RM45_HUMAN
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 03-AUG-2022, entry version 173.
DE RecName: Full=39S ribosomal protein L45, mitochondrial;
DE Short=L45mt;
DE Short=MRP-L45;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL45 {ECO:0000303|PubMed:25278503};
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};
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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; 7QH6; EM; 3.08 A; d=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; 7QH6; -.
DR AlphaFoldDB; Q9BRJ2; -.
DR SMR; Q9BRJ2; -.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9BRJ2; -.
DR DIP; DIP-53786N; -.
DR IntAct; Q9BRJ2; 62.
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; Q9BRJ2; -.
DR PeptideAtlas; Q9BRJ2; -.
DR PRIDE; Q9BRJ2; -.
DR ProteomicsDB; 78769; -.
DR DNASU; 84311; -.
DR Ensembl; ENST00000621878.4; ENSP00000483030.1; ENSG00000277936.4.
DR UCSC; uc032gks.2; human.
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; Chromosome 17.
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; IC:ComplexPortal.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR007379; Tim44-like_dom.
DR Pfam; PF04280; Tim44; 1.
DR SMART; SM00978; Tim44; 1.
DR SUPFAM; SSF54427; SSF54427; 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="39S ribosomal protein L45, mitochondrial"
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:7OI9"
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
