Q07954 (LRP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Cleaved into the following 3 chains:

1. Low-density lipoprotein receptor-related protein 1 85 kDa subunit
   Short name=LRP-85
2. Low-density lipoprotein receptor-related protein 1 515 kDa subunit
   Short name=LRP-515
3. Low-density lipoprotein receptor-related protein 1 intracellular domain
   Short name=LRPICD

Gene names

Name:	LRP1
Synonyms:	A2MR, APR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	4544 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Membrane › coated pit. Low-density lipoprotein receptor-related protein 1 515 kDa subunit: Cell membrane; Peripheral membrane protein; Extracellular side. Membrane › coated 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 process	Endocytosis
Cellular component	Cell membrane Coated pit Cytoplasm Membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Developmental protein Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 cholesterol metabolic process Inferred from electronic annotation. Source: Compara negative regulation of Wnt receptor signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL 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 receptor-mediated endocytosis Inferred from electronic annotation. Source: Compara regulation of actin cytoskeleton organization 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_component	coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell endocytic vesicle membrane Traceable author statement. Source: Reactome integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	apolipoprotein 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 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
Jag1	Q63722	4	EBI-1046087,EBI-4567800	From a different organism.
Thbs2	Q03350	2	EBI-1046087,EBI-4567830	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Chain

