GenomeNet

Database: UniProt
Entry: O75581
LinkDB: O75581
Original site: O75581 
ID   LRP6_HUMAN              Reviewed;        1613 AA.
AC   O75581; Q17RZ2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   10-APR-2019, entry version 173.
DE   RecName: Full=Low-density lipoprotein receptor-related protein 6;
DE            Short=LRP-6;
DE   Flags: Precursor;
GN   Name=LRP6;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-1062.
RC   TISSUE=Kidney;
RX   PubMed=9704021; DOI=10.1006/bbrc.1998.9061;
RA   Brown S.D., Twells R.C., Hey P.J., Cox R.D., Levy E.R., Soderman A.R.,
RA   Metzker M.L., Caskey C.T., Todd J.A., Hess J.F.;
RT   "Isolation and characterization of LRP6, a novel member of the low
RT   density lipoprotein receptor gene family.";
RL   Biochem. Biophys. Res. Commun. 248:879-888(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH DKK1, AND FUNCTION.
RX   PubMed=11448771; DOI=10.1016/S0960-9822(01)00290-1;
RA   Semenov M.V., Tamai K., Brott B.K., Kuhl M., Sokol S., He X.;
RT   "Head inducer Dickkopf-1 is a ligand for Wnt coreceptor LRP6.";
RL   Curr. Biol. 11:951-961(2001).
RN   [5]
RP   INTERACTION WITH WNT1, AND FUNCTION.
RX   PubMed=11357136; DOI=10.1038/35077108;
RA   Mao B., Wu W., Li Y., Hoppe D., Stannek P., Glinka A., Niehrs C.;
RT   "LDL-receptor-related protein 6 is a receptor for Dickkopf proteins.";
RL   Nature 411:321-325(2001).
RN   [6]
RP   INTERACTION WITH FZD5; DKK1 AND DKK2.
RX   PubMed=12857724; DOI=10.1074/jbc.M300191200;
RA   Caricasole A., Ferraro T., Iacovelli L., Barletta E., Caruso A.,
RA   Melchiorri D., Terstappen G.C., Nicoletti F.;
RT   "Functional characterization of WNT7A signaling in PC12 cells:
RT   interaction with A FZD5 x LRP6 receptor complex and modulation by
RT   Dickkopf proteins.";
RL   J. Biol. Chem. 278:37024-37031(2003).
RN   [7]
RP   INTERACTION WITH SOST, AND FUNCTION.
RX   PubMed=15778503; DOI=10.1074/jbc.M413274200;
RA   Li X., Zhang Y., Kang H., Liu W., Liu P., Zhang J., Harris S.E.,
RA   Wu D.;
RT   "Sclerostin binds to LRP5/6 and antagonizes canonical Wnt signaling.";
RL   J. Biol. Chem. 280:19883-19887(2005).
RN   [8]
RP   INTERACTION WITH WNT1 IN THE WNT-FZD-LRP5-LRP6 COMPLEX, AND
RP   INTERACTION WITH SOST.
RX   PubMed=15908424; DOI=10.1074/jbc.M504308200;
RA   Semenov M., Tamai K., He X.;
RT   "SOST is a ligand for LRP5/LRP6 and a Wnt signaling inhibitor.";
RL   J. Biol. Chem. 280:26770-26775(2005).
RN   [9]
RP   PHOSPHORYLATION OF PPPSP MOTIFS, PHOSPHORYLATION AT SER-1490 AND
RP   THR-1493, AND FUNCTION.
RX   PubMed=16341017; DOI=10.1038/nature04185;
RA   Zeng X., Tamai K., Doble B., Li S., Huang H., Habas R., Okamura H.,
RA   Woodgett J., He X.;
RT   "A dual-kinase mechanism for Wnt co-receptor phosphorylation and
RT   activation.";
RL   Nature 438:873-877(2005).
RN   [10]
RP   INTERACTION WITH MACF1.
RX   PubMed=16815997; DOI=10.1101/gad.1411206;
RA   Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.;
RT   "The role of microtubule actin cross-linking factor 1 (MACF1) in the
RT   Wnt signaling pathway.";
RL   Genes Dev. 20:1933-1945(2006).
RN   [11]
RP   PHOSPHORYLATION AT SER-1420 AND SER-1430, FUNCTION, INTERACTION WITH
RP   CSNKIE AND AXIN1, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS
RP   OF SER-1420 AND SER-1430.
RX   PubMed=16513652; DOI=10.1074/jbc.M510580200;
RA   Swiatek W., Kang H., Garcia B.A., Shabanowitz J., Coombs G.S.,
RA   Hunt D.F., Virshup D.M.;
RT   "Negative regulation of LRP6 function by casein kinase I epsilon
RT   phosphorylation.";
RL   J. Biol. Chem. 281:12233-12241(2006).
RN   [12]
RP   INTERACTION WITH RSPO1, FUNCTION, AND PHOSPHORYLATION.
RX   PubMed=17400545; DOI=10.1074/jbc.M701927200;
RA   Wei Q., Yokota C., Semenov M.V., Doble B., Woodgett J., He X.;
RT   "R-spondin1 is a high affinity ligand for LRP6 and induces LRP6
RT   phosphorylation and beta-catenin signaling.";
RL   J. Biol. Chem. 282:15903-15911(2007).
RN   [13]
RP   PROTEOLYTIC PROCESSING, AND FUNCTION.
RX   PubMed=17326769; DOI=10.1111/j.1471-4159.2007.04447.x;
RA   Mi K., Johnson G.V.;
RT   "Regulated proteolytic processing of LRP6 results in release of its
RT   intracellular domain.";
RL   J. Neurochem. 101:517-529(2007).
RN   [14]
RP   GLYCOSYLATION, PHOSPHORYLATION AT SER-1490, INTERACTION WITH AXIN1,
RP   HOMODIMERIZATION, INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17698587; DOI=10.1128/MCB.00773-07;
RA   Khan Z., Vijayakumar S., de la Torre T.V., Rotolo S., Bafico A.;
RT   "Analysis of endogenous LRP6 function reveals a novel feedback
RT   mechanism by which Wnt negatively regulates its receptor.";
RL   Mol. Cell. Biol. 27:7291-7301(2007).
RN   [15]
RP   INTERACTION WITH KREM1 AND DKK1.
RX   PubMed=17804805; DOI=10.1073/pnas.0702305104;
RA   Binnerts M.E., Kim K.A., Bright J.M., Patel S.M., Tran K., Zhou M.,
RA   Leung J.M., Liu Y., Lomas W.E. III, Dixon M., Hazell S.A., Wagle M.,
RA   Nie W.S., Tomasevic N., Williams J., Zhan X., Levy M.D., Funk W.D.,
RA   Abo A.;
RT   "R-Spondin1 regulates Wnt signaling by inhibiting internalization of
RT   LRP6.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:14700-14705(2007).
RN   [16]
RP   PHOSPHORYLATION AT THR-1479, INTERACTION WITH AXIN1, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=17569865; DOI=10.1126/science.1137065;
RA   Bilic J., Huang Y.L., Davidson G., Zimmermann T., Cruciat C.M.,
RA   Bienz M., Niehrs C.;
RT   "Wnt induces LRP6 signalosomes and promotes dishevelled-dependent LRP6
RT   phosphorylation.";
RL   Science 316:1619-1622(2007).
RN   [17]
RP   INTERACTION WITH AXIN1, PHOSPHORYLATION, AND MUTAGENESIS OF LEU-1485;
RP   ASN-1486; PRO-1487; PRO-1488; PRO-1489; SER-1490; PRO-1491; ALA-1492;
RP   THR-1493; GLU-1494; ARG-1495; THR-1529; THR-1530; PRO-1531; THR-1572;
RP   SER-1590 AND SER-1607.
RX   PubMed=18362152; DOI=10.1074/jbc.M800327200;
RA   MacDonald B.T., Yokota C., Tamai K., Zeng X., He X.;
RT   "Wnt signal amplification via activity, cooperativity, and regulation
RT   of multiple intracellular PPPSP motifs in the Wnt co-receptor LRP6.";
RL   J. Biol. Chem. 283:16115-16123(2008).
RN   [18]
RP   INTERACTION WITH CAPRIN2, AND PHOSPHORYLATION AT SER-1490.
