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Q07954 (LRP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prolow-density lipoprotein receptor-related protein 1

Short name=LRP-1
Alternative name(s):
Alpha-2-macroglobulin receptor
Short name=A2MR
Apolipoprotein E receptor
Short name=APOER
CD_antigen=CD91
Gene names
Name:LRP1
Synonyms:A2MR, APR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4544 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Ref.10 Ref.11 Ref.14 Ref.15 Ref.16

Functions as a receptor for Pseudomonas aeruginosa exotoxin A. Ref.10 Ref.11 Ref.14 Ref.15 Ref.16

Subunit structure

Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a non-covalently attached 515-kDa N-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. Can weakly interact (via NPXY motif) with DAB2 (via PID domain); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif. Interacts with bacterial exotoxins. Ref.12 Ref.13 Ref.17 Ref.18 Ref.20

Subcellular location

Low-density lipoprotein receptor-related protein 1 85 kDa subunit: Cell membrane; Single-pass type I membrane protein. Membranecoated pit.

Low-density lipoprotein receptor-related protein 1 515 kDa subunit: Cell membrane; Peripheral membrane protein; Extracellular side. Membranecoated pit.

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.

Post-translational modification

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.

The N-terminus is blocked.

Phosphorylated on serine and threonine residues. Ref.13 Ref.17

Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1. Ref.13 Ref.17

Sequence similarities

Belongs to the LDLR family.

Contains 22 EGF-like domains.

Contains 31 LDL-receptor class A domains.

Contains 34 LDL-receptor class B repeats.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Coated pit
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionDevelopmental protein
Receptor
   PTMAcetylation
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

aorta morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

apoptotic cell clearance

Inferred from sequence or structural similarity. Source: BHF-UCL

beta-amyloid clearance

Traceable author statement PubMed 19098903. Source: BHF-UCL

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein metabolic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein transport

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of Wnt signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of platelet-derived growth factor receptor-beta signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of smooth muscle cell migration

Inferred from sequence or structural similarity. Source: BHF-UCL

phototransduction, visible light

Traceable author statement. Source: Reactome

positive regulation of cholesterol efflux

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of lipid transport

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of protein transport

Inferred from electronic annotation. Source: Ensembl

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

receptor-mediated endocytosis

Inferred from electronic annotation. Source: Ensembl

regulation of actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cholesterol transport

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of phospholipase A2 activity

Inferred from sequence or structural similarity. Source: BHF-UCL

retinoid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentclathrin-coated vesicle

Inferred from electronic annotation. Source: Ensembl

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle membrane

Traceable author statement. Source: Reactome

endosome

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionapolipoprotein binding

Inferred from direct assay PubMed 2779654. Source: UniProtKB

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

lipoprotein particle receptor binding

Inferred by curator PubMed 18635818. Source: BHF-UCL

lipoprotein transporter activity

Non-traceable author statement Ref.1. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein complex binding

Inferred from direct assay PubMed 8626514. Source: BHF-UCL

receptor activity

Traceable author statement PubMed 10880251. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APBB1O002133EBI-1046087,EBI-81694
FCN2Q154852EBI-1046087,EBI-7468784
Jag1Q637224EBI-1046087,EBI-4567800From a different organism.
MBL2P112265EBI-1046087,EBI-5325353
Thbs2Q033502EBI-1046087,EBI-4567830From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 45444525Prolow-density lipoprotein receptor-related protein 1
PRO_0000017317
Chain20 – ?39433924Low-density lipoprotein receptor-related protein 1 515 kDa subunit
PRO_0000302750
Chain?3944 – 4544601Low-density lipoprotein receptor-related protein 1 85 kDa subunit
PRO_0000302751
Chain?4441 – 4544104Low-density lipoprotein receptor-related protein 1 intracellular domain
PRO_0000302752

