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Q07954

- LRP1_HUMAN

UniProt

Q07954 - LRP1_HUMAN

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Protein

Prolow-density lipoprotein receptor-related protein 1

Gene

LRP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
Functions as a receptor for Pseudomonas aeruginosa exotoxin A.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi871 – 8711Calcium 1; via carbonyl oxygen
Metal bindingi874 – 8741Calcium 1
Metal bindingi876 – 8761Calcium 1; via carbonyl oxygen
Metal bindingi878 – 8781Calcium 1
Metal bindingi884 – 8841Calcium 1
Metal bindingi885 – 8851Calcium 1
Metal bindingi1032 – 10321Calcium 2; via carbonyl oxygen
Metal bindingi1035 – 10351Calcium 2
Metal bindingi1037 – 10371Calcium 2; via carbonyl oxygen
Metal bindingi1039 – 10391Calcium 2
Metal bindingi1045 – 10451Calcium 2
Metal bindingi1046 – 10461Calcium 2
Metal bindingi1080 – 10801Calcium 3; via carbonyl oxygen
Metal bindingi1083 – 10831Calcium 3
Metal bindingi1085 – 10851Calcium 3; via carbonyl oxygen
Metal bindingi1087 – 10871Calcium 3
Metal bindingi1093 – 10931Calcium 3
Metal bindingi1094 – 10941Calcium 3

GO - Molecular functioni

  1. apolipoprotein binding Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. lipoprotein particle receptor binding Source: BHF-UCL
  4. lipoprotein transporter activity Source: UniProtKB
  5. poly(A) RNA binding Source: UniProtKB
  6. protein complex binding Source: BHF-UCL
  7. receptor activity Source: ProtInc

GO - Biological processi

  1. aging Source: Ensembl
  2. aorta morphogenesis Source: BHF-UCL
  3. apoptotic cell clearance Source: BHF-UCL
  4. beta-amyloid clearance Source: BHF-UCL
  5. cell proliferation Source: Ensembl
  6. cholesterol metabolic process Source: Ensembl
  7. lipoprotein metabolic process Source: Ensembl
  8. lipoprotein transport Source: UniProtKB
  9. negative regulation of neuron apoptotic process Source: Ensembl
  10. negative regulation of platelet-derived growth factor receptor-beta signaling pathway Source: BHF-UCL
  11. negative regulation of smooth muscle cell migration Source: BHF-UCL
  12. negative regulation of Wnt signaling pathway Source: BHF-UCL
  13. phototransduction, visible light Source: Reactome
  14. positive regulation of cholesterol efflux Source: BHF-UCL
  15. positive regulation of lipid transport Source: BHF-UCL
  16. positive regulation of protein transport Source: Ensembl
  17. protein kinase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
  18. receptor-mediated endocytosis Source: Ensembl
  19. regulation of actin cytoskeleton organization Source: BHF-UCL
  20. regulation of cholesterol transport Source: BHF-UCL
  21. regulation of phospholipase A2 activity Source: BHF-UCL
  22. retinoid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_160163. Scavenging of heme from plasma.
REACT_24968. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Name:LRP1
Synonyms:A2MR, APR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6692. LRP1.

Subcellular locationi

Chain 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.

GO - Cellular componenti

  1. clathrin-coated vesicle Source: Ensembl
  2. coated pit Source: UniProtKB-KW
  3. dendrite Source: Ensembl
  4. endocytic vesicle membrane Source: Reactome
  5. endosome Source: Ensembl
  6. focal adhesion Source: UniProtKB
  7. integral component of plasma membrane Source: UniProtKB
  8. lysosomal membrane Source: UniProtKB
  9. neuronal cell body Source: Ensembl
  10. nucleus Source: UniProtKB-KW
  11. plasma membrane Source: Reactome
  12. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4460 – 44601T → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4517; A-4520 and A-4523. 1 Publication
Mutagenesisi4470 – 44734NPTY → APTA: No effect on tyrosine phosphorylation. 1 Publication
Mutagenesisi4470 – 44701N → A: No effect on interaction with GULP1. 1 Publication
Mutagenesisi4472 – 44721T → A: No detectable effect on phosphorylation. 1 Publication
Mutagenesisi4504 – 45074NPVY → APVA: Loss of tyrosine phosphorylation. Abolishes interaction with SHC1 and GULP1. 1 Publication
Mutagenesisi4504 – 45041N → A: Loss of interaction with GULP1. 1 Publication
Mutagenesisi4517 – 45171S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4520 and A-4523. 1 Publication
Mutagenesisi4520 – 45201S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4523. 1 Publication
Mutagenesisi4523 – 45231S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4520. 1 Publication