20 – 4544

4525

Prolow-density lipoprotein receptor-related protein 1

PRO_0000017317

Chain

20 – ?3943

3924

Low-density lipoprotein receptor-related protein 1 515 kDa subunit

PRO_0000302750

Chain

?3944 – 4544

601

Low-density lipoprotein receptor-related protein 1 85 kDa subunit

PRO_0000302751

Chain

?4441 – 4544

104

Low-density lipoprotein receptor-related protein 1 intracellular domain

PRO_0000302752

Regions

Topological domain

20 – 4419

4400

Extracellular Potential

Transmembrane

4420 – 4444

25

Helical; Potential

Topological domain

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

Domain

3372 – 3410

39

LDL-receptor class A 22

Domain

3411 – 3450

40

LDL-receptor class A 23

Domain

3451 – 3491

41

LDL-receptor class A 24

Domain

3492 – 3533

42

LDL-receptor class A 25

Domain

3534 – 3572

39

LDL-receptor class A 26

Domain

3573 – 3611

39

LDL-receptor class A 27

Domain

3611 – 3649

39

LDL-receptor class A 28

Domain

3652 – 3692

41

LDL-receptor class A 29

Domain

3693 – 3733

41

LDL-receptor class A 30

Domain

3739 – 3778

40

LDL-receptor class A 31

Domain

3781 – 3823

43

EGF-like 14

Domain

3824 – 3861

38

EGF-like 15

Repeat

3912 – 3954

43

LDL-receptor class B 31

Repeat

3970 – 4012

43

LDL-receptor class B 32

Repeat

4013 – 4056

44

LDL-receptor class B 33

Repeat

4057 – 4101

45

LDL-receptor class B 34

Domain

4147 – 4183

37

EGF-like 16

Domain

4196 – 4232

37

EGF-like 17

Domain

4232 – 4268

37

EGF-like 18

Domain

4268 – 4304

37

EGF-like 19

Domain

4304 – 4340

37

EGF-like 20

Domain

4340 – 4375

36

EGF-like 21

Domain

4373 – 4409

37

EGF-like 22

Region

4445 – 4544

100

Interaction with MAFB By similarity

Motif

3940 – 3943

4

Recognition site for proteolytical processing Potential

Motif

4502 – 4507

6

NPXY motif

Sites

Metal binding

871

1

Calcium 1; via carbonyl oxygen

Metal binding

874

1

Calcium 1

Metal binding

876

1

Calcium 1; via carbonyl oxygen

Metal binding

878

1

Calcium 1

Metal binding

884

1

Calcium 1

Metal binding

885

1

Calcium 1

Metal binding

1032

1

Calcium 2; via carbonyl oxygen

Metal binding

1035

1

Calcium 2

Metal binding

1037

1

Calcium 2; via carbonyl oxygen

Metal binding

1039

1

Calcium 2

Metal binding

1045

1

Calcium 2

Metal binding

1046

1

Calcium 2

Metal binding

1080

1

Calcium 3; via carbonyl oxygen

Metal binding

1083

1

Calcium 3

Metal binding

1085

1

Calcium 3; via carbonyl oxygen

Metal binding

1087

1

Calcium 3

Metal binding

1093

1

Calcium 3

Metal binding

1094

1

Calcium 3

Amino acid modifications

Modified residue

4460

1

Phosphothreonine Probable

Modified residue

4507

1

Phosphotyrosine Ref.13

Modified residue

4517

1

Phosphoserine Probable

Modified residue

4520

1

Phosphoserine Probable

Modified residue

4523

1

Phosphoserine Probable

Modified residue

4524

1

Phosphothreonine By similarity

Glycosylation

114

1

N-linked (GlcNAc...) Potential

Glycosylation

136

1

N-linked (GlcNAc...) Potential

Glycosylation

185

1

N-linked (GlcNAc...) Potential

Glycosylation

239

1

N-linked (GlcNAc...) Potential

Glycosylation

274

1

N-linked (GlcNAc...) Potential

Glycosylation

357

1

N-linked (GlcNAc...) Potential

Glycosylation

446

1

N-linked (GlcNAc...) Ref.19 Ref.21

Glycosylation

729

1

N-linked (GlcNAc...) Ref.19 Ref.21

Glycosylation

928

1

N-linked (GlcNAc...) Potential

Glycosylation

1050

1

N-linked (GlcNAc...) Potential

Glycosylation

1154

1

N-linked (GlcNAc...) Potential

Glycosylation

1155

1

N-linked (GlcNAc...) Potential

Glycosylation

1195

1

N-linked (GlcNAc...) Potential

Glycosylation

1218

1

N-linked (GlcNAc...) Potential

Glycosylation

1511

1

N-linked (GlcNAc...) Ref.21

Glycosylation

