ID   RM40_HUMAN              Reviewed;         206 AA.
AC   Q9NQ50; B3KVZ7; O95134;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 174.
DE   RecName: Full=Large ribosomal subunit protein mL40 {ECO:0000303|PubMed:25278503};
DE   AltName: Full=39S ribosomal protein L40, mitochondrial;
DE            Short=L40mt;
DE            Short=MRP-L40;
DE   AltName: Full=Nuclear localization signal-containing protein deleted in velocardiofacial syndrome;
DE   AltName: Full=Up-regulated in metastasis;
DE   Flags: Precursor;
GN   Name=MRPL40; Synonyms=NLVCF, URIM;
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], TISSUE SPECIFICITY, AND VARIANTS PRO-11 AND
RP   HIS-129.
RX   PubMed=9790763; DOI=10.1006/geno.1998.5488;
RA   Funke B., Puech A., Saint-Jore B., Pandita R., Skoultchi A., Morrow B.;
RT   "Isolation and characterization of a human gene containing a nuclear
RT   localization signal from the critical region for velo-cardio-facial
RT   syndrome on 22q11.";
RL   Genomics 53:146-154(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10226592;
RA   Hildebrandt T., Weidle U.H., Preiherr J., van Muijen G.N.P.,
RA   Klostermann S., Kaul S., Zendman A.J.W.;
RT   "Identification of URIM, a novel gene up-regulated in metastasis.";
RL   Anticancer Res. 19:525-530(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [7]
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   [8]
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   [9] {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   [10] {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   [11] {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).
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. mL40 binds to the major groove of the anticodon
CC       stem of mt-tRNA(Val) in the central protuberance.
CC       {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC       ECO:0000269|PubMed:28892042}.
CC   -!- INTERACTION:
CC       Q9NQ50; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1053902, EBI-3867333;
CC       Q9NQ50; Q15323: KRT31; NbExp=3; IntAct=EBI-1053902, EBI-948001;
CC       Q9NQ50; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-1053902, EBI-9996449;
CC       Q9NQ50; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-1053902, EBI-945833;
CC       Q9NQ50; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1053902, EBI-22310682;
CC       Q9NQ50; Q12800: TFCP2; NbExp=3; IntAct=EBI-1053902, EBI-717422;
CC       Q9NQ50; P14373: TRIM27; NbExp=3; IntAct=EBI-1053902, EBI-719493;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC       ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9790763}.
CC   -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC       mL40 family. {ECO:0000305}.
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DR   EMBL; AF034091; AAC70904.1; -; mRNA.
DR   EMBL; AJ295637; CAC00535.1; -; mRNA.
DR   EMBL; CR456532; CAG30418.1; -; mRNA.
DR   EMBL; AK123768; BAG53959.1; -; mRNA.
DR   EMBL; CH471176; EAX03042.1; -; Genomic_DNA.
DR   EMBL; BC009707; AAH09707.1; -; mRNA.
DR   CCDS; CCDS13760.1; -.
DR   RefSeq; NP_003767.2; NM_003776.3.
DR   PDB; 3J7Y; EM; 3.40 A; 8=1-206.
DR   PDB; 3J9M; EM; 3.50 A; 8=1-206.
DR   PDB; 5OOL; EM; 3.06 A; 8=1-206.
DR   PDB; 5OOM; EM; 3.03 A; 8=1-206.
DR   PDB; 6I9R; EM; 3.90 A; 8=1-206.
DR   PDB; 6NU2; EM; 3.90 A; 8=83-181.
DR   PDB; 6NU3; EM; 4.40 A; 8=1-206.
DR   PDB; 6VLZ; EM; 2.97 A; 8=1-206.
DR   PDB; 6VMI; EM; 2.96 A; 8=1-206.
DR   PDB; 6ZM5; EM; 2.89 A; 8=1-206.
DR   PDB; 6ZM6; EM; 2.59 A; 8=1-206.
DR   PDB; 6ZS9; EM; 4.00 A; 8=1-206.
DR   PDB; 6ZSA; EM; 4.00 A; 8=1-206.
DR   PDB; 6ZSB; EM; 4.50 A; 8=1-206.
DR   PDB; 6ZSC; EM; 3.50 A; 8=1-206.
DR   PDB; 6ZSD; EM; 3.70 A; 8=1-206.
DR   PDB; 6ZSE; EM; 5.00 A; 8=1-206.
DR   PDB; 6ZSG; EM; 4.00 A; 8=1-206.
DR   PDB; 7A5F; EM; 4.40 A; A=1-206.
DR   PDB; 7A5G; EM; 4.33 A; A=1-206.
DR   PDB; 7A5H; EM; 3.30 A; 8=1-206.
DR   PDB; 7A5I; EM; 3.70 A; 83=1-206.
DR   PDB; 7A5J; EM; 3.10 A; 8=1-206.
DR   PDB; 7A5K; EM; 3.70 A; A=1-206.
DR   PDB; 7L08; EM; 3.49 A; 8=1-206.
DR   PDB; 7L20; EM; 3.15 A; 8=1-206.