Organism-specific databases

PharmGKBiPA233.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 45444525Prolow-density lipoprotein receptor-related protein 1PRO_0000017317Add
BLAST
Chaini20 – ?39433924Low-density lipoprotein receptor-related protein 1 515 kDa subunitPRO_0000302750Add
BLAST
Chaini?3944 – 4544601Low-density lipoprotein receptor-related protein 1 85 kDa subunitPRO_0000302751Add
BLAST
Chaini?4441 – 4544104Low-density lipoprotein receptor-related protein 1 intracellular domainPRO_0000302752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 40By similarity
Disulfide bondi34 ↔ 53By similarity
Disulfide bondi47 ↔ 64By similarity
Disulfide bondi72 ↔ 85By similarity
Disulfide bondi79 ↔ 98By similarity
Disulfide bondi92 ↔ 108By similarity
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi115 ↔ 124By similarity
Disulfide bondi120 ↔ 133By similarity
Disulfide bondi135 ↔ 148By similarity
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi154 ↔ 164By similarity
Disulfide bondi160 ↔ 173By similarity
Disulfide bondi175 ↔ 188By similarity
Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi446 – 4461N-linked (GlcNAc...)2 Publications
Disulfide bondi478 ↔ 493By similarity
Disulfide bondi489 ↔ 504By similarity
Disulfide bondi506 ↔ 519By similarity
Glycosylationi729 – 7291N-linked (GlcNAc...) (complex)3 Publications
Disulfide bondi807 ↔ 818By similarity
Disulfide bondi814 ↔ 827By similarity
Disulfide bondi829 ↔ 842By similarity
Disulfide bondi854 ↔ 866
Disulfide bondi861 ↔ 879
Disulfide bondi873 ↔ 890
Disulfide bondi895 ↔ 907By similarity
Disulfide bondi902 ↔ 920By similarity
Disulfide bondi914 ↔ 931By similarity
Glycosylationi928 – 9281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi936 ↔ 948
Disulfide bondi943 ↔ 961
Disulfide bondi955 ↔ 971
Disulfide bondi976 ↔ 989
Disulfide bondi984 ↔ 1002
Disulfide bondi996 ↔ 1011
Disulfide bondi1015 ↔ 1027
Disulfide bondi1022 ↔ 1040
Disulfide bondi1034 ↔ 1051
Glycosylationi1050 – 10501N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1062 ↔ 1075
Disulfide bondi1069 ↔ 1088
Disulfide bondi1082 ↔ 1097
Disulfide bondi1104 ↔ 1118By similarity
Disulfide bondi1112 ↔ 1131By similarity
Disulfide bondi1125 ↔ 1140By similarity
Disulfide bondi1145 ↔ 1159By similarity
Disulfide bondi1152 ↔ 1172By similarity
Glycosylationi1154 – 11541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1155 – 11551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1166 ↔ 1182By similarity
Disulfide bondi1185 ↔ 1196By similarity
Disulfide bondi1192 ↔ 1206By similarity
Glycosylationi1195 – 11951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1208 ↔ 1221By similarity
Glycosylationi1218 – 12181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1227 ↔ 1237By similarity
Disulfide bondi1233 ↔ 1246By similarity
Disulfide bondi1248 ↔ 1261By similarity
Glycosylationi1511 – 15111N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi1540 ↔ 1553By similarity
Disulfide bondi1549 ↔ 1563By similarity
Glycosylationi1558 – 15581N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1565 ↔ 1578By similarity
Glycosylationi1575 – 15751N-linked (GlcNAc...)1 Publication
Glycosylationi1616 – 16161N-linked (GlcNAc...)1 Publication
Glycosylationi1645 – 16451N-linked (GlcNAc...)1 Publication
