Full text data of MRPL44
MRPL44
[Confidence: low (only semi-automatic identification from reviews)]
39S ribosomal protein L44, mitochondrial; L44mt; MRP-L44; 3.1.26.-; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
39S ribosomal protein L44, mitochondrial; L44mt; MRP-L44; 3.1.26.-; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H9J2
ID RM44_HUMAN Reviewed; 332 AA.
AC Q9H9J2; Q53S16; Q6IA62; Q9H821;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=39S ribosomal protein L44, mitochondrial;
DE Short=L44mt;
DE Short=MRP-L44;
DE EC=3.1.26.-;
DE Flags: Precursor;
GN Name=MRPL44;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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
RT project: 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
RT of the 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of the 39S subunit of mitochondrial ribosome.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC -!- SIMILARITY: Contains 1 RNase III domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_075066.1; NM_022915.3.
DR UniGene; Hs.203559; -.
DR ProteinModelPortal; Q9H9J2; -.
DR IntAct; Q9H9J2; 20.
DR MINT; MINT-1384665; -.
DR STRING; 9606.ENSP00000258383; -.
DR PhosphoSite; Q9H9J2; -.
DR DMDM; 51316917; -.
DR PaxDb; Q9H9J2; -.
DR PeptideAtlas; Q9H9J2; -.
DR PRIDE; Q9H9J2; -.
DR DNASU; 65080; -.
DR Ensembl; ENST00000258383; ENSP00000258383; ENSG00000135900.
DR GeneID; 65080; -.
DR KEGG; hsa:65080; -.
DR UCSC; uc002vnr.4; human.
DR CTD; 65080; -.
DR GeneCards; GC02P224786; -.
DR HGNC; HGNC:16650; MRPL44.
DR HPA; HPA038147; -.
DR MIM; 611849; gene.
DR neXtProt; NX_Q9H9J2; -.
DR Orphanet; 352563; Infantile hypertrophic cardiomyopathy due to MRPL44 deficiency.
DR PharmGKB; PA30976; -.
DR eggNOG; NOG327595; -.
DR HOGENOM; HOG000046065; -.
DR HOVERGEN; HBG054127; -.
DR InParanoid; Q9H9J2; -.
DR KO; K17425; -.
DR OMA; WDYSKPK; -.
DR OrthoDB; EOG7WQ7SN; -.
DR PhylomeDB; Q9H9J2; -.
DR ChiTaRS; mRpL44; human.
DR GenomeRNAi; 65080; -.
DR NextBio; 67272; -.
DR PRO; PR:Q9H9J2; -.
DR Bgee; Q9H9J2; -.
DR CleanEx; HS_MRPL44; -.
DR Genevestigator; Q9H9J2; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.10.1520.10; -; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR InterPro; IPR014720; dsRNA-bd_dom.
DR InterPro; IPR000999; RNase_III_dom.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS00517; RNASE_3_1; FALSE_NEG.
DR PROSITE; PS50142; RNASE_3_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Endonuclease; Hydrolase; Mitochondrion; Nuclease;
KW Polymorphism; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; Transit peptide.
FT TRANSIT 1 30 Mitochondrion (Potential).
FT CHAIN 31 332 39S ribosomal protein L44, mitochondrial.
FT /FTId=PRO_0000030821.
FT DOMAIN 86 228 RNase III.
FT DOMAIN 236 306 DRBM.
FT VARIANT 138 138 T -> I (in dbSNP:rs11546406).
FT /FTId=VAR_034464.
FT CONFLICT 232 232 W -> R (in Ref. 1; BAB14802).
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
//
ID RM44_HUMAN Reviewed; 332 AA.
AC Q9H9J2; Q53S16; Q6IA62; Q9H821;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=39S ribosomal protein L44, mitochondrial;
DE Short=L44mt;
DE Short=MRP-L44;
DE EC=3.1.26.-;
DE Flags: Precursor;
GN Name=MRPL44;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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
RT project: 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
RT of the 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of the 39S subunit of mitochondrial ribosome.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC -!- SIMILARITY: Contains 1 RNase III domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_075066.1; NM_022915.3.
DR UniGene; Hs.203559; -.
DR ProteinModelPortal; Q9H9J2; -.
DR IntAct; Q9H9J2; 20.
