ID B7ZLD0_HUMAN Unreviewed; 1568 AA. AC B7ZLD0; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 03-AUG-2022, entry version 70. DE RecName: Full=Low-density lipoprotein receptor-related protein {ECO:0000256|PIRNR:PIRNR036314}; GN Name=LRP6 {ECO:0000313|EMBL:AAI43726.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAI43726.1}; RN [1] {ECO:0000313|EMBL:AAI43726.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum {ECO:0000313|EMBL:AAI43726.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers CC beta-catenin signaling through inducing aggregation of receptor-ligand CC complexes into ribosome-sized signalsomes. CC {ECO:0000256|PIRNR:PIRNR036314}. CC -!- SUBUNIT: Homodimer; disulfide-linked. Forms phosphorylated oligomer CC aggregates on Wnt-signaling. {ECO:0000256|PIRNR:PIRNR036314}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the LDLR family. CC {ECO:0000256|PIRNR:PIRNR036314}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC143725; AAI43726.1; -; mRNA. DR SMR; B7ZLD0; -. DR PeptideAtlas; B7ZLD0; -. DR PRIDE; B7ZLD0; -. DR ChiTaRS; LRP6; human. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:0071936; F:coreceptor activity involved in Wnt signaling pathway; IEA:UniProtKB-UniRule. DR GO; GO:0042813; F:Wnt receptor activity; IEA:InterPro. DR GO; GO:0017147; F:Wnt-protein binding; IEA:UniProtKB-UniRule. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:InterPro. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR CDD; cd00112; LDLa; 2. DR Gene3D; 2.120.10.30; -; 4. DR Gene3D; 4.10.400.10; -; 2. 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; 2. DR Pfam; PF00058; Ldl_recept_b; 11. DR PIRSF; PIRSF036314; LDL_recpt-rel_p5/6; 2. DR PRINTS; PR00261; LDLRECEPTOR. DR SMART; SM00181; EGF; 4. DR SMART; SM00192; LDLa; 2. DR SMART; SM00135; LY; 20. DR SUPFAM; SSF57424; SSF57424; 2. DR PROSITE; PS01209; LDLRA_1; 2. DR PROSITE; PS50068; LDLRA_2; 2. DR PROSITE; PS51120; LDLRB; 15. PE 2: Evidence at transcript level; KW Developmental protein {ECO:0000256|PIRNR:PIRNR036314}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536}; KW Endocytosis {ECO:0000256|ARBA:ARBA00022583}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR036314}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR036314}; KW Signal {ECO:0000256|PIRNR:PIRNR036314}; KW Transmembrane {ECO:0000256|PIRNR:PIRNR036314}; KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR036314}; KW Wnt signaling pathway {ECO:0000256|PIRNR:PIRNR036314}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|PIRNR:PIRNR036314" FT CHAIN 20..1568 FT /note="Low-density lipoprotein receptor-related protein" FT /evidence="ECO:0000256|PIRNR:PIRNR036314" FT /id="PRO_5010897968" FT TRANSMEM 1329..1349 FT /note="Helical" FT /evidence="ECO:0000256|PIRNR:PIRNR036314" FT REPEAT 63..106 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 107..149 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 150..193 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 194..236 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT DOMAIN 285..324 FT /note="EGF-like" FT /evidence="ECO:0000259|SMART:SM00181" FT REPEAT 372..414 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 415..457 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 458..501 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 502..544 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT DOMAIN 591..628 FT /note="EGF-like" FT /evidence="ECO:0000259|SMART:SM00181" FT REPEAT 674..716 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 717..759 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 760..802 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 843..885 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT DOMAIN 892..930 FT /note="EGF-like" FT /evidence="ECO:0000259|SMART:SM00181" FT REPEAT 1026..1068 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 1069..1113 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 1114..1156 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT DOMAIN 1206..1244 FT /note="EGF-like" FT /evidence="ECO:0000259|SMART:SM00181" FT REGION 1511..1568 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 1243..1255 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1250..1268 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1262..1277 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1281..1293 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1288..1306 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1300..1315 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" SQ SEQUENCE 1568 AA; 175450 MW; 2E159CC0D275E590 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 AIVVNPEKGY MYFTNLQERS PKIERAALDG TEREVLFFSG LSKPIALALD SRLGKLFWAD SDLRRIESSD LSGANRIVLE DSNILQPVGL TVFENWLYWI DKQQQMIEKI DMTGREGRTK VQARIAQLSD IHAVKELNLQ EYRQHPCAQD NGGCSHICLV KGDGTTRCSC PMHLVLLQDE LSCGESQFQC ASGQCIDGAL RCNGDANCQD KSDEKNCEVL CLIDQFRCAN GQCIGKHKKC DHNVDCSDKS DELDCYPTEE PAPQATNTVG SVIGVIVTIF VSGTVYFICQ RMLCPRMKGD GETMTNDYVV HGPASVPLGY VPHPSSLSGS LPGMSRGKSM ISSLSIMGGS SGPPYDRAHV TGASSSSSSS TKGTYFPAIL NPPPSPATER SHYTMEFGYS SNSPSTHRSY SYRPYSYRHF APPTTPCSTD VCDSDYAPSR RMTSVATAKG YTSDLNYDSE PVPPPPTPRS QYLSAEENYE SCPPSPYTER SYSHHLYPPP PSPCTDSS //