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Low-density lipoprotein receptor-related protein 5 (LRP-5)

 LRP5_HUMAN              Reviewed;        1615 AA.
O75197; Q96TD6; Q9UES7; Q9UP66;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 2.
27-SEP-2017, entry version 173.
RecName: Full=Low-density lipoprotein receptor-related protein 5;
Short=LRP-5;
Flags: Precursor;
Name=LRP5; Synonyms=LR3, LRP7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Osteoblast;
PubMed=9790987; DOI=10.1006/bbrc.1998.9545;
Dong Y., Lathrop W., Weaver D., Qiu Q., Cini J., Bertolini D.,
Chen D.;
"Molecular cloning and characterization of LR3, a novel LDL receptor
family protein with mitogenic activity.";
Biochem. Biophys. Res. Commun. 251:784-790(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-1525.
TISSUE=Osteoblast;
PubMed=9714764; DOI=10.1016/S0378-1119(98)00311-4;
Hey P.J., Twells R.C.J., Phillips M.S., Nakagawa Y., Brown S.D.,
Kawaguchi Y., Cox R., Xie G., Dugan V., Hammond H., Metzker M.L.,
Todd J.A., Hess J.F.;
"Cloning of a novel member of the low-density lipoprotein receptor
family.";
Gene 216:103-111(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11401438; DOI=10.1006/geno.2000.6492;
Twells R.C.J., Metzker M.L., Brown S.D., Cox R., Garey C., Hammond H.,
Hey P.J., Levy E., Nakagawa Y., Philips M.S., Todd J.A., Hess J.F.;
"The sequence and gene characterization of a 400-kb candidate region
for IDDM4 on chromosome 11q13.";
Genomics 72:231-242(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-1330.
PubMed=12509515; DOI=10.1073/pnas.0133792100;
Fujino T., Asaba H., Kang M.J., Ikeda Y., Sone H., Takada S.,
Kim D.H., Ioka R.X., Ono M., Tomoyori H., Okubo M., Murase T.,
Kamataki A., Yamamoto J., Magoori K., Takahashi S., Miyamoto Y.,
Oishi H., Nose M., Okazaki M., Usui S., Imaizumi K., Yanagisawa M.,
Sakai J., Yamamoto T.T.;
"Low-density lipoprotein receptor-related protein 5 (LRP5) is
essential for normal cholesterol metabolism and glucose-induced
insulin secretion.";
Proc. Natl. Acad. Sci. U.S.A. 100:229-234(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
INTERACTION WITH FZD8 IN WNT-FZD-LRP5-LRP6 COMPLEX, INTERACTION WITH
DKK1, AND FUNCTION.
PubMed=11448771; DOI=10.1016/S0960-9822(01)00290-1;
Semenov M.V., Tamai K., Brott B.K., Kuhl M., Sokol S., He X.;
"Head inducer Dickkopf-1 is a ligand for Wnt coreceptor LRP6.";
Curr. Biol. 11:951-961(2001).
[9]
FUNCTION, AND INTERACTION WITH AXIN1.
PubMed=11336703; DOI=10.1016/S1097-2765(01)00224-6;
Mao J., Wang J., Liu B., Pan W., Farr G.H. III, Flynn C., Yuan H.,
Takada S., Kimelman D., Li L., Wu D.;
"Low-density lipoprotein receptor-related protein-5 binds to Axin and
regulates the canonical Wnt signaling pathway.";
Mol. Cell 7:801-809(2001).
[10]
FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH AXIN1.
PubMed=14731402; DOI=10.1016/S1097-2765(03)00484-2;
Tamai K., Zeng X., Liu C., Zhang X., Harada Y., Chang Z., He X.;
"A mechanism for Wnt coreceptor activation.";
Mol. Cell 13:149-156(2004).
[11]
INTERACTION WITH MESD, AND CHARACTERIZATION OF VARIANT HBM VAL-171.
PubMed=15143163; DOI=10.1128/MCB.24.11.4677-4684.2004;
Zhang Y., Wang Y., Li X., Zhang J., Mao J., Li Z., Zheng J., Li L.,
Harris S., Wu D.;
"The LRP5 high-bone-mass G171V mutation disrupts LRP5 interaction with
Mesd.";
Mol. Cell. Biol. 24:4677-4684(2004).
[12]
INTERACTION WITH DKK1 AND SOST, AND FUNCTION.
PubMed=15778503; DOI=10.1074/jbc.M413274200;
Li X., Zhang Y., Kang H., Liu W., Liu P., Zhang J., Harris S.E.,
Wu D.;
"Sclerostin binds to LRP5/6 and antagonizes canonical Wnt signaling.";
J. Biol. Chem. 280:19883-19887(2005).
[13]
INTERACTION WITH WNT1 IN THE WNT-FZD-LRP5-LRP6 COMPLEX, AND
INTERACTION WITH SOST.
PubMed=15908424; DOI=10.1074/jbc.M504308200;
Semenov M., Tamai K., He X.;
"SOST is a ligand for LRP5/LRP6 and a Wnt signaling inhibitor.";
J. Biol. Chem. 280:26770-26775(2005).
[14]
INTERACTION WITH CSNK1E.
PubMed=16513652; DOI=10.1074/jbc.M510580200;
Swiatek W., Kang H., Garcia B.A., Shabanowitz J., Coombs G.S.,
Hunt D.F., Virshup D.M.;
"Negative regulation of LRP6 function by casein kinase I epsilon
phosphorylation.";
J. Biol. Chem. 281:12233-12241(2006).
[15]
INTERACTION WITH MESD.
PubMed=17488095; DOI=10.1021/bi700049g;
Koduri V., Blacklow S.C.;
"Requirement for natively unstructured regions of mesoderm development
candidate 2 in promoting low-density lipoprotein receptor-related
protein 6 maturation.";
Biochemistry 46:6570-6577(2007).
[16]
INTERACTION WITH CAPRIN2.
PubMed=18762581; DOI=10.1083/jcb.200803147;
Ding Y., Xi Y., Chen T., Wang J.Y., Tao D.L., Wu Z.L., Li Y.P., Li C.,
Zeng R., Li L.;
"Caprin-2 enhances canonical Wnt signaling through regulating LRP5/6
phosphorylation.";
J. Cell Biol. 182:865-872(2008).
[17]
INTERACTION WITH DKK1 AND MESD, AND CHARACTERIZATION OF VARIANT
VAL-171.
PubMed=19746449; DOI=10.1002/jcb.22335;
Murrills R.J., Matteo J.J., Bhat B.M., Coleburn V.E., Allen K.M.,
Chen W., Damagnez V., Bhat R.A., Bex F.J., Bodine P.V.;
"A cell-based Dkk1 binding assay reveals roles for extracellular
domains of LRP5 in Dkk1 interaction and highlights differences between
wild-type and the high bone mass mutant LRP5(G171V).";
J. Cell. Biochem. 108:1066-1075(2009).
[18]
INTERACTION WITH APCDD1.
PubMed=20393562; DOI=10.1038/nature08875;
Shimomura Y., Agalliu D., Vonica A., Luria V., Wajid M., Baumer A.,
Belli S., Petukhova L., Schinzel A., Brivanlou A.H., Barres B.A.,
Christiano A.M.;
"APCDD1 is a novel Wnt inhibitor mutated in hereditary hypotrichosis
simplex.";
Nature 464:1043-1047(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
VARIANTS OPPG GLN-494 AND TRP-570, AND VARIANT MET-667.
