ID RM45_HUMAN Reviewed; 306 AA. AC Q9BRJ2; A1L436; Q6ZMJ5; DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2003, sequence version 2. DT 24-JAN-2024, entry version 180. DE RecName: Full=Large ribosomal subunit protein mL45 {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein L45, mitochondrial; DE Short=L45mt; DE Short=MRP-L45; DE Flags: Precursor; GN Name=MRPL45; 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 [LARGE SCALE MRNA]. RC TISSUE=Adipose tissue; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Ovary; 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. RX PubMed=11551941; DOI=10.1074/jbc.m106510200; RA Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M., RA Moseley A., Spremulli L.L.; RT "The large subunit of the mammalian mitochondrial ribosome. Analysis of the RT complement of ribosomal proteins present."; RL J. Biol. Chem. 276:43958-43969(2001). RN [4] 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 [5] 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 [6] {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 [7] {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 [8] {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:25278503, PubMed:25838379, PubMed:28892042). 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 -!- INTERACTION: CC Q9BRJ2; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-2514313, EBI-2559016; CC Q9BRJ2; P50402: EMD; NbExp=3; IntAct=EBI-2514313, EBI-489887; CC Q9BRJ2; Q99471: PFDN5; NbExp=3; IntAct=EBI-2514313, EBI-357275; CC Q9BRJ2; Q9HB20: PLEKHA3; NbExp=3; IntAct=EBI-2514313, EBI-11079894; CC Q9BRJ2; P36406: TRIM23; NbExp=3; IntAct=EBI-2514313, EBI-740098; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503, CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}. CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein CC mL45 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BC006235; Type=Frameshift; Evidence={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; AK172741; BAD18730.1; -; mRNA. DR EMBL; BC006235; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC130382; AAI30383.1; -; mRNA. DR EMBL; BC130384; AAI30385.1; -; mRNA. DR CCDS; CCDS11326.1; -. DR PDB; 3J7Y; EM; 3.40 A; d=1-306. DR PDB; 3J9M; EM; 3.50 A; d=1-306. DR PDB; 5OOL; EM; 3.06 A; d=1-306. DR PDB; 5OOM; EM; 3.03 A; d=1-306. DR PDB; 6I9R; EM; 3.90 A; d=1-306. DR PDB; 6NU2; EM; 3.90 A; d=117-287. DR PDB; 6NU3; EM; 4.40 A; d=1-306. DR PDB; 6VLZ; EM; 2.97 A; d=1-306. DR PDB; 6VMI; EM; 2.96 A; d=1-306. DR PDB; 6ZM5; EM; 2.89 A; d=1-306. DR PDB; 6ZM6; EM; 2.59 A; d=1-306. DR PDB; 6ZS9; EM; 4.00 A; d=1-306. DR PDB; 6ZSA; EM; 4.00 A; d=55-306. DR PDB; 6ZSB; EM; 4.50 A; d=55-306. DR PDB; 6ZSC; EM; 3.50 A; d=55-306. DR PDB; 6ZSD; EM; 3.70 A; d=55-306. DR PDB; 6ZSE; EM; 5.00 A; d=56-306. DR PDB; 6ZSG; EM; 4.00 A; d=55-306. DR PDB; 7A5F; EM; 4.40 A; d3=1-306. DR PDB; 7A5G; EM; 4.33 A; d3=1-306. DR PDB; 7A5H; EM; 3.30 A; d=1-306. DR PDB; 7A5I; EM; 3.70 A; d3=1-306. DR PDB; 7A5J; EM; 3.10 A; d=1-306. DR PDB; 7A5K; EM; 3.70 A; d3=1-306. DR PDB; 7L08; EM; 3.49 A; d=1-306. DR PDB; 7L20; EM; 3.15 A; d=1-306. DR PDB; 7O9K; EM; 3.10 A; d=1-306. DR PDB; 7O9M; EM; 2.50 A; d=1-302. DR PDB; 7ODR; EM; 2.90 A; d=1-306. DR PDB; 7ODS; EM; 3.10 A; d=1-306. DR PDB; 7ODT; EM; 3.10 A; d=1-306. DR PDB; 7OF0; EM; 2.20 A; d=1-306. DR PDB; 7OF2; EM; 2.70 A; d=1-306. DR PDB; 7OF3; EM; 2.70 A; d=1-306. DR PDB; 7OF4; EM; 2.70 A; d=1-306. DR PDB; 7OF5; EM; 2.90 A; d=1-306. DR PDB; 7OF6; EM; 2.60 A; d=1-306. DR PDB; 7OF7; EM; 2.50 A; d=1-306. DR PDB; 7OG4; EM; 3.80 A; d=1-306. DR PDB; 7OI6; EM; 5.70 A; d=1-306. DR PDB; 7OI7; EM; 3.50 A; d=1-306. DR PDB; 7OI8; EM; 3.50 A; d=1-306. DR PDB; 7OI9; EM; 3.30 A; d=1-306. DR PDB; 7OIA; EM; 3.20 A; d=1-306. DR PDB; 7OIB; EM; 3.30 A; d=1-306. DR PDB; 7OIC; EM; 3.10 A; d=1-306. DR PDB; 7OID; EM; 3.70 A; d=1-306. DR PDB; 7OIE; EM; 3.50 A; d=1-306. DR PDB; 7PD3; EM; 3.40 A; d=1-306. DR PDB; 7PO4; EM; 2.56 A; d=1-306. DR PDB; 7QH6; EM; 3.08 A; d=1-306. DR PDB; 7QH7; EM; 2.89 A; d=117-285. DR PDB; 7QI4; EM; 2.21 A; d=1-306. DR PDB; 7QI5; EM; 2.63 A; d=1-306. DR PDB; 7QI6; EM; 2.98 A; d=1-306. DR PDB; 8ANY; EM; 2.85 A; d=1-306. DR PDB; 8OIR; EM; 3.10 A; Bu=1-306. DR PDB; 8OIT; EM; 2.90 A; Bu=1-306. 