Regions

Topological domain20 – 44194400Extracellular Potential
Transmembrane4420 – 444425Helical; Potential
Topological domain4445 – 4544100Cytoplasmic Potential
Domain25 – 6642LDL-receptor class A 1
Domain70 – 11041LDL-receptor class A 2
Domain111 – 14939EGF-like 1
Domain150 – 18940EGF-like 2; calcium-binding Potential
Repeat292 – 33443LDL-receptor class B 1
Repeat335 – 37844LDL-receptor class B 2
Repeat379 – 42244LDL-receptor class B 3
Domain474 – 52047EGF-like 3
Repeat571 – 61343LDL-receptor class B 4
Repeat614 – 65946LDL-receptor class B 5
Repeat660 – 71051LDL-receptor class B 6
Repeat711 – 75444LDL-receptor class B 7
Domain803 – 84341EGF-like 4
Domain852 – 89241LDL-receptor class A 3
Domain893 – 93341LDL-receptor class A 4
Domain934 – 97340LDL-receptor class A 5
Domain974 – 101340LDL-receptor class A 6
Domain1013 – 105341LDL-receptor class A 7
Domain1060 – 109940LDL-receptor class A 8
Domain1102 – 114241LDL-receptor class A 9
Domain1143 – 118240LDL-receptor class A 10
Domain1183 – 122240EGF-like 5
Domain1223 – 126240EGF-like 6
Repeat1309 – 135547LDL-receptor class B 8
Repeat1356 – 139843LDL-receptor class B 9
Repeat1399 – 144547LDL-receptor class B 10
Repeat1446 – 149045LDL-receptor class B 11
Repeat1491 – 153141LDL-receptor class B 12
Domain1536 – 157944EGF-like 7
Repeat1627 – 166943LDL-receptor class B 13
Repeat1670 – 171344LDL-receptor class B 14
Repeat1714 – 175340LDL-receptor class B 15
Repeat1754 – 179845LDL-receptor class B 16
Domain1846 – 188742EGF-like 8
Repeat1934 – 197643LDL-receptor class B 17
Repeat1977 – 201943LDL-receptor class B 18
Repeat2020 – 206344LDL-receptor class B 19
Repeat2064 – 210744LDL-receptor class B 20
Domain2155 – 219541EGF-like 9
Repeat2253 – 229442LDL-receptor class B 21
Repeat2295 – 234349LDL-receptor class B 22
Repeat2344 – 238845LDL-receptor class B 23
Repeat2389 – 243143LDL-receptor class B 24
Repeat2432 – 247342LDL-receptor class B 25
Domain2478 – 251841EGF-like 10
Domain2522 – 256342LDL-receptor class A 11
Domain2564 – 260239LDL-receptor class A 12
Domain2603 – 264139LDL-receptor class A 13
Domain2642 – 269049LDL-receptor class A 14
Domain2694 – 273239LDL-receptor class A 15
Domain2732 – 277140LDL-receptor class A 16
Domain2772 – 281443LDL-receptor class A 17
Domain2816 – 285540LDL-receptor class A 18
Domain2856 – 289944LDL-receptor class A 19
Domain2902 – 294039LDL-receptor class A 20
Domain2941 – 298141EGF-like 11
Domain2982 – 302241EGF-like 12; calcium-binding Potential
Repeat3069 – 311345LDL-receptor class B 26
Repeat3114 – 315643LDL-receptor class B 27
Repeat3157 – 320044LDL-receptor class B 28
Repeat3201 – 324343LDL-receptor class B 29
Repeat3244 – 328441LDL-receptor class B 30
Domain3290 – 333142EGF-like 13
Domain3332 – 337140LDL-receptor class A 21
Domain3372 – 341039LDL-receptor class A 22
Domain3411 – 345040LDL-receptor class A 23
Domain3451 – 349141LDL-receptor class A 24
Domain3492 – 353342LDL-receptor class A 25
Domain3534 – 357239LDL-receptor class A 26
Domain3573 – 361139LDL-receptor class A 27
Domain3611 – 364939LDL-receptor class A 28
Domain3652 – 369241LDL-receptor class A 29
Domain3693 – 373341LDL-receptor class A 30
Domain3739 – 377840LDL-receptor class A 31
Domain3781 – 382343EGF-like 14
Domain3824 – 386138EGF-like 15
Repeat3912 – 395443LDL-receptor class B 31
Repeat3970 – 401243LDL-receptor class B 32
Repeat4013 – 405644LDL-receptor class B 33
Repeat4057 – 410145LDL-receptor class B 34
Domain4147 – 418337EGF-like 16
Domain4196 – 423237EGF-like 17
Domain4232 – 426837EGF-like 18
Domain4268 – 430437EGF-like 19
Domain4304 – 434037EGF-like 20
Domain4340 – 437536EGF-like 21
Domain4373 – 440937EGF-like 22
Region4445 – 4544100Interaction with MAFB By similarity
Motif3940 – 39434Recognition site for proteolytical processing Potential
Motif4502 – 45076NPXY motif

Sites

Metal binding8711Calcium 1; via carbonyl oxygen
Metal binding8741Calcium 1
Metal binding8761Calcium 1; via carbonyl oxygen
Metal binding8781Calcium 1
Metal binding8841Calcium 1
Metal binding8851Calcium 1
Metal binding10321Calcium 2; via carbonyl oxygen
Metal binding10351Calcium 2
Metal binding10371Calcium 2; via carbonyl oxygen
Metal binding10391Calcium 2
Metal binding10451Calcium 2
Metal binding10461Calcium 2
Metal binding10801Calcium 3; via carbonyl oxygen
Metal binding10831Calcium 3
Metal binding10851Calcium 3; via carbonyl oxygen
Metal binding10871Calcium 3
Metal binding10931Calcium 3
Metal binding10941Calcium 3