RX   PubMed=18762581; DOI=10.1083/jcb.200803147;
RA   Ding Y., Xi Y., Chen T., Wang J.Y., Tao D.L., Wu Z.L., Li Y.P., Li C.,
RA   Zeng R., Li L.;
RT   "Caprin-2 enhances canonical Wnt signaling through regulating LRP5/6
RT   phosphorylation.";
RL   J. Cell Biol. 182:865-872(2008).
RN   [19]
RP   PHOSPHORYLATION ON PPPSP MOTIFS, AND FUNCTION.
RX   PubMed=19107203; DOI=10.1371/journal.pone.0004046;
RA   Piao S., Lee S.H., Kim H., Yum S., Stamos J.L., Xu Y., Lee S.J.,
RA   Lee J., Oh S., Han J.K., Park B.J., Weis W.I., Ha N.C.;
RT   "Direct inhibition of GSK3beta by the phosphorylated cytoplasmic
RT   domain of LRP6 in Wnt/beta-catenin signaling.";
RL   PLoS ONE 3:E4046-E4046(2008).
RN   [20]
RP   PALMITOYLATION AT CYS-1394 AND CYS-1399, UBIQUITINATION AT LYS-1403,
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-1394 AND CYS-1399.
RX   PubMed=18378904; DOI=10.1073/pnas.0710389105;
RA   Abrami L., Kunz B., Iacovache I., van der Goot F.G.;
RT   "Palmitoylation and ubiquitination regulate exit of the Wnt signaling
RT   protein LRP6 from the endoplasmic reticulum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5384-5389(2008).
RN   [21]
RP   DOMAIN PPPSP MOTIF, AND PHOSPHORYLATION AT SER-1490.
RX   PubMed=20059949; DOI=10.1016/j.devcel.2009.11.006;
RA   Davidson G., Shen J., Huang Y.L., Su Y., Karaulanov E.,
RA   Bartscherer K., Hassler C., Stannek P., Boutros M., Niehrs C.;
RT   "Cell cycle control of wnt receptor activation.";
RL   Dev. Cell 17:788-799(2009).
RN   [22]
RP   PHOSPHORYLATION OF PPPSP MOTIFS, PHOSPHORYLATION AT SER-1490, AND
RP   FUNCTION.
RX   PubMed=19801552; DOI=10.1074/jbc.M109.047456;
RA   Chen M., Philipp M., Wang J., Premont R.T., Garrison T.R., Caron M.G.,
RA   Lefkowitz R.J., Chen W.;
RT   "G Protein-coupled receptor kinases phosphorylate LRP6 in the Wnt
RT   pathway.";
RL   J. Biol. Chem. 284:35040-35048(2009).
RN   [23]
RP   PHOSPHORYLATION OF PPPSP MOTIFS, AND FUNCTION.
RX   PubMed=19293931; DOI=10.1371/journal.pone.0004926;
RA   Wu G., Huang H., Garcia Abreu J., He X.;
RT   "Inhibition of GSK3 phosphorylation of beta-catenin via phosphorylated
RT   PPPSPXS motifs of Wnt coreceptor LRP6.";
RL   PLoS ONE 4:E4926-E4926(2009).
RN   [24]
RP   INTERACTION WITH WNT3A; WNT9B AND FZD8 IN THE WNT/FZD/LRP6 COMPLEX,
RP   AND INTERACTION WITH DKK1.
RX   PubMed=20093360; DOI=10.1074/jbc.M109.092130;
RA   Bourhis E., Tam C., Franke Y., Bazan J.F., Ernst J., Hwang J.,
RA   Costa M., Cochran A.G., Hannoush R.N.;
RT   "Reconstitution of a frizzled8.Wnt3a.LRP6 signaling complex reveals
RT   multiple Wnt and Dkk1 binding sites on LRP6.";
RL   J. Biol. Chem. 285:9172-9179(2010).
RN   [25]
RP   INTERACTION WITH TMEM198.
RX   PubMed=21536646; DOI=10.1128/MCB.05103-11;
RA   Liang J., Fu Y., Cruciat C.M., Jia S., Wang Y., Tong Z., Tao Q.,
RA   Ingelfinger D., Boutros M., Meng A., Niehrs C., Wu W.;
RT   "Transmembrane protein 198 promotes LRP6 phosphorylation and Wnt
RT   signaling activation.";
RL   Mol. Cell. Biol. 31:2577-2590(2011).
RN   [26]
RP   INTERACTION WITH DAB2.
RX   PubMed=22491013; DOI=10.1038/emboj.2012.83;
RA   Jiang Y., He X., Howe P.H.;
RT   "Disabled-2 (Dab2) inhibits Wnt/beta-catenin signalling by binding
RT   LRP6 and promoting its internalization through clathrin.";
RL   EMBO J. 31:2336-2349(2012).
RN   [27]
RP   UBIQUITINATION BY ZNRF3.
RX   PubMed=22575959; DOI=10.1038/nature11019;
RA   Hao H.X., Xie Y., Zhang Y., Charlat O., Oster E., Avello M., Lei H.,
RA   Mickanin C., Liu D., Ruffner H., Mao X., Ma Q., Zamponi R.,
RA   Bouwmeester T., Finan P.M., Kirschner M.W., Porter J.A., Serluca F.C.,
RA   Cong F.;
RT   "ZNRF3 promotes Wnt receptor turnover in an R-spondin-sensitive
RT   manner.";
RL   Nature 485:195-200(2012).
RN   [28]
RP   INTERACTION WITH LYPD6, AND SUBCELLULAR LOCATION.
RX   PubMed=23987510; DOI=10.1016/j.devcel.2013.07.020;
RA   Oezhan G., Sezgin E., Wehner D., Pfister A.S., Kuehl S.J.,
RA   Kagermeier-Schenk B., Kuehl M., Schwille P., Weidinger G.;
RT   "Lypd6 enhances Wnt/beta-catenin signaling by promoting Lrp6
RT   phosphorylation in raft plasma membrane domains.";
RL   Dev. Cell 26:331-345(2013).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1490, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [30]
RP   INTERACTION WITH CAPRIN2, AND PHOSPHORYLATION AT SER-1490.
RX   PubMed=25331957; DOI=10.1074/jbc.M114.591636;
RA   Miao H., Jia Y., Xie S., Wang X., Zhao J., Chu Y., Zhou Z., Shi Z.,
RA   Song X., Li L.;
RT   "Structural insights into the C1q domain of Caprin-2 in canonical Wnt
RT   signaling.";
RL   J. Biol. Chem. 289:34104-34113(2014).
RN   [31]
RP   IDENTIFICATION IN A COMPLEX WITH CAPRIN2; CCNY AND CDK14, AND
RP   PHOSPHORYLATION AT SER-1490.
RX   PubMed=27821587; DOI=10.1074/jbc.M116.744607;
RA   Wang X., Jia Y., Fei C., Song X., Li L.;
RT   "Caprin-2 positively regulates CDK14/Cyclin Y-mediated LRP5/6
RT   constitutive phosphorylation.";
RL   J. Biol. Chem. 291:26427-26434(2016).
RN   [32]
RP   IDENTIFICATION IN A TERNARY COMPLEX WITH KREM1 AND LRP6.
RX   PubMed=27524201; DOI=10.1016/j.str.2016.06.020;
RA   Zebisch M., Jackson V.A., Zhao Y., Jones E.Y.;
RT   "Structure of the dual-mode wnt regulator Kremen1 and insight into
RT   ternary complex formation with LRP6 and Dickkopf.";
RL   Structure 24:1599-1605(2016).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 630-1246 IN COMPLEX WITH
RP   DKK1, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-692; ASN-859;
RP   ASN-865; ASN-926 AND ASN-1039.
RX   PubMed=22000856; DOI=10.1016/j.devcel.2011.09.003;
RA   Ahn V.E., Chu M.L., Choi H.J., Tran D., Abo A., Weis W.I.;
RT   "Structural basis of Wnt signaling inhibition by Dickkopf binding to
RT   LRP5/6.";
RL   Dev. Cell 21:862-873(2011).
RN   [34]
RP   VARIANT ADCAD2 CYS-611, AND CHARACTERIZATION OF VARIANT ADCAD2
RP   CYS-611.
