LPPRC_MOUSE
ID LPPRC_MOUSE Reviewed; 1392 AA.
AC Q6PB66; Q8K4V0; Q9CRX4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Leucine-rich PPR motif-containing protein, mitochondrial;
DE AltName: Full=130 kDa leucine-rich protein;
DE Short=LRP 130;
DE Short=mLRP130;
DE Flags: Precursor;
GN Name=Lrpprc; Synonyms=Lrp130;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12071956; DOI=10.1046/j.1432-1033.2002.02966.x;
RA Tsuchiya N., Fukuda H., Sugimura T., Nagao M., Nakagama H.;
RT "LRP130, a protein containing nine pentatricopeptide repeat motifs,
RT interacts with a single-stranded cytosine-rich sequence of mouse
RT hypervariable minisatellite Pc-1.";
RL Eur. J. Biochem. 269:2927-2933(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 681-1392.
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP RNA-BINDING.
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 [5]
RP INTERACTION WITH FOXO1.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-151; LYS-186; LYS-225 AND
RP LYS-462, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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 (By similarity). Binds single-stranded DNA.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CECR2, HEBP2, MAP1S and UXT (By similarity).
CC Interacts with PPARGC1A (By similarity). Interacts with FOXO1.
CC Component of mRNP complexes associated with HNRPA1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q6PB66; Q9R1E0: Foxo1; NbExp=2; IntAct=EBI-1371262, EBI-1371343;
CC Q6PB66; O70343: Ppargc1a; NbExp=2; IntAct=EBI-1371262, EBI-1371053;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:12071956}. Nucleus, nucleoplasm {ECO:0000250}.
CC Nucleus inner membrane {ECO:0000250}. Nucleus outer membrane
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart, liver and kidney.
CC Weakly expressed in brain, skeletal muscle and testes.
CC {ECO:0000269|PubMed:12071956}.
CC -!- DEVELOPMENTAL STAGE: Expressed at embryonic stages 7 dpc, 11 dpc, 15
CC dpc and 17 dpc with a slight increase of levels during development.
CC {ECO:0000269|PubMed:12071956}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH59862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29082.2; Type=Erroneous translation; Note=CTG leucine codon is translated as initiator methionine.; Evidence={ECO:0000305};
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DR EMBL; AB027124; BAB93528.1; ALT_SEQ; mRNA.
DR EMBL; BC059862; AAH59862.1; ALT_INIT; mRNA.
DR EMBL; AK013955; BAB29082.2; ALT_SEQ; mRNA.
DR CCDS; CCDS29003.2; -.
DR RefSeq; NP_082509.2; NM_028233.2.
DR AlphaFoldDB; Q6PB66; -.
DR BioGRID; 215365; 16.
DR IntAct; Q6PB66; 9.
DR MINT; Q6PB66; -.
DR STRING; 10090.ENSMUSP00000107927; -.
DR iPTMnet; Q6PB66; -.
DR PhosphoSitePlus; Q6PB66; -.
DR SwissPalm; Q6PB66; -.
DR EPD; Q6PB66; -.
DR jPOST; Q6PB66; -.
DR MaxQB; Q6PB66; -.
DR PaxDb; Q6PB66; -.
DR PeptideAtlas; Q6PB66; -.
DR PRIDE; Q6PB66; -.
DR ProteomicsDB; 252485; -.
DR Antibodypedia; 47400; 176 antibodies from 29 providers.
DR DNASU; 72416; -.
DR Ensembl; ENSMUST00000112308; ENSMUSP00000107927; ENSMUSG00000024120.
DR GeneID; 72416; -.
DR KEGG; mmu:72416; -.
DR UCSC; uc008dtc.1; mouse.
DR CTD; 10128; -.
DR MGI; MGI:1919666; Lrpprc.
DR VEuPathDB; HostDB:ENSMUSG00000024120; -.
DR eggNOG; KOG4318; Eukaryota.
DR GeneTree; ENSGT00960000186682; -.
DR HOGENOM; CLU_006166_0_0_1; -.
DR InParanoid; Q6PB66; -.
DR OMA; NVPMDIS; -.
DR OrthoDB; 1344243at2759; -.
DR PhylomeDB; Q6PB66; -.
DR TreeFam; TF323626; -.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 72416; 12 hits in 70 CRISPR screens.
DR ChiTaRS; Lrpprc; mouse.
DR PRO; PR:Q6PB66; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6PB66; protein.
DR Bgee; ENSMUSG00000024120; Expressed in cardiac muscle of left ventricle and 260 other tissues.
DR ExpressionAtlas; Q6PB66; baseline and differential.
DR Genevisible; Q6PB66; MM.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISS:HGNC-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISS:HGNC-UCL.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
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:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:HGNC-UCL.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0000957; P:mitochondrial RNA catabolic process; IMP:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0000961; P:negative regulation of mitochondrial RNA catabolic process; IMP:MGI.
DR GO; GO:0070129; P:regulation of mitochondrial translation; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 3.
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; 3.
DR Pfam; PF01535; PPR; 1.
DR Pfam; PF17177; PPR_long; 1.
DR TIGRFAMs; TIGR00756; PPR; 2.