Glycosylationi1723 – 17231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1733 – 17331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1763 – 17631N-linked (GlcNAc...)1 Publication
Glycosylationi1825 – 18251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1850 ↔ 1861By similarity
Disulfide bondi1857 ↔ 1871By similarity
Disulfide bondi1873 ↔ 1886By similarity
Glycosylationi1933 – 19331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1995 – 19951N-linked (GlcNAc...)Sequence Analysis
Modified residuei2009 – 20091N6-acetyllysineBy similarity
Glycosylationi2048 – 20481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2117 – 21171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2127 – 21271N-linked (GlcNAc...)2 Publications
Disulfide bondi2159 ↔ 2170By similarity
Disulfide bondi2166 ↔ 2180By similarity
Disulfide bondi2182 ↔ 2194By similarity
Glycosylationi2472 – 24721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2482 ↔ 2493By similarity
Disulfide bondi2489 ↔ 2503By similarity
Glycosylationi2502 – 25021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2505 ↔ 2517By similarity
Glycosylationi2521 – 25211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2524 ↔ 2537By similarity
Disulfide bondi2532 ↔ 2550By similarity
Glycosylationi2539 – 25391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2544 ↔ 2561By similarity
Disulfide bondi2566 ↔ 2578By similarity
Disulfide bondi2573 ↔ 2591By similarity
Disulfide bondi2585 ↔ 2600By similarity
Glycosylationi2601 – 26011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2605 ↔ 2617By similarity
Disulfide bondi2612 ↔ 2630By similarity
Glycosylationi2620 – 26201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2624 ↔ 2639By similarity
Glycosylationi2638 – 26381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2644 ↔ 2666By similarity
Disulfide bondi2660 ↔ 2679By similarity
Disulfide bondi2673 ↔ 2688By similarity
Disulfide bondi2696 ↔ 2708By similarity
Disulfide bondi2703 ↔ 2721By similarity
Disulfide bondi2715 ↔ 2730By similarity
Disulfide bondi2734 ↔ 2746By similarity
Disulfide bondi2741 ↔ 2759By similarity
Disulfide bondi2753 ↔ 2769By similarity
Disulfide bondi2774 ↔ 2787By similarity
Disulfide bondi2781 ↔ 2800By similarity
Disulfide bondi2794 ↔ 2812By similarity
Glycosylationi2815 – 28151N-linked (GlcNAc...)1 Publication
Disulfide bondi2818 ↔ 2830By similarity
Disulfide bondi2825 ↔ 2843By similarity
Disulfide bondi2837 ↔ 2853By similarity
Disulfide bondi2858 ↔ 2870By similarity
Disulfide bondi2865 ↔ 2884By similarity
Disulfide bondi2878 ↔ 2897By similarity
Disulfide bondi2904 ↔ 2917By similarity
Glycosylationi2905 – 29051N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2912 ↔ 2930By similarity
Disulfide bondi2924 ↔ 2939By similarity
Disulfide bondi2944 ↔ 2956By similarity
Disulfide bondi2952 ↔ 2965By similarity
Disulfide bondi2967 ↔ 2980By similarity
Disulfide bondi2986 ↔ 2996By similarity
Disulfide bondi2992 ↔ 3005By similarity
Disulfide bondi3007 ↔ 3021By similarity
Glycosylationi3048 – 30481N-linked (GlcNAc...)2 Publications
Glycosylationi3089 – 30891N-linked (GlcNAc...)1 Publication
Glycosylationi3264 – 32641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3294 ↔ 3305By similarity
Disulfide bondi3301 ↔ 3315By similarity
Disulfide bondi3317 ↔ 3330By similarity
Glycosylationi3333 – 33331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3334 ↔ 3346By similarity
