ID   LRP4_MOUSE              Reviewed;        1905 AA.
AC   Q8VI56; A2AGT4; Q8BPX5; Q8CBB3; Q8CCP5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Low-density lipoprotein receptor-related protein 4;
DE            Short=LRP-4;
DE   AltName: Full=LDLR dan;
DE   Flags: Precursor;
GN   Name=Lrp4; Synonyms=Kiaa0816;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISEASE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16517118; DOI=10.1016/j.ygeno.2006.01.007;
RA   Simon-Chazottes D., Tutois S., Kuehn M., Evans M., Bourgade F., Cook S.,
RA   Davisson M.T., Guenet J.L.;
RT   "Mutations in the gene encoding the low-density lipoprotein receptor LRP4
RT   cause abnormal limb development in the mouse.";
RL   Genomics 87:673-677(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-566 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 682-1905 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [6]
RP   FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, FUNCTION AS RECEPTOR FOR
RP   AGRIN, AND INTERACTION WITH AGRIN AND MUSK.
RX   PubMed=18848351; DOI=10.1016/j.cell.2008.10.002;
RA   Kim N., Stiegler A.L., Cameron T.O., Hallock P.T., Gomez A.M., Huang J.H.,
RA   Hubbard S.R., Dustin M.L., Burden S.J.;
RT   "Lrp4 is a receptor for Agrin and forms a complex with MuSK.";
RL   Cell 135:334-342(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   FUNCTION.
RX   PubMed=21471202; DOI=10.1074/jbc.m110.190330;
RA   Leupin O., Piters E., Halleux C., Hu S., Kramer I., Morvan F.,
RA   Bouwmeester T., Schirle M., Bueno-Lozano M., Fuentes F.J., Itin P.H.,
RA   Boudin E., de Freitas F., Jennes K., Brannetti B., Charara N.,
RA   Ebersbach H., Geisse S., Lu C.X., Bauer A., Van Hul W., Kneissel M.;
RT   "Bone overgrowth-associated mutations in the LRP4 gene impair sclerostin
RT   facilitator function.";
RL   J. Biol. Chem. 286:19489-19500(2011).
RN   [9]
RP   INTERACTION WITH MESD, GLYCOSYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=24140340; DOI=10.1016/j.febslet.2013.10.001;
RA   Hoshi T., Tezuka T., Yokoyama K., Iemura S., Natsume T., Yamanashi Y.;
RT   "Mesdc2 plays a key role in cell-surface expression of Lrp4 and
RT   postsynaptic specialization in myotubes.";
RL   FEBS Lett. 587:3749-3754(2013).
CC   -!- FUNCTION: Mediates SOST-dependent inhibition of bone formation.
CC       Functions as a specific facilitator of SOST-mediated inhibition of Wnt
CC       signaling. Plays a key role in the formation and the maintenance of the
CC       neuromuscular junction (NMJ), the synapse between motor neuron and
CC       skeletal muscle. Directly binds AGRIN and recruits it to the MUSK
CC       signaling complex. Mediates the AGRIN-induced phosphorylation of MUSK,
CC       the kinase of the complex. The activation of MUSK in myotubes induces
CC       the formation of NMJ by regulating different processes including the
CC       transcription of specific genes and the clustering of AChR in the
CC       postsynaptic membrane. Alternatively, may be involved in the negative
CC       regulation of the canonical Wnt signaling pathway, being able to
CC       antagonize the LRP6-mediated activation of this pathway. More
CC       generally, has been proposed to function as a cell surface endocytic
CC       receptor binding and internalizing extracellular ligands for
CC       degradation by lysosomes. Plays an essential role in the process of
CC       digit differentiation (PubMed:16517118). {ECO:0000269|PubMed:16517118,
CC       ECO:0000269|PubMed:18848351, ECO:0000269|PubMed:21471202}.
CC   -!- SUBUNIT: Homooligomer. Interacts with MUSK; the heterodimer forms an
CC       AGRIN receptor complex that binds AGRIN resulting in activation of
CC       MUSK. Interacts (via the extracellular domain) with SOST; the
CC       interaction facilitates the inhibition of Wnt signaling (By
CC       similarity). Interacts with MESD; the interaction promotes
CC       glycosylation of LRP4 and its cell-surface expression
CC       (PubMed:24140340). {ECO:0000250, ECO:0000269|PubMed:24140340}.
CC   -!- INTERACTION:
CC       Q8VI56; Q9ERE7: Mesd; NbExp=2; IntAct=EBI-2106160, EBI-6662606;
CC       Q8VI56; P25304: Agrn; Xeno; NbExp=3; IntAct=EBI-2106160, EBI-2106099;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24140340};
CC       Single-pass type I membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VI56-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VI56-2; Sequence=VSP_010034;
CC   -!- PTM: N-glycosylation is required for cell surface location.
