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Reviewed, UniProtKB/Swiss-Prot P42704 (LPPRC_HUMAN)

Last modified November 25, 2008. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Leucine-rich PPR motif-containing protein, mitochondrial
Alternative name(s):
    130 kDa leucine-rich protein
    LRP 130
    GP130
Gene names
Name: LRPPRC
Synonyms: LRP130
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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. Binds single-stranded DNA By similarity.

Subunit structure

Interacts with CECR2, HEBP2, MAP1S, RMP/C19orf2 and UXT. Interacts with PPARGC1A. Interacts with FOXO1 By similarity Component of mRNP complexes associated with HNRPA1.

Subcellular location

Mitochondrion. Nucleus › nucleoplasm. Nucleus inner membrane. Nucleus outer membrane. Note= Seems to be predominantly mitochondrial.

Tissue specificity

Expressed ubiquitously. Expression is highest in heart, skeletal muscle, kidney and liver, intermediate in brain, non-mucosal colon, spleen and placenta, and lowest in small intestine, thymus, lung and peripheral blood leukocytes.

Involvement in disease

Defects in LRPPRC are the cause of Leigh syndrome French-Canadian type (LSFC) [MIM:220111]. Leigh syndrome is a severe neurological disorder characterized by bilaterally symmetrical necrotic lesions in subcortical brain regions that is commonly associated with systemic cytochrome c oxidase (COX) deficiency. In the Saguenay-Lac Saint Jean region of Quebec province in Canada, a biochemically distinct form of Leigh syndrome with COX deficiency has been described. Patients have been observed to have a developmental delay, hypotonia, mild facial dysmorphism, chronic well-compensated metabolic acidosis, and high mortality due to episodes of severe acidosis and coma. Enzyme activity was close to normal in kidney and heart, 50% of normal in fibroblasts and skeletal muscle, and nearly absent in brain and liver. LSFC patients show reduced (<30%) levels of LRPPRC in both fibroblast and liver mitochondria and a specifically reduced translation of COX subunits MT-CO1/COXI and MT-CO3 (COXIII).

Sequence similarities

Contains 20 PPR (pentatricopeptide) repeats.

Sequence caution

The sequence AAA67549.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA67549.1 differs from that shown. Reason: Frameshift at several positions.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5959Mitochondrion Potential
Chain60 – 13941335Leucine-rich PPR motif-containing protein, mitochondrial
PRO_0000084467

Regions

Repeat126 – 16035PPR 1
Repeat161 – 19535PPR 2
Repeat196 – 23035PPR 3
Repeat231 – 26535PPR 4
Repeat266 – 30035PPR 5
Repeat301 – 33535PPR 6
Repeat403 – 43735PPR 7
Repeat438 – 47235PPR 8
Repeat678 – 70932PPR 9
Repeat710 – 74637PPR 10
Repeat747 – 78438PPR 11
Repeat785 – 82036PPR 12
Repeat821 – 85636PPR 13
Repeat954 – 98835PPR 14
Repeat1031 – 106535PPR 15
Repeat1066 – 110237PPR 16
Repeat1103 – 113735PPR 17
Repeat1138 – 117538PPR 18
Repeat1176 – 121035PPR 19
Repeat1317 – 135135PPR 20
Region1121 – 1394274RNA-binding

Natural variations

Natural variant3541A → V in LSFC.
VAR_018656

Experimental info

Sequence conflict541S → G in BAF82705. Ref.2
Sequence conflict2961S → F in AAA67549. Ref.5
Sequence conflict528 – 5314LKSN → YFPI in AAH26034. Ref.4
Sequence conflict5561L → V in AAA67549. Ref.5
Sequence conflict5831Y → N in AAA67549. Ref.5
Sequence conflict6481S → R in AAA67549. Ref.5
Sequence conflict6761Q → R in BAC86287. Ref.2
Sequence conflict7021K → R in BAC86287. Ref.2
Sequence conflict750 – 7523KYV → NYL in AAA67549. Ref.5
Sequence conflict7691N → K in AAA67549. Ref.5
Sequence conflict11921N → D in BAC86287. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P42704-1 [UniParc].