Amino acid modifications

Modified residue20091N6-acetyllysine By similarity
Modified residue44601Phosphothreonine Probable
Modified residue45071Phosphotyrosine Ref.13
Modified residue45171Phosphoserine Probable
Modified residue45201Phosphoserine Probable
Modified residue45231Phosphoserine Probable
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Glycosylation4461N-linked (GlcNAc...) Ref.19 Ref.21
Glycosylation7291N-linked (GlcNAc...) (complex) Ref.19 Ref.21 Ref.22
Glycosylation9281N-linked (GlcNAc...) Potential
Glycosylation10501N-linked (GlcNAc...) Potential
Glycosylation11541N-linked (GlcNAc...) Potential
Glycosylation11551N-linked (GlcNAc...) Potential
Glycosylation11951N-linked (GlcNAc...) Potential
Glycosylation12181N-linked (GlcNAc...) Potential
Glycosylation15111N-linked (GlcNAc...) (complex) Ref.21 Ref.22
Glycosylation15581N-linked (GlcNAc...) Potential
Glycosylation15751N-linked (GlcNAc...) Ref.21
Glycosylation16161N-linked (GlcNAc...) Ref.21
Glycosylation16451N-linked (GlcNAc...) Ref.21
Glycosylation17231N-linked (GlcNAc...) Potential
Glycosylation17331N-linked (GlcNAc...) Potential
Glycosylation17631N-linked (GlcNAc...) Ref.21
Glycosylation18251N-linked (GlcNAc...) Potential
Glycosylation19331N-linked (GlcNAc...) Potential
Glycosylation19951N-linked (GlcNAc...) Potential
Glycosylation20481N-linked (GlcNAc...) Potential
Glycosylation21171N-linked (GlcNAc...) Potential
Glycosylation21271N-linked (GlcNAc...) Ref.19 Ref.21
Glycosylation24721N-linked (GlcNAc...) Potential
Glycosylation25021N-linked (GlcNAc...) Potential
Glycosylation25211N-linked (GlcNAc...) Potential
Glycosylation25391N-linked (GlcNAc...) Potential
Glycosylation26011N-linked (GlcNAc...) Potential
Glycosylation26201N-linked (GlcNAc...) Potential
Glycosylation26381N-linked (GlcNAc...) Potential
Glycosylation28151N-linked (GlcNAc...) Ref.21
Glycosylation29051N-linked (GlcNAc...) Potential
Glycosylation30481N-linked (GlcNAc...) Ref.19 Ref.21
Glycosylation30891N-linked (GlcNAc...) Ref.21
Glycosylation32641N-linked (GlcNAc...) Potential
Glycosylation33331N-linked (GlcNAc...) Potential
Glycosylation34881N-linked (GlcNAc...) Ref.21
Glycosylation36621N-linked (GlcNAc...) Potential
Glycosylation37881N-linked (GlcNAc...) Ref.21
Glycosylation38391N-linked (GlcNAc...) Potential
Glycosylation39531N-linked (GlcNAc...) Ref.21
Glycosylation40751N-linked (GlcNAc...) Ref.21
Glycosylation41251N-linked (GlcNAc...) Ref.21
Glycosylation41791N-linked (GlcNAc...) Potential
Glycosylation42781N-linked (GlcNAc...) Potential
Glycosylation42791N-linked (GlcNAc...) Potential
Glycosylation43641N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 40 By similarity
Disulfide bond34 ↔ 53 By similarity
Disulfide bond47 ↔ 64 By similarity
Disulfide bond72 ↔ 85 By similarity
Disulfide bond79 ↔ 98 By similarity
Disulfide bond92 ↔ 108 By similarity
Disulfide bond115 ↔ 124 By similarity
Disulfide bond120 ↔ 133 By similarity
Disulfide bond135 ↔ 148 By similarity
Disulfide bond154 ↔ 164 By similarity
Disulfide bond160 ↔ 173 By similarity
Disulfide bond175 ↔ 188 By similarity
Disulfide bond478 ↔ 493 By similarity
Disulfide bond489 ↔ 504 By similarity
Disulfide bond506 ↔ 519 By similarity
Disulfide bond807 ↔ 818 By similarity
Disulfide bond814 ↔ 827 By similarity
Disulfide bond829 ↔ 842 By similarity
Disulfide bond854 ↔ 866 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond861 ↔ 879 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond873 ↔ 890 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond895 ↔ 907 By similarity
Disulfide bond902 ↔ 920 By similarity
Disulfide bond914 ↔ 931 By similarity
Disulfide bond936 ↔ 948 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond943 ↔ 961 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond955 ↔ 971 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond976 ↔ 989 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond984 ↔ 1002 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond996 ↔ 1011 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond1015 ↔ 1027 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond1022 ↔ 1040 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond1034 ↔ 1051 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond1062 ↔ 1075 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond1069 ↔ 1088 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond1082 ↔ 1097 Ref.24 Ref.25 Ref.26 Ref.27
Disulfide bond1104 ↔ 1118 By similarity
Disulfide bond1112 ↔ 1131 By similarity
Disulfide bond1125 ↔ 1140 By similarity
Disulfide bond1145 ↔ 1159 By similarity
Disulfide bond1152 ↔ 1172 By similarity
Disulfide bond1166 ↔ 1182 By similarity
Disulfide bond1185 ↔ 1196 By similarity