Disulfide bondi3341 ↔ 3359By similarity
Disulfide bondi3353 ↔ 3369By similarity
Disulfide bondi3374 ↔ 3386By similarity
Disulfide bondi3381 ↔ 3399By similarity
Disulfide bondi3393 ↔ 3408By similarity
Disulfide bondi3413 ↔ 3426By similarity
Disulfide bondi3420 ↔ 3439By similarity
Disulfide bondi3433 ↔ 3448By similarity
Disulfide bondi3453 ↔ 3466By similarity
Disulfide bondi3460 ↔ 3479By similarity
Disulfide bondi3473 ↔ 3489By similarity
Glycosylationi3488 – 34881N-linked (GlcNAc...)1 Publication
Disulfide bondi3494 ↔ 3507By similarity
Disulfide bondi3501 ↔ 3520By similarity
Disulfide bondi3514 ↔ 3531By similarity
Disulfide bondi3536 ↔ 3548By similarity
Disulfide bondi3543 ↔ 3561By similarity
Disulfide bondi3555 ↔ 3570By similarity
Disulfide bondi3575 ↔ 3587By similarity
Disulfide bondi3582 ↔ 3600By similarity
Disulfide bondi3594 ↔ 3609By similarity
Disulfide bondi3613 ↔ 3625By similarity
Disulfide bondi3620 ↔ 3638By similarity
Disulfide bondi3632 ↔ 3647By similarity
Disulfide bondi3654 ↔ 3666By similarity
Disulfide bondi3661 ↔ 3679By similarity
Glycosylationi3662 – 36621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3673 ↔ 3690By similarity
Disulfide bondi3695 ↔ 3709By similarity
Disulfide bondi3703 ↔ 3722By similarity
Disulfide bondi3716 ↔ 3731By similarity
Disulfide bondi3741 ↔ 3754By similarity
Disulfide bondi3749 ↔ 3767By similarity
Disulfide bondi3761 ↔ 3776By similarity
Disulfide bondi3785 ↔ 3798By similarity
Glycosylationi3788 – 37881N-linked (GlcNAc...)1 Publication
Disulfide bondi3792 ↔ 3807By similarity
Disulfide bondi3809 ↔ 3822By similarity
Disulfide bondi3828 ↔ 3838By similarity
Disulfide bondi3834 ↔ 3847By similarity
Glycosylationi3839 – 38391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3849 ↔ 3860By similarity
Glycosylationi3953 – 39531N-linked (GlcNAc...)1 Publication
Glycosylationi4075 – 40751N-linked (GlcNAc...)1 Publication
Glycosylationi4125 – 41251N-linked (GlcNAc...)1 Publication
Disulfide bondi4151 ↔ 4160By similarity
Disulfide bondi4156 ↔ 4169By similarity
Disulfide bondi4171 ↔ 4182By similarity
Glycosylationi4179 – 41791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4200 ↔ 4210By similarity
Disulfide bondi4204 ↔ 4220By similarity
Disulfide bondi4222 ↔ 4231By similarity
Disulfide bondi4236 ↔ 4246By similarity
Disulfide bondi4240 ↔ 4256By similarity
Disulfide bondi4258 ↔ 4267By similarity
Disulfide bondi4272 ↔ 4282By similarity
Disulfide bondi4276 ↔ 4292By similarity
Glycosylationi4278 – 42781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4279 – 42791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4294 ↔ 4303By similarity
Disulfide bondi4308 ↔ 4318By similarity
Disulfide bondi4312 ↔ 4328By similarity
Disulfide bondi4330 ↔ 4339By similarity
Disulfide bondi4344 ↔ 4352By similarity
Disulfide bondi4347 ↔ 4363By similarity
Glycosylationi4364 – 43641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4365 ↔ 4374By similarity
Disulfide bondi4377 ↔ 4387By similarity
Disulfide bondi4381 ↔ 4397By similarity
Disulfide bondi4399 ↔ 4408By similarity
Modified residuei4460 – 44601Phosphothreonine1 Publication
Modified residuei4507 – 45071Phosphotyrosine1 Publication
Modified residuei4517 – 45171Phosphoserine1 Publication
Modified residuei4520 – 45201Phosphoserine1 Publication
Modified residuei4523 – 45231Phosphoserine1 Publication