DR   PDB; 7O9K; EM; 3.10 A; 8=1-206.
DR   PDB; 7O9M; EM; 2.50 A; 8=1-206.
DR   PDB; 7ODR; EM; 2.90 A; 8=1-206.
DR   PDB; 7ODS; EM; 3.10 A; 8=1-206.
DR   PDB; 7ODT; EM; 3.10 A; 8=1-206.
DR   PDB; 7OF0; EM; 2.20 A; 8=1-206.
DR   PDB; 7OF2; EM; 2.70 A; 8=1-206.
DR   PDB; 7OF3; EM; 2.70 A; 8=1-206.
DR   PDB; 7OF4; EM; 2.70 A; 8=1-206.
DR   PDB; 7OF5; EM; 2.90 A; 8=1-206.
DR   PDB; 7OF6; EM; 2.60 A; 8=1-206.
DR   PDB; 7OF7; EM; 2.50 A; 8=1-206.
DR   PDB; 7OG4; EM; 3.80 A; 8=1-206.
DR   PDB; 7OI7; EM; 3.50 A; 8=1-206.
DR   PDB; 7OI8; EM; 3.50 A; 8=1-206.
DR   PDB; 7OI9; EM; 3.30 A; 8=1-206.
DR   PDB; 7OIA; EM; 3.20 A; 8=1-206.
DR   PDB; 7OIB; EM; 3.30 A; 8=1-206.
DR   PDB; 7OIC; EM; 3.10 A; 8=1-206.
DR   PDB; 7OID; EM; 3.70 A; 8=1-206.
DR   PDB; 7OIE; EM; 3.50 A; 8=1-206.
DR   PDB; 7PD3; EM; 3.40 A; 8=1-206.
DR   PDB; 7PO4; EM; 2.56 A; 8=1-206.
DR   PDB; 7QI4; EM; 2.21 A; 8=1-206.
DR   PDB; 7QI5; EM; 2.63 A; 8=1-206.
DR   PDB; 7QI6; EM; 2.98 A; 8=1-206.
DR   PDB; 8ANY; EM; 2.85 A; 8=1-206.
DR   PDB; 8OIR; EM; 3.10 A; Bp=1-206.
DR   PDB; 8OIT; EM; 2.90 A; Bp=1-206.
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; 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; 7PO4; -.
DR   PDBsum; 7QI4; -.
DR   PDBsum; 7QI5; -.
DR   PDBsum; 7QI6; -.
DR   PDBsum; 8ANY; -.
DR   PDBsum; 8OIR; -.
DR   PDBsum; 8OIT; -.
DR   AlphaFoldDB; Q9NQ50; -.
DR   EMDB; EMD-0514; -.
DR   EMDB; EMD-0515; -.
DR   EMDB; EMD-11278; -.
DR   EMDB; EMD-11279; -.
DR   EMDB; EMD-11390; -.
DR   EMDB; EMD-11391; -.
DR   EMDB; EMD-11392; -.
DR   EMDB; EMD-11393; -.
DR   EMDB; EMD-11394; -.
DR   EMDB; EMD-11395; -.
DR   EMDB; EMD-11397; -.
DR   EMDB; EMD-11641; -.
DR   EMDB; EMD-11642; -.
DR   EMDB; EMD-11643; -.
DR   EMDB; EMD-11644; -.
DR   EMDB; EMD-11645; -.
DR   EMDB; EMD-11646; -.
DR   EMDB; EMD-12763; -.
DR   EMDB; EMD-12764; -.
DR   EMDB; EMD-12845; -.
DR   EMDB; EMD-12846; -.
DR   EMDB; EMD-12847; -.
DR   EMDB; EMD-12865; -.
DR   EMDB; EMD-12867; -.
DR   EMDB; EMD-12868; -.
DR   EMDB; EMD-12869; -.
DR   EMDB; EMD-12870; -.
DR   EMDB; EMD-12871; -.
DR   EMDB; EMD-12872; -.
DR   EMDB; EMD-12877; -.
DR   EMDB; EMD-12920; -.
DR   EMDB; EMD-12921; -.
DR   EMDB; EMD-12922; -.
DR   EMDB; EMD-12923; -.
DR   EMDB; EMD-12924; -.
DR   EMDB; EMD-12925; -.
DR   EMDB; EMD-12926; -.
DR   EMDB; EMD-12927; -.
DR   EMDB; EMD-13329; -.
DR   EMDB; EMD-13562; -.
DR   EMDB; EMD-13980; -.
DR   EMDB; EMD-13981; -.
DR   EMDB; EMD-13982; -.
DR   EMDB; EMD-15544; -.
DR   EMDB; EMD-16897; -.
DR   EMDB; EMD-16899; -.
DR   EMDB; EMD-21233; -.
DR   EMDB; EMD-21242; -.
DR   EMDB; EMD-23096; -.
DR   EMDB; EMD-23121; -.
DR   EMDB; EMD-3842; -.
DR   EMDB; EMD-3843; -.
DR   EMDB; EMD-4434; -.