DR PROSITE; PS51375; PPR; 13.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Membrane; Mitochondrion; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Transit peptide; Transport.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 60..1392
FT /note="Leucine-rich PPR motif-containing protein,
FT mitochondrial"
FT /id="PRO_0000295546"
FT REPEAT 125..159
FT /note="PPR 1"
FT REPEAT 160..194
FT /note="PPR 2"
FT REPEAT 195..229
FT /note="PPR 3"
FT REPEAT 230..264
FT /note="PPR 4"
FT REPEAT 265..299
FT /note="PPR 5"
FT REPEAT 300..334
FT /note="PPR 6"
FT REPEAT 402..436
FT /note="PPR 7"
FT REPEAT 437..471
FT /note="PPR 8"
FT REPEAT 677..708
FT /note="PPR 9"
FT REPEAT 709..745
FT /note="PPR 10"
FT REPEAT 746..783
FT /note="PPR 11"
FT REPEAT 784..820
FT /note="PPR 12"
FT REPEAT 821..856
FT /note="PPR 13"
FT REPEAT 953..987
FT /note="PPR 14"
FT REPEAT 1030..1064
FT /note="PPR 15"
FT REPEAT 1065..1101
FT /note="PPR 16"
FT REPEAT 1102..1136
FT /note="PPR 17"
FT REPEAT 1137..1175
FT /note="PPR 18"
FT REPEAT 1176..1210
FT /note="PPR 19"
FT REPEAT 1315..1349
FT /note="PPR 20"
FT REGION 931..1050
FT /note="RNA-binding"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 186
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 225
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42704"
FT MOD_RES 462
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 749
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42704"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42704"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SGE0"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42704"
FT MOD_RES 1137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42704"
FT CONFLICT 35
FT /note="S -> F (in Ref. 1; BAB93528)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="R -> L (in Ref. 1; BAB93528)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="D -> V (in Ref. 1; BAB93528)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="K -> E (in Ref. 1; BAB93528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1392 AA; 156615 MW; CC774240FCDBB2A6 CRC64;
MAALLRPARW LLGAAAAPRL PLSLRLPAGV PGRLSSVVRV AAVGSRPAAG ERLSQARLYA
IVAEKRDLQE EPAPVRKNSS QFDWALMRLD NSVRRTGRIT KGLLQRVFES TCSSGSPGSN
QALLLLRSCG SLLPELSLAE RTEFAHKIWD KLQQLGVVYD VSHYNALLKV YLQNEYKFSP
TDFLAKMEGA NIQPNRVTYQ RLIAAYCNVG DIEGASKILG FMKTKDLPIT EAVFSALVTG
HARAGDMENA ENILTVMKQA GIEPGPDTYL ALLNAHAERG DIGQVRQILE KVEKSDHYFM
DRDFLQVIFS FSKAGYPQYV SEILEKITYE RRSIPDAMNL ILFLATEKLE DTAFQVLLAL
PLSKDESSDN FGSFFLRHCV TLDLPPEKLI DYCRRLRDAK LHSSSLQFTL HCALQANRTA
LAKAVMEALR EEGFPIRPHY FWPLLAGHQK TKNVQGIIDI LKIMNKVGVD PDQETYINYV
FPCFDSAQSV RAALQENECL LASSTFAQAE VKNEAINGNL QNILSFLESN TLPFSFSSLR
NSLILGFRRS MNIDLWSKIT ELLYKDERYC SKPPGPAEAV GYFLYNLIDS MSDSEVQAKE
ERLRQYFHQL QEMNVKVPEN IYKGICNLLN TYHVPELIKD IKVLVDREKV DSQKTSQVTS
SDLESTLEKL KAEGQPVGSA LKQLLLLLCS EENMQKALEV KAKYESDMVI GGYAALINLC
CRHDNAEDAW NLKQEVDRLD ASAILDTAKY VALVKVLGKH SRLQDAINIL KEMKEKDVVI
KDATVLSFFH ILNGAALRGE IETVKQLHEA IVTLGLAKPS SNISFPLVTV HLEKGDLPAA
LEASIACHKK YKVLPRIHDV LCKLVEKGET DLIQKAMDFV SQEQGEMTML YDLFFAFLQT
GNYKEAKKII ETPGIRARPT RLQWFCDRCI ASNQVEALEK LVELTEKLFE CDRDQMYYNL
LKLYKISSDW QRADAAWTKM QEENIIPRER TLRLLAEILK TSNQEVPFDV PELWFGDDRP
SLSPSSRSAG EDVTEKTLLS NCKLKKSKDA YNIFLKAEKQ NVVFSSETYS TLIGLLLSKD
DFTQAMHVKD FAETHIKGFT LNDAANSLLI IRQVRRDYLK GALATLRAAL DLKQVPSQIA
VTRLIQALAL KGDVESIEAI QRMVAGLDTI GLSKMVFINN IALAQMKNNK LDAAIENIEH
LLASENQAIE PQYFGLSYLF RKVIEEQMEP ALEKLSIMSE RMANQFALYK PVTDLFLQLV
DSGKVDEARA LLERCGAIAE QSSLLSVFCL RTSQKPKKAP VLKTLLELIP ELRDNDKVYS
CSMKSYALDK DVASAKALYE YLTAKNLKLD DLFLKRYAAL LKDVGEPVPF PEPPESFAFY
IKQLKEARES PS
