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UniProtKB/Swiss-Prot entry Q07954


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LRP1_HUMAN
Primary accession number Q07954
Secondary accession numbers Q2PP12 Q8IVG8
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 97)
Name and origin of the protein
Protein name Prolow-density lipoprotein receptor-related protein 1 [Precursor]
Synonyms LRP
Alpha-2-macroglobulin receptor
A2MR
Apolipoprotein E receptor
APOER
CD91 antigen
Contains Low-density lipoprotein receptor-related protein 1 85 kDa subunit
     (LRP-85)
Low-density lipoprotein receptor-related protein 1 515 kDa subunit
     (LRP-515)
Low-density lipoprotein receptor-related protein 1 intracellular domain
     (LRPICD)
Gene name
Name: LRP1
Synonyms: A2MR, APR
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3266596 [NCBI, ExPASy, EBI, Israel, Japan]
Herz J., Hamann U., Rogne S., Myklebost O., Gausepohl H., Stanley K.K.;
"Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor.";
EMBO J. 7:4119-4127(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/geno.1994.1584; PubMed=7534747 [NCBI, ExPASy, EBI, Israel, Japan]
Van Leuven F., Stas L., Hilliker C., Lorent K., Umans L., Serneels L., Overbergh L., Torrekens S., Moechars D., De Strooper B., Van den Berghe H.;
"Structure of the gene (LRP1) coding for the human alpha 2-macroglobulin receptor lipoprotein receptor-related protein.";
Genomics 24:78-89(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/geno.1998.5408; PubMed=9782078 [NCBI, ExPASy, EBI, Israel, Japan]
Van Leuven F., Stas L., Thiry E., Nelissen B., Miyake Y.;
"Strategy to sequence the 89 exons of the human LRP1 gene coding for the lipoprotein receptor related protein: identification of one expressed mutation among 48 polymorphisms.";
Genomics 52:138-144(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
TISSUE=Blood;
Glaeser C.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
PubMed=2597675 [NCBI, ExPASy, EBI, Israel, Japan]
Kutt H., Herz J., Stanley K.K.;
"Structure of the low-density lipoprotein receptor-related protein (LRP) promoter.";
Biochim. Biophys. Acta 1009:229-236(1989).
[7]
PROTEIN SEQUENCE OF 150-166; 234-252; 685-695; 902-916; 1096-1109; 1743-1756; 2863-2874; 2949-2960; 3023-3039 AND 3277-3291.
TISSUE=Placenta;
PubMed=1698775 [NCBI, ExPASy, EBI, Israel, Japan]
Strickland D.K., Ashcom J.D., Williams S., Burgess W.H., Migliorini M., Argraves W.S.;
"Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor.";
J. Biol. Chem. 265:17401-17404(1990).
[8]
PROTEOLYTIC PROCESSING.
PubMed=2112085 [NCBI, ExPASy, EBI, Israel, Japan]
Herz J., Kowal R.C., Goldstein J.L., Brown M.S.;
"Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment.";
EMBO J. 9:1769-1776(1990).
[9]
FUNCTION.
DOI=10.1016/0014-5793(90)80530-V; PubMed=1702392 [NCBI, ExPASy, EBI, Israel, Japan]
Kristensen T., Moestrup S.K., Gliemann J., Bendtsen L., Sand O., Sottrup-Jensen L.;
"Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor.";
FEBS Lett. 276:151-155(1990).
[10]
INTERACTION WITH GULP1, AND MUTAGENESIS OF ASN-4470 AND ASN-4504.
DOI=10.1074/jbc.M109336200; PubMed=11729193 [NCBI, ExPASy, EBI, Israel, Japan]
Su H.P., Nakada-Tsukui K., Tosello-Trampont A.-C., Li Y., Bu G., Henson P.M., Ravichandran K.S.;
"Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP).";
J. Biol. Chem. 277:11772-11779(2002).
[11]
PHOSPHORYLATION AT TYR-4507, MUTAGENESIS OF 4470-ASN--TYR-4473 AND 4504-ASN--TYR-4507, AND INTERACTION WITH PDGF.
DOI=10.1074/jbc.M200427200; PubMed=11854294 [NCBI, ExPASy, EBI, Israel, Japan]
Loukinova E., Ranganathan S., Kuznetsov S., Gorlatova N., Migliorini M.M., Loukinov D., Ulery P.G., Mikhailenko I., Lawrence D.A., Strickland D.K.;
"Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of the low density lipoprotein receptor-related protein (LRP). Evidence for integrated co-receptor function betwenn LRP and the PDGF.";
J. Biol. Chem. 277:15499-15506(2002).
[12]
FUNCTION, AND PROTEOLYTIC PROCESSING.
