LPPRC_HUMAN
ID LPPRC_HUMAN Reviewed; 1394 AA.
AC P42704; A0PJE3; A8K1V1; Q53PC0; Q53QN7; Q6ZUD8; Q7Z7A6; Q96D84;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Leucine-rich PPR motif-containing protein, mitochondrial;
DE AltName: Full=130 kDa leucine-rich protein;
DE Short=LRP 130;
DE AltName: Full=GP130;
DE Flags: Precursor;
GN Name=LRPPRC; Synonyms=LRP130;
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], FUNCTION IN COX ASSEMBLY, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15139850; DOI=10.1042/bj20040469;
RA Xu F., Morin C., Mitchell G., Ackerley C., Robinson B.H.;
RT "The role of the LRPPRC (leucine-rich pentatricopeptide repeat cassette)
RT gene in cytochrome oxidase assembly: mutation causes lowered levels of COX
RT (cytochrome c oxidase) I and COX III mRNA.";
RL Biochem. J. 382:331-336(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus, and Testis;
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 [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=Brain, Muscle, Placenta, and Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 108-1394.
RC TISSUE=Liver;
RX PubMed=8012652; DOI=10.1007/bf02631402;
RA Hou J., Wang F., McKeehan W.L.;
RT "Molecular cloning and expression of the gene for a major leucine-rich
RT protein from human hepatoblastoma cells (HepG2).";
RL In Vitro Cell. Dev. Biol. Anim. 30A:111-114(1994).
RN [6]
RP PROTEIN SEQUENCE OF 156-170; 260-280; 304-314; 454-463; 530-541; 656-672;
RP 740-750; 764-772; 1050-1059; 1091-1098; 1177-1189 AND 1339-1347, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP FUNCTION IN MRNA EXPORT, IDENTIFICATION IN NMRNP COMPLEXES, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11585913; DOI=10.1128/mcb.21.21.7307-7319.2001;
RA Mili S., Shu H.J., Zhao Y., Pinol-Roma S.;
RT "Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA:
RT candidate intermediates in formation and export of mRNA.";
RL Mol. Cell. Biol. 21:7307-7319(2001).
RN [8]
RP TISSUE SPECIFICITY, AND INTERACTION WITH CECR2; HEBP2; MAP1S AND UXT.
RX PubMed=11827465; DOI=10.1006/geno.2001.6679;
RA Liu L., McKeehan W.L.;
RT "Sequence analysis of LRPPRC and its SEC1 domain interaction partners
RT suggests roles in cytoskeletal organization, vesicular trafficking,
RT nucleocytosolic shuttling, and chromosome activity.";
RL Genomics 79:124-136(2002).
RN [9]
RP RNA-BINDING, FUNCTION IN MRNA EXPORT, AND SUBCELLULAR LOCATION.
RX PubMed=12832482; DOI=10.1128/mcb.23.14.4972-4982.2003;
RA Mili S., Pinol-Roma S.;
RT "LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding
RT domain, is bound in vivo to mitochondrial and nuclear RNAs.";
RL Mol. Cell. Biol. 23:4972-4982(2003).
RN [10]
RP FUNCTION IN MRNA EXPORT, AND SUBCELLULAR LOCATION.
RX PubMed=15081402; DOI=10.1016/j.bbrc.2004.03.103;
RA Tsuchiya N., Fukuda H., Nakashima K., Nagao M., Sugimura T., Nakagama H.;
RT "LRP130, a single-stranded DNA/RNA-binding protein, localizes at the outer
RT nuclear and endoplasmic reticulum membrane, and interacts with mRNA in
RT vivo.";
RL Biochem. Biophys. Res. Commun. 317:736-743(2004).
RN [11]
RP FUNCTION IN TRANSCRIPTION REGULATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15272088; DOI=10.1093/nar/gkh722;
RA Labialle S., Dayan G., Gayet L., Rigal D., Gambrelle J., Baggetto L.G.;
RT "New invMED1 element cis-activates human multidrug-related MDR1 and MVP
RT genes, involving the LRP130 protein.";
RL Nucleic Acids Res. 32:3864-3876(2004).
RN [12]
RP INTERACTION WITH MAP1S.