RX   PubMed=17332414; DOI=10.1126/science.1136370;
RA   Mani A., Radhakrishnan J., Wang H., Mani A., Mani M.-A.,
RA   Nelson-Williams C., Carew K.S., Mane S., Najmabadi H., Wu D.,
RA   Lifton R.P.;
RT   "LRP6 mutation in a family with early coronary disease and metabolic
RT   risk factors.";
RL   Science 315:1278-1282(2007).
RN   [35]
RP   VARIANTS ADCAD2 HIS-360; SER-433 AND GLN-473, AND CHARACTERIZATION OF
RP   VARIANT ADCAD2 GLN-473.
RX   PubMed=23703864; DOI=10.1002/humu.22360;
RA   Singh R., Smith E., Fathzadeh M., Liu W., Go G.W., Subrahmanyan L.,
RA   Faramarzi S., McKenna W., Mani A.;
RT   "Rare nonconservative LRP6 mutations are associated with metabolic
RT   syndrome.";
RL   Hum. Mutat. 34:1221-1225(2013).
RN   [36]
RP   INVOLVEMENT IN STHAG7, VARIANT STHAG7 VAL-19, CHARACTERIZATION OF
RP   VARIANT STHAG7 VAL-19, AND SUBCELLULAR LOCATION.
RX   PubMed=26387593; DOI=10.1016/j.ajhg.2015.08.014;
RA   Massink M.P., Creton M.A., Spanevello F., Fennis W.M., Cune M.S.,
RA   Savelberg S.M., Nijman I.J., Maurice M.M., van den Boogaard M.J.,
RA   van Haaften G.;
RT   "Loss-of-Function Mutations in the WNT Co-receptor LRP6 Cause
RT   Autosomal-Dominant Oligodontia.";
RL   Am. J. Hum. Genet. 97:621-626(2015).
CC   -!- FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers
CC       beta-catenin signaling through inducing aggregation of receptor-
CC       ligand complexes into ribosome-sized signalsomes. Cell-surface
CC       coreceptor of Wnt/beta-catenin signaling, which plays a pivotal
CC       role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor
CC       complex recruits DVL1 polymers to the plasma membrane which, in
CC       turn, recruits the AXIN1/GSK3B-complex to the cell surface
CC       promoting the formation of signalsomes and inhibiting AXIN1/GSK3-
CC       mediated phosphorylation and destruction of beta-catenin. Required
CC       for posterior patterning of the epiblast during gastrulation (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:11357136,
CC       ECO:0000269|PubMed:11448771, ECO:0000269|PubMed:15778503,
CC       ECO:0000269|PubMed:16341017, ECO:0000269|PubMed:16513652,
CC       ECO:0000269|PubMed:17326769, ECO:0000269|PubMed:17400545,
CC       ECO:0000269|PubMed:19107203, ECO:0000269|PubMed:19293931,
CC       ECO:0000269|PubMed:19801552}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Forms phosphorylated
CC       oligomer aggregates on Wnt-signaling. Forms a WNT-signaling
CC       complex formed of a WNT protein, a FZD protein and LRP5 or LRP6.
CC       Interacts (via the extracellular domain) with WNT1; the
CC       interaction is enhanced by prior formation of the Wnt/Fzd complex.
CC       Interacts (via the beta-propeller regions 3 and 4) with WNT3A.
CC       Interacts (via the beta-propeller regions 1 and 2) with WNT9B.
CC       Interacts with FZD5; the interaction forms a coreceptor complex
CC       for Wnt signaling and is inhibited by DKK1 and DRAXIN. Interacts
CC       (via beta propeller region) with DKK1; the interaction inhibits
CC       FZD5/LRP6 complex formation. Interacts with DKK2. Interacts with
CC       C1orf187/DRAXIN; the interaction inhibits Wnt signaling (By
CC       similarity). Interacts (via the phosphorylated PPPSP motifs) with
CC       AXIN1; the interaction recruits the AXIN1/GSK3B complex to cell
CC       surface LRP6 signalsomes. Interacts with GRB10; the interaction
CC       prevents AXIN1 binding, thus negatively regulating the Wnt
CC       signaling pathway (By similarity). Interacts (via the
CC       extracellular domain) with RSPO1; the interaction activates
CC       Wnt/beta-catenin signaling. Interacts (via the extracellular
CC       domain) with RSPO3 (via the cysteine rich domain); the interaction
CC       activates Wnt/beta-catenin signaling. Interacts (via the beta-
CC       propeller regions 1 and 2) with SOST; the interaction competes
CC       with DKK1 for binding for inhibiting beta-catenin signaling.
CC       Interacts with MESD; the interaction prevents the formation of
CC       LRP6 aggregates and targets LRP6 to the plasma membrane (By
CC       similarity). Interacts (via the cytoplasmic domain) with CSNKIE;
CC       the interaction phosphorylates LRP6, binds AXIN1 and inhibits
CC       AXIN1/GSK3B-mediated phosphorylation of beta-catenin. Interacts
CC       with MACF1. Interacts with DAB2; the interaction involves LRP6
CC       phosphorylation by CK2 and sequesters LRP6 towards clathrin-
CC       mediated endocytosis. Interacts with TMEM198. Interacts with
CC       CAPRIN2; the interaction promotes LRP6 phosphorylation at Ser-1490
CC       (PubMed:18762581, PubMed:25331957). Found in a complex with
CC       CAPRIN2, CCNY and CDK14 during G2/M stage; CAPRIN2 functions as a
CC       scaffold for the complex by binding to CCNY via its N terminus and
CC       to CDK14 via its C terminus (PubMed:27821587). Interacts with
CC       LYPD6 (PubMed:23987510). Forms a ternary complex with DKK1 and
CC       KREM1 (PubMed:27524201). Interacts with KREM1 in a DKK1-dependent
CC       manner (PubMed:17804805). {ECO:0000250|UniProtKB:O88572,
CC       ECO:0000269|PubMed:11357136, ECO:0000269|PubMed:11448771,
CC       ECO:0000269|PubMed:12857724, ECO:0000269|PubMed:15778503,
CC       ECO:0000269|PubMed:15908424, ECO:0000269|PubMed:16513652,
CC       ECO:0000269|PubMed:16815997, ECO:0000269|PubMed:17400545,
CC       ECO:0000269|PubMed:17569865, ECO:0000269|PubMed:17698587,
CC       ECO:0000269|PubMed:17804805, ECO:0000269|PubMed:18362152,
CC       ECO:0000269|PubMed:18762581, ECO:0000269|PubMed:20093360,
CC       ECO:0000269|PubMed:21536646, ECO:0000269|PubMed:22000856,
CC       ECO:0000269|PubMed:22491013, ECO:0000269|PubMed:23987510,
CC       ECO:0000269|PubMed:25331957, ECO:0000269|PubMed:27524201,
CC       ECO:0000269|PubMed:27821587}.
CC   -!- INTERACTION:
CC       Self; NbExp=4; IntAct=EBI-910915, EBI-910915;
CC       Q9Y4X0:AMMECR1; NbExp=5; IntAct=EBI-910915, EBI-8583355;
CC       Q9H6X2:ANTXR1; NbExp=3; IntAct=EBI-910915, EBI-905643;
CC       O15169-2:AXIN1; NbExp=3; IntAct=EBI-910915, EBI-10987526;
CC       O35625:Axin1 (xeno); NbExp=2; IntAct=EBI-910915, EBI-2365912;
CC       O70239:Axin1 (xeno); NbExp=12; IntAct=EBI-910915, EBI-6857773;
CC       Q03135:CAV1; NbExp=3; IntAct=EBI-910915, EBI-603614;
CC       P98082:DAB2; NbExp=20; IntAct=EBI-910915, EBI-1171238;
CC       O94907:DKK1; NbExp=14; IntAct=EBI-910915, EBI-742864;
CC       Q61091:Fzd8 (xeno); NbExp=4; IntAct=EBI-910915, EBI-6171689;
CC       P49840:GSK3A; NbExp=2; IntAct=EBI-910915, EBI-1044067;
CC       P49841:GSK3B; NbExp=4; IntAct=EBI-910915, EBI-373586;
CC       P47879:Igfbp4 (xeno); NbExp=4; IntAct=EBI-910915, EBI-15706768;
CC       Q5S007:LRRK2; NbExp=4; IntAct=EBI-910915, EBI-5323863;
CC       Q9ERE7:Mesd (xeno); NbExp=2; IntAct=EBI-910915, EBI-6662606;
CC       P09619:PDGFRB; NbExp=3; IntAct=EBI-910915, EBI-641237;
CC       Q9BQB4:SOST; NbExp=6; IntAct=EBI-910915, EBI-5746563;
CC       P04426:Wnt1 (xeno); NbExp=2; IntAct=EBI-910915, EBI-1570911;
CC       P56704:WNT3A; NbExp=2; IntAct=EBI-910915, EBI-6173037;
CC       P27467:Wnt3a (xeno); NbExp=4; IntAct=EBI-910915, EBI-2899665;
CC       Q9ULT6:ZNRF3; NbExp=2; IntAct=EBI-910915, EBI-949772;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26387593};
CC       Single-pass type I membrane protein. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:26387593}. Membrane raft
CC       {ECO:0000269|PubMed:23987510}. Note=On Wnt signaling, undergoes a
CC       cycle of caveolin- or clathrin-mediated endocytosis and plasma
CC       membrane location. Released from the endoplasmic reticulum on
CC       palmitoylation. Mono-ubiquitination retains it in the endoplasmic
CC       reticulum in the absence of palmitoylation. On Wnt signaling,
CC       phosphorylated, aggregates and colocalizes with AXIN1 and GSK3B at
CC       the plasma membrane in LRP6-signalsomes. Chaperoned to the plasma
CC       membrane by MESD (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely coexpressed with LRP5 during
CC       embryogenesis and in adult tissues.