1558

1

N-linked (GlcNAc...) Potential

Glycosylation

1575

1

N-linked (GlcNAc...) Ref.21

Glycosylation

1616

1

N-linked (GlcNAc...) Ref.21

Glycosylation

1645

1

N-linked (GlcNAc...) Ref.21

Glycosylation

1723

1

N-linked (GlcNAc...) Potential

Glycosylation

1733

1

N-linked (GlcNAc...) Potential

Glycosylation

1763

1

N-linked (GlcNAc...) Ref.21

Glycosylation

1825

1

N-linked (GlcNAc...) Potential

Glycosylation

1933

1

N-linked (GlcNAc...) Potential

Glycosylation

1995

1

N-linked (GlcNAc...) Potential

Glycosylation

2048

1

N-linked (GlcNAc...) Potential

Glycosylation

2117

1

N-linked (GlcNAc...) Potential

Glycosylation

2127

1

N-linked (GlcNAc...) Ref.19 Ref.21

Glycosylation

2472

1

N-linked (GlcNAc...) Potential

Glycosylation

2502

1

N-linked (GlcNAc...) Potential

Glycosylation

2521

1

N-linked (GlcNAc...) Potential

Glycosylation

2539

1

N-linked (GlcNAc...) Potential

Glycosylation

2601

1

N-linked (GlcNAc...) Potential

Glycosylation

2620

1

N-linked (GlcNAc...) Potential

Glycosylation

2638

1

N-linked (GlcNAc...) Potential

Glycosylation

2815

1

N-linked (GlcNAc...) Ref.21

Glycosylation

2905

1

N-linked (GlcNAc...) Potential

Glycosylation

3048

1

N-linked (GlcNAc...) Ref.19 Ref.21

Glycosylation

3089

1

N-linked (GlcNAc...) Ref.21

Glycosylation

3264

1

N-linked (GlcNAc...) Potential

Glycosylation

3333

1

N-linked (GlcNAc...) Potential

Glycosylation

3488

1

N-linked (GlcNAc...) Ref.21

Glycosylation

3662

1

N-linked (GlcNAc...) Potential

Glycosylation

3788

1

N-linked (GlcNAc...) Ref.21

Glycosylation

3839

1

N-linked (GlcNAc...) Potential

Glycosylation

3953

1

N-linked (GlcNAc...) Ref.21

Glycosylation

4075

1

N-linked (GlcNAc...) Ref.21

Glycosylation

4125

1

N-linked (GlcNAc...) Ref.21

Glycosylation

4179

1

N-linked (GlcNAc...) Potential

Glycosylation

4278

1

N-linked (GlcNAc...) Potential

Glycosylation

4279

1

N-linked (GlcNAc...) Potential

Glycosylation

4364

1

N-linked (GlcNAc...) Potential

Disulfide bond

27 ↔ 40

By similarity

Disulfide bond

34 ↔ 53

By similarity

Disulfide bond

47 ↔ 64

By similarity

Disulfide bond

72 ↔ 85

By similarity

Disulfide bond

79 ↔ 98

By similarity

Disulfide bond

92 ↔ 108

By similarity

Disulfide bond

115 ↔ 124

By similarity

Disulfide bond

120 ↔ 133

By similarity

Disulfide bond

135 ↔ 148

By similarity

Disulfide bond

154 ↔ 164

By similarity

Disulfide bond

160 ↔ 173

By similarity

Disulfide bond

175 ↔ 188

By similarity

Disulfide bond

478 ↔ 493

By similarity

Disulfide bond

489 ↔ 504

By similarity

Disulfide bond

506 ↔ 519

By similarity

Disulfide bond

807 ↔ 818

By similarity

Disulfide bond

814 ↔ 827

By similarity

Disulfide bond

829 ↔ 842

By similarity

Disulfide bond

854 ↔ 866

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

861 ↔ 879

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

873 ↔ 890

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

895 ↔ 907

By similarity

Disulfide bond

902 ↔ 920

By similarity

Disulfide bond

914 ↔ 931

By similarity

Disulfide bond

936 ↔ 948

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

943 ↔ 961

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

955 ↔ 971

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

976 ↔ 989

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

984 ↔ 1002

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

996 ↔ 1011

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

1015 ↔ 1027

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

1022 ↔ 1040

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

1034 ↔ 1051

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

1062 ↔ 1075

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

