGK MGNIYRTEYG LKVWRINTKH NIIYVNGSVP GHKNCLVKVK
DSKLPAYKDL GKNLPFPTYF PDGDEEELPE DLYDENVCQP GAPSITFA