DR MINT; MINT-1384665; -.
DR STRING; 9606.ENSP00000258383; -.
DR PhosphoSite; Q9H9J2; -.
DR DMDM; 51316917; -.
DR PaxDb; Q9H9J2; -.
DR PeptideAtlas; Q9H9J2; -.
DR PRIDE; Q9H9J2; -.
DR DNASU; 65080; -.
DR Ensembl; ENST00000258383; ENSP00000258383; ENSG00000135900.
DR GeneID; 65080; -.
DR KEGG; hsa:65080; -.
DR UCSC; uc002vnr.4; human.
DR CTD; 65080; -.
DR GeneCards; GC02P224786; -.
DR HGNC; HGNC:16650; MRPL44.
DR HPA; HPA038147; -.
DR MIM; 611849; gene.
DR neXtProt; NX_Q9H9J2; -.
DR Orphanet; 352563; Infantile hypertrophic cardiomyopathy due to MRPL44 deficiency.
DR PharmGKB; PA30976; -.
DR eggNOG; NOG327595; -.
DR HOGENOM; HOG000046065; -.
DR HOVERGEN; HBG054127; -.
DR InParanoid; Q9H9J2; -.
DR KO; K17425; -.
DR OMA; WDYSKPK; -.
DR OrthoDB; EOG7WQ7SN; -.
DR PhylomeDB; Q9H9J2; -.
DR ChiTaRS; mRpL44; human.
DR GenomeRNAi; 65080; -.
DR NextBio; 67272; -.
DR PRO; PR:Q9H9J2; -.
DR Bgee; Q9H9J2; -.
DR CleanEx; HS_MRPL44; -.
DR Genevestigator; Q9H9J2; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.10.1520.10; -; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR InterPro; IPR014720; dsRNA-bd_dom.
DR InterPro; IPR000999; RNase_III_dom.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS00517; RNASE_3_1; FALSE_NEG.
DR PROSITE; PS50142; RNASE_3_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Endonuclease; Hydrolase; Mitochondrion; Nuclease;
KW Polymorphism; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; Transit peptide.
FT TRANSIT 1 30 Mitochondrion (Potential).
FT CHAIN 31 332 39S ribosomal protein L44, mitochondrial.
FT /FTId=PRO_0000030821.
FT DOMAIN 86 228 RNase III.
FT DOMAIN 236 306 DRBM.
FT VARIANT 138 138 T -> I (in dbSNP:rs11546406).
FT /FTId=VAR_034464.
FT CONFLICT 232 232 W -> R (in Ref. 1; BAB14802).
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
//
MIM
611849
*RECORD*
*FIELD* NO
611849
*FIELD* TI
*611849 MITOCHONDRIAL RIBOSOMAL PROTEIN L44; MRPL44
*FIELD* TX
DESCRIPTION
Mitochondria have their own translation system for production of 13
read moreinner membrane proteins essential for oxidative phosphorylation. MRPL44
is a component of the large subunit of the mitochondrial ribosome that
is encoded by the nuclear genome (Koc et al., 2001).
CLONING
By searching databases using bovine Mrpl44 as query, Koc et al. (2001)
identified human MRPL44. They also identified MRPL44 homologs in mouse,
Drosophila, C. elegans, and yeast, but not in E. coli or Arabidopsis.
Mouse and human MRPL44 share 87% amino acid identity.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MRPL44
gene to chromosome 2 (TMAP RH12342).
MOLECULAR GENETICS
In 2 Finnish sisters with variable expression of combined oxidative
phosphorylation deficiency-16 (COXPD16; 615395), Carroll et al. (2013)
identified a homozygous mutation in the MRPL44 gene (L156R;
611849.0001). The mutation, which was found by whole-exome sequencing
and confirmed by Sanger sequencing, segregated with the disorder in the
family and was not found in several large control databases or in
controls. Haplotype analysis indicated distant consanguinity in the
family. One sister had hypertrophic cardiomyopathy resulting in death in
infancy, whereas the other had infantile-onset hypertrophic
cardiomyopathy, but was asymptomatic as a teenager. Both had hepatic
steatosis. The first patient had a combined deficiency of respiratory
complexes I and IV in heart and skeletal muscle, whereas the second had
a decrease of complex IV in fibroblasts. Transduction of wildtype MRPL44
into patient fibroblasts corrected the COX defects and restored assembly
of the large ribosomal subunit. The findings indicated that the MRPL44
mutation affected the respiratory chain in a tissue-specific manner, and
suggested that MRPL44 is required for assembly and stability of the
mitochondrial large ribosomal subunit.
