P42704 (LPPRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leucine-rich PPR motif-containing protein, mitochondrial

Alternative name(s):
130 kDa leucine-rich protein
Short name=LRP 130
GP130

Gene names

Name:	LRPPRC
Synonyms:	LRP130

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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. Ref.1 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13
Subunit structure	Interacts with CECR2, HEBP2, MAP1S and UXT. Interacts with PPARGC1A. Interacts with FOXO1 By similarity. Component of mRNP complexes associated with HNRPA1. Ref.7 Ref.8 Ref.12 Ref.13
Subcellular location	Mitochondrion. Nucleus › nucleoplasm. Nucleus inner membrane. Nucleus outer membrane. Note: Seems to be predominantly mitochondrial. Ref.1 Ref.9 Ref.10 Ref.11
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. Ref.1 Ref.8
Involvement in disease	Leigh syndrome French-Canadian type (LSFC) [MIM:220111]: 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). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Transport mRNA transport
Cellular component	Membrane Mitochondrion Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Leigh syndrome
Domain	Repeat Transit peptide
Ligand	DNA-binding RNA-binding
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion transport along microtubule Traceable author statement PubMed 12762840. Source: HGNC regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	condensed nuclear chromosome Inferred from direct assay PubMed 12762840. Source: HGNC microtubule Inferred from direct assay PubMed 21525035. Source: UniProtKB mitochondrial nucleoid Inferred from direct assay PubMed 18063578. Source: BHF-UCL nuclear inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from direct assay PubMed 12762840. Source: HGNC
Molecular_function	RNA binding Non-traceable author statement Ref.9. Source: UniProtKB beta-tubulin binding Inferred from direct assay PubMed 12762840. Source: HGNC microtubule binding Traceable author statement PubMed 12762840. Source: HGNC single-stranded DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPARGC1A	Q9UBK2	2	EBI-1050853,EBI-765486

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 59	59	Mitochondrion Potential
	Chain	60 – 1394	1335	Leucine-rich PPR motif-containing protein, mitochondrial		PRO_0000084467
Regions
	Repeat	126 – 160	35	PPR 1
	Repeat	161 – 195	35	PPR 2
	Repeat	196 – 230	35	PPR 3
	Repeat	231 – 265	35	PPR 4
	Repeat	266 – 300	35	PPR 5
	Repeat	301 – 335	35	PPR 6
	Repeat	403 – 437	35	PPR 7
	Repeat	438 – 472	35	PPR 8
	Repeat	678 – 709	32	PPR 9
	Repeat	710 – 746	37	PPR 10
	Repeat	747 – 784	38	PPR 11
	Repeat	785 – 820	36	PPR 12
	Repeat	821 – 856	36	PPR 13
	Repeat	954 – 988	35	PPR 14
	Repeat	1031 – 1065	35	PPR 15
	Repeat	1066 – 1102	37	PPR 16
	Repeat	1103 – 1137	35	PPR 17
	Repeat	1138 – 1175	38	PPR 18
	Repeat	1176 – 1210	35	PPR 19
	Repeat	1317 – 1351	35	PPR 20
	Region	1121 – 1394	274	RNA-binding
Amino acid modifications
	Modified residue	155	1	N6-acetyllysine Ref.14
	Modified residue	187	1	N6-acetyllysine Ref.14
	Modified residue	292	1	N6-acetyllysine Ref.14
	Modified residue	613	1	N6-acetyllysine Ref.14
	Modified residue	726	1	N6-acetyllysine Ref.14
	Modified residue	750	1	N6-acetyllysine Ref.14
Natural variations
	Natural variant	354	1	A → V in LSFC. Ref.16		VAR_018656
	Natural variant	478	1	T → A. Corresponds to variant rs35035668 [ dbSNP | Ensembl ].		VAR_052935
Experimental info
	Sequence conflict	54	1	S → G in BAF82705. Ref.2
	Sequence conflict	296	1	S → F in AAA67549. Ref.5
	Sequence conflict	528 – 531	4	LKSN → YFPI in AAH26034. Ref.4
	Sequence conflict	556	1	L → V in AAA67549. Ref.5
	Sequence conflict	583	1	Y → N in AAA67549. Ref.5
	Sequence conflict	648	1	S → R in AAA67549. Ref.5
	Sequence conflict	676	1	Q → R in BAC86287. Ref.2
	Sequence conflict	702	1	K → R in BAC86287. Ref.2
	Sequence conflict	750 – 752	3	KYV → NYL in AAA67549. Ref.5
	Sequence conflict	769	1	N → K in AAA67549. Ref.5
	Sequence conflict	1192	1	N → D in BAC86287. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P42704 [UniParc]. Last modified July 24, 2007. Version 3. Checksum: 61AB0C8BF8A972E6	FASTA	1,394	157,905
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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] [Europe PMC] [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. , 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] [Europe PMC] [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. , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INTERACTION WITH CECR2; HEBP2; MAP1S 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH PPARGC1A.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-155; LYS-187; LYS-292; LYS-613; LYS-726 AND LYS-750, MASS SPECTROMETRY.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"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] [Europe PMC] [Abstract] Cited for: VARIANT LSFC VAL-354.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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 mRNA. Translation: AAH26034.1. BC050311 mRNA. Translation: AAH50311.1. BC130285 mRNA. Translation: AAI30286.1. M92439 mRNA. Translation: AAA67549.1. Sequence problems.
IPI	IPI00783271.
PIR	S27954.
RefSeq	NP_573566.2. NM_133259.3.
UniGene	Hs.368084.
3D structure databases
ProteinModelPortal	P42704.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27543N.
IntAct	P42704. 18 interactions.
MINT	MINT-205076.
STRING	9606.ENSP00000260665.
Polymorphism databases
DMDM	156632706.
Proteomic databases
PaxDb	P42704.
PRIDE	P42704.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260665; ENSP00000260665; ENSG00000138095. ENST00000409946; ENSP00000386234; ENSG00000138095.
GeneID	10128.
KEGG	hsa:10128.
UCSC	uc002rtr.2. human.
Organism-specific databases
CTD	10128.
GeneCards	GC02M044113.
H-InvDB	HIX0023918.
HGNC	HGNC:15714. LRPPRC.
HPA	HPA036408.
MIM	220111. phenotype. 607544. gene.
neXtProt	NX_P42704.
Orphanet	70472. Saguenay-Lac-St. Jean cytochrome oxidase deficiency.
PharmGKB	PA30459.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG292283.
HOVERGEN	HBG097314.
InParanoid	P42704.
OMA	CVTMNTP.
OrthoDB	EOG4DR9BG.
Gene expression databases
ArrayExpress	P42704.
Bgee	P42704.
CleanEx	HS_LRPPRC.
Genevestigator	P42704.
GermOnline	ENSG00000138095. Homo sapiens.
Family and domain databases
Gene3D	1.25.40.10. 4 hits.
InterPro	IPR002885. Pentatricopeptide_repeat. IPR011990. TPR-like_helical. [Graphical view]
Pfam	PF01535. PPR. 6 hits. [Graphical view]
TIGRFAMs	TIGR00756. PPR. 2 hits.
PROSITE	PS51375. PPR. 11 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LRPPRC. human.
GenomeRNAi	10128.
NextBio	38311.
SOURCE	Search...

Entry information

Entry name

LPPRC_HUMAN

Accession

Primary (citable) accession number: P42704
Secondary accession number(s): A0PJE3 , A8K1V1, Q53PC0, Q53QN7, Q6ZUD8, Q7Z7A6, Q96D84

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	July 24, 2007
Last modified:	May 1, 2013
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.