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   24-JAN-2024, entry version 110.
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. Positively modulates
CC       nuclear export of mRNAs containing the EIF4E sensitivity element (4ESE)
CC       by binding simultaneously to both EIF4E and the 4ESE and acting as a
CC       platform for assembly for the RNA export complex (By similarity). Also
CC       binds to exportin XPO1/CRM1 to engage the nuclear pore and traffic the
CC       bound mRNAs to the cytoplasm (By similarity). May bind mature mRNA in
CC       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|UniProtKB:P42704}.
CC   -!- SUBUNIT: Interacts with CECR2, HEBP2, MAP1S, UXT, PPARGC1A and FOXO1.
CC       Component of mRNP complexes associated with HNRPA1. Interacts (via N-
CC       terminus) with EIF4E; the interaction promotes association of EIF4E
CC       with 4ESE-containing mRNAs (By similarity). Interacts with exportin
CC       XPO1/CRM1; interacts both alone and in complex with EIF4E and 4ESE-
CC       containing mRNAs to form an EIF4E-dependent mRNA export complex (By
CC       similarity). Interacts with importin IPO8; the interaction occurs when
CC       LRPPRC is in its RNA-free form and returns LRPPRC to the nucleus for
CC       further export rounds (By similarity). {ECO:0000250|UniProtKB:P42704}.
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   SMR; Q5SGE0; -.
DR   BioGRID; 260571; 1.
DR   STRING; 10116.ENSRNOP00000008200; -.
DR   iPTMnet; Q5SGE0; -.
DR   PhosphoSitePlus; Q5SGE0; -.
DR   SwissPalm; Q5SGE0; -.
DR   jPOST; Q5SGE0; -.
DR   PaxDb; 10116-ENSRNOP00000008200; -.
DR   GeneID; 313867; -.
DR   KEGG; rno:313867; -.
DR   UCSC; RGD:1306575; rat.
DR   AGR; RGD:1306575; -.
DR   CTD; 10128; -.
DR   RGD; 1306575; Lrpprc.
DR   eggNOG; KOG4318; Eukaryota.
DR   InParanoid; Q5SGE0; -.
DR   OrthoDB; 5479341at2759; -.
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:0000957; P:mitochondrial RNA catabolic process; 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; Tetratricopeptide repeat domain; 3.
DR   InterPro; IPR033490; LRP130.
DR   InterPro; IPR002885; Pentatricopeptide_rpt.
DR   InterPro; IPR033443; PPR_long.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR00756; PPR; 2.
DR   PANTHER; PTHR46669; LEUCINE-RICH PPR MOTIF-CONTAINING PROTEIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR46669:SF1; LEUCINE-RICH PPR MOTIF-CONTAINING PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF01535; PPR; 3.
DR   Pfam; PF13812; PPR_3; 1.
DR   Pfam; PF17177; PPR_long; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51375; PPR; 11.
DR   World-2DPAGE; 0004:Q5SGE0; -.
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
//