Disulfide bond1192 ↔ 1206 By similarity
Disulfide bond1208 ↔ 1221 By similarity
Disulfide bond1227 ↔ 1237 By similarity
Disulfide bond1233 ↔ 1246 By similarity
Disulfide bond1248 ↔ 1261 By similarity
Disulfide bond1540 ↔ 1553 By similarity
Disulfide bond1549 ↔ 1563 By similarity
Disulfide bond1565 ↔ 1578 By similarity
Disulfide bond1850 ↔ 1861 By similarity
Disulfide bond1857 ↔ 1871 By similarity
Disulfide bond1873 ↔ 1886 By similarity
Disulfide bond2159 ↔ 2170 By similarity
Disulfide bond2166 ↔ 2180 By similarity
Disulfide bond2182 ↔ 2194 By similarity
Disulfide bond2482 ↔ 2493 By similarity
Disulfide bond2489 ↔ 2503 By similarity
Disulfide bond2505 ↔ 2517 By similarity
Disulfide bond2524 ↔ 2537 By similarity
Disulfide bond2532 ↔ 2550 By similarity
Disulfide bond2544 ↔ 2561 By similarity
Disulfide bond2566 ↔ 2578 By similarity
Disulfide bond2573 ↔ 2591 By similarity
Disulfide bond2585 ↔ 2600 By similarity
Disulfide bond2605 ↔ 2617 By similarity
Disulfide bond2612 ↔ 2630 By similarity
Disulfide bond2624 ↔ 2639 By similarity
Disulfide bond2644 ↔ 2666 By similarity
Disulfide bond2660 ↔ 2679 By similarity
Disulfide bond2673 ↔ 2688 By similarity
Disulfide bond2696 ↔ 2708 By similarity
Disulfide bond2703 ↔ 2721 By similarity
Disulfide bond2715 ↔ 2730 By similarity
Disulfide bond2734 ↔ 2746 By similarity
Disulfide bond2741 ↔ 2759 By similarity
Disulfide bond2753 ↔ 2769 By similarity
Disulfide bond2774 ↔ 2787 By similarity
Disulfide bond2781 ↔ 2800 By similarity
Disulfide bond2794 ↔ 2812 By similarity
Disulfide bond2818 ↔ 2830 By similarity
Disulfide bond2825 ↔ 2843 By similarity
Disulfide bond2837 ↔ 2853 By similarity
Disulfide bond2858 ↔ 2870 By similarity
Disulfide bond2865 ↔ 2884 By similarity
Disulfide bond2878 ↔ 2897 By similarity
Disulfide bond2904 ↔ 2917 By similarity
Disulfide bond2912 ↔ 2930 By similarity
Disulfide bond2924 ↔ 2939 By similarity
Disulfide bond2944 ↔ 2956 By similarity
Disulfide bond2952 ↔ 2965 By similarity
Disulfide bond2967 ↔ 2980 By similarity
Disulfide bond2986 ↔ 2996 By similarity
Disulfide bond2992 ↔ 3005 By similarity
Disulfide bond3007 ↔ 3021 By similarity
Disulfide bond3294 ↔ 3305 By similarity
Disulfide bond3301 ↔ 3315 By similarity
Disulfide bond3317 ↔ 3330 By similarity
Disulfide bond3334 ↔ 3346 By similarity
Disulfide bond3341 ↔ 3359 By similarity
Disulfide bond3353 ↔ 3369 By similarity
Disulfide bond3374 ↔ 3386 By similarity
Disulfide bond3381 ↔ 3399 By similarity
Disulfide bond3393 ↔ 3408 By similarity
Disulfide bond3413 ↔ 3426 By similarity
Disulfide bond3420 ↔ 3439 By similarity
Disulfide bond3433 ↔ 3448 By similarity
Disulfide bond3453 ↔ 3466 By similarity
Disulfide bond3460 ↔ 3479 By similarity
Disulfide bond3473 ↔ 3489 By similarity
Disulfide bond3494 ↔ 3507 By similarity
Disulfide bond3501 ↔ 3520 By similarity
Disulfide bond3514 ↔ 3531 By similarity
Disulfide bond3536 ↔ 3548 By similarity
Disulfide bond3543 ↔ 3561 By similarity
Disulfide bond3555 ↔ 3570 By similarity
Disulfide bond3575 ↔ 3587 By similarity
Disulfide bond3582 ↔ 3600 By similarity
Disulfide bond3594 ↔ 3609 By similarity
Disulfide bond3613 ↔ 3625 By similarity
Disulfide bond3620 ↔ 3638 By similarity
Disulfide bond3632 ↔ 3647 By similarity
Disulfide bond3654 ↔ 3666 By similarity
Disulfide bond3661 ↔ 3679 By similarity
Disulfide bond3673 ↔ 3690 By similarity
Disulfide bond3695 ↔ 3709 By similarity
Disulfide bond3703 ↔ 3722 By similarity
Disulfide bond3716 ↔ 3731 By similarity
Disulfide bond3741 ↔ 3754 By similarity
Disulfide bond3749 ↔ 3767 By similarity
Disulfide bond3761 ↔ 3776 By similarity
Disulfide bond3785 ↔ 3798 By similarity
Disulfide bond3792 ↔ 3807 By similarity
Disulfide bond3809 ↔ 3822 By similarity
Disulfide bond3828 ↔ 3838 By similarity
Disulfide bond3834 ↔ 3847 By similarity
Disulfide bond3849 ↔ 3860 By similarity
Disulfide bond4151 ↔ 4160 By similarity
Disulfide bond4156 ↔ 4169 By similarity
Disulfide bond4171 ↔ 4182 By similarity
Disulfide bond4200 ↔ 4210 By similarity
Disulfide bond4204 ↔ 4220 By similarity
Disulfide bond4222 ↔ 4231 By similarity
Disulfide bond4236 ↔ 4246 By similarity
Disulfide bond4240 ↔ 4256 By similarity
Disulfide bond4258 ↔ 4267 By similarity
Disulfide bond4272 ↔ 4282 By similarity
Disulfide bond4276 ↔ 4292 By similarity
Disulfide bond4294 ↔ 4303 By similarity
Disulfide bond4308 ↔ 4318 By similarity
Disulfide bond4312 ↔ 4328 By similarity
Disulfide bond4330 ↔ 4339 By similarity
Disulfide bond4344 ↔ 4352 By similarity
Disulfide bond4347 ↔ 4363 By similarity
Disulfide bond4365 ↔ 4374 By similarity
Disulfide bond4377 ↔ 4387 By similarity
Disulfide bond4381 ↔ 4397 By similarity
Disulfide bond4399 ↔ 4408 By similarity

