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UniProtKB/Swiss-Prot entry P42704


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LPPRC_HUMAN
Primary accession number P42704
Secondary accession numbers A0PJE3 A8K1V1 Q53PC0 Q53QN7 Q6ZUD8 Q7Z7A6 Q96D84
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on July 24, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 74)
Name and origin of the protein
Protein name Leucine-rich PPR motif-containing protein, mitochondrial [Precursor]
Synonyms 130 kDa leucine-rich protein
LRP 130
GP130
Gene name
Name: LRPPRC
Synonyms: LRP130
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN COX ASSEMBLY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
DOI=10.1042/BJ20040469; PubMed=15139850 [NCBI, ExPASy, EBI, Israel, Japan]
Xu F., Morin C., Mitchell G., Ackerley C., Robinson B.H.;
"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.";
Biochem. J. 382:331-336(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hippocampus, and Testis;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Muscle, Placenta, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 108-1394.
TISSUE=Liver;
PubMed=8012652 [NCBI, ExPASy, EBI, Israel, Japan]
Hou J., Wang F., McKeehan W.L.;
"Molecular cloning and expression of the gene for a major leucine-rich protein from human hepatoblastoma cells (HepG2).";
In Vitro Cell. Dev. Biol. Anim. 30A:111-114(1994).
[6]
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, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma, and Colon carcinoma;
Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
Submitted (JUL-2007) to UniProtKB.
[7]
FUNCTION IN MRNA EXPORT, IDENTIFICATION IN NMRNP COMPLEXES, AND MASS SPECTROMETRY.
DOI=10.1128/MCB.21.21.7307-7319.2001; PubMed=11585913 [NCBI, ExPASy, EBI, Israel, Japan]
Mili S., Shu H.J., Zhao Y., Pinol-Roma S.;
"Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA: candidate intermediates in formation and export of mRNA.";
Mol. Cell. Biol. 21:7307-7319(2001).
[8]
TISSUE SPECIFICITY, AND INTERACTION WITH CECR2; HEBP2; MAP1S; RMP AND UXT.
DOI=10.1006/geno.2001.6679; PubMed=11827465 [NCBI, ExPASy, EBI, Israel, Japan]
Liu L., McKeehan W.L.;
"Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity.";
Genomics 79:124-136(2002).
[9]
RNA-BINDING, FUNCTION IN MRNA EXPORT, AND SUBCELLULAR LOCATION.
DOI=10.1128/MCB.23.14.4972-4982.2003; PubMed=12832482 [NCBI, ExPASy, EBI, Israel, Japan]
Mili S., Pinol-Roma S.;
"LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, is bound in vivo to mitochondrial and nuclear RNAs.";
Mol. Cell. Biol. 23:4972-4982(2003).
[10]
FUNCTION IN MRNA EXPORT, AND SUBCELLULAR LOCATION.
DOI=10.1016/j.bbrc.2004.03.103; PubMed=15081402 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuchiya N., Fukuda H., Nakashima K., Nagao M., Sugimura T., Nakagama H.;
"LRP130, a single-stranded DNA/RNA-binding protein, localizes at the outer nuclear and endoplasmic reticulum membrane, and interacts with mRNA in vivo.";
Biochem. Biophys. Res. Commun. 317:736-743(2004).
[11]
FUNCTION IN TRANSCRIPTION REGULATION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
DOI=10.1093/nar/gkh722; PubMed=15272088 [NCBI, ExPASy, EBI, Israel, Japan]
Labialle S., Dayan G., Gayet L., Rigal D., Gambrelle J., Baggetto L.G.;
"New invMED1 element cis-activates human multidrug-related MDR1 and MVP genes, involving the LRP130 protein.";
Nucleic Acids Res. 32:3864-3876(2004).
[12]
INTERACTION WITH MAP1S.
DOI=10.1016/j.bbrc.2005.05.006; PubMed=15907802 [NCBI, ExPASy, EBI, Israel, Japan]
Liu L., Vo A., Liu G., McKeehan W.L.;
"Putative tumor suppressor RASSF1 interactive protein and cell death inducer C19ORF5 is a DNA binding protein.";
Biochem. Biophys. Res. Commun. 332:670-676(2005).
[13]
FUNCTION IN TRANSCRIPTION REGULATION, AND INTERACTION WITH PPARGC1A.
DOI=10.1101/gad.1483906; PubMed=17050673 [NCBI, ExPASy, EBI, Israel, Japan]
Cooper M.P., Qu L., Rohas L.M., Lin J., Yang W., Erdjument-Bromage H., Tempst P., Spiegelman B.M.;
"Defects in energy homeostasis in Leigh syndrome French Canadian variant through PGC-1alpha/LRP130 complex.";
Genes Dev. 20:2996-3009(2006).
[14]
VARIANT LSFC VAL-354.
DOI=10.1073/pnas.242716699; PubMed=12529507 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Identification of a gene causing human cytochrome c oxidase deficiency by integrative genomics.";
Proc. Natl. Acad. Sci. U.S.A. 100:605-610(2003).
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: Interacts with CECR2, HEBP2, MAP1S, RMP/C19orf2 and UXT. Interacts with PPARGC1A. Interacts with FOXO1 (By similarity) Component of mRNP complexes associated with HNRPA1.
  • INTERACTION:
    P62330:ARF6; NbExp=1; IntAct=EBI-1050853, EBI-638181;
    P60520:GABARAPL2; NbExp=1; IntAct=EBI-1050853, EBI-720116;
    Q9Y2Q3:GSTK1; NbExp=1; IntAct=EBI-1050853, EBI-1053767;
    Q14164:IKBKE; NbExp=1; IntAct=EBI-1050853, EBI-307369;
    P43360:MAGEA6; NbExp=1; IntAct=EBI-1050853, EBI-1045155;
    Q9Y5V3:MAGED1; NbExp=1; IntAct=EBI-1050853, EBI-716006;
    Q9HC98:NEK6; NbExp=1; IntAct=EBI-1050853, EBI-740364;
    Q9Y5J5:PHLDA3; NbExp=1; IntAct=EBI-1050853, EBI-1055859;
    Q9UBK2:PPARGC1A; NbExp=2; IntAct=EBI-1050853, EBI-765486;
    O75365:PTP4A3; NbExp=1; IntAct=EBI-1050853, EBI-1043866;
    Q9UBN6:TNFRSF10D; NbExp=1; IntAct=EBI-1050853, EBI-1044859;
    Q9P2S5:WDR8; NbExp=1; IntAct=EBI-1050853, EBI-1054904;
  • 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.
  • 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).
  • SIMILARITY: Contains 20 PPR (pentatricopeptide) repeats.
  • SEQUENCE CAUTION:
    • Sequence=AAA67549.1; Type=Erroneous initiation; Note=Translation N-terminally extended
    • Sequence=AAA67549.1; Type=Frameshift; Positions=Several;
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=LRPPRC";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY289212; AAP41922.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK125781; BAC86287.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK290016; BAF82705.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC108476; AAY24012.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC127379; AAY24043.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010282; AAH10282.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026034; AAH26034.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050311; AAH50311.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC130285; AAI30286.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M92439; AAA67549.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S27954; S27954.
RefSeq NP_573566.2; -.
UniGene Hs.368084
3D structure databases
ModBase P42704.
Protein-protein interaction databases
DIP DIP:27543N; -.
IntAct P42704; -.
PTM databases
PhosphoSite P42704; -.
Organism-specific databases
H-InvDB HIX0023918; -.
HGNC HGNC:15714; LRPPRC.
GenAtlas LRPPRC.
MIM 220111; phenotype. [NCBI / EBI]
607544; gene. [NCBI / EBI]
Orphanet 506; Leigh syndrome.
PharmGKB PA30459; -.
GeneCards P42704.
Gene expression databases
ArrayExpress P42704; -.
CleanEx HS_LRPPRC; -.
GermOnline ENSG00000138095; Homo sapiens.
Ontologies
GO
GO:0000794; Cellular component: condensed nuclear chromosome (inferred from direct assay from HGNC).
GO:0005856; Cellular component: cytoskeleton (inferred from direct assay from HGNC).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from direct assay from HGNC).
GO:0048487; Molecular function: beta-tubulin binding (inferred from direct assay from HGNC).
GO:0008017; Molecular function: microtubule binding (traceable author statement from HGNC).
GO:0003723; Molecular function: RNA binding (non-traceable author statement from UniProtKB).
GO:0047497; Biological process: mitochondrion transport along microtubule (traceable author statement from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR002885; PPR.
Graphical view of domain structure.
Pfam PF01535; PPR; 9.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00756; PPR; 7.
PROSITE PS51375; PPR; 11.
PROSITE graphical view of domain structure (profiles).
BLOCKS P42704.
Genome annotation databases
Ensembl ENSG00000138095; Homo sapiens. [Contig view]
GeneID 10128; -.
KEGG hsa:10128; -.
Phylogenomic databases
HOVERGEN P42704; -.
Other
SOURCE LRPPRC; Homo sapiens.
ProtoNet P42704.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Disease mutation; DNA-binding; Leigh syndrome; Membrane; Mitochondrion; mRNA transport; Nucleus; Repeat; RNA-binding; Transcription; Transcription regulation; Transit peptide; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
TRANSIT   1     59  59     Mitochondrion (Potential). 
CHAIN   60   1394  1335     Leucine-rich PPR motif-containing protein, mitochondrial. PRO_0000084467
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. 
VARIANT   354    354  1     A -> V (in LSFC). VAR_018656 
CONFLICT   54     54        S -> G (in Ref. 2; BAF82705). 
CONFLICT   296    296        S -> F (in Ref. 5; AAA67549). 
CONFLICT   528    531        LKSN -> YFPI (in Ref. 4; AAH26034). 
CONFLICT   556    556        L -> V (in Ref. 5; AAA67549). 
CONFLICT   583    583        Y -> N (in Ref. 5; AAA67549). 
CONFLICT   648    648        S -> R (in Ref. 5; AAA67549). 
CONFLICT   676    676        Q -> R (in Ref. 2; BAC86287). 
CONFLICT   702    702        K -> R (in Ref. 2; BAC86287). 
CONFLICT   750    752        KYV -> NYL (in Ref. 5; AAA67549). 
CONFLICT   769    769        N -> K (in Ref. 5; AAA67549). 
CONFLICT   1192   1192        N -> D (in Ref. 2; BAC86287). 
Sequence information
Length: 1394 AA [This is the length of the unprocessed precursor] Molecular weight: 157905 Da [This is the MW of the unprocessed precursor] CRC64: 61AB0C8BF8A972E6 [This is a checksum on the sequence]
        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 

P42704 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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