CC       {ECO:0000269|PubMed:24140340}.
CC   -!- DISEASE: Note=Defects in Lrp4 are the cause of digitation anormale
CC       (dan) phenotype, this mutation is the consequence of a retroviral
CC       insertion. Dan mice shown growth retardation in 10-day-old mice dan/dan
CC       and polysyndactyly (PubMed:16517118). Defects in Lrp4 are the cause of
CC       malformed digits (mdig) phenotype. It is a spontaneous, autosomal
CC       recessive mutation resulting in polysyndactyly (PubMed:16517118).
CC       {ECO:0000269|PubMed:16517118}.
CC   -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27835.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=BAC29416.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AF247637; AAL36970.1; -; mRNA.
DR   EMBL; AL691489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL732478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC132240; AAI32241.1; -; mRNA.
DR   EMBL; AK032360; BAC27835.1; ALT_TERM; mRNA.
DR   EMBL; AK036406; BAC29416.1; ALT_SEQ; mRNA.
DR   EMBL; AK129224; BAC98034.1; -; Transcribed_RNA.
DR   CCDS; CCDS16432.1; -. [Q8VI56-1]
DR   RefSeq; NP_001139329.1; NM_001145857.1.
DR   RefSeq; NP_766256.3; NM_172668.3. [Q8VI56-1]
DR   AlphaFoldDB; Q8VI56; -.
DR   SMR; Q8VI56; -.
DR   BioGRID; 230726; 4.
DR   IntAct; Q8VI56; 14.
DR   MINT; Q8VI56; -.
DR   STRING; 10090.ENSMUSP00000028689; -.
DR   GlyConnect; 2486; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q8VI56; 7 sites, 1 glycan.
DR   GlyGen; Q8VI56; 7 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q8VI56; -.
DR   PhosphoSitePlus; Q8VI56; -.
DR   MaxQB; Q8VI56; -.
DR   PaxDb; 10090-ENSMUSP00000028689; -.
DR   PeptideAtlas; Q8VI56; -.
DR   ProteomicsDB; 252678; -. [Q8VI56-1]
DR   ProteomicsDB; 252679; -. [Q8VI56-2]
DR   ABCD; Q8VI56; 2 sequenced antibodies.
DR   Antibodypedia; 1985; 388 antibodies from 38 providers.
DR   DNASU; 228357; -.
DR   Ensembl; ENSMUST00000028689.4; ENSMUSP00000028689.4; ENSMUSG00000027253.16. [Q8VI56-1]
DR   GeneID; 228357; -.
DR   KEGG; mmu:228357; -.
DR   UCSC; uc008kvx.2; mouse. [Q8VI56-1]
DR   AGR; MGI:2442252; -.
DR   CTD; 4038; -.
DR   MGI; MGI:2442252; Lrp4.
DR   VEuPathDB; HostDB:ENSMUSG00000027253; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   GeneTree; ENSGT00940000158287; -.
DR   HOGENOM; CLU_000085_4_1_1; -.
DR   InParanoid; Q8VI56; -.
DR   OMA; NNRYTAI; -.
DR   OrthoDB; 3107655at2759; -.
DR   PhylomeDB; Q8VI56; -.
DR   TreeFam; TF315253; -.
DR   BioGRID-ORCS; 228357; 1 hit in 81 CRISPR screens.
DR   ChiTaRS; Lrp4; mouse.
DR   PRO; PR:Q8VI56; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8VI56; Protein.
DR   Bgee; ENSMUSG00000027253; Expressed in glomerular capsule and 226 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0044853; C:plasma membrane raft; ISS:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
DR   GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0015026; F:coreceptor activity; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR   GO; GO:0097110; F:scaffold protein binding; ISS:UniProtKB.
DR   GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; ISO:MGI.
DR   GO; GO:0048856; P:anatomical structure development; IMP:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007167; P:enzyme-linked receptor protein signaling pathway; IDA:MGI.
DR   GO; GO:0048699; P:generation of neurons; IBA:GO_Central.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0060173; P:limb development; ISO:MGI.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; IMP:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:MGI.
DR   GO; GO:0030279; P:negative regulation of ossification; ISO:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
DR   GO; GO:1901631; P:positive regulation of presynaptic membrane organization; IDA:UniProtKB.
DR   GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IDA:MGI.
DR   GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IDA:MGI.
DR   GO; GO:0097104; P:postsynaptic membrane assembly; IMP:UniProtKB.