Natural variations

Natural variant1661N → D.
Corresponds to variant rs2306691 [ dbSNP | Ensembl ].
VAR_021885
Natural variant2171A → V.
Corresponds to variant rs1800127 [ dbSNP | Ensembl ].
VAR_014725
Natural variant8691E → K in a colorectal cancer sample; somatic mutation. Ref.28
VAR_035994
Natural variant20591V → L.
Corresponds to variant rs2229278 [ dbSNP | Ensembl ].
VAR_029181
Natural variant20801D → N.
Corresponds to variant rs34577247 [ dbSNP | Ensembl ].
VAR_047525
Natural variant29001Q → P. Ref.1 Ref.3 Ref.4
Corresponds to variant rs7397167 [ dbSNP | Ensembl ].
VAR_047526
Natural variant32581H → Q Found in a patient with severe mental retardation, seizures, stereotypic behavior, high pain threshold and sleep disturbances. Ref.29
VAR_069388
Natural variant37601R → H in a colorectal cancer sample; somatic mutation. Ref.28
VAR_035995
Natural variant45361E → G.
Corresponds to variant rs17357542 [ dbSNP | Ensembl ].
VAR_047527

Experimental info

Mutagenesis44601T → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4517; A-4520 and A-4523. Ref.17
Mutagenesis4470 – 44734NPTY → APTA: No effect on tyrosine phosphorylation. Ref.12 Ref.13
Mutagenesis44701N → A: No effect on interaction with GULP1. Ref.12
Mutagenesis44721T → A: No detectable effect on phosphorylation. Ref.17
Mutagenesis4504 – 45074NPVY → APVA: Loss of tyrosine phosphorylation. Abolishes interaction with SHC1 and GULP1. Ref.12 Ref.13
Mutagenesis45041N → A: Loss of interaction with GULP1. Ref.12
Mutagenesis45171S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4520 and A-4523. Ref.17
Mutagenesis45201S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4523. Ref.17
Mutagenesis45231S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4520. Ref.17
Sequence conflict6851D → G AA sequence Ref.8
Sequence conflict17431G → S AA sequence Ref.8
Sequence conflict2871 – 28722LS → IA AA sequence Ref.8
Sequence conflict30361R → M AA sequence Ref.8

Secondary structure

............................................................................. 4544
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07954 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 5A11CC02FAB127BE

FASTA4,544504,606
        10         20         30         40         50         60 
MLTPPLLLLL PLLSALVAAA IDAPKTCSPK QFACRDQITC ISKGWRCDGE RDCPDGSDEA 

        70         80         90        100        110        120 
PEICPQSKAQ RCQPNEHNCL GTELCVPMSR LCNGVQDCMD GSDEGPHCRE LQGNCSRLGC 

       130        140        150        160        170        180 
QHHCVPTLDG PTCYCNSSFQ LQADGKTCKD FDECSVYGTC SQLCTNTDGS FICGCVEGYL 

       190        200        210        220        230        240 
LQPDNRSCKA KNEPVDRPPV LLIANSQNIL ATYLSGAQVS TITPTSTRQT TAMDFSYANE 

       250        260        270        280        290        300 
TVCWVHVGDS AAQTQLKCAR MPGLKGFVDE HTINISLSLH HVEQMAIDWL TGNFYFVDDI 

       310        320        330        340        350        360 
DDRIFVCNRN GDTCVTLLDL ELYNPKGIAL DPAMGKVFFT DYGQIPKVER CDMDGQNRTK 

       370        380        390        400        410        420 
LVDSKIVFPH GITLDLVSRL VYWADAYLDY IEVVDYEGKG RQTIIQGILI EHLYGLTVFE 

       430        440        450        460        470        480 
NYLYATNSDN ANAQQKTSVI RVNRFNSTEY QVVTRVDKGG ALHIYHQRRQ PRVRSHACEN 

       490        500        510        520        530        540 
DQYGKPGGCS DICLLANSHK ARTCRCRSGF SLGSDGKSCK KPEHELFLVY GKGRPGIIRG 

       550        560        570        580        590        600 
MDMGAKVPDE HMIPIENLMN PRALDFHAET GFIYFADTTS YLIGRQKIDG TERETILKDG 

       610        620        630        640        650        660 
IHNVEGVAVD WMGDNLYWTD DGPKKTISVA RLEKAAQTRK TLIEGKMTHP RAIVVDPLNG 

       670        680        690        700        710        720 
WMYWTDWEED PKDSRRGRLE RAWMDGSHRD IFVTSKTVLW PNGLSLDIPA GRLYWVDAFY 

       730        740        750        760        770        780 
DRIETILLNG TDRKIVYEGP ELNHAFGLCH HGNYLFWTEY RSGSVYRLER GVGGAPPTVT 

       790        800        810        820        830        840 
LLRSERPPIF EIRMYDAQQQ QVGTNKCRVN NGGCSSLCLA TPGSRQCACA EDQVLDADGV 

       850        860        870        880        890        900 
TCLANPSYVP PPQCQPGEFA CANSRCIQER WKCDGDNDCL DNSDEAPALC HQHTCPSDRF 

       910        920        930        940        950        960 
KCENNRCIPN RWLCDGDNDC GNSEDESNAT CSARTCPPNQ FSCASGRCIP ISWTCDLDDD 

       970        980        990       1000       1010       1020 
CGDRSDESAS CAYPTCFPLT QFTCNNGRCI NINWRCDNDN DCGDNSDEAG CSHSCSSTQF 

      1030       1040       1050       1060       1070       1080 
KCNSGRCIPE HWTCDGDNDC GDYSDETHAN CTNQATRPPG GCHTDEFQCR LDGLCIPLRW 

      1090       1100       1110       1120       1130       1140 
RCDGDTDCMD SSDEKSCEGV THVCDPSVKF GCKDSARCIS KAWVCDGDND CEDNSDEENC 

      1150       1160       1170       1180       1190       1200 
ESLACRPPSH PCANNTSVCL PPDKLCDGND DCGDGSDEGE LCDQCSLNNG GCSHNCSVAP 

      1210       1220       1230       1240       1250       1260 
GEGIVCSCPL GMELGPDNHT CQIQSYCAKH LKCSQKCDQN KFSVKCSCYE GWVLEPDGES 

      1270       1280       1290       1300       1310       1320 
CRSLDPFKPF IIFSNRHEIR RIDLHKGDYS VLVPGLRNTI ALDFHLSQSA LYWTDVVEDK 

      1330       1340       1350       1360       1370       1380 
IYRGKLLDNG ALTSFEVVIQ YGLATPEGLA VDWIAGNIYW VESNLDQIEV AKLDGTLRTT 

      1390       1400       1410       1420       1430       1440 
LLAGDIEHPR AIALDPRDGI LFWTDWDASL PRIEAASMSG AGRRTVHRET GSGGWPNGLT 

      1450       1460       1470       1480       1490       1500 
VDYLEKRILW IDARSDAIYS ARYDGSGHME VLRGHEFLSH PFAVTLYGGE VYWTDWRTNT 

      1510       1520       1530       1540       1550       1560 
LAKANKWTGH NVTVVQRTNT QPFDLQVYHP SRQPMAPNPC EANGGQGPCS HLCLINYNRT 

      1570       1580       1590       1600       1610       1620 
VSCACPHLMK LHKDNTTCYE FKKFLLYARQ MEIRGVDLDA PYYNYIISFT VPDIDNVTVL 

