LPPRC_RAT
ID LPPRC_RAT Reviewed; 1392 AA.
AC Q5SGE0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=Leucine rich protein 157;
DE Short=rLRP157;
DE Flags: Precursor;
GN Name=Lrpprc; Synonyms=Lrp157;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=15525270; DOI=10.1111/j.1460-9568.2004.03703.x;
RA Eilers H., Trilk S.L., Lee S.Y., Xue Q., Jong B.E., Moff I., Levine J.D.,
RA Schumacher M.A.;
RT "Isolation of an mRNA binding protein homologue that is expressed in
RT nociceptors.";
RL Eur. J. Neurosci. 20:2283-2293(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1026, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
CC -!- SUBUNIT: Interacts with CECR2, HEBP2, MAP1S, UXT, PPARGC1A and FOXO1.
CC Component of mRNP complexes associated with HNRPA1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15525270}.
CC Nucleus {ECO:0000269|PubMed:15525270}. Nucleus, nucleoplasm
CC {ECO:0000250}. Nucleus inner membrane {ECO:0000250}. Nucleus outer
CC membrane {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in liver, brain and a
CC subset of small diameter sensory neurons in the dorsal root ganglion
CC (at protein level). {ECO:0000269|PubMed:15525270}.
CC -!- INDUCTION: Induced by NGF in nociceptors.
CC {ECO:0000269|PubMed:15525270}.
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DR EMBL; AY293808; AAQ74626.1; -; mRNA.
DR RefSeq; NP_001008519.1; NM_001008519.1.
DR AlphaFoldDB; Q5SGE0; -.
DR BioGRID; 260571; 1.
DR STRING; 10116.ENSRNOP00000008200; -.
DR iPTMnet; Q5SGE0; -.
DR PhosphoSitePlus; Q5SGE0; -.
DR World-2DPAGE; 0004:Q5SGE0; -.
DR jPOST; Q5SGE0; -.
DR PaxDb; Q5SGE0; -.
DR PRIDE; Q5SGE0; -.
DR GeneID; 313867; -.
DR KEGG; rno:313867; -.
DR UCSC; RGD:1306575; rat.
DR CTD; 10128; -.
DR RGD; 1306575; Lrpprc.
DR eggNOG; KOG4318; Eukaryota.
DR InParanoid; Q5SGE0; -.
DR OrthoDB; 1344243at2759; -.
DR PhylomeDB; Q5SGE0; -.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR PRO; PR:Q5SGE0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISS:HGNC-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISS:HGNC-UCL.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
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; ISS:HGNC-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0000961; P:negative regulation of mitochondrial RNA catabolic process; ISO:RGD.
DR GO; GO:0070129; P:regulation of mitochondrial translation; ISO:RGD.
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; 2.
DR Pfam; PF01535; PPR; 3.
DR Pfam; PF13812; PPR_3; 1.
DR Pfam; PF17177; PPR_long; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR00756; PPR; 2.
DR PROSITE; PS51375; PPR; 11.
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..77
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 78..1392
FT /note="Leucine-rich PPR motif-containing protein,
FT mitochondrial"
FT /id="PRO_0000295547"
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..1173
FT /note="PPR 18"
FT REPEAT 1174..1208
FT /note="PPR 19"
FT REPEAT 1315..1349
FT /note="PPR 20"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PB66"
FT MOD_RES 186
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42704"
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:0000250|UniProtKB:Q6PB66"
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:0007744|PubMed:22673903"
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"
SQ SEQUENCE 1392 AA; 156653 MW; 80D6040F4671D097 CRC64;
MSALLRPARW LLGAAAVPRL PLSLRLPAGG PGRLPSVVRV AAAGGRPAAG ELLSQARLYA
IVAEKKDLPE EPAPVRRSGS QFDWALMRLD NSVRRTGRIT KGLLQKVFES TCRSGSPGSN
QALLLLRSCG SLLPELSLAE RTEFAHKIWD KLQQLGTVYD VSHYNALLKV YLQNEYRFSP
TDFLAKMEGA NIQPNRVTYQ RLIAAYCSVG DIEGASKILG FMKTRDLPIT EAVFSALVTG
HARAGDMESA ENILTVMKQA GIEPGPDTYL ALLNAHAEKG DIDHVKQILE KVEKSDHYFM
DRDFLQIIVS FSKAGYPQYV SEILEKITYE RRSIPDAMNL ILLLVTEKLE DTAFQVLLAL
PLARDETSSS FGSFFLRHCV TMDTPAEKLI DYCKRLRDAK VHSSSLQFTL HCALQANKTA
LAKAVMEALR DEGFPIRTHY FWPLLVGHQK TKNVQGIIDI LKIMKEMGVD PDQETYINYV
FPCFGSVQSA RAALQENKCL PKSTTFAQAE VRNEAINGNL QNILSFLESN ALPFSFNSLR
GSLILGFRRS MNIDLWSKIT ELLYKDDRYC QKPPGPTEAV GYFLYNLIDS MSDSEVQAKE
ERLRQYFHQL REMNVKVSEN IYKGICNLLD NYHVPELIKD VKVLVDREKI DSRKTSQFTS
SDLESTLEKL KAEGHPVGDP LKQLILLLCS EENMQKALEV KAKYESDMVI GGYAALINLC
CRHDNAEDAL NLKQEFDRLD PSAVLDTAKY VALVKVLGKH GRVQDAINIL KEMKEKDVVI
KDAAVLSFFH ILNGAALRGE IETVKQLHEA IVTLGLAKPS SNISFPLVTV HLEKDDLPAA
LEASIACHEK YKVLPRIHDV LCKLIEKGET DLIQKAMDFV SQEQGEMSML YDLFFAFLQT
GNYKEAKKII ETPGIRARPT RLQWFCDRCI ANNQVETLEK LVELTEKLFE CDRDQMYYNL
LKLYKISGDW QRADAVWNKM QEENLIPRER TLRLLAGILK TSNQEVPFDV PELWFGDDRS
SLSSSSPSAG DTVTEKMLLS DCRLKKSKDA YNIFLKAEKQ DVVFSSEAYS TLVGLLLSKD
DFTRAMHVKD FAETHIKGFT LNGAASSLLI IAQVRRDYLK VALETLKAAL DLEQVPSELA
VTRLIQALAL QGDVKSIETI QKMVKGLDAI ELSRMVFINN IALAQMKNNE IDAAIENIEH
MLASENQTVE HQYFGLSYLF RKVIEEQMEP ALEKLSIMSE RLANQFALYK PVTDLFLQLV
DSGKVDEARA LLERCGAIAE QTSILSVFCL RTSQKPKKAP VLKTLLELIP ELRENDRVYS
CSMKSYVADK DVASAKALYE HLTAKNMKLD DLFLKRYASL LKDVGEPVPF TEPPESFGFY
IKQLKEAREN PS