*FIELD* AV
.0001
COMBINED OXIDATIVE PHOSPHORYLATION DEFICIENCY 16 (1 family)
MRPL44, LEU156ARG
In 2 Finnish sisters with variable expression of combined oxidative
phosphorylation deficiency-16 (COXPD16; 615395), Carroll et al. (2013)
identified a homozygous c.467T-G transversion in the MRPL44 gene,
resulting in a leu156-to-arg (L156R) substitution at a highly conserved
residue in the RNase III-like domain. The mutation, which was found by
whole-exome sequencing and confirmed by Sanger sequencing, segregated
with the disorder in the family and was not found in several large
control databases or in 436 control chromosomes. Haplotype analysis
indicated distant consanguinity in the family. One sister had
hypertrophic cardiomyopathy resulting in death in infancy, whereas the
other had infantile-onset hypertrophic cardiomyopathy, but was
asymptomatic as a teenager. Both had hepatic steatosis. The first
patient had a combined deficiency of respiratory complexes I and IV in
heart and skeletal muscle, whereas the second had a decrease of complex
IV in fibroblasts. Molecular modeling predicted that the mutation would
impair correct folding, resulting in protein instability. Western blot
analysis showed decreased levels of MRPL44 protein in the heart and
skeletal muscle from the deceased sib and decreased amounts of protein
in fibroblasts from the surviving sib. In vitro studies showed that the
mutant protein affected the stability or assembly of COX subunits,
although de novo synthesis of the polypeptides appeared to be
unaffected. Patient fibroblasts had decreased amounts of assembled large
ribosomal subunit and decreased levels of 16S rRNA, leading to complex
IV deficiency. Transduction of wildtype MRPL44 into patient fibroblasts
corrected the COX defects and restored assembly of the large ribosomal
subunit. The findings indicated that the MRPL44 mutation affected the
respiratory chain in a tissue-specific manner, and suggested that MRPL44
is required for assembly and stability of the mitochondrial large
ribosomal subunit.
*FIELD* RF
1. Carroll, C. J.; Isohanni, P.; Poyhonen, R.; Euro, L.; Richter,
U.; Brilhante, V.; Gotz, A.; Lahtinen, T.; Paetau, A.; Pihko, H.;
Battersby, B. J.; Tyynismaa, H.; Suomalainen, A.: Whole-exome sequencing
identifies a mutation in the mitochondrial ribosome protein MRPL44
to underlie mitochondrial infantile cardiomyopathy. J. Med. Genet. 50:
151-59, 2013.
2. Koc, E. C.; Burkhart, W.; Blackburn, K.; Moyer, M. B.; Schlatzer,
D. M.; Moseley, A.; Spremulli, L. L.: The large subunit of the mammalian
mitochondrial ribosome: analysis of the complement of ribosomal proteins
present. J. Biol. Chem. 276: 43958-43969, 2001.
*FIELD* CN
Cassandra L. Kniffin - updated: 9/3/2013
*FIELD* CD
Patricia A. Hartz: 2/26/2008
*FIELD* ED
carol: 09/06/2013
ckniffin: 9/3/2013
mgross: 3/4/2008
*RECORD*
*FIELD* NO
611849
*FIELD* TI
*611849 MITOCHONDRIAL RIBOSOMAL PROTEIN L44; MRPL44
*FIELD* TX
DESCRIPTION
Mitochondria have their own translation system for production of 13
read moreinner membrane proteins essential for oxidative phosphorylation. MRPL44
is a component of the large subunit of the mitochondrial ribosome that
is encoded by the nuclear genome (Koc et al., 2001).
CLONING
By searching databases using bovine Mrpl44 as query, Koc et al. (2001)
identified human MRPL44. They also identified MRPL44 homologs in mouse,
Drosophila, C. elegans, and yeast, but not in E. coli or Arabidopsis.
Mouse and human MRPL44 share 87% amino acid identity.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MRPL44
gene to chromosome 2 (TMAP RH12342).