PubMed=11719191; DOI=10.1016/S0092-8674(01)00571-2;
Gong Y., Slee R.B., Fukai N., Rawadi G., Roman-Roman S.,
Reginato A.M., Wang H., Cundy T., Glorieux F.H., Lev D., Zacharin M.,
Oexle K., Marcelino J., Suwairi W., Heeger S., Sabatakos G., Apte S.,
Adkins W.N., Allgrove J., Arslan-Kirchner M., Batch J.A., Beighton P.,
Black G.C., Boles R.G., Boon L.M., Borrone C., Brunner H.G.,
Carle G.F., Dallapiccola B., De Paepe A., Floege B., Halfhide M.L.,
Hall B., Hennekam R.C.M., Hirose T., Jans A., Jueppner H., Kim C.A.,
Keppler-Noreuil K., Kohlschuetter A., LaCombe D., Lambert M.,
Lemyre E., Letteboer T., Peltonen L., Ramesar R.S., Romanengo M.,
Somer H., Steichen-Gersdorf E., Steinmann B., Sullivan B.,
Superti-Furga A., Swoboda W., van den Boogaard M.-J., Van Hul W.,
Vikkula M., Votruba M., Zabel B., Garcia T., Baron R., Olsen B.R.,
Warman M.L.;
"LDL receptor-related protein 5 (LRP5) affects bone accrual and eye
development.";
Cell 107:513-523(2001).
[21]
VARIANT HBM VAL-171, AND POLYMORPHISM.
PubMed=11741193; DOI=10.1086/338450;
Little R.D., Carulli J.P., Del Mastro R.G., Dupuis J., Osborne M.,
Folz C., Manning S.P., Swain P.M., Zhao S.-C., Eustace B., Lappe M.M.,
Spitzer L., Zweier S., Braunschweiger K., Benchekroun Y., Hu X.,
Adair R., Chee L., FitzGerald M.G., Tulig C., Caruso A., Tzellas N.,
Bawa A., Franklin B., McGuire S., Nogues X., Gong G., Allen K.M.,
Anisowicz A., Morales A.J., Lomedico P.T., Recker S.M.,
Van Eerdewegh P., Recker R.R., Johnson M.L.;
"A mutation in the LDL receptor-related protein 5 gene results in the
autosomal dominant high-bone-mass trait.";
Am. J. Hum. Genet. 70:11-19(2002).
[22]
VARIANT HBM VAL-171, AND CHARACTERIZATION OF VARIANT HBM VAL-171.
PubMed=12015390; DOI=10.1056/NEJMoa013444;
Boyden L.M., Mao J., Belsky J., Mitzner L., Farhi A., Mitnick M.A.,
Wu D., Insogna K., Lifton R.P.;
"High bone density due to a mutation in LDL-receptor-related protein
5.";
N. Engl. J. Med. 346:1513-1521(2002).
[23]
VARIANTS OPTA1 TYR-111; ARG-171; THR-242 AND ILE-253, VARIANTS WENHY
THR-214; VAL-214 AND THR-242, VARIANT VBCH2 THR-242, AND VARIANTS
18-LEU--LEU-20 DEL; LEU-20 INS; ARG-89; MET-667 AND VAL-1330.
PubMed=12579474; DOI=10.1086/368277;
Van Wesenbeeck L., Cleiren E., Gram J., Beals R.K., Benichou O.,
Scopelliti D., Key L., Renton T., Bartels C., Gong Y., Warman M.L.,
de Vernejoul M.-C., Bollerslev J., Van Hul W.;
"Six novel missense mutations in the LDL receptor-related protein 5
(LRP5) gene in different conditions with an increased bone density.";
Am. J. Hum. Genet. 72:763-771(2003).
[24]
VARIANTS EVR4 MET-173; HIS-1168 AND GLY-1361, AND VARIANT VAL-1525.
PubMed=15024691; DOI=10.1086/383202;
Toomes C., Bottomley H.M., Jackson R.M., Towns K.V., Scott S.,
Mackey D.A., Craig J.E., Jiang L., Yang Z., Trembath R., Woodruff G.,
Gregory-Evans C.Y., Gregory-Evans K., Parker M.J., Black G.C.M.,
Downey L.M., Zhang K., Inglehearn C.F.;
"Mutations in LRP5 or FZD4 underlie the common familial exudative
vitreoretinopathy locus on chromosome 11q.";
Am. J. Hum. Genet. 74:721-730(2004).
[25]
VARIANTS MET-667 AND VAL-1330.
PubMed=15077203; DOI=10.1086/420771;
Ferrari S.L., Deutsch S., Choudhury U., Chevalley T., Bonjour J.-P.,
Dermitzakis E.T., Rizzoli R., Antonarakis S.E.;
"Polymorphisms in the low-density lipoprotein receptor-related protein
5 (LRP5) gene are associated with variation in vertebral bone mass,
vertebral bone size, and stature in whites.";
Am. J. Hum. Genet. 74:866-875(2004).
[26]
VARIANTS EVR4 GLN-570; GLY-752 AND LYS-1367.
PubMed=15346351; DOI=10.1086/425080;
Jiao X., Ventruto V., Trese M.T., Shastry B.S., Hejtmancik J.F.;
"Autosomal recessive familial exudative vitreoretinopathy is
associated with mutations in LRP5.";
Am. J. Hum. Genet. 75:878-884(2004).
[27]
VARIANTS ARG-89 AND VAL-1330, FUNCTION, AND INVOLVEMENT IN
OSTEOPOROSIS.
PubMed=14727154; DOI=10.1007/s10038-003-0111-6;
Mizuguchi T., Furuta I., Watanabe Y., Tsukamoto K., Tomita H.,
Tsujihata M., Ohta T., Kishino T., Matsumoto N., Minakami H.,
Niikawa N., Yoshiura K.;
"LRP5, low-density-lipoprotein-receptor-related protein 5, is a
determinant for bone mineral density.";
J. Hum. Genet. 49:80-86(2004).
[28]
VARIANTS OPPG ASN-203; MET-244; PHE-307; TRP-348; GLN-353; LEU-356;
LYS-390; GLU-400; ARG-404; ASN-434; LYS-460; GLN-494; VAL-520;
TRP-570; ARG-610; ASN-683; HIS-733; TYR-1099; CYS-1113 AND ASP-1401,
CHARACTERIZATION OF VARIANTS OPPG MET-244; LEU-356; LYS-390; ARG-404;
ASN-434; VAL-520 AND ARG-610, AND CHARACTERIZATION OF VARIANTS EVR4
MET-173; GLN-570; HIS-1168; GLY-1361 AND LYS-1367.
PubMed=16252235; DOI=10.1086/497706;
Osteoporosis-Pseudoglioma collaborative group;
Ai M., Heeger S., Bartels C.F., Schelling D.K.;
"Clinical and molecular findings in osteoporosis-pseudoglioma
syndrome.";
Am. J. Hum. Genet. 77:741-753(2005).
[29]
VARIANTS EVR4 PHE-145; CYS-444; THR-522; MET-535; ARG-610; CYS-617;
ALA-798 AND ASP-1121, AND VARIANTS VAL-97 AND MET-1540.
PubMed=15981244; DOI=10.1002/humu.20191;
Qin M., Hayashi H., Oshima K., Tahira T., Hayashi K., Kondo H.;
"Complexity of the genotype-phenotype correlation in familial
exudative vitreoretinopathy with mutations in the LRP5 and/or FZD4
genes.";
Hum. Mutat. 26:104-112(2005).