DOI=10.1074/jbc.M201979200; PubMed=11907044 [NCBI, ExPASy, EBI, Israel, Japan]
May P., Reddy Y.K., Herz J.;
"Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain.";
J. Biol. Chem. 277:18736-18743(2002).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M306403200; PubMed=12888553 [NCBI, ExPASy, EBI, Israel, Japan]
Kinoshita A., Shah T., Tangredi M.M., Strickland D.K., Hyman B.T.;
"The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65.";
J. Biol. Chem. 278:41182-41188(2003).
[14]
FUNCTION.
PubMed=12713657 [NCBI, ExPASy, EBI, Israel, Japan]
May P., Herz J.;
"LDL receptor-related proteins in neurodevelopment.";
Traffic 4:291-301(2003).
[15]
PHOSPHORYLATION AT THR-4460; SER-4517; SER-4520 AND SER-4523, MUTAGENESIS OF THR-4460; THR-4472; SER-4517; SER-4520 AND SER-4523, AND INTERACTION WITH SHC1; GULP1 AND DAB1.
DOI=10.1074/jbc.M407592200; PubMed=15272003 [NCBI, ExPASy, EBI, Israel, Japan]
Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F., Peltan I.D., Mikhailenko I., Hyman B.T., Strickland D.K.;
"Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase Calpha regulates endocytosis and association with adaptor molecules.";
J. Biol. Chem. 279:40536-40544(2004).
[16]
INTERACTION WITH SNX17.
DOI=10.1016/j.jmb.2005.02.004; PubMed=15769472 [NCBI, ExPASy, EBI, Israel, Japan]
Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V., Schreckenberger S., Hahn H., Bohnensack R.;
"Functions of sorting nexin 17 domains and recognition motif for P-selectin trafficking.";
J. Mol. Biol. 347:813-825(2005).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-2127 AND ASN-3048, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[18]
IDENTIFICATION IN A COMPLEX WITH CUBN AND PID1, AND INTERACTION WITH CUBN AND PID1.
DOI=10.1074/mcp.M600289-MCP200; PubMed=17124247 [NCBI, ExPASy, EBI, Israel, Japan]
Caratu G., Allegra D., Bimonte M., Schiattarella G.G., D'Ambrosio C., Scaloni A., Napolitano M., Russo T., Zambrano N.;
"Identification of the ligands of protein interaction domains through a functional approach.";
Mol. Cell. Proteomics 6:333-345(2007).
[19]
STRUCTURE BY NMR OF 1059-1100 IN COMPLEX WITH CALCIUM IONS, AND DISULFIDE BONDS.
DOI=10.1074/jbc.274.20.14130; PubMed=10318830 [NCBI, ExPASy, EBI, Israel, Japan]
Huang W., Dolmer K., Gettins P.G.W.;
"NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.";
J. Biol. Chem. 274:14130-14136(1999).
[20]
STRUCTURE BY NMR OF 851-893 IN COMPLEX WITH CALCIUM IONS, AND DISULFIDE BONDS.
DOI=10.1074/jbc.275.5.3264; PubMed=10652313 [NCBI, ExPASy, EBI, Israel, Japan]
Dolmer K., Huang W., Gettins P.G.W.;
"NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin.";
J. Biol. Chem. 275:3264-3269(2000).
[21]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1012-1054 IN COMPLEX WITH CALCIUM IONS, AND DISULFIDE BONDS.
DOI=10.1021/bi015688m; PubMed=11735395 [NCBI, ExPASy, EBI, Israel, Japan]
Simonovic M., Dolmer K., Huang W., Strickland D.K., Volz K., Gettins P.G.;
"Calcium coordination and pH dependence of the calcium affinity of ligand-binding repeat CR7 from the LRP. Comparison with related domains from the LRP and the LDL receptor.";
Biochemistry 40:15127-15134(2001).
[22]
STRUCTURE BY NMR OF 932-1013 IN COMPLEX WITH LRPAP1 AND CALCIUM IONS, AND DISULFIDE BONDS.
DOI=10.1016/j.jmb.2006.07.013; PubMed=16938309 [NCBI, ExPASy, EBI, Israel, Japan]
Jensen G.A., Andersen O.M.J.J., Bonvin A.M., Bjerrum-Bohr I., Etzerodt M., Thoegersen H.C., O'Shea C., Poulsen F.M., Kragelund B.B.;
"Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif.";
J. Mol. Biol. 362:700-716(2006).
[23]
VARIANTS [LARGE SCALE ANALYSIS] LYS-869 AND HIS-3760.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
  • FUNCTION: Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission.
  • SUBUNIT: Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a non-covalently attached 515-kDa amino-terminal subunit. Intracellular domain interacts with MAFB (By similarity). Found in a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with SNX17, PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with SHC1, GULP1 and DAB1. Interacts with LRPAP1.
  • SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related protein 1 85 kDa subunit: Cell membrane; Single-pass type I membrane protein. Membrane, coated pit.
  • SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related protein 1 515 kDa subunit: Cell membrane; Peripheral membrane protein; Extracellular side. Membrane, coated pit.
  • SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related protein 1 intracellular domain: Cytoplasm. Nucleus. Note=After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus.
  • TISSUE SPECIFICITY: Most abundant in liver, brain and lung.
  • PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515) that remains non-covalently associated. Gamma-secretase-dependent cleavage of LRP-85 releases the intracellular domain from the membrane.
  • PTM: The N-terminus is blocked.
  • PTM: Phosphorylated on serine and threonine residues.
  • PTM: Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1.
  • SIMILARITY: Belongs to the LDLR family.
  • SIMILARITY: Contains 22 EGF-like domains.
  • SIMILARITY: Contains 31 LDL-receptor class A domains.
  • SIMILARITY: Contains 34 LDL-receptor class B repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X13916; CAA32112.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF058427; AAC64265.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y18524; CAD57169.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ314873; ABC40732.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15424; CAA33464.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S02392; S02392.
RefSeq NP_002323.2; -.
UniGene Hs.162757
3D structure databases
PDB
1CR8; NMR; -; A=1059-1100.[ExPASy / RCSB / EBI]
1D2L; NMR; -; A=851-893.[ExPASy / RCSB / EBI]
1J8E; X-ray; 1.85 A; A=1012-1054.[ExPASy / RCSB / EBI]
2FYJ; NMR; -; A=932-1013.[ExPASy / RCSB / EBI]
2FYL; NMR; -; B=932-1013.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CR8; -.
1D2L; -.
1J8E; -.
2FYJ; -.
2FYL; -.
ModBase Q07954.
PTM databases
PhosphoSite Q07954; -.
Organism-specific databases
H-InvDB HIX0026381; -.
HGNC HGNC:6692; LRP1.
GenAtlas LRP1.
MIM 107770; gene. [NCBI / EBI]
PharmGKB PA142671549; -.
GeneCards Q07954.
Gene expression databases
ArrayExpress Q07954; -.
CleanEx HS_LRP1; -.
GermOnline ENSG00000123384; Homo sapiens.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005624; Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0005509; Molecular function: calcium ion binding (traceable author statement from ProtInc).
GO:0005319; Molecular function: lipid transporter activity (traceable author statement from ProtInc).
GO:0008034; Molecular function: lipoprotein binding (traceable author statement from ProtInc).
GO:0004872; Molecular function: receptor activity (traceable author statement from ProtInc).
GO:0008283; Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0006629; Biological process: lipid metabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR011042; 6-blade_b-propeller_TolB-like.
IPR006210; EGF.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR013091; EGF_Ca_bd_2.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR002172; LDL_rcpt_classA_cys-rich.
IPR000033; LDLR.
Graphical view of domain structure.
Gene3D G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 8.
G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 29.
Pfam PF00008; EGF; 11.
PF07645; EGF_CA; 3.
PF00057; Ldl_recept_a; 30.
PF00058; Ldl_recept_b; 33.
Pfam graphical view of domain structure.
PRINTS PR00261; LDLRECEPTOR.
SMART SM00181; EGF; 18.
SM00179; EGF_CA; 3.
SM00192; LDLa; 31.
SM00135; LY; 35.
SMART graphical view of domain structure.
PROSITE PS00010; ASX_HYDROXYL; 3.
PS00022; EGF_1; 5.
PS01186; EGF_2; 8.
PS50026; EGF_3; 6.
PS01187; EGF_CA; 2.
PS01209; LDLRA_1; 27.
PS50068; LDLRA_2; 31.
PS51120; LDLRB; 34.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q07954.
Genome annotation databases
Ensembl ENSG00000123384; Homo sapiens. [Contig view]
GeneID 4035; -.
KEGG hsa:4035; -.
Phylogenomic databases
HOGENOM Q07954; -.
HOVERGEN Q07954; -.
Other
DrugBank DB00009; Alteplase.
DB00029; Anistreplase.
DB00025; Antihemophilic Factor.
DB00102; Becaplermin.
DB00100; Coagulation Factor IX.
DB00031; Tenecteplase.
LinkHub Q07954; -.
SOURCE LRP1; Homo sapiens.
ProtoNet Q07954.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Cell membrane; Coated pit; Cytoplasm; Developmental protein; Direct protein sequencing; EGF-like domain; Endocytosis; Glycoprotein; Membrane; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor; Repeat; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom     To Length Description FTId
SIGNAL   1      19  19     Potential. 
CHAIN   20    4544  4525     Prolow-density lipoprotein receptor-related protein 1. PRO_0000017317
CHAIN   20   ?3943        Low-density lipoprotein receptor-related protein 1 515 kDa subunit. PRO_0000302750
CHAIN   ?3944    4544        Low-density lipoprotein receptor-related protein 1 85 kDa subunit. PRO_0000302751
CHAIN   ?4441    4544        Low-density lipoprotein receptor-related protein 1 intracellular domain. PRO_0000302752
TOPO_DOM   20    4419  4400     Extracellular (Potential). 