      1630       1640       1650       1660       1670       1680 
DYDAREQRVY WSDVRTQAIK RAFINGTGVE TVVSADLPNA HGLAVDWVSR NLFWTSYDTN 

      1690       1700       1710       1720       1730       1740 
KKQINVARLD GSFKNAVVQG LEQPHGLVVH PLRGKLYWTD GDNISMANMD GSNRTLLFSG 

      1750       1760       1770       1780       1790       1800 
QKGPVGLAID FPESKLYWIS SGNHTINRCN LDGSGLEVID AMRSQLGKAT ALAIMGDKLW 

      1810       1820       1830       1840       1850       1860 
WADQVSEKMG TCSKADGSGS VVLRNSTTLV MHMKVYDESI QLDHKGTNPC SVNNGDCSQL 

      1870       1880       1890       1900       1910       1920 
CLPTSETTRS CMCTAGYSLR SGQQACEGVG SFLLYSVHEG IRGIPLDPND KSDALVPVSG 

      1930       1940       1950       1960       1970       1980 
TSLAVGIDFH AENDTIYWVD MGLSTISRAK RDQTWREDVV TNGIGRVEGI AVDWIAGNIY 

      1990       2000       2010       2020       2030       2040 
WTDQGFDVIE VARLNGSFRY VVISQGLDKP RAITVHPEKG YLFWTEWGQY PRIERSRLDG 

      2050       2060       2070       2080       2090       2100 
TERVVLVNVS ISWPNGISVD YQDGKLYWCD ARTDKIERID LETGENREVV LSSNNMDMFS 

      2110       2120       2130       2140       2150       2160 
VSVFEDFIYW SDRTHANGSI KRGSKDNATD SVPLRTGIGV QLKDIKVFNR DRQKGTNVCA 

      2170       2180       2190       2200       2210       2220 
VANGGCQQLC LYRGRGQRAC ACAHGMLAED GASCREYAGY LLYSERTILK SIHLSDERNL 

      2230       2240       2250       2260       2270       2280 
NAPVQPFEDP EHMKNVIALA FDYRAGTSPG TPNRIFFSDI HFGNIQQIND DGSRRITIVE 

      2290       2300       2310       2320       2330       2340 
NVGSVEGLAY HRGWDTLYWT SYTTSTITRH TVDQTRPGAF ERETVITMSG DDHPRAFVLD 

      2350       2360       2370       2380       2390       2400 
ECQNLMFWTN WNEQHPSIMR AALSGANVLT LIEKDIRTPN GLAIDHRAEK LYFSDATLDK 

      2410       2420       2430       2440       2450       2460 
IERCEYDGSH RYVILKSEPV HPFGLAVYGE HIFWTDWVRR AVQRANKHVG SNMKLLRVDI 

      2470       2480       2490       2500       2510       2520 
PQQPMGIIAV ANDTNSCELS PCRINNGGCQ DLCLLTHQGH VNCSCRGGRI LQDDLTCRAV 

      2530       2540       2550       2560       2570       2580 
NSSCRAQDEF ECANGECINF SLTCDGVPHC KDKSDEKPSY CNSRRCKKTF RQCSNGRCVS 

      2590       2600       2610       2620       2630       2640 
NMLWCNGADD CGDGSDEIPC NKTACGVGEF RCRDGTCIGN SSRCNQFVDC EDASDEMNCS 

      2650       2660       2670       2680       2690       2700 
ATDCSSYFRL GVKGVLFQPC ERTSLCYAPS WVCDGANDCG DYSDERDCPG VKRPRCPLNY 

      2710       2720       2730       2740       2750       2760 
FACPSGRCIP MSWTCDKEDD CEHGEDETHC NKFCSEAQFE CQNHRCISKQ WLCDGSDDCG 

      2770       2780       2790       2800       2810       2820 
DGSDEAAHCE GKTCGPSSFS CPGTHVCVPE RWLCDGDKDC ADGADESIAA GCLYNSTCDD 

      2830       2840       2850       2860       2870       2880 
REFMCQNRQC IPKHFVCDHD RDCADGSDES PECEYPTCGP SEFRCANGRC LSSRQWECDG 

      2890       2900       2910       2920       2930       2940 
ENDCHDQSDE APKNPHCTSQ EHKCNASSQF LCSSGRCVAE ALLCNGQDDC GDSSDERGCH 

      2950       2960       2970       2980       2990       3000 
INECLSRKLS GCSQDCEDLK IGFKCRCRPG FRLKDDGRTC ADVDECSTTF PCSQRCINTH 

      3010       3020       3030       3040       3050       3060 
GSYKCLCVEG YAPRGGDPHS CKAVTDEEPF LIFANRYYLR KLNLDGSNYT LLKQGLNNAV 

      3070       3080       3090       3100       3110       3120 
ALDFDYREQM IYWTDVTTQG SMIRRMHLNG SNVQVLHRTG LSNPDGLAVD WVGGNLYWCD 

      3130       3140       3150       3160       3170       3180 
KGRDTIEVSK LNGAYRTVLV SSGLREPRAL VVDVQNGYLY WTDWGDHSLI GRIGMDGSSR 

      3190       3200       3210       3220       3230       3240 
SVIVDTKITW PNGLTLDYVT ERIYWADARE DYIEFASLDG SNRHVVLSQD IPHIFALTLF 

      3250       3260       3270       3280       3290       3300 
EDYVYWTDWE TKSINRAHKT TGTNKTLLIS TLHRPMDLHV FHALRQPDVP NHPCKVNNGG 

      3310       3320       3330       3340       3350       3360 
CSNLCLLSPG GGHKCACPTN FYLGSDGRTC VSNCTASQFV CKNDKCIPFW WKCDTEDDCG 

      3370       3380       3390       3400       3410       3420 
DHSDEPPDCP EFKCRPGQFQ CSTGICTNPA FICDGDNDCQ DNSDEANCDI HVCLPSQFKC 