CC   -!- INDUCTION: Decreased levels on WNT3A stimulation.
CC       {ECO:0000269|PubMed:17698587}.
CC   -!- DOMAIN: The YWTD-EGF-like domains 1 and 2 are required for the
CC       interaction with Wnt-frizzled complex. The YWTD-EGF-like domains 3
CC       and 4 are required for the interaction with DKK1.
CC       {ECO:0000269|PubMed:20059949}.
CC   -!- DOMAIN: The PPPSP motifs play a central role in signal
CC       transduction by being phosphorylated, leading to activate the Wnt
CC       signaling pathway. {ECO:0000269|PubMed:20059949}.
CC   -!- PTM: Dual phosphorylation of cytoplasmic PPPSP motifs sequentially
CC       by GSK3 and CK1 is required for AXIN1-binding, and subsequent
CC       stabilization and activation of beta-catenin via preventing GSK3-
CC       mediated phosphorylation of beta-catenin. Phosphorylated, in
CC       vitro, by GRK5/6 within and outside the PPPSP motifs.
CC       Phosphorylation at Ser-1490 by CDK14 during G2/M phase leads to
CC       regulation of the Wnt signaling pathway during the cell cycle.
CC       Phosphorylation by GSK3B is induced by RPSO1 binding and inhibited
CC       by DKK1. Phosphorylated, in vitro, by casein kinase I on Thr-1479.
CC       {ECO:0000269|PubMed:16341017, ECO:0000269|PubMed:16513652,
CC       ECO:0000269|PubMed:17400545, ECO:0000269|PubMed:17569865,
CC       ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:18362152,
CC       ECO:0000269|PubMed:19107203, ECO:0000269|PubMed:19293931,
CC       ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20059949}.
CC   -!- PTM: Undergoes gamma-secretase-dependent regulated intramembrane
CC       proteolysis (RIP). The extracellular domain is first released by
CC       shedding, and then, through the action of gamma-secretase, the
CC       intracellular domain (ICD) is released into the cytoplasm where it
CC       is free to bind to GSK3B and to activate canonical Wnt signaling.
CC   -!- PTM: Palmitoylation on the two sites near the transmembrane domain
CC       leads to release of LRP6 from the endoplasmic reticulum.
CC       {ECO:0000269|PubMed:18378904}.
CC   -!- PTM: Mono-ubiquitinated which retains LRP6 in the endoplasmic
CC       reticulum. Ubiquitinated by ZNRF3, leading to its degradation by
CC       the proteasome. {ECO:0000269|PubMed:18378904,
CC       ECO:0000269|PubMed:22575959}.
CC   -!- PTM: N-glycosylation is required for cell surface location.
CC       {ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:22000856}.
CC   -!- DISEASE: Coronary artery disease, autosomal dominant, 2 (ADCAD2)
CC       [MIM:610947]: A common heart disease characterized by reduced or
CC       absent blood flow in one or more of the arteries that encircle and
CC       supply the heart. Its most important complication is acute
CC       myocardial infarction. {ECO:0000269|PubMed:17332414,
CC       ECO:0000269|PubMed:23703864}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Tooth agenesis, selective, 7 (STHAG7) [MIM:616724]: An
CC       autosomal dominant form of selective tooth agenesis, a common
CC       anomaly characterized by the congenital absence of one or more
CC       teeth. Selective tooth agenesis without associated systemic
CC       disorders has sometimes been divided into 2 types: oligodontia,
CC       defined as agenesis of 6 or more permanent teeth, and hypodontia,
CC       defined as agenesis of less than 6 teeth. The number in both cases
CC       does not include absence of third molars (wisdom teeth).
CC       {ECO:0000269|PubMed:26387593}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
DR   EMBL; AF074264; AAC33006.1; -; mRNA.
DR   EMBL; AC007537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC007621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC117136; AAI17137.1; -; mRNA.
DR   EMBL; BC126405; AAI26406.1; -; mRNA.
DR   CCDS; CCDS8647.1; -.
DR   PIR; JE0272; JE0272.
DR   RefSeq; NP_002327.2; NM_002336.2.
DR   RefSeq; XP_006719141.1; XM_006719078.3.
DR   UniGene; Hs.584775; -.
DR   UniGene; Hs.658913; -.
DR   PDB; 3S2K; X-ray; 2.80 A; A/B=630-1246.
DR   PDB; 3S8V; X-ray; 3.10 A; A/B=629-1243.
DR   PDB; 3S8Z; X-ray; 2.80 A; A=629-1243.
DR   PDB; 3S94; X-ray; 2.80 A; A/B=20-630.
DR   PDB; 3SOB; X-ray; 1.90 A; B=20-335.
DR   PDB; 3SOQ; X-ray; 1.90 A; A=20-326.
DR   PDB; 3SOV; X-ray; 1.27 A; A=20-326.
DR   PDB; 4A0P; X-ray; 1.90 A; A=629-1244.
DR   PDB; 4DG6; X-ray; 2.90 A; A=20-635.
DR   PDB; 4NM5; X-ray; 2.30 A; C=1568-1575.
DR   PDB; 4NM7; X-ray; 2.30 A; C=1603-1610.
DR   PDB; 5AIR; X-ray; 2.53 A; A/B=1565-1575.
DR   PDB; 5FWW; X-ray; 3.50 A; A=630-1246.
DR   PDB; 5GJE; EM; 21.00 A; A=20-630, B=631-1246.
DR   PDB; 6H15; X-ray; 2.60 A; A/B=630-1244.
DR   PDB; 6H16; X-ray; 2.90 A; A=630-1244.
DR   PDBsum; 3S2K; -.
DR   PDBsum; 3S8V; -.
DR   PDBsum; 3S8Z; -.
DR   PDBsum; 3S94; -.
DR   PDBsum; 3SOB; -.
DR   PDBsum; 3SOQ; -.
DR   PDBsum; 3SOV; -.
DR   PDBsum; 4A0P; -.
DR   PDBsum; 4DG6; -.
DR   PDBsum; 4NM5; -.
DR   PDBsum; 4NM7; -.
DR   PDBsum; 5AIR; -.
DR   PDBsum; 5FWW; -.
DR   PDBsum; 5GJE; -.
DR   PDBsum; 6H15; -.
DR   PDBsum; 6H16; -.
DR   ProteinModelPortal; O75581; -.
DR   SMR; O75581; -.
DR   BioGrid; 110219; 54.
DR   CORUM; O75581; -.
DR   DIP; DIP-29884N; -.
DR   IntAct; O75581; 39.
DR   MINT; O75581; -.
DR   STRING; 9606.ENSP00000261349; -.
DR   BindingDB; O75581; -.
DR   ChEMBL; CHEMBL3745588; -.
DR   iPTMnet; O75581; -.
DR   PhosphoSitePlus; O75581; -.
DR   SwissPalm; O75581; -.
DR   BioMuta; LRP6; -.
DR   EPD; O75581; -.
DR   jPOST; O75581; -.