MOLECULAR GENETICS
In 2 Finnish sisters with variable expression of combined oxidative
phosphorylation deficiency-16 (COXPD16; 615395), Carroll et al. (2013)
identified a homozygous mutation in the MRPL44 gene (L156R;
611849.0001). The mutation, which was found by whole-exome sequencing
and confirmed by Sanger sequencing, segregated with the disorder in the
family and was not found in several large control databases or in
controls. Haplotype analysis indicated distant consanguinity in the
family. One sister had hypertrophic cardiomyopathy resulting in death in
infancy, whereas the other had infantile-onset hypertrophic
cardiomyopathy, but was asymptomatic as a teenager. Both had hepatic
steatosis. The first patient had a combined deficiency of respiratory
complexes I and IV in heart and skeletal muscle, whereas the second had
a decrease of complex IV in fibroblasts. Transduction of wildtype MRPL44
into patient fibroblasts corrected the COX defects and restored assembly
of the large ribosomal subunit. The findings indicated that the MRPL44
mutation affected the respiratory chain in a tissue-specific manner, and
suggested that MRPL44 is required for assembly and stability of the
mitochondrial large ribosomal subunit.
*FIELD* AV
.0001
COMBINED OXIDATIVE PHOSPHORYLATION DEFICIENCY 16 (1 family)
MRPL44, LEU156ARG
In 2 Finnish sisters with variable expression of combined oxidative
phosphorylation deficiency-16 (COXPD16; 615395), Carroll et al. (2013)
identified a homozygous c.467T-G transversion in the MRPL44 gene,
resulting in a leu156-to-arg (L156R) substitution at a highly conserved
residue in the RNase III-like domain. The mutation, which was found by
whole-exome sequencing and confirmed by Sanger sequencing, segregated
with the disorder in the family and was not found in several large
control databases or in 436 control chromosomes. Haplotype analysis
indicated distant consanguinity in the family. One sister had
hypertrophic cardiomyopathy resulting in death in infancy, whereas the
other had infantile-onset hypertrophic cardiomyopathy, but was
asymptomatic as a teenager. Both had hepatic steatosis. The first
patient had a combined deficiency of respiratory complexes I and IV in
heart and skeletal muscle, whereas the second had a decrease of complex
IV in fibroblasts. Molecular modeling predicted that the mutation would
impair correct folding, resulting in protein instability. Western blot
analysis showed decreased levels of MRPL44 protein in the heart and
skeletal muscle from the deceased sib and decreased amounts of protein
in fibroblasts from the surviving sib. In vitro studies showed that the
mutant protein affected the stability or assembly of COX subunits,
although de novo synthesis of the polypeptides appeared to be
unaffected. Patient fibroblasts had decreased amounts of assembled large
ribosomal subunit and decreased levels of 16S rRNA, leading to complex
IV deficiency. Transduction of wildtype MRPL44 into patient fibroblasts
corrected the COX defects and restored assembly of the large ribosomal
subunit. The findings indicated that the MRPL44 mutation affected the
respiratory chain in a tissue-specific manner, and suggested that MRPL44
is required for assembly and stability of the mitochondrial large
ribosomal subunit.
*FIELD* RF
1. Carroll, C. J.; Isohanni, P.; Poyhonen, R.; Euro, L.; Richter,
U.; Brilhante, V.; Gotz, A.; Lahtinen, T.; Paetau, A.; Pihko, H.;
Battersby, B. J.; Tyynismaa, H.; Suomalainen, A.: Whole-exome sequencing
identifies a mutation in the mitochondrial ribosome protein MRPL44
to underlie mitochondrial infantile cardiomyopathy. J. Med. Genet. 50:
151-59, 2013.
2. Koc, E. C.; Burkhart, W.; Blackburn, K.; Moyer, M. B.; Schlatzer,
D. M.; Moseley, A.; Spremulli, L. L.: The large subunit of the mammalian
mitochondrial ribosome: analysis of the complement of ribosomal proteins
present. J. Biol. Chem. 276: 43958-43969, 2001.
*FIELD* CN
Cassandra L. Kniffin - updated: 9/3/2013
*FIELD* CD
Patricia A. Hartz: 2/26/2008
*FIELD* ED
carol: 09/06/2013
ckniffin: 9/3/2013
mgross: 3/4/2008