      3430       3440       3450       3460       3470       3480 
TNTNRCIPGI FRCNGQDNCG DGEDERDCPE VTCAPNQFQC SITKRCIPRV WVCDRDNDCV 

      3490       3500       3510       3520       3530       3540 
DGSDEPANCT QMTCGVDEFR CKDSGRCIPA RWKCDGEDDC GDGSDEPKEE CDERTCEPYQ 

      3550       3560       3570       3580       3590       3600 
FRCKNNRCVP GRWQCDYDND CGDNSDEESC TPRPCSESEF SCANGRCIAG RWKCDGDHDC 

      3610       3620       3630       3640       3650       3660 
ADGSDEKDCT PRCDMDQFQC KSGHCIPLRW RCDADADCMD GSDEEACGTG VRTCPLDEFQ 

      3670       3680       3690       3700       3710       3720 
CNNTLCKPLA WKCDGEDDCG DNSDENPEEC ARFVCPPNRP FRCKNDRVCL WIGRQCDGTD 

      3730       3740       3750       3760       3770       3780 
NCGDGTDEED CEPPTAHTTH CKDKKEFLCR NQRCLSSSLR CNMFDDCGDG SDEEDCSIDP 

      3790       3800       3810       3820       3830       3840 
KLTSCATNAS ICGDEARCVR TEKAAYCACR SGFHTVPGQP GCQDINECLR FGTCSQLCNN 

      3850       3860       3870       3880       3890       3900 
TKGGHLCSCA RNFMKTHNTC KAEGSEYQVL YIADDNEIRS LFPGHPHSAY EQAFQGDESV 

      3910       3920       3930       3940       3950       3960 
RIDAMDVHVK AGRVYWTNWH TGTISYRSLP PAAPPTTSNR HRRQIDRGVT HLNISGLKMP 

      3970       3980       3990       4000       4010       4020 
RGIAIDWVAG NVYWTDSGRD VIEVAQMKGE NRKTLISGMI DEPHAIVVDP LRGTMYWSDW 

      4030       4040       4050       4060       4070       4080 
GNHPKIETAA MDGTLRETLV QDNIQWPTGL AVDYHNERLY WADAKLSVIG SIRLNGTDPI 

      4090       4100       4110       4120       4130       4140 
VAADSKRGLS HPFSIDVFED YIYGVTYINN RVFKIHKFGH SPLVNLTGGL SHASDVVLYH 

      4150       4160       4170       4180       4190       4200 
QHKQPEVTNP CDRKKCEWLC LLSPSGPVCT CPNGKRLDNG TCVPVPSPTP PPDAPRPGTC 

      4210       4220       4230       4240       4250       4260 
NLQCFNGGSC FLNARRQPKC RCQPRYTGDK CELDQCWEHC RNGGTCAASP SGMPTCRCPT 

      4270       4280       4290       4300       4310       4320 
GFTGPKCTQQ VCAGYCANNS TCTVNQGNQP QCRCLPGFLG DRCQYRQCSG YCENFGTCQM 

      4330       4340       4350       4360       4370       4380 
AADGSRQCRC TAYFEGSRCE VNKCSRCLEG ACVVNKQSGD VTCNCTDGRV APSCLTCVGH 

      4390       4400       4410       4420       4430       4440 
CSNGGSCTMN SKMMPECQCP PHMTGPRCEE HVFSQQQPGH IASILIPLLL LLLLVLVAGV 

      4450       4460       4470       4480       4490       4500 
VFWYKRRVQG AKGFQHQRMT NGAMNVEIGN PTYKMYEGGE PDDVGGLLDA DFALDPDKPT 