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; 7PO4; -. DR PDBsum; 7QH6; -. DR PDBsum; 7QH7; -. DR PDBsum; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIT; -. DR AlphaFoldDB; Q9BRJ2; -. DR EMDB; EMD-0514; -. 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-12919; -. 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-13965; -. DR EMDB; EMD-13967; -. 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; Q9BRJ2; -. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; Q9BRJ2; -. DR DIP; DIP-53786N; -. DR IntAct; Q9BRJ2; 63. DR MINT; Q9BRJ2; -. DR STRING; 9606.ENSP00000484903; -. DR iPTMnet; Q9BRJ2; -. DR MetOSite; Q9BRJ2; -. DR PhosphoSitePlus; Q9BRJ2; -. DR SwissPalm; Q9BRJ2; -. DR BioMuta; MRPL45; -. DR DMDM; 29611869; -. DR EPD; Q9BRJ2; -. DR jPOST; Q9BRJ2; -. DR MassIVE; Q9BRJ2; -. DR MaxQB; Q9BRJ2; -. DR PaxDb; 9606-ENSP00000484903; -. DR PeptideAtlas; Q9BRJ2; -. DR ProteomicsDB; 78769; -. DR Pumba; Q9BRJ2; -. DR DNASU; 84311; -. DR Ensembl; ENST00000621878.4; ENSP00000483030.1; ENSG00000277936.4. DR UCSC; uc032gks.2; human. DR AGR; HGNC:16651; -. DR GeneCards; MRPL45; -. DR HGNC; HGNC:16651; MRPL45. DR MIM; 611850; gene. DR neXtProt; NX_Q9BRJ2; -. DR eggNOG; KOG4599; Eukaryota. DR InParanoid; Q9BRJ2; -. DR PhylomeDB; Q9BRJ2; -. DR TreeFam; TF105825; -. DR PathwayCommons; Q9BRJ2; -. 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; Q9BRJ2; -. DR SIGNOR; Q9BRJ2; -. DR ChiTaRS; MRPL45; human. DR Pharos; Q9BRJ2; Tdark. DR PRO; PR:Q9BRJ2; -. DR Proteomes; UP000005640; Unplaced. DR RNAct; Q9BRJ2; Protein. 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:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR Gene3D; 3.10.450.240; -; 1. DR InterPro; IPR032710; NTF2-like_dom_sf. DR InterPro; IPR007379; Tim44-like_dom. DR PANTHER; PTHR28554; 39S RIBOSOMAL PROTEIN L45, MITOCHONDRIAL; 1. DR PANTHER; PTHR28554:SF1; 39S RIBOSOMAL PROTEIN L45, MITOCHONDRIAL; 1. DR Pfam; PF04280; Tim44; 1. DR SMART; SM00978; Tim44; 1. DR SUPFAM; SSF54427; NTF2-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; Transit peptide. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..306 FT /note="Large ribosomal subunit protein mL45" FT /id="PRO_0000030563" FT REGION 287..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 298 FT /note="G -> V (in dbSNP:rs34749623)" FT /id="VAR_061810" FT CONFLICT 139 FT /note="E -> G (in Ref. 1; BAD18730)" FT /evidence="ECO:0000305" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 53..63 FT /evidence="ECO:0007829|PDB:5OOM" FT HELIX 119..129 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 137..154 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 157..163 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 169..173 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 175..178 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 184..198 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 209..221 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:7OIB" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 240..251 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 260..265 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 276..278 FT /evidence="ECO:0007829|PDB:7QH6" FT STRAND 280..282 FT /evidence="ECO:0007829|PDB:7OF0" SQ SEQUENCE 306 AA; 35351 MW; C00CC379D337910A CRC64; MAAPIPQGFS CLSRFLGWWF RQPVLVTQSA AIVPVRTKKR FTPPIYQPKF KTEKEFMQHA RKAGLVIPPE KSDRSIHLAC TAGIFDAYVP PEGDARISSL SKEGLIERTE RMKKTMASQV SIRRIKDYDA NFKIKDFPEK AKDIFIEAHL CLNNSDHDRL HTLVTEHCFP DMTWDIKYKT VRWSFVESLE PSHVVQVRCS SMMNQGNVYG QITVRMHTRQ TLAIYDRFGR LMYGQEDVPK DVLEYVVFEK QLTNPYGSWR MHTKIVPPWA PPKQPILKTV MIPGPQLKPE EEYEEAQGEA QKPQLA //