RM44_HUMAN
ID RM44_HUMAN Reviewed; 332 AA.
AC Q9H9J2; Q53S16; Q6IA62; Q9H821;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=39S ribosomal protein L44, mitochondrial;
DE Short=L44mt;
DE Short=MRP-L44;
DE EC=3.1.26.-;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL44 {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL44;
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].
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] {ECO:0000305, ECO:0000312|EMBL:BAB14234.1}
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].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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.
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 [6]
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 [7]
RP FUNCTION, AND VARIANT COXPD16 ARG-156.
RX PubMed=23315540; DOI=10.1136/jmedgenet-2012-101375;
RA Carroll C.J., Isohanni P., Poeyhoenen R., Euro L., Richter U.,
RA Brilhante V., Goetz A., Lahtinen T., Paetau A., Pihko H., Battersby B.J.,
RA Tyynismaa H., Suomalainen A.;
RT "Whole-exome sequencing identifies a mutation in the mitochondrial ribosome
RT protein MRPL44 to underlie mitochondrial infantile cardiomyopathy.";
RL J. Med. Genet. 50:151-159(2013).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
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 [10] {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 [11] {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 [12] {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 -!- FUNCTION: Component of the 39S subunit of mitochondrial ribosome. May
CC have a function in the assembly/stability of nascent mitochondrial
CC polypeptides exiting the ribosome. {ECO:0000269|PubMed:23315540}.
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 -!- INTERACTION:
CC Q9H9J2; Q9NYB9: ABI2; NbExp=3; IntAct=EBI-713619, EBI-743598;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 16 (COXPD16)
CC [MIM:615395]: An autosomal recessive, mitochondrial disorder
CC characterized by hypertrophic cardiomyopathy, liver steatosis, and
CC decreased levels of mitochondrial complexes I and IV in heart and
CC skeletal muscle. {ECO:0000269|PubMed:23315540}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. Mitochondrion-
CC specific ribosomal protein mL44 subfamily. {ECO:0000305}.
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DR EMBL; AK022763; BAB14234.1; -; mRNA.
DR EMBL; AK024052; BAB14802.1; -; mRNA.
DR EMBL; CR457293; CAG33574.1; -; mRNA.
DR EMBL; AC073641; AAY14925.1; -; Genomic_DNA.
DR EMBL; BC012058; AAH12058.1; -; mRNA.
DR CCDS; CCDS2459.1; -.
DR RefSeq; NP_075066.1; NM_022915.3.
DR PDB; 3J7Y; EM; 3.40 A; c=1-332.
DR PDB; 3J9M; EM; 3.50 A; c=1-332.
DR PDB; 5OOL; EM; 3.06 A; c=1-332.
DR PDB; 5OOM; EM; 3.03 A; c=1-332.
DR PDB; 6I9R; EM; 3.90 A; c=1-332.
DR PDB; 6NU2; EM; 3.90 A; c=31-316.
DR PDB; 6NU3; EM; 4.40 A; c=1-332.
DR PDB; 6VLZ; EM; 2.97 A; c=1-332.
DR PDB; 6VMI; EM; 2.96 A; c=1-332.
DR PDB; 6ZM5; EM; 2.89 A; c=1-332.
DR PDB; 6ZM6; EM; 2.59 A; c=1-332.
DR PDB; 6ZS9; EM; 4.00 A; c=1-332.
DR PDB; 6ZSA; EM; 4.00 A; c=1-332.
DR PDB; 6ZSB; EM; 4.50 A; c=1-332.
DR PDB; 6ZSC; EM; 3.50 A; c=1-332.
DR PDB; 6ZSD; EM; 3.70 A; c=1-332.
DR PDB; 6ZSE; EM; 5.00 A; c=1-332.
DR PDB; 6ZSG; EM; 4.00 A; c=1-332.
DR PDB; 7A5F; EM; 4.40 A; c3=1-332.
DR PDB; 7A5G; EM; 4.33 A; c3=1-332.
DR PDB; 7A5H; EM; 3.30 A; c=1-332.
DR PDB; 7A5I; EM; 3.70 A; c3=1-332.
DR PDB; 7A5J; EM; 3.10 A; c=1-332.
DR PDB; 7A5K; EM; 3.70 A; c3=1-332.
DR PDB; 7L08; EM; 3.49 A; c=1-332.
DR PDB; 7L20; EM; 3.15 A; c=1-332.
DR PDB; 7O9K; EM; 3.10 A; c=1-332.
DR PDB; 7O9M; EM; 2.50 A; c=1-332.
DR PDB; 7ODR; EM; 2.90 A; c=1-332.
DR PDB; 7ODS; EM; 3.10 A; c=1-332.
DR PDB; 7ODT; EM; 3.10 A; c=1-332.
DR PDB; 7OF0; EM; 2.20 A; c=1-332.
DR PDB; 7OF2; EM; 2.70 A; c=1-332.
DR PDB; 7OF3; EM; 2.70 A; c=1-332.
DR PDB; 7OF4; EM; 2.70 A; c=1-332.
DR PDB; 7OF5; EM; 2.90 A; c=1-332.
DR PDB; 7OF6; EM; 2.60 A; c=1-332.
DR PDB; 7OF7; EM; 2.50 A; c=1-332.
DR PDB; 7OG4; EM; 3.80 A; c=1-332.
DR PDB; 7OI6; EM; 5.70 A; c=1-332.
DR PDB; 7OI7; EM; 3.50 A; c=1-332.
DR PDB; 7OI8; EM; 3.50 A; c=1-332.
DR PDB; 7OI9; EM; 3.30 A; c=1-332.
DR PDB; 7OIA; EM; 3.20 A; c=1-332.