DR   MaxQB; O75581; -.
DR   PaxDb; O75581; -.
DR   PeptideAtlas; O75581; -.
DR   PRIDE; O75581; -.
DR   ProteomicsDB; 50097; -.
DR   Ensembl; ENST00000261349; ENSP00000261349; ENSG00000070018.
DR   Ensembl; ENST00000628182; ENSP00000486315; ENSG00000281324.
DR   GeneID; 4040; -.
DR   KEGG; hsa:4040; -.
DR   UCSC; uc001rah.6; human.
DR   CTD; 4040; -.
DR   DisGeNET; 4040; -.
DR   EuPathDB; HostDB:ENSG00000070018.8; -.
DR   GeneCards; LRP6; -.
DR   H-InvDB; HIX0036693; -.
DR   HGNC; HGNC:6698; LRP6.
DR   HPA; CAB004490; -.
DR   HPA; HPA029925; -.
DR   MalaCards; LRP6; -.
DR   MIM; 603507; gene.
DR   MIM; 610947; phenotype.
DR   MIM; 616724; phenotype.
DR   neXtProt; NX_O75581; -.
DR   OpenTargets; ENSG00000070018; -.
DR   Orphanet; 411969; NON RARE IN EUROPE: Metabolic syndrome.
DR   Orphanet; 99798; Oligodontia.
DR   PharmGKB; PA30456; -.
DR   eggNOG; ENOG410IPT4; Eukaryota.
DR   eggNOG; ENOG410XSY5; LUCA.
DR   GeneTree; ENSGT00940000158990; -.
DR   HOGENOM; HOG000230697; -.
DR   HOVERGEN; HBG049167; -.
DR   InParanoid; O75581; -.
DR   KO; K03068; -.
DR   OMA; WQELDQP; -.
DR   OrthoDB; 121310at2759; -.
DR   PhylomeDB; O75581; -.
DR   TreeFam; TF315253; -.
DR   Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR   Reactome; R-HSA-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
DR   Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR   Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
DR   Reactome; R-HSA-5340588; RNF mutants show enhanced WNT signaling and proliferation.
DR   SignaLink; O75581; -.
DR   SIGNOR; O75581; -.
DR   ChiTaRS; LRP6; human.
DR   EvolutionaryTrace; O75581; -.
DR   GeneWiki; LRP6; -.
DR   GenomeRNAi; 4040; -.
DR   PRO; PR:O75581; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000070018; Expressed in 234 organ(s), highest expression level in metanephros.
DR   ExpressionAtlas; O75581; baseline and differential.
DR   Genevisible; O75581; HS.
DR   GO; GO:0005901; C:caveola; IBA:GO_Central.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1990851; C:Wnt-Frizzled-LRP5/6 complex; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0034185; F:apolipoprotein binding; IBA:GO_Central.
DR   GO; GO:1904928; F:coreceptor activity involved in canonical Wnt signaling pathway; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0071936; F:coreceptor activity involved in Wnt signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0005109; F:frizzled binding; IPI:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019210; F:kinase inhibitor activity; IMP:BHF-UCL.
DR   GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR   GO; GO:0019534; F:toxin transmembrane transporter activity; IMP:BHF-UCL.
DR   GO; GO:0042813; F:Wnt-activated receptor activity; IEA:InterPro.
DR   GO; GO:0017147; F:Wnt-protein binding; IPI:BHF-UCL.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IBA:GO_Central.
DR   GO; GO:0090245; P:axis elongation involved in somitogenesis; IBA:GO_Central.
DR   GO; GO:1904886; P:beta-catenin destruction complex disassembly; TAS:Reactome.
DR   GO; GO:0060349; P:bone morphogenesis; IBA:GO_Central.
DR   GO; GO:0046849; P:bone remodeling; IBA:GO_Central.
DR   GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IBA:GO_Central.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0044335; P:canonical Wnt signaling pathway involved in neural crest cell differentiation; IC:BHF-UCL.
DR   GO; GO:0044340; P:canonical Wnt signaling pathway involved in regulation of cell proliferation; IC:BHF-UCL.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0071397; P:cellular response to cholesterol; IMP:BHF-UCL.
DR   GO; GO:0021587; P:cerebellum morphogenesis; IBA:GO_Central.
DR   GO; GO:0021987; P:cerebral cortex development; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0060026; P:convergent extension; IBA:GO_Central.
DR   GO; GO:0071542; P:dopaminergic neuron differentiation; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IBA:GO_Central.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IBA:GO_Central.
DR   GO; GO:0009880; P:embryonic pattern specification; IBA:GO_Central.
DR   GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IBA:GO_Central.
DR   GO; GO:0035261; P:external genitalia morphogenesis; IBA:GO_Central.
DR   GO; GO:0060325; P:face morphogenesis; IBA:GO_Central.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IBA:GO_Central.
DR   GO; GO:0030901; P:midbrain development; IBA:GO_Central.
DR   GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0030917; P:midbrain-hindbrain boundary development; IBA:GO_Central.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:BHF-UCL.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IDA:BHF-UCL.
DR   GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IMP:BHF-UCL.
DR   GO; GO:0014033; P:neural crest cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0014029; P:neural crest formation; IDA:BHF-UCL.
DR   GO; GO:0001843; P:neural tube closure; IBA:GO_Central.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IBA:GO_Central.
DR   GO; GO:0003344; P:pericardium morphogenesis; IBA:GO_Central.
DR   GO; GO:0045787; P:positive regulation of cell cycle; IMP:BHF-UCL.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
DR   GO; GO:0090009; P:primitive streak formation; IBA:GO_Central.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IBA:GO_Central.
DR   GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR   GO; GO:0060021; P:roof of mouth development; IBA:GO_Central.
DR   GO; GO:0021794; P:thalamus development; IBA:GO_Central.
DR   GO; GO:0060535; P:trachea cartilage morphogenesis; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1904953; P:Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0090244; P:Wnt signaling pathway involved in somitogenesis; IBA:GO_Central.
DR   CDD; cd00112; LDLa; 3.
DR   Gene3D; 2.120.10.30; -; 4.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR017049; LRP5/6.
DR   Pfam; PF00057; Ldl_recept_a; 3.
DR   Pfam; PF00058; Ldl_recept_b; 11.
DR   PIRSF; PIRSF036314; LDL_recpt-rel_p5/6; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00192; LDLa; 3.
DR   SMART; SM00135; LY; 20.
DR   SUPFAM; SSF57424; SSF57424; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01209; LDLRA_1; 3.
DR   PROSITE; PS50068; LDLRA_2; 3.
DR   PROSITE; PS51120; LDLRB; 19.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Complete proteome; Developmental protein;
KW   Disease mutation; Disulfide bond; EGF-like domain; Endocytosis;
KW   Endoplasmic reticulum; Glycoprotein; Isopeptide bond; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Polymorphism; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Ubl conjugation; Wnt signaling pathway.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20   1613       Low-density lipoprotein receptor-related
FT                                protein 6.
FT                                /FTId=PRO_0000017330.
FT   TOPO_DOM     20   1370       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1371   1393       Helical. {ECO:0000255}.
FT   TOPO_DOM   1394   1613       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       63    106       LDL-receptor class B 1.
FT   REPEAT      107    149       LDL-receptor class B 2.
FT   REPEAT      150    193       LDL-receptor class B 3.
FT   REPEAT      194    236       LDL-receptor class B 4.
FT   REPEAT      237    276       LDL-receptor class B 5.
FT   DOMAIN      282    324       EGF-like 1.
FT   REPEAT      372    414       LDL-receptor class B 6.
FT   REPEAT      415    457       LDL-receptor class B 7.
FT   REPEAT      458    501       LDL-receptor class B 8.
FT   REPEAT      502    542       LDL-receptor class B 9.
FT   REPEAT      543    584       LDL-receptor class B 10.
FT   DOMAIN      588    628       EGF-like 2.
FT   REPEAT      674    716       LDL-receptor class B 11.
FT   REPEAT      717    759       LDL-receptor class B 12.
FT   REPEAT      760    802       LDL-receptor class B 13.
FT   REPEAT      803    842       LDL-receptor class B 14.
FT   REPEAT      843    885       LDL-receptor class B 15.
FT   DOMAIN      889    930       EGF-like 3.
FT   REPEAT      977   1025       LDL-receptor class B 16.