[30]
VARIANTS PRIMARY OSTEOPOROSIS THR-29 AND GLN-1036.
PubMed=15824851; DOI=10.1359/JBMR.050101;
Hartikka H., Makitie O., Mannikko M., Doria A.S., Daneman A.,
Cole W.G., Ala-Kokko L., Sochett E.B.;
"Heterozygous mutations in the LDL receptor-related protein 5 (LRP5)
gene are associated with primary osteoporosis in children.";
J. Bone Miner. Res. 20:783-789(2005).
[31]
VARIANT HBM MET-154.
PubMed=15824861; DOI=10.1359/JBMR.041223;
Rickels M.R., Zhang X., Mumm S., Whyte M.P.;
"Oropharyngeal skeletal disease accompanying high bone mass and novel
LRP5 mutation.";
J. Bone Miner. Res. 20:878-885(2005).
[32]
VARIANTS IDIOPATHIC OSTEOPOROSIS LEU-356 AND LEU-455, VARIANT
THR-1537, CHARACTERIZATION OF VARIANTS IDIOPATHIC OSTEOPOROSIS LEU-356
AND LEU-455, AND CHARACTERIZATION OF VARIANT THR-1537.
PubMed=16234968; DOI=10.1359/JBMR.050705;
Crabbe P., Balemans W., Willaert A., van Pottelbergh I., Cleiren E.,
Coucke P.J., Ai M., Goemaere S., van Hul W., de Paepe A.,
Kaufman J.-M.;
"Missense mutations in LRP5 are not a common cause of idiopathic
osteoporosis in adult men.";
J. Bone Miner. Res. 20:1951-1959(2005).
[33]
VARIANTS OPPG ARG-478 AND CYS-504.
PubMed=16679074; DOI=10.1016/j.bone.2006.02.069;
Cheung W.M.W., Jin L.Y., Smith D.K., Cheung P.T., Kwan E.Y.W., Low L.,
Kung A.W.C.;
"A family with osteoporosis pseudoglioma syndrome due to compound
heterozygosity of two novel mutations in the LRP5 gene.";
Bone 39:470-476(2006).
[34]
VARIANT EVR4 ARG-550.
PubMed=16929062; DOI=10.1136/bjo.2006.092114;
Downey L.M., Bottomley H.M., Sheridan E., Ahmed M., Gilmour D.F.,
Inglehearn C.F., Reddy A., Agrawal A., Bradbury J., Toomes C.;
"Reduced bone mineral density and hyaloid vasculature remnants in a
consanguineous recessive FEVR family with a mutation in LRP5.";
Br. J. Ophthalmol. 90:1163-1167(2006).
[35]
VARIANT HBM VAL-282, AND CHARACTERIZATION OF VARIANT HBM VAL-282.
PubMed=17295608; DOI=10.1359/jbmr.070211;
Balemans W., Devogelaer J.P., Cleiren E., Piters E., Caussin E.,
Van Hul W.;
"Novel LRP5 missense mutation in a patient with a high bone mass
phenotype results in decreased DKK1-mediated inhibition of Wnt
signaling.";
J. Bone Miner. Res. 22:708-716(2007).
[36]
VARIANT OPPG ILE-531.
PubMed=17437160; DOI=10.1007/s00198-007-0360-x;
Barros E.R., Dias da Silva M.R., Kunii I.S., Hauache O.M.,
Lazaretti-Castro M.;
"A novel mutation in the LRP5 gene is associated with osteoporosis-
pseudoglioma syndrome.";
Osteoporos. Int. 18:1017-1018(2007).
[37]
VARIANT OPPG ALA-409.
PubMed=18602879; DOI=10.1016/j.bone.2008.04.020;
Streeten E.A., McBride D., Puffenberger E., Hoffman M.E., Pollin T.I.,
Donnelly P., Sack P., Morton H.;
"Osteoporosis-pseudoglioma syndrome: description of 9 new cases and
beneficial response to bisphosphonates.";
Bone 43:584-590(2008).
[38]
VARIANT 15-LEU--LEU-20 DEL.
PubMed=19177549; DOI=10.1002/humu.20916;
Chung B.D., Kayserili H., Ai M., Freudenberg J., Uzumcu A.,
Uyguner O., Bartels C.F., Honing S., Ramirez A., Hanisch F.G.,
Nurnberg G., Nurnberg P., Warman M.L., Wollnik B., Kubisch C.,
Netzer C.;
"A mutation in the signal sequence of LRP5 in a family with an
osteoporosis-pseudoglioma syndrome (OPPG)-like phenotype indicates a
novel disease mechanism for trinucleotide repeats.";
Hum. Mutat. 30:641-648(2009).
[39]
VARIANTS EVR4 ALA-511 AND TRP-805.
PubMed=19324841; DOI=10.1167/iovs.08-3320;
Boonstra F.N., van Nouhuys C.E., Schuil J., de Wijs I.J.,
van der Donk K.P., Nikopoulos K., Mukhopadhyay A., Scheffer H.,
Tilanus M.A.D., Cremers F.P.M., Hoefsloot L.H.;
"Clinical and molecular evaluation of probands and family members with
familial exudative vitreoretinopathy.";
Invest. Ophthalmol. Vis. Sci. 50:4379-4385(2009).
[40]
VARIANTS EVR4 LYS-441 AND PHE-1253.
PubMed=20340138; DOI=10.1002/humu.21250;
Nikopoulos K., Venselaar H., Collin R.W.J., Riveiro-Alvarez R.,
Boonstra F.N., Hooymans J.M., Mukhopadhyay A., Shears D., van Bers M.,
de Wijs I.J., van Essen A.J., Sijmons R.H., Tilanus M.A.D.,
van Nouhuys C.E., Ayuso C., Hoefsloot L.H., Cremers F.P.M.;
"Overview of the mutation spectrum in familial exudative
vitreoretinopathy and Norrie disease with identification of 21 novel
variants in FZD4, LRP5, and NDP.";
Hum. Mutat. 31:656-666(2010).
[41]
VARIANT PRO-816, VARIANTS EVR4 THR-422; PRO-540 AND MET-852,
CHARACTERIZATION OF VARIANTS EVR4 THR-422; PRO-540 AND MET-852, AND
CHARACTERIZATION OF VARIANT PRO-816.
PubMed=24715757;
Fei P., Zhang Q., Huang L., Xu Y., Zhu X., Tai Z., Gong B., Ma S.,
Yao Q., Li J., Zhao P., Yang Z.;
"Identification of two novel LRP5 mutations in families with familial
exudative vitreoretinopathy.";
Mol. Vis. 20:395-409(2014).
[42]
VARIANTS EVR1 TRP-348; ASN-381; TRP-624 AND CYS-1517, CHARACTERIZATION
OF VARIANTS EVR1 TRP-348; ASN-381; TRP-624 AND CYS-1517, AND FUNCTION.
PubMed=27228167; DOI=10.1089/gtmb.2015.0322;
Zhang L., Yang Y., Li S., Tai Z., Huang L., Liu Y., Zhu X., Di Y.,
Qu C., Jiang Z., Li Y., Zhang G., Kim R., Sundaresan P., Yang Z.,
Zhu X.;
"Whole Exome Sequencing Analysis Identifies Mutations in LRP5 in
Indian Families with Familial Exudative Vitreoretinopathy.";
Genet. Test. Mol. Biomarkers 20:346-351(2016).