DR PDB; 7OIB; EM; 3.30 A; c=1-332.
DR PDB; 7OIC; EM; 3.10 A; c=1-332.
DR PDB; 7OID; EM; 3.70 A; c=1-332.
DR PDB; 7OIE; EM; 3.50 A; c=1-332.
DR PDB; 7PD3; EM; 3.40 A; c=1-332.
DR PDB; 7QH6; EM; 3.08 A; c=1-332.
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; Q9H9J2; -.
DR SMR; Q9H9J2; -.
DR BioGRID; 122389; 218.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9H9J2; -.
DR IntAct; Q9H9J2; 65.
DR MINT; Q9H9J2; -.
DR STRING; 9606.ENSP00000258383; -.
DR GlyGen; Q9H9J2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H9J2; -.
DR PhosphoSitePlus; Q9H9J2; -.
DR SwissPalm; Q9H9J2; -.
DR BioMuta; MRPL44; -.
DR DMDM; 51316917; -.
DR EPD; Q9H9J2; -.
DR jPOST; Q9H9J2; -.
DR MassIVE; Q9H9J2; -.
DR MaxQB; Q9H9J2; -.
DR PaxDb; Q9H9J2; -.
DR PeptideAtlas; Q9H9J2; -.
DR PRIDE; Q9H9J2; -.
DR ProteomicsDB; 81324; -.
DR TopDownProteomics; Q9H9J2; -.
DR Antibodypedia; 34365; 164 antibodies from 23 providers.
DR DNASU; 65080; -.
DR Ensembl; ENST00000258383.4; ENSP00000258383.3; ENSG00000135900.4.
DR GeneID; 65080; -.
DR KEGG; hsa:65080; -.
DR MANE-Select; ENST00000258383.4; ENSP00000258383.3; NM_022915.5; NP_075066.1.
DR UCSC; uc002vnr.4; human.
DR CTD; 65080; -.
DR DisGeNET; 65080; -.
DR GeneCards; MRPL44; -.
DR HGNC; HGNC:16650; MRPL44.
DR HPA; ENSG00000135900; Low tissue specificity.
DR MalaCards; MRPL44; -.
DR MIM; 611849; gene.
DR MIM; 615395; phenotype.
DR neXtProt; NX_Q9H9J2; -.
DR OpenTargets; ENSG00000135900; -.
DR Orphanet; 352563; Infantile hypertrophic cardiomyopathy due to MRPL44 deficiency.
DR PharmGKB; PA30976; -.
DR VEuPathDB; HostDB:ENSG00000135900; -.
DR eggNOG; KOG3769; Eukaryota.
DR GeneTree; ENSGT00390000016956; -.
DR HOGENOM; CLU_058895_0_0_1; -.
DR InParanoid; Q9H9J2; -.
DR OMA; CYIRSEE; -.
DR OrthoDB; 877695at2759; -.
DR PhylomeDB; Q9H9J2; -.
DR TreeFam; TF324185; -.
DR PathwayCommons; Q9H9J2; -.
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; Q9H9J2; -.
DR SIGNOR; Q9H9J2; -.
DR BioGRID-ORCS; 65080; 286 hits in 1085 CRISPR screens.
DR ChiTaRS; MRPL44; human.
DR GenomeRNAi; 65080; -.
DR Pharos; Q9H9J2; Tbio.
DR PRO; PR:Q9H9J2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H9J2; protein.
DR Bgee; ENSG00000135900; Expressed in oocyte and 171 other tissues.
DR ExpressionAtlas; Q9H9J2; baseline and differential.
DR Genevisible; Q9H9J2; 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:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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:0070125; P:mitochondrial translational elongation; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR CDD; cd19874; DSRM_MRPL44; 1.
DR Gene3D; 1.10.1520.10; -; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR044444; MRPL44_DSRM.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR11207; PTHR11207; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
DR PROSITE; PS50137; DS_RBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Endonuclease; Hydrolase; Mitochondrion;
KW Nuclease; Primary mitochondrial disease; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..332
FT /note="39S ribosomal protein L44, mitochondrial"
FT /id="PRO_0000030821"
FT DOMAIN 86..228
FT /note="RNase III"
FT DOMAIN 236..306
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT VARIANT 138
FT /note="T -> I (in dbSNP:rs11546406)"
FT /id="VAR_034464"
FT VARIANT 156
FT /note="L -> R (in COXPD16; dbSNP:rs143697995)"
FT /evidence="ECO:0000269|PubMed:23315540"
FT /id="VAR_070568"
FT CONFLICT 232
FT /note="W -> R (in Ref. 1; BAB14802)"
FT /evidence="ECO:0000305"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 123..144
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 188..206
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 208..218
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 289..305
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5OOL"
SQ SEQUENCE 332 AA; 37535 MW; DD0CF6BD66CF3D9E CRC64;
MASGLVRLLQ QGHRCLLAPV APKLVPPVRG VKKGFRAAFR FQKELERQRL LRCPPPPVRR
SEKPNWDYHA EIQAFGHRLQ ENFSLDLLKT AFVNSCYIKS EEAKRQQLGI EKEAVLLNLK
SNQELSEQGT SFSQTCLTQF LEDEYPDMPT EGIKNLVDFL TGEEVVCHVA RNLAVEQLTL
SEEFPVPPAV LQQTFFAVIG ALLQSSGPER TALFIRDFLI TQMTGKELFE MWKIINPMGL
LVEELKKRNV SAPESRLTRQ SGGTTALPLY FVGLYCDKKL IAEGPGETVL VAEEEAARVA
LRKLYGFTEN RRPWNYSKPK ETLRAEKSIT AS