RX PubMed=15907802; DOI=10.1016/j.bbrc.2005.05.006;
RA Liu L., Vo A., Liu G., McKeehan W.L.;
RT "Putative tumor suppressor RASSF1 interactive protein and cell death
RT inducer C19ORF5 is a DNA binding protein.";
RL Biochem. Biophys. Res. Commun. 332:670-676(2005).
RN [13]
RP FUNCTION IN TRANSCRIPTION REGULATION, AND INTERACTION WITH PPARGC1A.
RX PubMed=17050673; DOI=10.1101/gad.1483906;
RA Cooper M.P., Qu L., Rohas L.M., Lin J., Yang W., Erdjument-Bromage H.,
RA Tempst P., Spiegelman B.M.;
RT "Defects in energy homeostasis in Leigh syndrome French Canadian variant
RT through PGC-1alpha/LRP130 complex.";
RL Genes Dev. 20:2996-3009(2006).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-155; LYS-187; LYS-292; LYS-613;
RP LYS-726 AND LYS-750, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1026; SER-1029; THR-1136 AND
RP SER-1138, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
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 [18]
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 [19]
RP VARIANT MC4DN5 VAL-354.
RX PubMed=12529507; DOI=10.1073/pnas.242716699;
RA Mootha V.K., Lepage P., Miller K., Bunkenborg J., Reich M., Hjerrild M.,
RA Delmonte T., Villeneuve A., Sladek R., Xu F., Mitchell G.A., Morin C.,
RA Mann M., Hudson T.J., Robinson B., Rioux J.D., Lander E.S.;
RT "Identification of a gene causing human cytochrome c oxidase deficiency by
RT integrative genomics.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:605-610(2003).
RN [20]
RP VARIANTS MC4DN5 VAL-866 DEL AND LYS-909 DEL.
RX PubMed=26510951; DOI=10.1093/brain/awv291;
RA Olahova M., Hardy S.A., Hall J., Yarham J.W., Haack T.B., Wilson W.C.,
RA Alston C.L., He L., Aznauryan E., Brown R.M., Brown G.K., Morris A.A.,
RA Mundy H., Broomfield A., Barbosa I.A., Simpson M.A., Deshpande C.,
RA Moeslinger D., Koch J., Stettner G.M., Bonnen P.E., Prokisch H.,
RA Lightowlers R.N., McFarland R., Chrzanowska-Lightowlers Z.M., Taylor R.W.;
RT "LRPPRC mutations cause early-onset multisystem mitochondrial disease
RT outside of the French-Canadian population.";
RL Brain 138:3503-3519(2015).
CC -!- FUNCTION: May play a role in RNA metabolism in both nuclei and
CC mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs
CC and is part of nmRNP complexes at late stages of mRNA maturation which
CC are possibly associated with nuclear mRNA export. May bind mature mRNA
CC in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA.
CC Plays a role in translation or stability of mitochondrially encoded
CC cytochrome c oxidase (COX) subunits. May be involved in transcription
CC regulation. Cooperates with PPARGC1A to regulate certain
CC mitochondrially encoded genes and gluconeogenic genes and may regulate
CC docking of PPARGC1A to transcription factors. Seems to be involved in
CC the transcription regulation of the multidrug-related genes MDR1 and
CC MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1
CC and MVP gene promoters. Binds single-stranded DNA (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:11585913, ECO:0000269|PubMed:12832482,
CC ECO:0000269|PubMed:15081402, ECO:0000269|PubMed:15139850,
CC ECO:0000269|PubMed:15272088, ECO:0000269|PubMed:17050673}.
CC -!- SUBUNIT: Interacts with CECR2, HEBP2, MAP1S and UXT. Interacts with
CC PPARGC1A. Interacts with FOXO1 (By similarity). Component of mRNP
CC complexes associated with HNRPA1. {ECO:0000250,
CC ECO:0000269|PubMed:11585913, ECO:0000269|PubMed:11827465,
CC ECO:0000269|PubMed:15907802, ECO:0000269|PubMed:17050673}.