DR   GO; GO:0097105; P:presynaptic membrane assembly; IMP:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR   GO; GO:0043113; P:receptor clustering; IMP:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
DR   GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IMP:UniProtKB.
DR   GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
DR   GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IDA:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00112; LDLa; 7.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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   PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR   PANTHER; PTHR22722:SF14; MEGALIN, ISOFORM A; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF14670; FXa_inhibition; 2.
DR   Pfam; PF00057; Ldl_recept_a; 8.
DR   Pfam; PF00058; Ldl_recept_b; 16.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00192; LDLa; 8.
DR   SMART; SM00135; LY; 20.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 8.
DR   SUPFAM; SSF63825; YWTD domain; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 8.
DR   PROSITE; PS50068; LDLRA_2; 8.
DR   PROSITE; PS51120; LDLRB; 20.
DR   Genevisible; Q8VI56; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell membrane; Developmental protein;
KW   Differentiation; Disulfide bond; EGF-like domain; Endocytosis;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1905
FT                   /note="Low-density lipoprotein receptor-related protein 4"
FT                   /id="PRO_0000017326"
FT   TOPO_DOM        21..1725
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1726..1746
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1747..1905
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..67
FT                   /note="LDL-receptor class A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          70..106
FT                   /note="LDL-receptor class A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          109..144
FT                   /note="LDL-receptor class A 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          147..183
FT                   /note="LDL-receptor class A 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          190..226
FT                   /note="LDL-receptor class A 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          230..266
FT                   /note="LDL-receptor class A 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          269..305
FT                   /note="LDL-receptor class A 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          311..350
FT                   /note="LDL-receptor class A 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          354..394
FT                   /note="EGF-like 1; atypical"
FT   DOMAIN          395..434
FT                   /note="EGF-like 2; calcium-binding"
FT   REPEAT          480..522
FT                   /note="LDL-receptor class B 1"
FT   REPEAT          523..565
FT                   /note="LDL-receptor class B 2"
FT   REPEAT          566..609
FT                   /note="LDL-receptor class B 3"
FT   REPEAT          610..652
FT                   /note="LDL-receptor class B 4"
FT   REPEAT          653..693
FT                   /note="LDL-receptor class B 5"
FT   DOMAIN          698..737
FT                   /note="EGF-like 3"
FT   REPEAT          785..827
FT                   /note="LDL-receptor class B 6"
FT   REPEAT          828..870
FT                   /note="LDL-receptor class B 7"
FT   REPEAT          871..914
FT                   /note="LDL-receptor class B 8"
FT   REPEAT          915..956
FT                   /note="LDL-receptor class B 9"
FT   REPEAT          957..998
FT                   /note="LDL-receptor class B 10"
FT   REPEAT          1093..1135
FT                   /note="LDL-receptor class B 11"
FT   REPEAT          1136..1178
FT                   /note="LDL-receptor class B 12"
FT   REPEAT          1179..1222
FT                   /note="LDL-receptor class B 13"
FT   REPEAT          1223..1263
FT                   /note="LDL-receptor class B 14"
FT   REPEAT          1264..1306
FT                   /note="LDL-receptor class B 15"
FT   REPEAT          1397..1439
FT                   /note="LDL-receptor class B 16"
FT   REPEAT          1440..1482
FT                   /note="LDL-receptor class B 17"
FT   REPEAT          1483..1526
FT                   /note="LDL-receptor class B 18"
FT   REPEAT          1527..1568
FT                   /note="LDL-receptor class B 19"
FT   REPEAT          1569..1610
FT                   /note="LDL-receptor class B 20"
FT   REGION          1661..1696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1852..1905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1666..1691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1852..1881
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1888..1905
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        498
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        719
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        901
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1077
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1467
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        34..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        51..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        71..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        78..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        90..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        110..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        117..135
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        129..143
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        148..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        155..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        167..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        191..203
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        198..216
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        210..225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        231..243
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        238..256
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        250..265
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        270..282
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        277..295
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        289..304
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        312..324
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        319..337
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        331..349
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        358..369
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        365..378
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        380..393
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        399..409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        405..418
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        420..433
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        702..713
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        709..722
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        724..736
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   VAR_SEQ         1564..1620
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_010034"
FT   CONFLICT        196
FT                   /note="F -> L (in Ref. 4; BAC27835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="I -> L (in Ref. 4; BAC29416)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="C -> R (in Ref. 1; AAL36970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        682..685
FT                   /note="HFPM -> LHTP (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1330
FT                   /note="G -> S (in Ref. 1; AAL36970)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1905 AA;  211954 MW;  282CA859B76D9BAD CRC64;
     MRRWWGALLL GALLCAHGIA SSLECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH
     SDEDGCTLPT CSPLDFHCDN GKCIRRSWVC DGDNDCEDDS DEQDCPPREC EEDEFPCQNG
     YCIRSLWHCD GDNDCGDNSD EQCDMRKCSD KEFRCSDGSC IAEHWYCDGD TDCKDGSDEE
     SCPSAVPSPP CNLEEFQCAY GRCILDIYHC DGDDDCGDWS DESDCSSHQP CRSGEFMCDS
     GLCINSGWRC DGDADCDDQS DERNCTTSMC TAEQFRCRSG RCVRLSWRCD GEDDCADNSD
     EENCENTGSP QCASDQFLCW NGRCIGQRKL CNGINDCGDS SDESPQQNCR PRTGEENCNV
     NNGGCAQKCQ MVRGAVQCTC HTGYRLTEDG RTCQDVNECA EEGYCSQGCT NTEGAFQCWC
     EAGYELRPDR RSCKALGPEP VLLFANRIDI RQVLPHRSEY TLLLNNLENA IALDFHHRRE
     LVFWSDVTLD RILRANLNGS NVEEVVSTGL ESPGGLAVDW VHDKLYWTDS GTSRIEVANL
     DGAHRKVLLW QSLEKPRAIA LHPMEGTIYW TDWGNTPRIE ASSMDGSGRR IIADTHLFWP
     NGLTIDYAGR RMYWVDAKHH VIERANLDGS HRKAVISQGL PHPFAITVFE DSLYWTDWHT
     KSINSANKFT GKNQEIIRNK LHFPMDIHTL HPQRQPAGKN RCGDNNGGCT HLCLPSGQNY
     TCACPTGFRK INSHACAQSL DKFLLFARRM DIRRISFDTE DLSDDVIPLA DVRSAVALDW
     DSRDDHVYWT DVSTDTISRA KWDGTGQEVV VDTSLESPAG LAIDWVTNKL YWTDAGTDRI
     EVANTDGSMR TVLIWENLDR PRDIVVEPMG GYMYWTDWGA SPKIERAGMD ASSRQVIISS
     NLTWPNGLAI DYGSQRLYWA DAGMKTIEFA GLDGSKRKVL IGSQLPHPFG LTLYGQRIYW
     TDWQTKSIQS ADRLTGLDRE TLQENLENLM DIHVFHRQRP PVTTLCAVEN GGCSHLCLRS
     PNPSGFSCTC PTGINLLRDG KTCSPGMNSF LIFARRIDVR MVSLDIPYFA DVVVPINMTM
     KNTIAIGVDP LEGKVYWSDS TLHRISRASL DGSQHEDIIT TGLQTTDGLA VDAIGRKVYW
     TDTGTNRIEV GNLDGSMRKV LVWQNLDSPR AIVLYHEMGF MYWTDWGENA KLERSGMDGS
     DRTVLINNNL GWPNGLTVDK TSSQLLWADA HTERIEVADL NGANRHTLVS PVQHPYGLTL
     LDSYIYWTDW QTRSIHRADK STGSNVILVR SNLPGLMDIQ AVDRAQPLGF NKCGSRNGGC
     SHLCLPRPSG FSCACPTGIQ LKGDRKTCDP SPETYLLFSS RGSIRRISLD TDDHTDVHVP
     VPGLNNVISL DYDSVHGKVY YTDVFLDVIR RADLNGSNME TVIGHGLKTT DGLAVDWVAR
     NLYWTDTGRN TIEASRLDGS CRKVLINNSL DEPRAIAVFP RKGYLFWTDW GHIAKIERAN
     LDGSERKVLI NTDLGWPNGL TLDYDTRRIY WVDAHLDRIE SADLNGKLRQ VLVSHVSHPF
     ALTQQDRWIY WTDWQTKSIQ RVDKYSGRNK ETVLANVEGL MDIIVVSPQR QTGTNACGVN
     NGGCTHLCFA RASDFVCACP DEPDGHPCSL VPGLVPPAPR ATSMNEKSPV LPNTLPTTLH
     SSTTKTRTSL EGAGGRCSER DAQLGLCAHS NEAVPAAPGE GLHVSYAIGG LLSILLILLV
     IAALMLYRHR KSKFTDPGMG NLTYSNPSYR TSTQEVKLEA APKPAVYNQL CYKKEGGPDH
     SYTKEKIKIV EGIRLLAGDD AEWGDLKQLR SSRGGLLRDH VCMKTDTVSI QASSGSLDDT
     ETEQLLQEEQ SECSSVHTAA TPERRGSLPD TGWKHERKLS SESQV
//