-!- FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers
beta-catenin signaling through inducing aggregation of receptor-
ligand complexes into ribosome-sized signalsomes. Cell-surface
coreceptor of Wnt/beta-catenin signaling, which plays a pivotal
role in bone formation. Plays a role in norrin (NDP) signal
transduction (PubMed:27228167). The Wnt-induced Fzd/LRP6
coreceptor complex recruits DVL1 polymers to the plasma membrane
which, in turn, recruits the AXIN1/GSK3B-complex to the cell
surface promoting the formation of signalsomes and inhibiting
AXIN1/GSK3-mediated phosphorylation and destruction of beta-
catenin. Appears be required for postnatal control of vascular
regression in the eye (By similarity). Required for posterior
patterning of the epiblast during gastrulation (By similarity).
{ECO:0000250|UniProtKB:Q91VN0, ECO:0000269|PubMed:11336703,
ECO:0000269|PubMed:11448771, ECO:0000269|PubMed:14727154,
ECO:0000269|PubMed:14731402, ECO:0000269|PubMed:15778503,
ECO:0000269|PubMed:27228167}.
-!- SUBUNIT: Homodimer; disulfide-linked. Forms phosphorylated
oligomer aggregates on Wnt-signaling (By similarity). Component of
a Wnt-signaling complex that contains a WNT protein, a FZD protein
and LRP5 or LRP6. Interacts with FZD8; the interaction is formed
on WNT-binding and signaling. Interacts (via the phosphorylated
PPPSP motif domains) with AXIN1; the interaction prevents
inhibition of beta-catenin phosphorylation and signaling and is
enhanced in the presence of GSK3B and WNT1 or WNT3A. Interacts
(via beta-propeller regions 3 and 4) with DKK1; the interaction,
enhanced by MESD and/or KREMEN, inhibits beta-catenin signaling by
preventing GSK3-mediated phosphorylation of the PPPSP motifs and
subsequent, AXIN1 binding. Interacts with MESD; the interaction
prevents the formation of LRP5 aggregates, targets LRP5 to the
plasma membrane and, when complexed with KREMEN2, increases DKK1
binding. Interacts with CSNK1E. Interacts with SOST; the
interaction antagonizes canonical Wnt signaling. Interacts with
APCDD1. Interacts with CAPRIN2 (PubMed:18762581). {ECO:0000250,
ECO:0000269|PubMed:11336703, ECO:0000269|PubMed:11448771,
ECO:0000269|PubMed:14731402, ECO:0000269|PubMed:15143163,
ECO:0000269|PubMed:15778503, ECO:0000269|PubMed:15908424,
ECO:0000269|PubMed:16513652, ECO:0000269|PubMed:17488095,
ECO:0000269|PubMed:18762581, ECO:0000269|PubMed:19746449,
ECO:0000269|PubMed:20393562}.
-!- INTERACTION:
Q6IMN6:CAPRIN2; NbExp=3; IntAct=EBI-2466421, EBI-6918449;
Q9BQB4:SOST; NbExp=2; IntAct=EBI-2466421, EBI-5746563;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Endoplasmic reticulum {ECO:0000250}. Note=Chaperoned to
the plasma membrane by MESD. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed, with the highest level of
expression in the liver and in aorta.
{ECO:0000269|PubMed:9790987}.
-!- PTM: Phosphorylation of cytoplasmic PPPSP motifs regulates the
signal transduction of the Wnt signaling pathway through acting as
a docking site for AXIN1. {ECO:0000250}.
-!- POLYMORPHISM: Genetic variations in LRP5 define the bone mineral
density quantitative trait locus 1 (BMND1) [MIM:601884]. Variance
in bone mineral density influences bone mass and contributes to
size determination in the general population.
{ECO:0000269|PubMed:11741193}.
-!- DISEASE: Vitreoretinopathy, exudative 1 (EVR1) [MIM:133780]: A
disorder of the retinal vasculature characterized by an abrupt
cessation of growth of peripheral capillaries, leading to an
avascular peripheral retina. This may lead to compensatory retinal
neovascularization, which is thought to be induced by hypoxia from
the initial avascular insult. New vessels are prone to leakage and
rupture causing exudates and bleeding, followed by scarring,
retinal detachment and blindness. Clinical features can be highly
variable, even within the same family. Patients with mild forms of
the disease are asymptomatic, and their only disease related
abnormality is an arc of avascular retina in the extreme temporal
periphery. In many ways the disease resembles retinopathy of
prematurity but there is no evidence of prematurity or small birth
weight in the patient history. {ECO:0000269|PubMed:27228167}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Vitreoretinopathy, exudative 4 (EVR4) [MIM:601813]: A
disorder of the retinal vasculature characterized by an abrupt
cessation of growth of peripheral capillaries, leading to an
avascular peripheral retina. This may lead to compensatory retinal
neovascularization, which is thought to be induced by hypoxia from
the initial avascular insult. New vessels are prone to leakage and
rupture causing exudates and bleeding, followed by scarring,
retinal detachment and blindness. Clinical features can be highly
variable, even within the same family. Patients with mild forms of
the disease are asymptomatic, and their only disease related
abnormality is an arc of avascular retina in the extreme temporal
periphery. {ECO:0000269|PubMed:15024691,
ECO:0000269|PubMed:15346351, ECO:0000269|PubMed:15981244,
ECO:0000269|PubMed:16252235, ECO:0000269|PubMed:16929062,
ECO:0000269|PubMed:19324841, ECO:0000269|PubMed:20340138,
ECO:0000269|PubMed:24715757}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal
disorder characterized by decreased bone mass and deterioration of
bone microarchitecture without alteration in the composition of
bone. The result is fragile bones and an increased risk of
fractures, even after minimal trauma. Osteoporosis is a chronic
condition of multifactorial etiology and is usually clinically
silent until a fracture occurs. {ECO:0000269|PubMed:14727154,
ECO:0000269|PubMed:15824851, ECO:0000269|PubMed:16234968}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Osteoporosis-pseudoglioma syndrome (OPPG) [MIM:259770]: A
disease characterized by congenital or infancy-onset blindness and
severe juvenile-onset osteoporosis and spontaneous fractures.
Additional clinical manifestations may include microphthalmos,
abnormalities of the iris, lens or vitreous, cataracts, short
stature, microcephaly, ligamental laxity, mental retardation and
hypotonia. {ECO:0000269|PubMed:11719191,
ECO:0000269|PubMed:16252235, ECO:0000269|PubMed:16679074,
ECO:0000269|PubMed:17437160, ECO:0000269|PubMed:18602879}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: High bone mass trait (HBM) [MIM:601884]: Rare phenotype
characterized by exceptionally dense bones. HBM individuals show
otherwise a completely normal skeletal structure and no other
unusual clinical findings. {ECO:0000269|PubMed:11741193,
ECO:0000269|PubMed:12015390, ECO:0000269|PubMed:15143163,
ECO:0000269|PubMed:15824861, ECO:0000269|PubMed:17295608}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Endosteal hyperostosis, Worth type (WENHY) [MIM:144750]:
An autosomal dominant sclerosing bone dysplasia clinically
characterized by elongation of the mandible, increased gonial
angle, flattened forehead, and the presence of a slowly enlarging
osseous prominence of the hard palate (torus palatinus). Serum
calcium, phosphorus and alkaline phosphatase levels are normal.