Last modified July 24, 2007. Version 3.
Checksum: 61AB0C8BF8A972E6

FASTA1,394157,905
        10         20         30         40         50         60 
MAALLRSARW LLRAGAAPRL PLSLRLLPGG PGRLHAASYL PAARAGPVAG GLLSPARLYA 

        70         80         90        100        110        120 
IAAKEKDIQE ESTFSSRKIS NQFDWALMRL DLSVRRTGRI PKKLLQKVFN DTCRSGGLGG 

       130        140        150        160        170        180 
SHALLLLRSC GSLLPELKLE ERTEFAHRIW DTLQKLGAVY DVSHYNALLK VYLQNEYKFS 

       190        200        210        220        230        240 
PTDFLAKMEE ANIQPNRVTY QRLIASYCNV GDIEGASKIL GFMKTKDLPV TEAVFSALVT 

       250        260        270        280        290        300 
GHARAGDMEN AENILTVMRD AGIEPGPDTY LALLNAYAEK GDIDHVKQTL EKVEKSELHL 

       310        320        330        340        350        360 
MDRDLLQIIF SFSKAGYPQY VSEILEKVTC ERRYIPDAMN LILLLVTEKL EDVALQILLA 

       370        380        390        400        410        420 
CPVSKEDGPS VFGSFFLQHC VTMNTPVEKL TDYCKKLKEV QMHSFPLQFT LHCALLANKT 

       430        440        450        460        470        480 
DLAKALMKAV KEEGFPIRPH YFWPLLVGRR KEKNVQGIIE ILKGMQELGV HPDQETYTDY 

       490        500        510        520        530        540 
VIPCFDSVNS ARAILQENGC LSDSDMFSQA GLRSEAANGN LDFVLSFLKS NTLPISLQSI 

       550        560        570        580        590        600 
RSSLLLGFRR SMNINLWSEI TELLYKDGRY CQEPRGPTEA VGYFLYNLID SMSDSEVQAK 

       610        620        630        640        650        660 
EEHLRQYFHQ LEKMNVKIPE NIYRGIRNLL ESYHVPELIK DAHLLVESKN LDFQKTVQLT 

       670        680        690        700        710        720 
SSELESTLET LKAENQPIRD VLKQLILVLC SEENMQKALE LKAKYESDMV TGGYAALINL 

       730        740        750        760        770        780 
CCRHDKVEDA LNLKEEFDRL DSSAVLDTGK YVGLVRVLAK HGKLQDAINI LKEMKEKDVL 

       790        800        810        820        830        840 
IKDTTALSFF HMLNGAALRG EIETVKQLHE AIVTLGLAEP STNISFPLVT VHLEKGDLST 

       850        860        870        880        890        900 
ALEVAIDCYE KYKVLPRIHD VLCKLVEKGE TDLIQKAMDF VSQEQGEMVM LYDLFFAFLQ 

       910        920        930        940        950        960 
TGNYKEAKKI IETPGIRARS ARLQWFCDRC VANNQVETLE KLVELTQKLF ECDRDQMYYN 

       970        980        990       1000       1010       1020 
LLKLYKINGD WQRADAVWNK IQEENVIPRE KTLRLLAEIL REGNQEVPFD VPELWYEDEK 

      1030       1040       1050       1060       1070       1080 
HSLNSSSAST TEPDFQKDIL IACRLNQKKG AYDIFLNAKE QNIVFNAETY SNLIKLLMSE 

      1090       1100       1110       1120       1130       1140 
DYFTQAMEVK AFAETHIKGF TLNDAANSRL IITQVRRDYL KEAVTTLKTV LDQQQTPSRL 

      1150       1160       1170       1180       1190       1200 
AVTRVIQALA MKGDVENIEV VQKMLNGLED SIGLSKMVFI NNIALAQIKN NNIDAAIENI 

      1210       1220       1230       1240       1250       1260 
ENMLTSENKV IEPQYFGLAY LFRKVIEEQL EPAVEKISIM AERLANQFAI YKPVTDFFLQ 

      1270       1280       1290       1300       1310       1320 
LVDAGKVDDA RALLQRCGAI AEQTPILLLF LLRNSRKQGK ASTVKSVLEL IPELNEKEEA 

      1330       1340       1350       1360       1370       1380 
YNSLMKSYVS EKDVTSAKAL YEHLTAKNTK LDDLFLKRYA SLLKYAGEPV PFIEPPESFE 