1069 ↔ 1088

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

1082 ↔ 1097

Ref.23 Ref.24 Ref.25 Ref.26

Disulfide bond

1104 ↔ 1118

By similarity

Disulfide bond

1112 ↔ 1131

By similarity

Disulfide bond

1125 ↔ 1140

By similarity

Disulfide bond

1145 ↔ 1159

By similarity

Disulfide bond

1152 ↔ 1172

By similarity

Disulfide bond

1166 ↔ 1182

By similarity

Disulfide bond

1185 ↔ 1196

By similarity

Disulfide bond

1192 ↔ 1206

By similarity

Disulfide bond

1208 ↔ 1221

By similarity

Disulfide bond

1227 ↔ 1237

By similarity

Disulfide bond

1233 ↔ 1246

By similarity

Disulfide bond

1248 ↔ 1261

By similarity

Disulfide bond

1540 ↔ 1553

By similarity

Disulfide bond

1549 ↔ 1563

By similarity

Disulfide bond

1565 ↔ 1578

By similarity

Disulfide bond

1850 ↔ 1861

By similarity

Disulfide bond

1857 ↔ 1871

By similarity

Disulfide bond

1873 ↔ 1886

By similarity

Disulfide bond

2159 ↔ 2170

By similarity

Disulfide bond

2166 ↔ 2180

By similarity

Disulfide bond

2182 ↔ 2194

By similarity

Disulfide bond

2482 ↔ 2493

By similarity

Disulfide bond

2489 ↔ 2503

By similarity

Disulfide bond

2505 ↔ 2517

By similarity

Disulfide bond

2524 ↔ 2537

By similarity

Disulfide bond

2532 ↔ 2550

By similarity

Disulfide bond

2544 ↔ 2561

By similarity

Disulfide bond

2566 ↔ 2578

By similarity

Disulfide bond

2573 ↔ 2591

By similarity

Disulfide bond

2585 ↔ 2600

By similarity

Disulfide bond

2605 ↔ 2617

By similarity

Disulfide bond

2612 ↔ 2630

By similarity

Disulfide bond

2624 ↔ 2639

By similarity

Disulfide bond

2644 ↔ 2666

By similarity

Disulfide bond

2660 ↔ 2679

By similarity

Disulfide bond

2673 ↔ 2688

By similarity

Disulfide bond

2696 ↔ 2708

By similarity

Disulfide bond

2703 ↔ 2721

By similarity

Disulfide bond

2715 ↔ 2730

By similarity

Disulfide bond

2734 ↔ 2746

By similarity

Disulfide bond

2741 ↔ 2759

By similarity

Disulfide bond

2753 ↔ 2769

By similarity

Disulfide bond

2774 ↔ 2787

By similarity

Disulfide bond

2781 ↔ 2800

By similarity

Disulfide bond

2794 ↔ 2812

By similarity

Disulfide bond

2818 ↔ 2830

By similarity

Disulfide bond

2825 ↔ 2843

By similarity

Disulfide bond

2837 ↔ 2853

By similarity

Disulfide bond

2858 ↔ 2870

By similarity

Disulfide bond

2865 ↔ 2884

By similarity

Disulfide bond

2878 ↔ 2897

By similarity

Disulfide bond

2904 ↔ 2917

By similarity

Disulfide bond

2912 ↔ 2930

By similarity

Disulfide bond

2924 ↔ 2939

By similarity

Disulfide bond

2944 ↔ 2956

By similarity

Disulfide bond

2952 ↔ 2965

By similarity

Disulfide bond

2967 ↔ 2980

By similarity

Disulfide bond

2986 ↔ 2996

By similarity

Disulfide bond

2992 ↔ 3005

By similarity

Disulfide bond

3007 ↔ 3021

By similarity

Disulfide bond

3294 ↔ 3305

By similarity

Disulfide bond

3301 ↔ 3315

By similarity

Disulfide bond

3317 ↔ 3330

By similarity

Disulfide bond

3334 ↔ 3346

By similarity

Disulfide bond

3341 ↔ 3359

By similarity

Disulfide bond

3353 ↔ 3369

By similarity

Disulfide bond

3374 ↔ 3386

By similarity

Disulfide bond

3381 ↔ 3399

By similarity

Disulfide bond

3393 ↔ 3408

By similarity

Disulfide bond

3413 ↔ 3426

By similarity

Disulfide bond

3420 ↔ 3439

By similarity

Disulfide bond

3433 ↔ 3448

By similarity

Disulfide bond

3453 ↔ 3466

By similarity

Disulfide bond

3460 ↔ 3479

By similarity

Disulfide bond

3473 ↔ 3489

By similarity

Disulfide bond

3494 ↔ 3507

By similarity

Disulfide bond

3501 ↔ 3520

By similarity

Disulfide bond

3514 ↔ 3531

By similarity

Disulfide bond

3536 ↔ 3548

By similarity

Disulfide bond

3543 ↔ 3561

By similarity

Disulfide bond

3555 ↔ 3570

By similarity

Disulfide bond

3575 ↔ 3587

By similarity

Disulfide bond

3582 ↔ 3600

By similarity

Disulfide bond