Radiologically, it is characterized by early thickening of the
endosteum of long bones, the skull and of the mandible. With
advancing age, the trabeculae of the metaphysis become thickened.
WENHY becomes clinically and radiologically evident by
adolescence, does not cause deformity except in the skull and
mandible, and is not associated with bone pain or fracture.
Affected patients have normal height, proportion, intelligence and
longevity. {ECO:0000269|PubMed:12579474}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Osteopetrosis, autosomal dominant 1 (OPTA1) [MIM:607634]:
A rare genetic disease characterized by abnormally dense bone, due
to defective resorption of immature bone. Osteopetrosis occurs in
two forms: a severe autosomal recessive form occurring in utero,
infancy, or childhood, and a benign autosomal dominant form
occurring in adolescence or adulthood. OPTA1 is an autosomal
dominant form characterized by generalized osteosclerosis most
pronounced in the cranial vault. Patients are often asymptomatic,
but some suffer from pain and hearing loss. It appears to be the
only type of osteopetrosis not associated with an increased
fracture rate. {ECO:0000269|PubMed:12579474}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Van Buchem disease 2 (VBCH2) [MIM:607636]: VBCH2 is an
autosomal dominant sclerosing bone dysplasia characterized by
cranial osteosclerosis, thickened calvaria and cortices of long
bones, enlarged mandible and normal serum alkaline phosphatase
levels. {ECO:0000269|PubMed:12579474}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/LRP5ID44282ch11q13.html";
-----------------------------------------------------------------------
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EMBL; AF077820; AAC72791.1; -; mRNA.
EMBL; AF064548; AAC36467.1; -; mRNA.
EMBL; AF283321; AAK52433.1; -; Genomic_DNA.
EMBL; AF283320; AAK52433.1; JOINED; Genomic_DNA.
EMBL; AB017498; BAA33051.1; -; mRNA.
EMBL; AP000807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW74705.1; -; Genomic_DNA.
EMBL; BC150595; AAI50596.1; -; mRNA.
CCDS; CCDS8181.1; -.
PIR; JE0372; JE0372.
RefSeq; NP_001278831.1; NM_001291902.1.
RefSeq; NP_002326.2; NM_002335.3.
UniGene; Hs.6347; -.
ProteinModelPortal; O75197; -.
SMR; O75197; -.
BioGrid; 110220; 41.
DIP; DIP-47265N; -.
ELM; O75197; -.
IntAct; O75197; 9.
MINT; MINT-1189744; -.
STRING; 9606.ENSP00000294304; -.
iPTMnet; O75197; -.
PhosphoSitePlus; O75197; -.
BioMuta; LRP5; -.
EPD; O75197; -.
PaxDb; O75197; -.
PeptideAtlas; O75197; -.
PRIDE; O75197; -.
Ensembl; ENST00000294304; ENSP00000294304; ENSG00000162337.
GeneID; 4041; -.
KEGG; hsa:4041; -.
UCSC; uc001ont.4; human.
CTD; 4041; -.
DisGeNET; 4041; -.
EuPathDB; HostDB:ENSG00000162337.11; -.
GeneCards; LRP5; -.
GeneReviews; LRP5; -.
HGNC; HGNC:6697; LRP5.
HPA; CAB013001; -.
HPA; HPA030505; -.
MalaCards; LRP5; -.
MIM; 133780; phenotype.
MIM; 144750; phenotype.
MIM; 166710; phenotype.
MIM; 259770; phenotype.
MIM; 601813; phenotype.
MIM; 601884; phenotype.
MIM; 603506; gene.
MIM; 607634; phenotype.
MIM; 607636; phenotype.
neXtProt; NX_O75197; -.
OpenTargets; ENSG00000162337; -.
Orphanet; 2783; Autosomal dominant osteopetrosis type 1.
Orphanet; 2790; Autosomal dominant osteosclerosis, Worth type.
Orphanet; 891; Familial exudative vitreoretinopathy.
Orphanet; 3416; Hyperostosis corticalis generalisata.
Orphanet; 85193; Idiopathic juvenile osteoporosis.
Orphanet; 2924; Isolated polycystic liver disease.
Orphanet; 2788; Osteoporosis - pseudoglioma.
Orphanet; 178377; Osteosclerosis-developmental delay-craniosynostosis syndrome.
Orphanet; 90050; Retinopathy of prematurity.
PharmGKB; PA30455; -.
eggNOG; ENOG410IPT4; Eukaryota.
eggNOG; ENOG410XSY5; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000230697; -.
HOVERGEN; HBG049167; -.
InParanoid; O75197; -.
KO; K03068; -.
OMA; DKFIYWV; -.
OrthoDB; EOG091G0178; -.
PhylomeDB; O75197; -.
TreeFam; TF315253; -.
Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
Reactome; R-HSA-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
Reactome; R-HSA-5339717; Misspliced LRP5 mutants have enhanced beta-catenin-dependent signaling.
Reactome; R-HSA-5340588; RNF mutants show enhanced WNT signaling and proliferation.
SignaLink; O75197; -.
SIGNOR; O75197; -.
ChiTaRS; LRP5; human.
GeneWiki; LRP5; -.
GenomeRNAi; 4041; -.
PRO; PR:O75197; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000162337; -.
CleanEx; HS_LRP5; -.
ExpressionAtlas; O75197; baseline and differential.
Genevisible; O75197; HS.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:1990909; C:Wnt signalosome; NAS:ParkinsonsUK-UCL.
GO; GO:1990851; C:Wnt-Frizzled-LRP5/6 complex; TAS:ParkinsonsUK-UCL.
GO; GO:1904928; F:coreceptor activity involved in canonical Wnt signaling pathway; NAS:ParkinsonsUK-UCL.
GO; GO:0071936; F:coreceptor activity involved in Wnt signaling pathway; IPI:ParkinsonsUK-UCL.
GO; GO:0042813; F:Wnt-activated receptor activity; ISS:ParkinsonsUK-UCL.
GO; GO:0017147; F:Wnt-protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0060612; P:adipose tissue development; IMP:BHF-UCL.
GO; GO:0060033; P:anatomical structure regression; IEA:Ensembl.
GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IEA:Ensembl.
GO; GO:1904886; P:beta-catenin destruction complex disassembly; TAS:Reactome.
GO; GO:0048539; P:bone marrow development; IMP:BHF-UCL.
GO; GO:0060349; P:bone morphogenesis; IMP:BHF-UCL.
GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0042074; P:cell migration involved in gastrulation; IEA:Ensembl.
GO; GO:0060764; P:cell-cell signaling involved in mammary gland development; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0035426; P:extracellular matrix-cell signaling; IEA:Ensembl.
GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
GO; GO:0006007; P:glucose catabolic process; IMP:BHF-UCL.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:BHF-UCL.
GO; GO:0002076; P:osteoblast development; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:BHF-UCL.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:BHF-UCL.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:BHF-UCL.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
GO; GO:0008217; P:regulation of blood pressure; IMP:BHF-UCL.
GO; GO:0046850; P:regulation of bone remodeling; IEA:Ensembl.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IBA:GO_Central.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:BHF-UCL.
GO; GO:0061304; P:retinal blood vessel morphogenesis; IMP:BHF-UCL.
GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
GO; GO:0016055; P:Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0044332; P:Wnt signaling pathway involved in dorsal/ventral axis specification; IDA:BHF-UCL.
Gene3D; 2.120.10.30; -; 4.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR017049; LRP5/6.