CC -!- INTERACTION:
CC P42704; P05067: APP; NbExp=8; IntAct=EBI-1050853, EBI-77613;
CC P42704; P06730: EIF4E; NbExp=6; IntAct=EBI-1050853, EBI-73440;
CC P42704; Q9UBK2: PPARGC1A; NbExp=2; IntAct=EBI-1050853, EBI-765486;
CC P42704; Q9GZT3: SLIRP; NbExp=3; IntAct=EBI-1050853, EBI-1050793;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Nucleus, nucleoplasm. Nucleus
CC inner membrane. Nucleus outer membrane. Note=Seems to be predominantly
CC mitochondrial.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. Expression is highest in
CC heart, skeletal muscle, kidney and liver, intermediate in brain, non-
CC mucosal colon, spleen and placenta, and lowest in small intestine,
CC thymus, lung and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:11827465, ECO:0000269|PubMed:15139850}.
CC -!- DISEASE: Mitochondrial complex IV deficiency, nuclear type 5 (MC4DN5)
CC [MIM:220111]: An autosomal recessive, severe mitochondrial disease with
CC multisystemic manifestations and early onset. Clinical features include
CC delayed psychomotor development, impaired intellectual development with
CC speech delay, mild dysmorphic facial features, hypotonia, ataxia, and
CC seizures. Brain imaging shows bilaterally symmetrical necrotic lesions
CC in subcortical brain regions. Mortality is high, due to episodes of
CC severe metabolic acidosis and coma. {ECO:0000269|PubMed:12529507,
CC ECO:0000269|PubMed:26510951}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67549.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA67549.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY289212; AAP41922.1; -; mRNA.
DR EMBL; AK125781; BAC86287.1; -; mRNA.
DR EMBL; AK290016; BAF82705.1; -; mRNA.
DR EMBL; AC108476; AAY24012.1; -; Genomic_DNA.
DR EMBL; AC127379; AAY24043.1; -; Genomic_DNA.
DR EMBL; BC010282; AAH10282.1; -; mRNA.
DR EMBL; BC026034; AAH26034.1; -; mRNA.
DR EMBL; BC050311; AAH50311.1; -; mRNA.
DR EMBL; BC130285; AAI30286.1; -; mRNA.
DR EMBL; M92439; AAA67549.1; ALT_SEQ; mRNA.
DR CCDS; CCDS33189.1; -.
DR PIR; S27954; S27954.
DR RefSeq; NP_573566.2; NM_133259.3.
DR AlphaFoldDB; P42704; -.
DR BioGRID; 115432; 659.
DR CORUM; P42704; -.
DR DIP; DIP-27543N; -.
DR IntAct; P42704; 113.
DR MINT; P42704; -.
DR STRING; 9606.ENSP00000260665; -.
DR ChEMBL; CHEMBL4295762; -.
DR CarbonylDB; P42704; -.
DR GlyGen; P42704; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P42704; -.
DR MetOSite; P42704; -.
DR PhosphoSitePlus; P42704; -.
DR SwissPalm; P42704; -.
DR BioMuta; LRPPRC; -.
DR DMDM; 156632706; -.
DR EPD; P42704; -.
DR jPOST; P42704; -.
DR MassIVE; P42704; -.
DR MaxQB; P42704; -.
DR PaxDb; P42704; -.
DR PeptideAtlas; P42704; -.
DR PRIDE; P42704; -.
DR ProteomicsDB; 55547; -.
DR Antibodypedia; 47400; 176 antibodies from 29 providers.
DR DNASU; 10128; -.
DR Ensembl; ENST00000260665.12; ENSP00000260665.7; ENSG00000138095.20.
DR GeneID; 10128; -.
DR KEGG; hsa:10128; -.
DR MANE-Select; ENST00000260665.12; ENSP00000260665.7; NM_133259.4; NP_573566.2.
DR UCSC; uc002rtr.3; human.
DR CTD; 10128; -.
DR DisGeNET; 10128; -.
DR GeneCards; LRPPRC; -.
DR HGNC; HGNC:15714; LRPPRC.
DR HPA; ENSG00000138095; Low tissue specificity.
DR MalaCards; LRPPRC; -.
DR MIM; 220111; phenotype.
DR MIM; 607544; gene.
DR neXtProt; NX_P42704; -.
DR OpenTargets; ENSG00000138095; -.
DR Orphanet; 70472; Congenital lactic acidosis, Saguenay-Lac-Saint-Jean type.
DR PharmGKB; PA30459; -.
DR VEuPathDB; HostDB:ENSG00000138095; -.
DR eggNOG; KOG4318; Eukaryota.