3594 ↔ 3609

By similarity

Disulfide bond

3613 ↔ 3625

By similarity

Disulfide bond

3620 ↔ 3638

By similarity

Disulfide bond

3632 ↔ 3647

By similarity

Disulfide bond

3654 ↔ 3666

By similarity

Disulfide bond

3661 ↔ 3679

By similarity

Disulfide bond

3673 ↔ 3690

By similarity

Disulfide bond

3695 ↔ 3709

By similarity

Disulfide bond

3703 ↔ 3722

By similarity

Disulfide bond

3716 ↔ 3731

By similarity

Disulfide bond

3741 ↔ 3754

By similarity

Disulfide bond

3749 ↔ 3767

By similarity

Disulfide bond

3761 ↔ 3776

By similarity

Disulfide bond

3785 ↔ 3798

By similarity

Disulfide bond

3792 ↔ 3807

By similarity

Disulfide bond

3809 ↔ 3822

By similarity

Disulfide bond

3828 ↔ 3838

By similarity

Disulfide bond

3834 ↔ 3847

By similarity

Disulfide bond

3849 ↔ 3860

By similarity

Disulfide bond

4151 ↔ 4160

By similarity

Disulfide bond

4156 ↔ 4169

By similarity

Disulfide bond

4171 ↔ 4182

By similarity

Disulfide bond

4200 ↔ 4210

By similarity

Disulfide bond

4204 ↔ 4220

By similarity

Disulfide bond

4222 ↔ 4231

By similarity

Disulfide bond

4236 ↔ 4246

By similarity

Disulfide bond

4240 ↔ 4256

By similarity

Disulfide bond

4258 ↔ 4267

By similarity

Disulfide bond

4272 ↔ 4282

By similarity

Disulfide bond

4276 ↔ 4292

By similarity

Disulfide bond

4294 ↔ 4303

By similarity

Disulfide bond

4308 ↔ 4318

By similarity

Disulfide bond

4312 ↔ 4328

By similarity

Disulfide bond

4330 ↔ 4339

By similarity

Disulfide bond

4344 ↔ 4352

By similarity

Disulfide bond

4347 ↔ 4363

By similarity

Disulfide bond

4365 ↔ 4374

By similarity

Disulfide bond

4377 ↔ 4387

By similarity

Disulfide bond

4381 ↔ 4397

By similarity

Disulfide bond

4399 ↔ 4408

By similarity

Natural variations

Natural variant

166

1

N → D.
Corresponds to variant rs2306691 [ dbSNP | Ensembl ].

VAR_021885

Natural variant

217

1

A → V.
Corresponds to variant rs1800127 [ dbSNP | Ensembl ].

VAR_014725

Natural variant

869

1

E → K in a colorectal cancer sample; somatic mutation. Ref.27

VAR_035994

Natural variant

2059

1

V → L.
Corresponds to variant rs2229278 [ dbSNP | Ensembl ].

VAR_029181

Natural variant

2080

1

D → N.
Corresponds to variant rs34577247 [ dbSNP | Ensembl ].

VAR_047525

Natural variant

2900

1

Q → P. Ref.1 Ref.3 Ref.4
Corresponds to variant rs7397167 [ dbSNP | Ensembl ].

VAR_047526

Natural variant

3760

1

R → H in a colorectal cancer sample; somatic mutation. Ref.27

VAR_035995

Natural variant

4536

1

E → G.
Corresponds to variant rs17357542 [ dbSNP | Ensembl ].

VAR_047527

Experimental info

Mutagenesis

4460

1

T → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4517; A-4520 and A-4523. Ref.17

Mutagenesis

4470 – 4473

4

NPTY → APTA: No effect on tyrosine phosphorylation. Ref.12 Ref.13

Mutagenesis

4470

1

N → A: No effect on interaction with GULP1. Ref.12

Mutagenesis

4472

1

T → A: No detectable effect on phosphorylation. Ref.17

Mutagenesis

4504 – 4507

4

NPVY → APVA: Loss of tyrosine phosphorylation. Abolishes interaction with SHC1 and GULP1. Ref.12 Ref.13

Mutagenesis

4504

1

N → A: Loss of interaction with GULP1. Ref.12

Mutagenesis

4517

1

S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4520 and A-4523. Ref.17

Mutagenesis

4520

1

S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4523. Ref.17

Mutagenesis

4523

1

S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4520. Ref.17

Sequence conflict

685

1

D → G AA sequence Ref.8

Sequence conflict

1743

1

G → S AA sequence Ref.8

Sequence conflict

2871 – 2872

2

LS → IA AA sequence Ref.8

Sequence conflict

3036

1

R → M AA sequence Ref.8

Secondary structure

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4544

Helix Strand Turn

Details...