      1390 
FYAQQLRKLR ENSS

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References

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[1]"The role of the LRPPRC (leucine-rich pentatricopeptide repeat cassette) gene in cytochrome oxidase assembly: mutation causes lowered levels of COX (cytochrome c oxidase) I and COX III mRNA."
Xu F., Morin C., Mitchell G., Ackerley C., Robinson B.H.
Biochem. J. 382:331-336(2004) [PubMed: 15139850] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN COX ASSEMBLY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hippocampus and Testis.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Muscle, Placenta and Testis.
[5]"Molecular cloning and expression of the gene for a major leucine-rich protein from human hepatoblastoma cells (HepG2)."
Hou J., Wang F., McKeehan W.L.
In Vitro Cell. Dev. Biol. Anim. 30A:111-114(1994) [PubMed: 8012652] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 108-1394.
Tissue: Liver.
[6]Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 156-170; 260-280; 304-314; 454-463; 530-541; 656-672; 740-750; 764-772; 1050-1059; 1091-1098; 1177-1189 AND 1339-1347, MASS SPECTROMETRY.
Tissue: B-cell lymphoma and Colon carcinoma.
[7]"Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA: candidate intermediates in formation and export of mRNA."
Mili S., Shu H.J., Zhao Y., Pinol-Roma S.
Mol. Cell. Biol. 21:7307-7319(2001) [PubMed: 11585913] [Abstract]
Cited for: FUNCTION IN MRNA EXPORT, IDENTIFICATION IN NMRNP COMPLEXES, MASS SPECTROMETRY.
[8]"Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity."
Liu L., McKeehan W.L.
Genomics 79:124-136(2002) [PubMed: 11827465] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH CECR2; HEBP2; MAP1S; RMP AND UXT.
[9]"LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, is bound in vivo to mitochondrial and nuclear RNAs."
Mili S., Pinol-Roma S.
Mol. Cell. Biol. 23:4972-4982(2003) [PubMed: 12832482] [Abstract]
Cited for: RNA-BINDING, FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION.
[10]"LRP130, a single-stranded DNA/RNA-binding protein, localizes at the outer nuclear and endoplasmic reticulum membrane, and interacts with mRNA in vivo."
Tsuchiya N., Fukuda H., Nakashima K., Nagao M., Sugimura T., Nakagama H.
Biochem. Biophys. Res. Commun. 317:736-743(2004) [PubMed: 15081402] [Abstract]
Cited for: FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION.
[11]"New invMED1 element cis-activates human multidrug-related MDR1 and MVP genes, involving the LRP130 protein."
Labialle S., Dayan G., Gayet L., Rigal D., Gambrelle J., Baggetto L.G.
Nucleic Acids Res. 32:3864-3876(2004) [PubMed: 15272088] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION REGULATION, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[12]"Putative tumor suppressor RASSF1 interactive protein and cell death inducer C19ORF5 is a DNA binding protein."
Liu L., Vo A., Liu G., McKeehan W.L.
Biochem. Biophys. Res. Commun. 332:670-676(2005) [PubMed: 15907802] [Abstract]
Cited for: INTERACTION WITH MAP1S.
[13]"Defects in energy homeostasis in Leigh syndrome French Canadian variant through PGC-1alpha/LRP130 complex."
Cooper M.P., Qu L., Rohas L.M., Lin J., Yang W., Erdjument-Bromage H., Tempst P., Spiegelman B.M.
Genes Dev. 20:2996-3009(2006) [PubMed: 17050673] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH PPARGC1A.
[14]"Identification of a gene causing human cytochrome c oxidase deficiency by integrative genomics."
Mootha V.K., Lepage P., Miller K., Bunkenborg J., Reich M., Hjerrild M., Delmonte T., Villeneuve A., Sladek R., Xu F., Mitchell G.A., Morin C., Mann M., Hudson T.J., Robinson B., Rioux J.D., Lander E.S.
Proc. Natl. Acad. Sci. U.S.A. 100:605-610(2003) [PubMed: 12529507] [Abstract]
Cited for: VARIANT LSFC VAL-354.

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Web resources

GeneReviews

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Cross-references

Sequence databases

AY289212 mRNA. Translation: AAP41922.1.
AK125781 mRNA. Translation: BAC86287.1.
AK290016 mRNA. Translation: BAF82705.1.
AC108476 Genomic DNA. Translation: AAY24012.1.
AC127379 Genomic DNA. Translation: AAY24043.1.
BC010282 mRNA. Translation: AAH10282.1.
BC026034