Pfam; PF00057; Ldl_recept_a; 3.
Pfam; PF00058; Ldl_recept_b; 13.
PIRSF; PIRSF036314; LDL_recpt-rel_p5/6; 1.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 4.
SMART; SM00192; LDLa; 3.
SMART; SM00135; LY; 20.
SUPFAM; SSF57424; SSF57424; 3.
PROSITE; PS01209; LDLRA_1; 3.
PROSITE; PS50068; LDLRA_2; 3.
PROSITE; PS51120; LDLRB; 20.
1: Evidence at protein level;
Complete proteome; Developmental protein; Disease mutation;
Disulfide bond; EGF-like domain; Endocytosis; Endoplasmic reticulum;
Glycoprotein; Membrane; Osteogenesis imperfecta; Osteopetrosis;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix; Wnt signaling pathway.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 1615 Low-density lipoprotein receptor-related
protein 5.
/FTId=PRO_0000017328.
TOPO_DOM 32 1384 Extracellular. {ECO:0000255}.
TRANSMEM 1385 1407 Helical. {ECO:0000255}.
TOPO_DOM 1408 1615 Cytoplasmic. {ECO:0000255}.
REPEAT 75 119 LDL-receptor class B 1.
REPEAT 78 81 YWTD 1.
REPEAT 120 162 LDL-receptor class B 2.
REPEAT 123 126 YWTD 2.
REPEAT 163 206 LDL-receptor class B 3.
REPEAT 166 169 YWTD 3.
REPEAT 207 247 LDL-receptor class B 4.
REPEAT 248 290 LDL-receptor class B 5.
REPEAT 251 254 YWTD 4.
DOMAIN 295 337 EGF-like 1.
REPEAT 385 427 LDL-receptor class B 6.
REPEAT 388 391 YWTD 5.
REPEAT 428 470 LDL-receptor class B 7.
REPEAT 431 434 YWTD 6.
REPEAT 471 514 LDL-receptor class B 8.
REPEAT 474 477 YWTD 7.
REPEAT 515 557 LDL-receptor class B 9.
REPEAT 558 600 LDL-receptor class B 10.
REPEAT 559 562 YWTD 8.
DOMAIN 601 641 EGF-like 2.
REPEAT 687 729 LDL-receptor class B 11.
REPEAT 690 693 YWTD 9.
REPEAT 730 772 LDL-receptor class B 12.
REPEAT 773 815 LDL-receptor class B 13.
REPEAT 816 855 LDL-receptor class B 14.
REPEAT 819 822 YWTD 10.
REPEAT 856 898 LDL-receptor class B 15.
REPEAT 859 862 YWTD 11.
DOMAIN 902 942 EGF-like 3.
REPEAT 989 1035 LDL-receptor class B 16.
REPEAT 1036 1078 LDL-receptor class B 17.
REPEAT 1079 1123 LDL-receptor class B 18.
REPEAT 1124 1164 LDL-receptor class B 19.
REPEAT 1165 1207 LDL-receptor class B 20.
DOMAIN 1213 1254 EGF-like 4.
DOMAIN 1258 1296 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1297 1333 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1335 1371 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
REGION 32 288 Beta-propeller 1.
REGION 341 602 Beta-propeller 2.
REGION 644 903 Beta-propeller 3.
REGION 945 1212 Beta-propeller 4.
MOTIF 1500 1506 PPPSP motif A.
MOTIF 1538 1545 PPPSP motif B.
MOTIF 1574 1581 PPPSP motif C.
MOTIF 1591 1596 PPPSP motif D.
MOTIF 1605 1612 PPPSP motif E.
COMPBIAS 1495 1610 Pro-rich.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 446 446 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 499 499 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 705 705 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 878 878 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 299 310 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 306 321 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 323 336 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 605 616 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 612 625 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 627 640 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 906 917 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 913 926 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 928 941 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1217 1228 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1224 1238 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1240 1253 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1259 1273 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1266 1286 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1280 1295 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1298 1310 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1305 1323 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1317 1332 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1336 1348 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1343 1361 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1355 1370 {ECO:0000255|PROSITE-ProRule:PRU00124}.
VARIANT 15 20 Missing (found in a family with
osteoporosis pseudoglioma syndrome;
impairs protein trafficking to the
endoplasmic reticulum and cell membrane).
{ECO:0000269|PubMed:19177549}.
/FTId=VAR_058582.
VARIANT 18 20 Missing. {ECO:0000269|PubMed:12579474}.
/FTId=VAR_021804.
VARIANT 20 20 L -> LL. {ECO:0000269|PubMed:12579474}.
/FTId=VAR_021805.
VARIANT 29 29 A -> T (in primary osteoporosis).
{ECO:0000269|PubMed:15824851}.
/FTId=VAR_063941.
VARIANT 89 89 Q -> R (in dbSNP:rs41494349).
{ECO:0000269|PubMed:12579474,
ECO:0000269|PubMed:14727154}.
/FTId=VAR_021806.
VARIANT 97 97 A -> V (in dbSNP:rs143433231).
{ECO:0000269|PubMed:15981244}.
/FTId=VAR_063942.
VARIANT 111 111 D -> Y (in OPTA1).
{ECO:0000269|PubMed:12579474}.
/FTId=VAR_021807.
VARIANT 145 145 L -> F (in EVR4; dbSNP:rs80358305).
{ECO:0000269|PubMed:15981244}.
/FTId=VAR_063943.
VARIANT 154 154 R -> M (in HBM).
{ECO:0000269|PubMed:15824861}.
/FTId=VAR_063944.
VARIANT 171 171 G -> R (in OPTA1; dbSNP:rs121908669).
{ECO:0000269|PubMed:12579474}.
/FTId=VAR_021808.
VARIANT 171 171 G -> V (in HBM; also in HBM individuals
with enlarged mandible and torus
palatinus; abolishes interaction with
MESD; impairs transport to cell surface;
no enhancement of DKK1 binding by MESD
resulting in impaired inhibition of Wnt
signaling by DKK1; dbSNP:rs121908668).
{ECO:0000269|PubMed:11741193,
ECO:0000269|PubMed:12015390,
ECO:0000269|PubMed:15143163,
ECO:0000269|PubMed:19746449}.
/FTId=VAR_021809.
VARIANT 173 173 T -> M (in EVR4; an individual with
abnormal retinal vasculature and retinal
folds; dbSNP:rs80358306).
{ECO:0000269|PubMed:15024691,
ECO:0000269|PubMed:16252235}.
/FTId=VAR_018465.
VARIANT 203 203 D -> N (in OPPG; dbSNP:rs760548029).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063945.
VARIANT 214 214 A -> T (in WENHY; dbSNP:rs121908671).
{ECO:0000269|PubMed:12579474}.
/FTId=VAR_021810.
VARIANT 214 214 A -> V (in WENHY; dbSNP:rs121908672).
{ECO:0000269|PubMed:12579474}.
/FTId=VAR_021811.
VARIANT 242 242 A -> T (in OPTA1, VBCH2 and WENHY;
dbSNP:rs121908670).
{ECO:0000269|PubMed:12579474}.
/FTId=VAR_021812.
VARIANT 244 244 T -> M (in OPPG; appears to traffic less
well than does the wild-type protein;
appears to be post-translationally
modified similar to wild-type protein; is
unable to transduce Wnt signal; has a
significantly reduced ability to
transduce Norrin signal;
dbSNP:rs397514665).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063946.