FT   REPEAT     1026   1068       LDL-receptor class B 17.
FT   REPEAT     1069   1113       LDL-receptor class B 18.
FT   REPEAT     1114   1156       LDL-receptor class B 19.
FT   REPEAT     1157   1198       LDL-receptor class B 20.
FT   DOMAIN     1203   1244       EGF-like 4.
FT   DOMAIN     1248   1286       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1287   1323       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1325   1361       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   REGION       20    275       Beta-propeller 1.
FT   REGION      328    589       Beta-propeller 2.
FT   REGION      631    890       Beta-propeller 3.
FT   REGION      933   1202       Beta-propeller 4.
FT   MOTIF      1487   1493       PPPSP motif A.
FT   MOTIF      1527   1534       PPPSP motif B.
FT   MOTIF      1568   1575       PPPSP motif C.
FT   MOTIF      1588   1593       PPPSP motif D.
FT   MOTIF      1603   1610       PPPSP motif E.
FT   MOD_RES    1420   1420       Phosphoserine; by CK1.
FT                                {ECO:0000269|PubMed:16513652}.
FT   MOD_RES    1430   1430       Phosphoserine; by CK1.
FT                                {ECO:0000269|PubMed:16513652}.
FT   MOD_RES    1479   1479       Phosphothreonine.
FT                                {ECO:0000269|PubMed:17569865}.
FT   MOD_RES    1490   1490       Phosphoserine; by CDK14, GRK5 and GRK6.
FT                                {ECO:0000244|PubMed:23186163,
FT                                ECO:0000269|PubMed:16341017,
FT                                ECO:0000269|PubMed:17698587,
FT                                ECO:0000269|PubMed:18762581,
FT                                ECO:0000269|PubMed:19801552,
FT                                ECO:0000269|PubMed:20059949,
FT                                ECO:0000269|PubMed:25331957,
FT                                ECO:0000269|PubMed:27821587}.
FT   MOD_RES    1493   1493       Phosphothreonine; by CK1.
FT                                {ECO:0000269|PubMed:16341017}.
FT   LIPID      1394   1394       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:18378904}.
FT   LIPID      1399   1399       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:18378904}.
FT   CARBOHYD     42     42       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     81     81       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    281    281       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    433    433       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    486    486       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    692    692       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:22000856}.
FT   CARBOHYD    859    859       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:22000856}.
FT   CARBOHYD    865    865       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:22000856}.
FT   CARBOHYD    926    926       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:22000856}.
FT   CARBOHYD   1039   1039       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:22000856}.
FT   DISULFID    286    297       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    293    308       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    310    323       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    592    603       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    599    612       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    614    627       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    893    904       {ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:22000856}.
FT   DISULFID    900    914       {ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:22000856}.
FT   DISULFID    916    929       {ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:22000856}.
FT   DISULFID   1207   1218       {ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:22000856}.
FT   DISULFID   1214   1228       {ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:22000856}.
FT   DISULFID   1230   1243       {ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:22000856}.
FT   DISULFID   1249   1263       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1256   1276       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1270   1285       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1288   1300       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1295   1313       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1307   1322       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1326   1338       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1333   1351       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1345   1360       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   CROSSLNK   1403   1403       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:18378904}.
FT   VARIANT      19     19       A -> V (in STHAG7; impairs Wnt signaling;
FT                                prevents transport to plasma membrane
FT                                location; dbSNP:rs864309648).
FT                                {ECO:0000269|PubMed:26387593}.
FT                                /FTId=VAR_076207.
FT   VARIANT     360    360       R -> H (in ADCAD2; dbSNP:rs141212743).
FT                                {ECO:0000269|PubMed:23703864}.
FT                                /FTId=VAR_076208.
FT   VARIANT     433    433       N -> S (in ADCAD2; dbSNP:rs397515473).
FT                                {ECO:0000269|PubMed:23703864}.
FT                                /FTId=VAR_076209.
FT   VARIANT     473    473       R -> Q (in ADCAD2; impairs Wnt signaling;
FT                                dbSNP:rs397515474).
FT                                {ECO:0000269|PubMed:23703864}.
FT                                /FTId=VAR_076210.
FT   VARIANT     483    483       V -> I (in dbSNP:rs7975614).
FT                                /FTId=VAR_030349.
FT   VARIANT     611    611       R -> C (in ADCAD2; impairs Wnt signaling
FT                                in vitro; dbSNP:rs121918313).
FT                                {ECO:0000269|PubMed:17332414}.
FT                                /FTId=VAR_034701.
FT   VARIANT     817    817       S -> C (in dbSNP:rs2302686).
FT                                /FTId=VAR_030350.
FT   VARIANT    1062   1062       V -> I (in dbSNP:rs2302685).
FT                                {ECO:0000269|PubMed:9704021}.
FT                                /FTId=VAR_024520.
FT   VARIANT    1401   1401       R -> H (in dbSNP:rs34815107).
FT                                /FTId=VAR_034702.
FT   MUTAGEN    1394   1394       C->A: Some reduction of palmitoylation,
FT                                little change in plasma membrane location
FT                                in the presence of MESD nor in Wnt-
FT                                signaling activity. Completely abolishes
FT                                palmitoylation, no plasma membrane
FT                                location, greatly reduced Wnt-signaling
FT                                activity but no effect on ubiquitination;
FT                                when associated with A-1399. Exhibits
FT                                full Wnt-signaling activity and no change
FT                                in plasma membrane location; when
FT                                associated with A-1399 and R-1403.
FT                                {ECO:0000269|PubMed:18378904}.
FT   MUTAGEN    1399   1399       C->A: Some reduction of palmitoylation,
FT                                and little change in plasma membrane
FT                                location in the presence of MESD nor in
FT                                Wnt-signaling activity. Completely
FT                                abolishes palmitoylation, no plasma
FT                                membrane location, greatly reduced Wnt-
FT                                signaling activity but no effect on
FT                                ubiquitination; when associated with A-
FT                                1394. Exhibits full Wnt-signaling
FT                                activity and no change in plasma membrane
FT                                location in the in presence of MESD; when
FT                                associated with A-1394 and R-1403.
FT                                {ECO:0000269|PubMed:18378904}.
FT   MUTAGEN    1403   1403       K->R: Abolishes ubiquitination, no change
FT                                in plasma membrane location in the
FT                                presence of MESD but greatly reduced Wnt-
FT                                signaling activity. Exhibits full Wnt-
FT                                signaling activity and no change in
FT                                plasma membrane location; when associated
FT                                with A-1394 and A-1399.
FT   MUTAGEN    1420   1420       S->A: Enhanced AXIN1 binding and
FT                                increased beta-catenin activity by 2.2-
FT                                fold. Further enhanced AXIN1 binding and
FT                                increases beta-catenin activity by 3.3-
FT                                fold; when associated with A-1430.
FT                                {ECO:0000269|PubMed:16513652}.
FT   MUTAGEN    1430   1430       S->A: Enhanced AXIN1 binding. Further
FT                                enhanced AXIN1 binding and increases
FT                                beta-catenin activity by 3.3-fold; when
FT                                associated with A-1420.
FT                                {ECO:0000269|PubMed:16513652}.
FT   MUTAGEN    1485   1485       L->A: No change in the phosphorylation
FT                                state of PPPSP motif. Some reduction in
FT                                Wnt/beta-catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1486   1486       N->A: No change in the phosphorylation
FT                                state of PPPSP motif. Increased Wnt/beta-
FT                                catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1487   1487       P->A: No change in the phosphorylation
FT                                state of PPPSP motif A. Greatly reduced
FT                                Wnt/beta-catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1487   1487       P->C: No change in the phosphorylation
FT                                state of PPPSP motif A. Greatly reduced
FT                                Wnt/beta-catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1488   1488       P->A: No change in the phosphorylation
FT                                state of PPPSP motif A. Greatly reduced
FT                                Wnt/beta-catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1489   1489       P->A: No change in the phosphorylation
FT                                state of PPPSP motif A. Greatly reduced
FT                                Wnt/beta-catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1490   1490       S->A: Greatly reduced phosphorylation of
FT                                PPPSP motif A. Greatly reduced Wnt/beta-
FT                                catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1490   1490       S->T: Some loss of phosphorylation of
FT                                PPPSP motif A. Little reduction in
FT                                Wnt/beta-catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1491   1491       P->A: Greatly reduced phosphorylation of
FT                                PPPSP motif A. Greatly reduced Wnt/beta-
FT                                catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1492   1492       A->G: No change in the phosphorylation
FT                                state of PPPSP motif A. Greatly reduced
FT                                Wnt/beta-catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1493   1493       T->A: No change in the phosphorylation
FT                                state of PPPSP motif A. Greatly reduced
FT                                Wnt/beta-catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1494   1494       E->A: No change in the phosphorylation
FT                                state of PPPSP motif A. Little reduction
FT                                of Wnt/beta-catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1495   1495       R->A: No change in the phosphorylation
FT                                state of PPPSP motif. No reduction of
FT                                Wnt/beta-catenin signaling.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1529   1529       T->A: No effect on the phosphorylation
FT                                state of PPPSP motif B.