      4510       4520       4530       4540 
NFTNPVYATL YMGGHGSRHS LASTDEKREL LGRGPEDEIG DPLA 

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References

« Hide 'large scale' references
[1]"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."
Herz J., Hamann U., Rogne S., Myklebost O., Gausepohl H., Stanley K.K.
EMBO J. 7:4119-4127(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-2900.
Tissue: Liver.
[2]"Structure of the gene (LRP1) coding for the human alpha 2-macroglobulin receptor lipoprotein receptor-related protein."
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.
Genomics 24:78-89(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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."
Van Leuven F., Stas L., Thiry E., Nelissen B., Miyake Y.
Genomics 52:138-144(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-2900.
[4]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-2900.
[5]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Structure of the low-density lipoprotein receptor-related protein (LRP) promoter."
Kutt H., Herz J., Stanley K.K.
Biochim. Biophys. Acta 1009:229-236(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
[7]Glaeser C.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
Tissue: Blood.
[8]"Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor."
Strickland D.K., Ashcom J.D., Williams S., Burgess W.H., Migliorini M., Argraves W.S.
J. Biol. Chem. 265:17401-17404(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[9]"Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment."
Herz J., Kowal R.C., Goldstein J.L., Brown M.S.
EMBO J. 9:1769-1776(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[10]"Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor."
Kristensen T., Moestrup S.K., Gliemann J., Bendtsen L., Sand O., Sottrup-Jensen L.
FEBS Lett. 276:151-155(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A."
Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J., Strickland D.K., Saelinger C.B.
J. Biol. Chem. 267:12420-12423(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RECEPTOR FOR P.AERUGINOSA EXOA TOXIN.
[12]"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)."
Su H.P., Nakada-Tsukui K., Tosello-Trampont A.-C., Li Y., Bu G., Henson P.M., Ravichandran K.S.
J. Biol. Chem. 277:11772-11779(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GULP1, MUTAGENESIS OF ASN-4470 AND ASN-4504.
[13]"Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of the low density lipoprotein receptor-related protein (LRP). Evidence for integrated co-receptor function between LRP and the PDGF."
Loukinova E., Ranganathan S., Kuznetsov S., Gorlatova N., Migliorini M.M., Loukinov D., Ulery P.G., Mikhailenko I., Lawrence D.A., Strickland D.K.
J. Biol. Chem. 277:15499-15506(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-4507, MUTAGENESIS OF 4470-ASN--TYR-4473 AND 4504-ASN--TYR-4507, INTERACTION WITH PDGF.
[14]"Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain."
May P., Reddy Y.K., Herz J.
J. Biol. Chem. 277:18736-18743(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PROTEOLYTIC PROCESSING.
[15]"The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65."
Kinoshita A., Shah T., Tangredi M.M., Strickland D.K., Hyman B.T.
J. Biol. Chem. 278:41182-41188(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]"LDL receptor-related proteins in neurodevelopment."
May P., Herz J.
Traffic 4:291-301(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase Calpha regulates endocytosis and association with adaptor molecules."
Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F., Peltan I.D., Mikhailenko I., Hyman B.T., Strickland D.K.
J. Biol. Chem. 279:40536-40544(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-4460; SER-4517; SER-4520 AND SER-4523, MUTAGENESIS OF THR-4460; THR-4472; SER-4517; SER-4520 AND SER-4523, INTERACTION WITH SHC1; GULP1 AND DAB1.
[18]"Functions of sorting nexin 17 domains and recognition motif for P-selectin trafficking."
Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V., Schreckenberger S., Hahn H., Bohnensack R.
J. Mol. Biol. 347:813-825(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX17.
[19]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-2127 AND ASN-3048.
Tissue: Plasma.
[20]"Identification of the ligands of protein interaction domains through a functional approach."
Caratu G., Allegra D., Bimonte M., Schiattarella G.G., D'Ambrosio C., Scaloni A., Napolitano M., Russo T., Zambrano N.
Mol. Cell. Proteomics 6:333-345(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CUBN AND PID1, INTERACTION WITH CUBN AND PID1.
[21]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-1511; ASN-1575; ASN-1616; ASN-1645; ASN-1763; ASN-2127; ASN-2815; ASN-3048; ASN-3089; ASN-3488; ASN-3788; ASN-3953; ASN-4075 AND ASN-4125.
Tissue: Liver.
[22]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-729 AND ASN-1511.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein."
Huang W., Dolmer K., Gettins P.G.W.
J. Biol. Chem. 274:14130-14136(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1059-1100 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.
[25]"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."
Dolmer K., Huang W., Gettins P.G.W.
J. Biol. Chem. 275:3264-3269(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 851-893 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.
[26]"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."
Simonovic M., Dolmer K., Huang W., Strickland D.K., Volz K., Gettins P.G.
Biochemistry 40:15127-15134(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1012-1054 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.
[27]"Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif."
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.
J. Mol. Biol. 362:700-716(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 932-1013 IN COMPLEX WITH LRPAP1 AND CALCIUM IONS, DISULFIDE BONDS.
[28]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-869 AND HIS-3760.
[29]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-3258.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13916 mRNA. Translation: CAA32112.1.
AF058427 Genomic DNA. Translation: AAC64265.1.
DQ314873 Genomic DNA. Translation: ABC40732.1.
AC023237 Genomic DNA. No translation available.
AC137628 Genomic DNA. No translation available.
AC137834 Genomic DNA. No translation available.
X15424 Genomic DNA. Translation: CAA33464.1.
Y18524 Genomic DNA. Translation: CAD57169.1.
PIRS02392.
RefSeqNP_002323.2. NM_002332.2.
UniGeneHs.162757.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CR8NMR-A1059-1100[»]
1D2LNMR-A851-893[»]
1J8EX-ray1.85A1012-1054[»]
2FYJNMR-A932-1013[»]
2FYLNMR-B932-1013[»]
2KNXNMR-A2770-2817[»]
2KNYNMR-A2770-2817[»]
ProteinModelPortalQ07954.
SMRQ07954. Positions 851-893, 932-1054, 1059-1100, 2770-2815, 2856-2896, 3571-3606.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110215. 50 interactions.
IntActQ07954. 16 interactions.
MINTMINT-5004471.

Chemistry

DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00025. Antihemophilic Factor.
DB00102. Becaplermin.
DB00100. Coagulation Factor IX.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteQ07954.

Polymorphism databases

DMDM317373384.

Proteomic databases

PaxDbQ07954.
PRIDEQ07954.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243077; ENSP00000243077; ENSG00000123384.
GeneID4035.
KEGGhsa:4035.
UCSCuc001snd.3. human.

Organism-specific databases

CTD4035.
GeneCardsGC12P057497.
HGNCHGNC:6692. LRP1.
HPACAB018621.
HPA004182.
HPA022903.
MIM107770. gene.
neXtProtNX_Q07954.
PharmGKBPA233.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG235850.
HOGENOMHOG000230574.
HOVERGENHBG006292.
InParanoidQ07954.
KOK04550.
OMAAYFEGPR.
OrthoDBEOG790FZT.
PhylomeDBQ07954.
TreeFamTF315253.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressQ07954.
BgeeQ07954.
CleanExHS_LRP1.
GenevestigatorQ07954.

Family and domain databases

Gene3D2.120.10.30. 8 hits.
4.10.400.10. 29 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00181. EGF. 18 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 35 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 9 hits.
SSF57424. SSF57424. 30 hits.
PROSITEPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 2 hits.
PS01209. LDLRA_1. 27 hits.
PS50068. LDLRA_2. 31 hits.
PS51120. LDLRB. 34 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLRP1. human.
EvolutionaryTraceQ07954.
GeneWikiLRP1.
GenomeRNAi4035.
NextBio15806.
PROQ07954.
SOURCESearch...

Entry information

Entry nameLRP1_HUMAN
AccessionPrimary (citable) accession number: Q07954
Secondary accession number(s): Q2PP12, Q8IVG8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries