LRP4_MOUSE
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 03-AUG-2022, entry version 175.
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 GlyGen; Q8VI56; 7 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8VI56; -.
DR PhosphoSitePlus; Q8VI56; -.
DR MaxQB; Q8VI56; -.
DR PaxDb; Q8VI56; -.
DR PeptideAtlas; Q8VI56; -.
DR PRIDE; Q8VI56; -.
DR ProteomicsDB; 252678; -. [Q8VI56-1]
DR ProteomicsDB; 252679; -. [Q8VI56-2]
DR ABCD; Q8VI56; 2 sequenced antibodies.
DR Antibodypedia; 1985; 366 antibodies from 38 providers.
DR DNASU; 228357; -.
DR Ensembl; ENSMUST00000028689; ENSMUSP00000028689; ENSMUSG00000027253. [Q8VI56-1]
DR GeneID; 228357; -.
DR KEGG; mmu:228357; -.
DR UCSC; uc008kvx.2; mouse. [Q8VI56-1]
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; 121310at2759; -.
DR PhylomeDB; Q8VI56; -.
DR TreeFam; TF315253; -.
DR BioGRID-ORCS; 228357; 1 hit in 76 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 224 other tissues.
DR Genevisible; Q8VI56; MM.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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: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:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IMP:UniProtKB.
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; cd00112; LDLa; 7.
DR Gene3D; 2.120.10.30; -; 4.
DR Gene3D; 4.10.400.10; -; 8.
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 Pfam; PF12662; cEGF; 1.
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; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57424; SSF57424; 8.
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.
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