Turn

853 – 857

5

Beta strand

859 – 861

3

Turn

862 – 864

3

Beta strand

865 – 867

3

Helix

869 – 871

3

Beta strand

874 – 876

3

Turn

878 – 881

4

Beta strand

934 – 936

3

Beta strand

940 – 942

3

Turn

944 – 946

3

Beta strand

948 – 950

3

Beta strand

953 – 956

4

Beta strand

958 – 961

4

Turn

964 – 968

5

Turn

969 – 971

3

Beta strand

974 – 976

3

Beta strand

978 – 983

6

Turn

985 – 987

3

Beta strand

989 – 991

3

Beta strand

995 – 1000

6

Beta strand

1003 – 1007

5

Beta strand

1009 – 1011

3

Beta strand

1013 – 1015

3

Beta strand

1019 – 1021

3

Beta strand

1027 – 1029

3

Helix

1030 – 1032

3

Beta strand

1035 – 1037

3

Beta strand

1040 – 1043

4

Helix

1044 – 1046

3

Helix

1048 – 1051

4

Turn

1070 – 1072

3

Helix

1078 – 1080

3

Beta strand

1081 – 1085

5

Beta strand

1088 – 1091

4

Turn

1092 – 1096

5

Beta strand

2778 – 2781

4

Turn

2782 – 2785

4

Beta strand

2786 – 2789

4

Turn

2790 – 2794

5

Beta strand

2795 – 2797

3

Beta strand

2800 – 2803

4

Helix

2804 – 2806

3

Helix

2808 – 2810

3

Beta strand

2813 – 2816

4

Sequences

	Sequence		Length	Mass (Da)
	Q07954 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: 5A11CC02FAB127BE	FASTA	4,544	504,606
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[22]	"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].
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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. , 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.
+	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.

IPI

IPI00020557.

PIR

S02392.

RefSeq

NP_002323.2. NM_002332.2.

UniGene

Hs.162757.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CR8	NMR	-	A	1059-1100	[»]
1D2L	NMR	-	A	851-893	[»]
1J8E	X-ray	1.85	A	1012-1054	[»]
2FYJ	NMR	-	A	932-1013	[»]
2FYL	NMR	-	B	932-1013	[»]
2KNX	NMR	-	A	2770-2817	[»]
2KNY	NMR	-	A	2770-2817	[»]

ProteinModelPortal

Q07954.

SMR

Q07954. Positions 851-893, 932-1054, 1059-1100, 2770-2815, 2856-2896, 3571-3606.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q07954. 7 interactions.

MINT

MINT-5004471.

PTM databases

PhosphoSite

Q07954.

Polymorphism databases

DMDM

1708865.

Proteomic databases

PaxDb

Q07954.

PRIDE

Q07954.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000243077; ENSP00000243077; ENSG00000123384.

GeneID

4035.

KEGG

hsa:4035.

UCSC

uc001snd.3. human.

Organism-specific databases

CTD

4035.

GeneCards

GC12P057497.

HGNC

HGNC:6692. LRP1.

HPA

CAB018621.
HPA004182.
HPA022903.

MIM

107770. gene.

neXtProt

NX_Q07954.

PharmGKB

PA233.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG235850.

HOGENOM

HOG000230574.

HOVERGEN

HBG006292.

InParanoid

Q07954.

KO

K04550.

OMA

ESVTAGC.

OrthoDB

EOG42BX7K.

PhylomeDB

Q07954.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
pdgfrbpathway. PDGFR-beta signaling pathway.

Gene expression databases

ArrayExpress

Q07954.

Bgee

Q07954.

CleanEx

HS_LRP1.

Genevestigator

Q07954.

GermOnline

ENSG00000123384. Homo sapiens.

Family and domain databases

Gene3D

2.120.10.30. 8 hits.
4.10.400.10. 29 hits.

InterPro

IPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
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]

Pfam

PF12662. cEGF. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view]

SMART

SM00181. EGF. 18 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 35 hits.
[Graphical view]

SUPFAM

SSF57184. Grow_fac_recept. 2 hits.
SSF57424. LDL_rcpt_classA_cys-rich. 28 hits.

PROSITE

PS00010. 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]

ProtoNet

Search...

Other

ChiTaRS

LRP1. human.

DrugBank

DB00009. Alteplase.
DB00029. Anistreplase.
DB00025. Antihemophilic Factor.
DB00102. Becaplermin.
DB00100. Coagulation Factor IX.
DB00031. Tenecteplase.

EvolutionaryTrace

Q07954.

GenomeRNAi

4035.

NextBio

15806.

SOURCE

Search...

Entry information

Entry name

LRP1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 150 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.