CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015244
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Leucine-rich PPR motif-containing protein, mitochondrial 
Protein Synonyms/Alias
 130 kDa leucine-rich protein; LRP 130; mLRP130 
Gene Name
 Lrpprc 
Gene Synonyms/Alias
 Lrp130 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
147ERTEFAHKIWDKLQQacetylation[1]
151FAHKIWDKLQQLGVVacetylation[2]
186SPTDFLAKMEGANIQacetylation[1, 2, 3]
223SKILGFMKTKDLPITacetylation[1]
225ILGFMKTKDLPITEAacetylation[2]
291QVRQILEKVEKSDHYacetylation[1, 2, 3]
462QGIIDILKIMNKVGVacetylation[1, 2, 3, 4, 5, 6]
565KITELLYKDERYCSKacetylation[1, 6]
642PELIKDIKVLVDREKacetylation[2, 3]
669DLESTLEKLKAEGQPacetylation[3, 5, 7]
849EASIACHKKYKVLPRacetylation[2]
863RIHDVLCKLVEKGETacetylation[1]
867VLCKLVEKGETDLIQacetylation[1, 3, 6]
965YNLLKLYKISSDWQRacetylation[8]
965YNLLKLYKISSDWQRsuccinylation[8]
1036AGEDVTEKTLLSNCKacetylation[1, 3]
1048NCKLKKSKDAYNIFLacetylation[1]
1056DAYNIFLKAEKQNVVacetylation[1, 3, 7]
1120QVRRDYLKGALATLRacetylation[8]
1120QVRRDYLKGALATLRsuccinylation[8]
1133LRAALDLKQVPSQIAacetylation[3]
1317PELRDNDKVYSCSMKacetylation[6]
1330MKSYALDKDVASAKAacetylation[1]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [6] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [8] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters (By similarity). Binds single-stranded DNA. 
Sequence Annotation
 REPEAT 125 159 PPR 1.
 REPEAT 160 194 PPR 2.
 REPEAT 195 229 PPR 3.
 REPEAT 230 264 PPR 4.
 REPEAT 265 299 PPR 5.
 REPEAT 300 334 PPR 6.
 REPEAT 402 436 PPR 7.
 REPEAT 437 471 PPR 8.
 REPEAT 677 708 PPR 9.
 REPEAT 709 745 PPR 10.
 REPEAT 746 783 PPR 11.
 REPEAT 784 820 PPR 12.
 REPEAT 821 856 PPR 13.
 REPEAT 953 987 PPR 14.
 REPEAT 1030 1064 PPR 15.
 REPEAT 1065 1101 PPR 16.
 REPEAT 1102 1136 PPR 17.
 REPEAT 1137 1175 PPR 18.
 REPEAT 1176 1210 PPR 19.
 REPEAT 1315 1349 PPR 20.
 REGION 931 1050 RNA-binding.
 MOD_RES 186 186 N6-acetyllysine (By similarity).
 MOD_RES 291 291 N6-acetyllysine (By similarity).
 MOD_RES 749 749 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; DNA-binding; Membrane; Mitochondrion; mRNA transport; Nucleus; Reference proteome; Repeat; RNA-binding; Transcription; Transcription regulation; Transit peptide; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1392 AA 
Protein Sequence
MAALLRPARW LLGAAAAPRL PLSLRLPAGV PGRLSSVVRV AAVGSRPAAG ERLSQARLYA 60
IVAEKRDLQE EPAPVRKNSS QFDWALMRLD NSVRRTGRIT KGLLQRVFES TCSSGSPGSN 120
QALLLLRSCG SLLPELSLAE RTEFAHKIWD KLQQLGVVYD VSHYNALLKV YLQNEYKFSP 180
TDFLAKMEGA NIQPNRVTYQ RLIAAYCNVG DIEGASKILG FMKTKDLPIT EAVFSALVTG 240
HARAGDMENA ENILTVMKQA GIEPGPDTYL ALLNAHAERG DIGQVRQILE KVEKSDHYFM 300
DRDFLQVIFS FSKAGYPQYV SEILEKITYE RRSIPDAMNL ILFLATEKLE DTAFQVLLAL 360
PLSKDESSDN FGSFFLRHCV TLDLPPEKLI DYCRRLRDAK LHSSSLQFTL HCALQANRTA 420
LAKAVMEALR EEGFPIRPHY FWPLLAGHQK TKNVQGIIDI LKIMNKVGVD PDQETYINYV 480
FPCFDSAQSV RAALQENECL LASSTFAQAE VKNEAINGNL QNILSFLESN TLPFSFSSLR 540
NSLILGFRRS MNIDLWSKIT ELLYKDERYC SKPPGPAEAV GYFLYNLIDS MSDSEVQAKE 600
ERLRQYFHQL QEMNVKVPEN IYKGICNLLN TYHVPELIKD IKVLVDREKV DSQKTSQVTS 660
SDLESTLEKL KAEGQPVGSA LKQLLLLLCS EENMQKALEV KAKYESDMVI GGYAALINLC 720
CRHDNAEDAW NLKQEVDRLD ASAILDTAKY VALVKVLGKH SRLQDAINIL KEMKEKDVVI 780
KDATVLSFFH ILNGAALRGE IETVKQLHEA IVTLGLAKPS SNISFPLVTV HLEKGDLPAA 840
LEASIACHKK YKVLPRIHDV LCKLVEKGET DLIQKAMDFV SQEQGEMTML YDLFFAFLQT 900
GNYKEAKKII ETPGIRARPT RLQWFCDRCI ASNQVEALEK LVELTEKLFE CDRDQMYYNL 960
LKLYKISSDW QRADAAWTKM QEENIIPRER TLRLLAEILK TSNQEVPFDV PELWFGDDRP 1020
SLSPSSRSAG EDVTEKTLLS NCKLKKSKDA YNIFLKAEKQ NVVFSSETYS TLIGLLLSKD 1080
DFTQAMHVKD FAETHIKGFT LNDAANSLLI IRQVRRDYLK GALATLRAAL DLKQVPSQIA 1140
VTRLIQALAL KGDVESIEAI QRMVAGLDTI GLSKMVFINN IALAQMKNNK LDAAIENIEH 1200
LLASENQAIE PQYFGLSYLF RKVIEEQMEP ALEKLSIMSE RMANQFALYK PVTDLFLQLV 1260
DSGKVDEARA LLERCGAIAE QSSLLSVFCL RTSQKPKKAP VLKTLLELIP ELRDNDKVYS 1320
CSMKSYALDK DVASAKALYE YLTAKNLKLD DLFLKRYAAL LKDVGEPVPF PEPPESFAFY 1380
IKQLKEARES PS 1392 
Gene Ontology
 GO:0000794; C:condensed nuclear chromosome; ISS:HGNC.
 GO:0005856; C:cytoskeleton; ISS:HGNC.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0042645; C:mitochondrial nucleoid; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
 GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC.
 GO:0030529; C:ribonucleoprotein complex; IDA:MGI.
 GO:0048487; F:beta-tubulin binding; ISS:HGNC.
 GO:0003723; F:RNA binding; IDA:MGI.
 GO:0003697; F:single-stranded DNA binding; IDA:MGI.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0000961; P:negative regulation of mitochondrial RNA catabolic process; IMP:MGI.
 GO:0070129; P:regulation of mitochondrial translation; IMP:MGI.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR002885; Pentatricopeptide_repeat. 
Pfam
 PF01535; PPR
 PF13812; PPR_3 
SMART
  
PROSITE
 PS51375; PPR 
PRINTS