FT                                {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1530   1530       T->A: Abolishes phosphorylation of PPPSP
FT                                motif B. Reduced Wnt/beta-catenin
FT                                signaling. {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1531   1531       P->A: Abolishes phosphorylation of PPPSP
FT                                motif B. Reduced Wnt/beta-catenin
FT                                signaling. {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1572   1572       T->A: Abolishes Wnt/beta-catenin
FT                                signaling. {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1590   1590       S->A: Abolishes Wnt/beta-catenin
FT                                signaling. {ECO:0000269|PubMed:18362152}.
FT   MUTAGEN    1607   1607       S->A: Abolishes Wnt/beta-catenin
FT                                signaling. {ECO:0000269|PubMed:18362152}.
FT   STRAND       22     26       {ECO:0000244|PDB:3SOV}.
FT   STRAND       28     35       {ECO:0000244|PDB:3SOV}.
FT   HELIX        36     38       {ECO:0000244|PDB:3SOB}.
FT   STRAND       44     59       {ECO:0000244|PDB:3SOV}.
FT   HELIX        60     62       {ECO:0000244|PDB:3SOV}.
FT   STRAND       64     69       {ECO:0000244|PDB:3SOV}.
FT   TURN         70     73       {ECO:0000244|PDB:3SOV}.
FT   STRAND       74     79       {ECO:0000244|PDB:3SOV}.
FT   STRAND       82     84       {ECO:0000244|PDB:3SOV}.
FT   STRAND       88     92       {ECO:0000244|PDB:3SOV}.
FT   STRAND       99    103       {ECO:0000244|PDB:3SOV}.
FT   TURN        104    107       {ECO:0000244|PDB:3SOV}.
FT   STRAND      108    113       {ECO:0000244|PDB:3SOV}.
FT   TURN        114    117       {ECO:0000244|PDB:3SOV}.
FT   STRAND      118    123       {ECO:0000244|PDB:3SOV}.
FT   STRAND      130    133       {ECO:0000244|PDB:3SOV}.
FT   STRAND      138    146       {ECO:0000244|PDB:3SOV}.
FT   HELIX       147    149       {ECO:0000244|PDB:3SOV}.
FT   STRAND      151    156       {ECO:0000244|PDB:3SOV}.
FT   STRAND      158    160       {ECO:0000244|PDB:3SOV}.
FT   STRAND      162    167       {ECO:0000244|PDB:3SOV}.
FT   STRAND      174    177       {ECO:0000244|PDB:3SOV}.
FT   STRAND      184    190       {ECO:0000244|PDB:3SOV}.
FT   TURN        191    194       {ECO:0000244|PDB:3SOV}.
FT   STRAND      195    200       {ECO:0000244|PDB:3SOV}.
FT   TURN        201    204       {ECO:0000244|PDB:3SOV}.
FT   STRAND      205    210       {ECO:0000244|PDB:3SOV}.
FT   STRAND      217    220       {ECO:0000244|PDB:3SOV}.
FT   STRAND      227    233       {ECO:0000244|PDB:3SOV}.
FT   STRAND      236    241       {ECO:0000244|PDB:3SOV}.
FT   TURN        242    245       {ECO:0000244|PDB:3SOV}.
FT   STRAND      246    251       {ECO:0000244|PDB:3SOV}.
FT   TURN        252    254       {ECO:0000244|PDB:3SOV}.
FT   STRAND      259    262       {ECO:0000244|PDB:3SOV}.
FT   STRAND      271    274       {ECO:0000244|PDB:3SOV}.
FT   HELIX       276    278       {ECO:0000244|PDB:3SOV}.
FT   TURN        285    289       {ECO:0000244|PDB:3SOV}.
FT   HELIX       290    292       {ECO:0000244|PDB:3SOV}.
FT   STRAND      294    299       {ECO:0000244|PDB:3SOV}.
FT   STRAND      305    309       {ECO:0000244|PDB:3SOV}.
FT   STRAND      328    337       {ECO:0000244|PDB:3S94}.
FT   STRAND      339    346       {ECO:0000244|PDB:3S94}.
FT   STRAND      360    368       {ECO:0000244|PDB:3S94}.
FT   TURN        369    372       {ECO:0000244|PDB:3S94}.
FT   STRAND      373    378       {ECO:0000244|PDB:3S94}.
FT   TURN        379    382       {ECO:0000244|PDB:3S94}.
FT   STRAND      383    388       {ECO:0000244|PDB:3S94}.
FT   STRAND      389    391       {ECO:0000244|PDB:4DG6}.
FT   STRAND      395    398       {ECO:0000244|PDB:3S94}.
FT   STRAND      407    411       {ECO:0000244|PDB:3S94}.
FT   TURN        412    415       {ECO:0000244|PDB:3S94}.
FT   STRAND      416    421       {ECO:0000244|PDB:3S94}.
FT   TURN        422    425       {ECO:0000244|PDB:3S94}.
FT   STRAND      426    431       {ECO:0000244|PDB:3S94}.
FT   STRAND      438    441       {ECO:0000244|PDB:3S94}.
FT   STRAND      447    454       {ECO:0000244|PDB:3S94}.
FT   TURN        455    458       {ECO:0000244|PDB:3S94}.
FT   STRAND      459    464       {ECO:0000244|PDB:3S94}.
FT   STRAND      466    468       {ECO:0000244|PDB:3S94}.
FT   STRAND      470    475       {ECO:0000244|PDB:3S94}.
FT   STRAND      482    485       {ECO:0000244|PDB:3S94}.
FT   STRAND      492    498       {ECO:0000244|PDB:3S94}.
FT   TURN        499    502       {ECO:0000244|PDB:3S94}.
FT   STRAND      503    508       {ECO:0000244|PDB:3S94}.
FT   TURN        509    512       {ECO:0000244|PDB:3S94}.
FT   STRAND      513    521       {ECO:0000244|PDB:3S94}.
FT   STRAND      525    529       {ECO:0000244|PDB:3S94}.
FT   STRAND      538    541       {ECO:0000244|PDB:3S94}.
FT   STRAND      544    548       {ECO:0000244|PDB:3S94}.
FT   STRAND      555    562       {ECO:0000244|PDB:3S94}.
FT   STRAND      565    569       {ECO:0000244|PDB:3S94}.
FT   STRAND      575    584       {ECO:0000244|PDB:3S94}.
FT   HELIX       591    593       {ECO:0000244|PDB:3S94}.
FT   HELIX       595    598       {ECO:0000244|PDB:3S94}.
FT   STRAND      600    606       {ECO:0000244|PDB:3S94}.
FT   STRAND      609    613       {ECO:0000244|PDB:3S94}.
FT   STRAND      633    638       {ECO:0000244|PDB:4A0P}.
FT   STRAND      641    648       {ECO:0000244|PDB:4A0P}.
FT   STRAND      653    655       {ECO:0000244|PDB:4A0P}.
FT   STRAND      664    670       {ECO:0000244|PDB:4A0P}.
FT   TURN        671    674       {ECO:0000244|PDB:4A0P}.
FT   STRAND      675    680       {ECO:0000244|PDB:4A0P}.
FT   TURN        681    684       {ECO:0000244|PDB:4A0P}.
FT   STRAND      685    690       {ECO:0000244|PDB:4A0P}.
FT   STRAND      697    700       {ECO:0000244|PDB:4A0P}.
FT   STRAND      709    713       {ECO:0000244|PDB:4A0P}.
FT   TURN        714    717       {ECO:0000244|PDB:4A0P}.
FT   STRAND      718    723       {ECO:0000244|PDB:4A0P}.
FT   TURN        724    727       {ECO:0000244|PDB:4A0P}.
FT   STRAND      728    733       {ECO:0000244|PDB:4A0P}.
FT   STRAND      740    743       {ECO:0000244|PDB:4A0P}.
FT   STRAND      750    756       {ECO:0000244|PDB:4A0P}.
FT   TURN        757    760       {ECO:0000244|PDB:4A0P}.
FT   STRAND      761    766       {ECO:0000244|PDB:4A0P}.
FT   STRAND      768    770       {ECO:0000244|PDB:4A0P}.
FT   STRAND      772    777       {ECO:0000244|PDB:4A0P}.
FT   STRAND      784    787       {ECO:0000244|PDB:4A0P}.
FT   STRAND      791    799       {ECO:0000244|PDB:4A0P}.
FT   TURN        800    803       {ECO:0000244|PDB:4A0P}.
FT   STRAND      804    809       {ECO:0000244|PDB:4A0P}.
FT   TURN        810    813       {ECO:0000244|PDB:4A0P}.
FT   STRAND      814    819       {ECO:0000244|PDB:4A0P}.
FT   STRAND      826    830       {ECO:0000244|PDB:4A0P}.
FT   STRAND      835    841       {ECO:0000244|PDB:4A0P}.
FT   STRAND      844    849       {ECO:0000244|PDB:4A0P}.
FT   TURN        850    853       {ECO:0000244|PDB:4A0P}.
FT   STRAND      854    859       {ECO:0000244|PDB:4A0P}.
FT   TURN        860    862       {ECO:0000244|PDB:4A0P}.
FT   STRAND      867    870       {ECO:0000244|PDB:4A0P}.
FT   STRAND      878    882       {ECO:0000244|PDB:4A0P}.
FT   HELIX       884    886       {ECO:0000244|PDB:4A0P}.
FT   TURN        892    896       {ECO:0000244|PDB:4A0P}.
FT   HELIX       897    899       {ECO:0000244|PDB:4A0P}.
FT   STRAND      901    907       {ECO:0000244|PDB:4A0P}.
FT   TURN        908    910       {ECO:0000244|PDB:4A0P}.
FT   STRAND      911    915       {ECO:0000244|PDB:4A0P}.
FT   STRAND      933    940       {ECO:0000244|PDB:4A0P}.
FT   STRAND      943    947       {ECO:0000244|PDB:4A0P}.
FT   STRAND      967    973       {ECO:0000244|PDB:4A0P}.
FT   TURN        974    977       {ECO:0000244|PDB:4A0P}.
FT   STRAND      978    983       {ECO:0000244|PDB:4A0P}.
FT   TURN        984    987       {ECO:0000244|PDB:4A0P}.
FT   STRAND      988    993       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1000   1003       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1016   1022       {ECO:0000244|PDB:4A0P}.
FT   TURN       1023   1026       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1027   1032       {ECO:0000244|PDB:4A0P}.
FT   TURN       1033   1036       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1037   1042       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1047   1052       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1059   1065       {ECO:0000244|PDB:4A0P}.
FT   TURN       1066   1069       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1070   1077       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1080   1087       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1094   1097       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1104   1110       {ECO:0000244|PDB:4A0P}.
FT   TURN       1111   1114       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1115   1120       {ECO:0000244|PDB:4A0P}.
FT   TURN       1121   1124       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1125   1130       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1137   1140       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1147   1153       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1156   1161       {ECO:0000244|PDB:4A0P}.
FT   TURN       1162   1165       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1166   1171       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1174   1176       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1179   1182       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1188   1194       {ECO:0000244|PDB:4A0P}.
FT   HELIX      1199   1204       {ECO:0000244|PDB:4A0P}.
FT   TURN       1206   1209       {ECO:0000244|PDB:4A0P}.
FT   HELIX      1210   1213       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1215   1220       {ECO:0000244|PDB:4A0P}.
FT   TURN       1222   1224       {ECO:0000244|PDB:3S8Z}.
FT   STRAND     1226   1229       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1234   1236       {ECO:0000244|PDB:4A0P}.
FT   STRAND     1238   1241       {ECO:0000244|PDB:3S8Z}.
SQ   SEQUENCE   1613 AA;  180429 MW;  413D2CF70A5D8B5C CRC64;
     MGAVLRSLLA CSFCVLLRAA PLLLYANRRD LRLVDATNGK ENATIVVGGL EDAAAVDFVF
     SHGLIYWSDV SEEAIKRTEF NKTESVQNVV VSGLLSPDGL ACDWLGEKLY WTDSETNRIE
     VSNLDGSLRK VLFWQELDQP RAIALDPSSG FMYWTDWGEV PKIERAGMDG SSRFIIINSE
     IYWPNGLTLD YEEQKLYWAD AKLNFIHKSN LDGTNRQAVV KGSLPHPFAL TLFEDILYWT
     DWSTHSILAC NKYTGEGLRE IHSDIFSPMD IHAFSQQRQP NATNPCGIDN GGCSHLCLMS
     PVKPFYQCAC PTGVKLLENG KTCKDGATEL LLLARRTDLR RISLDTPDFT DIVLQLEDIR
     HAIAIDYDPV EGYIYWTDDE VRAIRRSFID GSGSQFVVTA QIAHPDGIAV DWVARNLYWT
     DTGTDRIEVT RLNGTMRKIL ISEDLEEPRA IVLDPMVGYM YWTDWGEIPK IERAALDGSD
     RVVLVNTSLG WPNGLALDYD EGKIYWGDAK TDKIEVMNTD GTGRRVLVED KIPHIFGFTL
     LGDYVYWTDW QRRSIERVHK RSAEREVIID QLPDLMGLKA TNVHRVIGSN PCAEENGGCS
     HLCLYRPQGL RCACPIGFEL ISDMKTCIVP EAFLLFSRRA DIRRISLETN NNNVAIPLTG
     VKEASALDFD VTDNRIYWTD ISLKTISRAF MNGSALEHVV EFGLDYPEGM AVDWLGKNLY
     WADTGTNRIE VSKLDGQHRQ VLVWKDLDSP RALALDPAEG FMYWTEWGGK PKIDRAAMDG
     SERTTLVPNV GRANGLTIDY AKRRLYWTDL DTNLIESSNM LGLNREVIAD DLPHPFGLTQ
     YQDYIYWTDW SRRSIERANK TSGQNRTIIQ GHLDYVMDIL VFHSSRQSGW NECASSNGHC
     SHLCLAVPVG GFVCGCPAHY SLNADNRTCS APTTFLLFSQ KSAINRMVID EQQSPDIILP
     IHSLRNVRAI DYDPLDKQLY WIDSRQNMIR KAQEDGSQGF TVVVSSVPSQ NLEIQPYDLS
     IDIYSRYIYW TCEATNVINV TRLDGRSVGV VLKGEQDRPR AVVVNPEKGY MYFTNLQERS
     PKIERAALDG TEREVLFFSG LSKPIALALD SRLGKLFWAD SDLRRIESSD LSGANRIVLE
     DSNILQPVGL TVFENWLYWI DKQQQMIEKI DMTGREGRTK VQARIAQLSD IHAVKELNLQ
     EYRQHPCAQD NGGCSHICLV KGDGTTRCSC PMHLVLLQDE LSCGEPPTCS PQQFTCFTGE
     IDCIPVAWRC DGFTECEDHS DELNCPVCSE SQFQCASGQC IDGALRCNGD ANCQDKSDEK
     NCEVLCLIDQ FRCANGQCIG KHKKCDHNVD CSDKSDELDC YPTEEPAPQA TNTVGSVIGV
     IVTIFVSGTV YFICQRMLCP RMKGDGETMT NDYVVHGPAS VPLGYVPHPS SLSGSLPGMS
     RGKSMISSLS IMGGSSGPPY DRAHVTGASS SSSSSTKGTY FPAILNPPPS PATERSHYTM
     EFGYSSNSPS THRSYSYRPY SYRHFAPPTT PCSTDVCDSD YAPSRRMTSV ATAKGYTSDL
     NYDSEPVPPP PTPRSQYLSA EENYESCPPS PYTERSYSHH LYPPPPSPCT DSS
//
DBGET integrated database retrieval system