VARIANT 253 253 T -> I (in OPTA1; dbSNP:rs121908673).
{ECO:0000269|PubMed:12579474}.
/FTId=VAR_021813.
VARIANT 282 282 M -> V (in HBM; unknown pathological
significance; lowered LRP5-mediated Wnt
signaling; no effect on DKK1 binding).
{ECO:0000269|PubMed:17295608}.
/FTId=VAR_063412.
VARIANT 307 307 S -> F (in OPPG).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063947.
VARIANT 348 348 R -> W (in OPPG and EVR1; reduces Norrin
signal transduction).
{ECO:0000269|PubMed:16252235,
ECO:0000269|PubMed:27228167}.
/FTId=VAR_063948.
VARIANT 353 353 R -> Q (in OPPG).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063949.
VARIANT 356 356 S -> L (in idiopathic osteoporosis and
OPPG; appears to traffic comparably than
does the wild-type protein; appears to be
post-translationally modified similar to
wild-type protein; is unable to transduce
Wnt signal; has a significantly reduced
ability to transduce Norrin signal).
{ECO:0000269|PubMed:16234968,
ECO:0000269|PubMed:16252235}.
/FTId=VAR_063950.
VARIANT 381 381 D -> N (in EVR1; reduces Norrin signal
transduction).
{ECO:0000269|PubMed:27228167}.
/FTId=VAR_076548.
VARIANT 390 390 T -> K (in OPPG; is unable to traffic
normally; appears to be post-
translationally modified similar to wild-
type protein; is unable to transduce Wnt
signal; has a significantly reduced
ability to transduce Norrin signal).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063951.
VARIANT 400 400 A -> E (in OPPG).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063952.
VARIANT 404 404 G -> R (in OPPG; appears to traffic less
well than does the wild-type protein;
appears to be post-translationally
modified similar to wild-type protein;
has 50% of wild-type activity to
transduce Wnt signal; has a significantly
reduced ability to transduce Norrin
signal; dbSNP:rs750791263).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063953.
VARIANT 409 409 T -> A (in OPPG).
{ECO:0000269|PubMed:18602879}.
/FTId=VAR_063954.
VARIANT 422 422 A -> T (in EVR4; the mutation results in
significantly reduced Norrin signal
transduction).
{ECO:0000269|PubMed:24715757}.
/FTId=VAR_071012.
VARIANT 434 434 D -> N (in OPPG; appears to traffic less
well than does the wild-type protein;
appears to be post-translationally
modified similar to wild-type protein;
has 50% of wild-type activity to
transduce Wnt signal; has a significantly
reduced ability to transduce Norrin
signal; dbSNP:rs757888034).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063955.
VARIANT 441 441 E -> K (in EVR4; dbSNP:rs376152274).
{ECO:0000269|PubMed:20340138}.
/FTId=VAR_063956.
VARIANT 444 444 R -> C (in EVR4; associated in a EVR1
patient with mutation GLN-417 in FZD4;
dbSNP:rs80358308).
{ECO:0000269|PubMed:15981244}.
/FTId=VAR_063957.
VARIANT 455 455 S -> L (in idiopathic osteoporosis; shows
an inhibitory effect on Wnt signal
transduction).
{ECO:0000269|PubMed:16234968}.
/FTId=VAR_063958.
VARIANT 460 460 E -> K (in OPPG; dbSNP:rs866606166).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063959.
VARIANT 478 478 W -> R (in OPPG).
{ECO:0000269|PubMed:16679074}.
/FTId=VAR_063960.
VARIANT 494 494 R -> Q (in OPPG; dbSNP:rs121908664).
{ECO:0000269|PubMed:11719191,
ECO:0000269|PubMed:16252235}.
/FTId=VAR_021814.
VARIANT 504 504 W -> C (in OPPG).
{ECO:0000269|PubMed:16679074}.
/FTId=VAR_063961.
VARIANT 511 511 D -> A (in EVR4).
{ECO:0000269|PubMed:19324841}.
/FTId=VAR_063962.
VARIANT 520 520 G -> V (in OPPG; appears to traffic
comparably than does the wild-type
protein; appears to be post-
translationally modified similar to wild-
type protein; is unable to transduce Wnt
signal; has a significantly reduced
ability to transduce Norrin signal).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063963.
VARIANT 522 522 A -> T (in EVR4; dbSNP:rs80358309).
{ECO:0000269|PubMed:15981244}.
/FTId=VAR_063964.
VARIANT 531 531 N -> I (in OPPG).
{ECO:0000269|PubMed:17437160}.
/FTId=VAR_063965.
VARIANT 535 535 T -> M (in EVR4; autosomal recessive;
dbSNP:rs80358310).
{ECO:0000269|PubMed:15981244}.
/FTId=VAR_063966.
VARIANT 540 540 L -> P (in EVR4; the mutation results in
significantly reduced Norrin signal
transduction).
{ECO:0000269|PubMed:24715757}.
/FTId=VAR_071013.
VARIANT 550 550 G -> R (in EVR4; autosomal recessive;
dbSNP:rs80358311).
{ECO:0000269|PubMed:16929062}.
/FTId=VAR_063967.
VARIANT 570 570 R -> Q (in EVR4; autosomal recessive; has
significantly reduced Wnt or Norrin
signal transduction; dbSNP:rs80358312).
{ECO:0000269|PubMed:15346351,
ECO:0000269|PubMed:16252235}.
/FTId=VAR_021222.
VARIANT 570 570 R -> W (in OPPG; dbSNP:rs121908665).
{ECO:0000269|PubMed:11719191,
ECO:0000269|PubMed:16252235}.
/FTId=VAR_021815.
VARIANT 610 610 G -> R (in EVR4 and OPPG; appears to
traffic less well than does the wild-type
protein; appears to be post-
translationally modified similar to wild-
type protein; has 60% of wild-type
activity to transduce Wnt signal; has a
significantly reduced ability to
transduce Norrin signal;
dbSNP:rs80358313).
{ECO:0000269|PubMed:15981244,
ECO:0000269|PubMed:16252235}.
/FTId=VAR_063968.
VARIANT 617 617 F -> C (in EVR4; autosomal recessive;
dbSNP:rs80358314).
{ECO:0000269|PubMed:15981244}.
/FTId=VAR_063969.
VARIANT 624 624 R -> W (in EVR1; reduces Norrin signal
transduction).
{ECO:0000269|PubMed:27228167}.
/FTId=VAR_076549.
VARIANT 667 667 V -> M (in dbSNP:rs4988321).
{ECO:0000269|PubMed:11719191,
ECO:0000269|PubMed:12579474,
ECO:0000269|PubMed:15077203}.
/FTId=VAR_021816.
VARIANT 683 683 D -> N (in OPPG).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063970.
VARIANT 733 733 Y -> H (in OPPG; dbSNP:rs746701187).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063971.
VARIANT 752 752 R -> G (in EVR4; autosomal recessive;
dbSNP:rs121908674).
{ECO:0000269|PubMed:15346351}.
/FTId=VAR_021223.
VARIANT 798 798 T -> A (in EVR4; dbSNP:rs80358316).
{ECO:0000269|PubMed:15981244}.
/FTId=VAR_063972.
VARIANT 805 805 R -> W (in EVR4; dbSNP:rs765952535).
{ECO:0000269|PubMed:19324841}.
/FTId=VAR_063973.
VARIANT 816 816 Q -> P (rare polymorphism; no effect on
Norrin signal transduction).
{ECO:0000269|PubMed:24715757}.
/FTId=VAR_071014.
VARIANT 852 852 T -> M (in EVR4; de novo mutation found
in a patient also carrying mutation P-
540; unknown pathological significance;
the mutation results in significantly
reduced Norrin signal transduction).
{ECO:0000269|PubMed:24715757}.
/FTId=VAR_071015.
VARIANT 1036 1036 R -> Q (in primary osteoporosis;
dbSNP:rs61889560).
{ECO:0000269|PubMed:15824851}.
/FTId=VAR_063974.
VARIANT 1099 1099 D -> Y (in OPPG).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063975.
VARIANT 1113 1113 R -> C (in OPPG; dbSNP:rs377258285).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063976.
VARIANT 1121 1121 N -> D (in EVR4; dbSNP:rs80358317).
{ECO:0000269|PubMed:15981244}.
/FTId=VAR_063977.
VARIANT 1168 1168 Y -> H (in EVR4; an individual with total
retinal detachment and retinoschisis; is
unable to transduce Wnt or Norrin signal
transduction; dbSNP:rs80358318).
{ECO:0000269|PubMed:15024691,
ECO:0000269|PubMed:16252235}.
/FTId=VAR_018466.
VARIANT 1204 1204 V -> L (in dbSNP:rs11607268).
/FTId=VAR_035208.
VARIANT 1253 1253 C -> F (in EVR4; dbSNP:rs768615287).
{ECO:0000269|PubMed:20340138}.
/FTId=VAR_063978.
VARIANT 1330 1330 A -> V (in dbSNP:rs3736228).
{ECO:0000269|PubMed:12509515,
ECO:0000269|PubMed:12579474,
ECO:0000269|PubMed:14727154,
ECO:0000269|PubMed:15077203}.
/FTId=VAR_021817.
VARIANT 1361 1361 C -> G (in EVR4; autosomal dominant; has
mildly reduced Wnt or Norrin signal
transduction; dbSNP:rs80358320).
{ECO:0000269|PubMed:15024691,
ECO:0000269|PubMed:16252235}.
/FTId=VAR_018467.
VARIANT 1367 1367 E -> K (in EVR4; autosomal recessive;
dbSNP:rs28939709).
{ECO:0000269|PubMed:15346351,
ECO:0000269|PubMed:16252235}.
/FTId=VAR_021224.
VARIANT 1401 1401 G -> D (in OPPG).
{ECO:0000269|PubMed:16252235}.
/FTId=VAR_063979.
VARIANT 1517 1517 Y -> C (in EVR1; decreases protein
abundance; dbSNP:rs201030241).
{ECO:0000269|PubMed:27228167}.
/FTId=VAR_076550.
VARIANT 1525 1525 A -> V (in dbSNP:rs1127291).
{ECO:0000269|PubMed:15024691,
ECO:0000269|PubMed:9714764}.
/FTId=VAR_021225.
VARIANT 1537 1537 A -> T (could be associated with
idiopathic osteoporosis; does not result
in a significant alteration of Wnt signal
transduction; dbSNP:rs144376510).
{ECO:0000269|PubMed:16234968}.
/FTId=VAR_063980.
VARIANT 1540 1540 T -> M (in dbSNP:rs141407040).
{ECO:0000269|PubMed:15981244}.
/FTId=VAR_063981.
CONFLICT 1525 1528 Missing (in Ref. 3; AAK52433).
{ECO:0000305}.
SEQUENCE 1615 AA; 179145 MW; 8BA25D07F51E02CA CRC64;
MEAAPPGPPW PLLLLLLLLL ALCGCPAPAA ASPLLLFANR RDVRLVDAGG VKLESTIVVS
GLEDAAAVDF QFSKGAVYWT DVSEEAIKQT YLNQTGAAVQ NVVISGLVSP DGLACDWVGK
KLYWTDSETN RIEVANLNGT SRKVLFWQDL DQPRAIALDP AHGYMYWTDW GETPRIERAG
MDGSTRKIIV DSDIYWPNGL TIDLEEQKLY WADAKLSFIH RANLDGSFRQ KVVEGSLTHP
FALTLSGDTL YWTDWQTRSI HACNKRTGGK RKEILSALYS PMDIQVLSQE RQPFFHTRCE
EDNGGCSHLC LLSPSEPFYT CACPTGVQLQ DNGRTCKAGA EEVLLLARRT DLRRISLDTP
DFTDIVLQVD DIRHAIAIDY DPLEGYVYWT DDEVRAIRRA YLDGSGAQTL VNTEINDPDG
IAVDWVARNL YWTDTGTDRI EVTRLNGTSR KILVSEDLDE PRAIALHPVM GLMYWTDWGE
NPKIECANLD GQERRVLVNA SLGWPNGLAL DLQEGKLYWG DAKTDKIEVI NVDGTKRRTL
LEDKLPHIFG FTLLGDFIYW TDWQRRSIER VHKVKASRDV IIDQLPDLMG LKAVNVAKVV
GTNPCADRNG GCSHLCFFTP HATRCGCPIG LELLSDMKTC IVPEAFLVFT SRAAIHRISL
ETNNNDVAIP LTGVKEASAL DFDVSNNHIY WTDVSLKTIS RAFMNGSSVE HVVEFGLDYP
EGMAVDWMGK NLYWADTGTN RIEVARLDGQ FRQVLVWRDL DNPRSLALDP TKGYIYWTEW
GGKPRIVRAF MDGTNCMTLV DKVGRANDLT IDYADQRLYW TDLDTNMIES SNMLGQERVV
IADDLPHPFG LTQYSDYIYW TDWNLHSIER ADKTSGRNRT LIQGHLDFVM DILVFHSSRQ
DGLNDCMHNN GQCGQLCLAI PGGHRCGCAS HYTLDPSSRN CSPPTTFLLF SQKSAISRMI
PDDQHSPDLI LPLHGLRNVK AIDYDPLDKF IYWVDGRQNI KRAKDDGTQP FVLTSLSQGQ
NPDRQPHDLS IDIYSRTLFW TCEATNTINV HRLSGEAMGV VLRGDRDKPR AIVVNAERGY
LYFTNMQDRA AKIERAALDG TEREVLFTTG LIRPVALVVD NTLGKLFWVD ADLKRIESCD
LSGANRLTLE DANIVQPLGL TILGKHLYWI DRQQQMIERV EKTTGDKRTR IQGRVAHLTG
IHAVEEVSLE EFSAHPCARD NGGCSHICIA KGDGTPRCSC PVHLVLLQNL LTCGEPPTCS
PDQFACATGE IDCIPGAWRC DGFPECDDQS DEEGCPVCSA AQFPCARGQC VDLRLRCDGE
ADCQDRSDEA DCDAICLPNQ FRCASGQCVL IKQQCDSFPD CIDGSDELMC EITKPPSDDS
PAHSSAIGPV IGIILSLFVM GGVYFVCQRV VCQRYAGANG PFPHEYVSGT PHVPLNFIAP
GGSQHGPFTG IACGKSMMSS VSLMGGRGGV PLYDRNHVTG ASSSSSSSTK ATLYPPILNP
PPSPATDPSL YNMDMFYSSN IPATARPYRP YIIRGMAPPT TPCSTDVCDS DYSASRWKAS
KYYLDLNSDS DPYPPPPTPH SQYLSAEDSC PPSPATERSY FHLFPPPPSP CTDSS


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