DR GeneTree; ENSGT00960000186682; -.
DR HOGENOM; CLU_006166_0_0_1; -.
DR InParanoid; P42704; -.
DR OMA; NVPMDIS; -.
DR OrthoDB; 1344243at2759; -.
DR PhylomeDB; P42704; -.
DR TreeFam; TF323626; -.
DR PathwayCommons; P42704; -.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR SignaLink; P42704; -.
DR BioGRID-ORCS; 10128; 407 hits in 1088 CRISPR screens.
DR ChiTaRS; LRPPRC; human.
DR GeneWiki; LRPPRC; -.
DR GenomeRNAi; 10128; -.
DR Pharos; P42704; Tbio.
DR PRO; PR:P42704; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P42704; protein.
DR Bgee; ENSG00000138095; Expressed in skeletal muscle tissue of rectus abdominis and 218 other tissues.
DR ExpressionAtlas; P42704; baseline and differential.
DR Genevisible; P42704; HS.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:HGNC-UCL.
DR GO; GO:0005856; C:cytoskeleton; IDA:HGNC-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:HGNC-UCL.
DR GO; GO:0008017; F:microtubule binding; TAS:HGNC-UCL.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0000957; P:mitochondrial RNA catabolic process; IEA:Ensembl.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; TAS:HGNC-UCL.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0000961; P:negative regulation of mitochondrial RNA catabolic process; IEA:Ensembl.
DR GO; GO:0070129; P:regulation of mitochondrial translation; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR033490; LRP130.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR033443; PPR_long.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR46669; PTHR46669; 2.
DR Pfam; PF01535; PPR; 3.
DR Pfam; PF13812; PPR_3; 1.
DR Pfam; PF17177; PPR_long; 1.
DR TIGRFAMs; TIGR00756; PPR; 2.
DR PROSITE; PS51375; PPR; 11.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Disease variant; DNA-binding;
KW Leigh syndrome; Membrane; Mitochondrion; mRNA transport; Nucleus;
KW Phosphoprotein; Primary mitochondrial disease; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation; Transit peptide;
KW Transport.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 60..1394
FT /note="Leucine-rich PPR motif-containing protein,
FT mitochondrial"
FT /id="PRO_0000084467"
FT REPEAT 126..160
FT /note="PPR 1"
FT REPEAT 161..195
FT /note="PPR 2"
FT REPEAT 196..230
FT /note="PPR 3"
FT REPEAT 231..265
FT /note="PPR 4"
FT REPEAT 266..300
FT /note="PPR 5"
FT REPEAT 301..335
FT /note="PPR 6"
FT REPEAT 403..437
FT /note="PPR 7"
FT REPEAT 438..472
FT /note="PPR 8"
FT REPEAT 678..709
FT /note="PPR 9"
FT REPEAT 710..746
FT /note="PPR 10"
FT REPEAT 747..784
FT /note="PPR 11"
FT REPEAT 785..820
FT /note="PPR 12"
FT REPEAT 821..856
FT /note="PPR 13"
FT REPEAT 954..988
FT /note="PPR 14"
FT REPEAT 1031..1065
FT /note="PPR 15"
FT REPEAT 1066..1102
FT /note="PPR 16"
FT REPEAT 1103..1137
FT /note="PPR 17"
FT REPEAT 1138..1175
FT /note="PPR 18"
FT REPEAT 1176..1210
FT /note="PPR 19"
FT REPEAT 1317..1351
FT /note="PPR 20"
FT REGION 1121..1394
FT /note="RNA-binding"
FT MOD_RES 155
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 187
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 226
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PB66"
FT MOD_RES 292
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 463
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PB66"
FT MOD_RES 613