DR   SMR; Q9NQ50; -.
DR   BioGRID; 122364; 174.
DR   ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR   CORUM; Q9NQ50; -.
DR   IntAct; Q9NQ50; 51.
DR   MINT; Q9NQ50; -.
DR   STRING; 9606.ENSP00000333401; -.
DR   GlyGen; Q9NQ50; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NQ50; -.
DR   MetOSite; Q9NQ50; -.
DR   PhosphoSitePlus; Q9NQ50; -.
DR   BioMuta; MRPL40; -.
DR   DMDM; 21263795; -.
DR   EPD; Q9NQ50; -.
DR   jPOST; Q9NQ50; -.
DR   MassIVE; Q9NQ50; -.
DR   MaxQB; Q9NQ50; -.
DR   PaxDb; 9606-ENSP00000333401; -.
DR   PeptideAtlas; Q9NQ50; -.
DR   ProteomicsDB; 82081; -.
DR   Pumba; Q9NQ50; -.
DR   TopDownProteomics; Q9NQ50; -.
DR   Antibodypedia; 209; 166 antibodies from 24 providers.
DR   DNASU; 64976; -.
DR   Ensembl; ENST00000333130.4; ENSP00000333401.3; ENSG00000185608.9.
DR   GeneID; 64976; -.
DR   KEGG; hsa:64976; -.
DR   MANE-Select; ENST00000333130.4; ENSP00000333401.3; NM_003776.4; NP_003767.2.
DR   UCSC; uc002zpg.4; human.
DR   AGR; HGNC:14491; -.
DR   CTD; 64976; -.
DR   DisGeNET; 64976; -.
DR   GeneCards; MRPL40; -.
DR   HGNC; HGNC:14491; MRPL40.
DR   HPA; ENSG00000185608; Low tissue specificity.
DR   MIM; 605089; gene.
DR   neXtProt; NX_Q9NQ50; -.
DR   OpenTargets; ENSG00000185608; -.
DR   PharmGKB; PA30972; -.
DR   VEuPathDB; HostDB:ENSG00000185608; -.
DR   eggNOG; KOG4778; Eukaryota.
DR   GeneTree; ENSGT00390000010239; -.
DR   HOGENOM; CLU_087493_0_0_1; -.
DR   InParanoid; Q9NQ50; -.
DR   OMA; KQREHEM; -.
DR   OrthoDB; 2996073at2759; -.
DR   PhylomeDB; Q9NQ50; -.
DR   TreeFam; TF105982; -.
DR   PathwayCommons; Q9NQ50; -.
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; Q9NQ50; -.
DR   SIGNOR; Q9NQ50; -.
DR   BioGRID-ORCS; 64976; 263 hits in 1166 CRISPR screens.
DR   ChiTaRS; MRPL40; human.
DR   GeneWiki; MRPL40; -.
DR   GenomeRNAi; 64976; -.
DR   Pharos; Q9NQ50; Tbio.
DR   PRO; PR:Q9NQ50; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9NQ50; Protein.
DR   Bgee; ENSG00000185608; Expressed in skeletal muscle tissue of rectus abdominis and 216 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0005761; C:mitochondrial ribosome; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR   GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal.
DR   Gene3D; 6.10.250.3440; -; 1.
DR   InterPro; IPR019192; Ribosomal_mL40.
DR   InterPro; IPR039145; Ribosomal_mL40_metazoa/plant.
DR   PANTHER; PTHR13359; 39S RIBOSOMAL PROTEIN L40, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13359:SF2; 39S RIBOSOMAL PROTEIN L40, MITOCHONDRIAL; 1.
DR   Pfam; PF09812; MRP-L28; 1.
DR   Genevisible; Q9NQ50; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P83565"
FT   CHAIN           47..206
FT                   /note="Large ribosomal subunit protein mL40"
FT                   /id="PRO_0000030558"
FT   REGION          168..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         11
FT                   /note="L -> P (in dbSNP:rs1128399)"
FT                   /evidence="ECO:0000269|PubMed:9790763"
FT                   /id="VAR_061809"
FT   VARIANT         129
FT                   /note="R -> H (in dbSNP:rs7575)"
FT                   /evidence="ECO:0000269|PubMed:9790763"
FT                   /id="VAR_016088"
FT   TURN            92..95
FT                   /evidence="ECO:0007829|PDB:7OIA"
FT   HELIX           108..153
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           158..161
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:5OOL"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:7OF0"
SQ   SEQUENCE   206 AA;  24490 MW;  AE6262A9A94B05FD CRC64;
     MTASVLRSIS LALRPTSGLL GTWQTQLRET HQRASLLSFW ELIPMRSEPL RKKKKVDPKK
     DQEAKERLKR KIRKLEKATQ ELIPIEDFIT PLKFLDKARE RPQVELTFEE TERRALLLKK
     WSLYKQQERK MERDTIRAML EAQQEALEEL QLESPKLHAE AIKRDPNLFP FEKEGPHYTP
     PIPNYQPPEG RYNDITKVYT QVEFKR
//