TRANSMEM   4420    4444  25     Potential. 
TOPO_DOM   4445    4544  100     Cytoplasmic (Potential). 
DOMAIN   25      66  42     LDL-receptor class A 1. 
DOMAIN   70     110  41     LDL-receptor class A 2. 
DOMAIN   111     149  39     EGF-like 1. 
DOMAIN   150     189  40     EGF-like 2; calcium-binding (Potential). 
REPEAT   292     334  43     LDL-receptor class B 1. 
REPEAT   335     378  44     LDL-receptor class B 2. 
REPEAT   379     422  44     LDL-receptor class B 3. 
DOMAIN   474     520  47     EGF-like 3. 
REPEAT   571     613  43     LDL-receptor class B 4. 
REPEAT   614     659  46     LDL-receptor class B 5. 
REPEAT   660     710  51     LDL-receptor class B 6. 
REPEAT   711     754  44     LDL-receptor class B 7. 
DOMAIN   803     843  41     EGF-like 4. 
DOMAIN   852     892  41     LDL-receptor class A 3. 
DOMAIN   893     933  41     LDL-receptor class A 4. 
DOMAIN   934     973  40     LDL-receptor class A 5. 
DOMAIN   974    1013  40     LDL-receptor class A 6. 
DOMAIN   1013    1053  41     LDL-receptor class A 7. 
DOMAIN   1060    1099  40     LDL-receptor class A 8. 
DOMAIN   1102    1142  41     LDL-receptor class A 9. 
DOMAIN   1143    1182  40     LDL-receptor class A 10. 
DOMAIN   1183    1222  40     EGF-like 5. 
DOMAIN   1223    1262  40     EGF-like 6. 
REPEAT   1309    1355  47     LDL-receptor class B 8. 
REPEAT   1356    1398  43     LDL-receptor class B 9. 
REPEAT   1399    1445  47     LDL-receptor class B 10. 
REPEAT   1446    1490  45     LDL-receptor class B 11. 
REPEAT   1491    1531  41     LDL-receptor class B 12. 
DOMAIN   1536    1579  44     EGF-like 7. 
REPEAT   1627    1669  43     LDL-receptor class B 13. 
REPEAT   1670    1713  44     LDL-receptor class B 14. 
REPEAT   1714    1753  40     LDL-receptor class B 15. 
REPEAT   1754    1798  45     LDL-receptor class B 16. 
DOMAIN   1846    1887  42     EGF-like 8. 
REPEAT   1934    1976  43     LDL-receptor class B 17. 
REPEAT   1977    2019  43     LDL-receptor class B 18. 
REPEAT   2020    2063  44     LDL-receptor class B 19. 
REPEAT   2064    2107  44     LDL-receptor class B 20. 
DOMAIN   2155    2195  41     EGF-like 9. 
REPEAT   2253    2294  42     LDL-receptor class B 21. 
REPEAT   2295    2343  49     LDL-receptor class B 22. 
REPEAT   2344    2388  45     LDL-receptor class B 23. 
REPEAT   2389    2431  43     LDL-receptor class B 24. 
REPEAT   2432    2473  42     LDL-receptor class B 25. 
DOMAIN   2478    2518  41     EGF-like 10. 
DOMAIN   2522    2563  42     LDL-receptor class A 11. 
DOMAIN   2564    2602  39     LDL-receptor class A 12. 
DOMAIN   2603    2641  39     LDL-receptor class A 13. 
DOMAIN   2642    2690  49     LDL-receptor class A 14. 
DOMAIN   2694    2732  39     LDL-receptor class A 15. 
DOMAIN   2732    2771  40     LDL-receptor class A 16. 
DOMAIN   2772    2814  43     LDL-receptor class A 17. 
DOMAIN   2816    2855  40     LDL-receptor class A 18. 
DOMAIN   2856    2899  44     LDL-receptor class A 19. 
DOMAIN   2902    2940  39     LDL-receptor class A 20. 
DOMAIN   2941    2981  41     EGF-like 11. 
DOMAIN   2982    3022  41     EGF-like 12; calcium-binding (Potential). 
REPEAT   3069    3113  45     LDL-receptor class B 26. 
REPEAT   3114    3156  43     LDL-receptor class B 27. 
REPEAT   3157    3200  44     LDL-receptor class B 28. 
REPEAT   3201    3243  43     LDL-receptor class B 29. 
REPEAT   3244    3284  41     LDL-receptor class B 30. 
DOMAIN   3290    3331  42     EGF-like 13. 
DOMAIN   3332    3371  40     LDL-receptor class A 21.