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 726
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 750
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SGE0"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1136
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 354
FT /note="A -> V (in MC4DN5; dbSNP:rs119466000)"
FT /evidence="ECO:0000269|PubMed:12529507"
FT /id="VAR_018656"
FT VARIANT 478
FT /note="T -> A (in dbSNP:rs35035668)"
FT /id="VAR_052935"
FT VARIANT 866
FT /note="Missing (in MC4DN5; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26510951"
FT /id="VAR_075428"
FT VARIANT 909
FT /note="Missing (in MC4DN5; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26510951"
FT /id="VAR_075429"
FT CONFLICT 54
FT /note="S -> G (in Ref. 2; BAF82705)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="S -> F (in Ref. 5; AAA67549)"
FT /evidence="ECO:0000305"
FT CONFLICT 528..531
FT /note="LKSN -> YFPI (in Ref. 4; AAH26034)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="L -> V (in Ref. 5; AAA67549)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="Y -> N (in Ref. 5; AAA67549)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="S -> R (in Ref. 5; AAA67549)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="Q -> R (in Ref. 2; BAC86287)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="K -> R (in Ref. 2; BAC86287)"
FT /evidence="ECO:0000305"
FT CONFLICT 750..752
FT /note="KYV -> NYL (in Ref. 5; AAA67549)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="N -> K (in Ref. 5; AAA67549)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="N -> D (in Ref. 2; BAC86287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1394 AA; 157905 MW; 61AB0C8BF8A972E6 CRC64;
MAALLRSARW LLRAGAAPRL PLSLRLLPGG PGRLHAASYL PAARAGPVAG GLLSPARLYA
IAAKEKDIQE ESTFSSRKIS NQFDWALMRL DLSVRRTGRI PKKLLQKVFN DTCRSGGLGG
SHALLLLRSC GSLLPELKLE ERTEFAHRIW DTLQKLGAVY DVSHYNALLK VYLQNEYKFS
PTDFLAKMEE ANIQPNRVTY QRLIASYCNV GDIEGASKIL GFMKTKDLPV TEAVFSALVT
GHARAGDMEN AENILTVMRD AGIEPGPDTY LALLNAYAEK GDIDHVKQTL EKVEKSELHL
MDRDLLQIIF SFSKAGYPQY VSEILEKVTC ERRYIPDAMN LILLLVTEKL EDVALQILLA
CPVSKEDGPS VFGSFFLQHC VTMNTPVEKL TDYCKKLKEV QMHSFPLQFT LHCALLANKT
DLAKALMKAV KEEGFPIRPH YFWPLLVGRR KEKNVQGIIE ILKGMQELGV HPDQETYTDY
VIPCFDSVNS ARAILQENGC LSDSDMFSQA GLRSEAANGN LDFVLSFLKS NTLPISLQSI
RSSLLLGFRR SMNINLWSEI TELLYKDGRY CQEPRGPTEA VGYFLYNLID SMSDSEVQAK
EEHLRQYFHQ LEKMNVKIPE NIYRGIRNLL ESYHVPELIK DAHLLVESKN LDFQKTVQLT
SSELESTLET LKAENQPIRD VLKQLILVLC SEENMQKALE LKAKYESDMV TGGYAALINL
CCRHDKVEDA LNLKEEFDRL DSSAVLDTGK YVGLVRVLAK HGKLQDAINI LKEMKEKDVL
IKDTTALSFF HMLNGAALRG EIETVKQLHE AIVTLGLAEP STNISFPLVT VHLEKGDLST
ALEVAIDCYE KYKVLPRIHD VLCKLVEKGE TDLIQKAMDF VSQEQGEMVM LYDLFFAFLQ
TGNYKEAKKI IETPGIRARS ARLQWFCDRC VANNQVETLE KLVELTQKLF ECDRDQMYYN
LLKLYKINGD WQRADAVWNK IQEENVIPRE KTLRLLAEIL REGNQEVPFD VPELWYEDEK
HSLNSSSAST TEPDFQKDIL IACRLNQKKG AYDIFLNAKE QNIVFNAETY SNLIKLLMSE
DYFTQAMEVK AFAETHIKGF TLNDAANSRL IITQVRRDYL KEAVTTLKTV LDQQQTPSRL
AVTRVIQALA MKGDVENIEV VQKMLNGLED SIGLSKMVFI NNIALAQIKN NNIDAAIENI
ENMLTSENKV IEPQYFGLAY LFRKVIEEQL EPAVEKISIM AERLANQFAI YKPVTDFFLQ
LVDAGKVDDA RALLQRCGAI AEQTPILLLF LLRNSRKQGK ASTVKSVLEL IPELNEKEEA
YNSLMKSYVS EKDVTSAKAL YEHLTAKNTK LDDLFLKRYA SLLKYAGEPV PFIEPPESFE
FYAQQLRKLR ENSS