Post-translational modificationi

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.2 Publications
The N-terminus is blocked.
Phosphorylated on serine and threonine residues.
Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1.

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ07954.
PaxDbiQ07954.
PRIDEiQ07954.

PTM databases

PhosphoSiteiQ07954.

Expressioni

Tissue specificityi

Most abundant in liver, brain and lung.

Gene expression databases

BgeeiQ07954.
CleanExiHS_LRP1.
ExpressionAtlasiQ07954. baseline and differential.
GenevestigatoriQ07954.

Organism-specific databases

HPAiCAB018621.
HPA004182.
HPA022903.

Interactioni

Subunit structurei

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.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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.

Protein-protein interaction databases

BioGridi110215. 54 interactions.
DIPiDIP-50613N.
IntActiQ07954. 18 interactions.
MINTiMINT-5004471.

Structurei

Secondary structure

1
4544
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni853 – 8575
Beta strandi859 – 8613
Turni862 – 8643
Beta strandi865 – 8673
Helixi869 – 8713
Beta strandi874 – 8763
Turni878 – 8814
Beta strandi934 – 9363
Beta strandi940 – 9423
Turni944 – 9463
Beta strandi948 – 9503
Beta strandi953 – 9564
Beta strandi958 – 9614
Turni964 – 9685
Turni969 – 9713
Beta strandi974 – 9763
Beta strandi978 – 9836
Turni985 – 9873
Beta strandi989 – 9913
Beta strandi995 – 10006
Beta strandi1003 – 10075
Beta strandi1009 – 10113
Beta strandi1013 – 10153
Beta strandi1019 – 10213
Beta strandi1027 – 10293
Helixi1030 – 10323
Beta strandi1035 – 10373
Beta strandi1040 – 10434
Helixi1044 – 10463
Helixi1048 – 10514
Turni1070 – 10723
Helixi1078 – 10803
Beta strandi1081 – 10855
Beta strandi1088 – 10914
Turni1092 – 10965
Beta strandi2778 – 27814
Turni2782 – 27854
Beta strandi2786 – 27894
Turni2790 – 27945
Beta strandi2795 – 27973
Beta strandi2800 – 28034
Helixi2804 – 28063
Helixi2808 – 28103
Beta strandi2813 – 28164

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CR8NMR-A1059-1100[»]
1D2LNMR-A851-893[»]
1J8EX-ray1.85A1011-1054[»]
2FYJNMR-A932-1013[»]
2FYLNMR-B932-1013[»]
2KNXNMR-A2770-2817[»]
2KNYNMR-A2770-2817[»]
ProteinModelPortaliQ07954.
SMRiQ07954. Positions 851-893, 932-1054, 1059-1100, 2770-2815, 2856-2896, 3571-3606.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07954.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 44194400ExtracellularSequence AnalysisAdd
BLAST
Topological domaini4445 – 4544100CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4420 – 444425HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 6642LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini70 – 11041LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini111 – 14939EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini150 – 18940EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati292 – 33443LDL-receptor class B 1Add
BLAST
Repeati335 – 37844LDL-receptor class B 2Add
BLAST
Repeati379 – 42244LDL-receptor class B 3Add
BLAST
Domaini474 – 52047EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Repeati571 – 61343LDL-receptor class B 4Add
BLAST
Repeati614 – 65946LDL-receptor class B 5Add
BLAST
Repeati660 – 71051LDL-receptor class B 6Add
BLAST
Repeati711 – 75444LDL-receptor class B 7Add
BLAST
Domaini803 – 84341EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini852 – 89241LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini893 – 93341LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini934 – 97340LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini974 – 101340LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini1013 – 105341LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini1060 – 109940LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini1102 – 114241LDL-receptor class A 9PROSITE-ProRule annotationAdd
BLAST
Domaini1143 – 118240LDL-receptor class A 10PROSITE-ProRule annotationAdd
BLAST
Domaini1183 – 122240EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini1223 – 126240EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Repeati1309 – 135547LDL-receptor class B 8Add
BLAST
Repeati1356 – 139843LDL-receptor class B 9Add
BLAST
Repeati1399 – 144547LDL-receptor class B 10Add
BLAST
Repeati1446 – 149045LDL-receptor class B 11Add
BLAST
Repeati1491 – 153141LDL-receptor class B 12Add
BLAST
Domaini1536 – 157944EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Repeati1627 – 166943LDL-receptor class B 13Add
BLAST
Repeati1670 – 171344LDL-receptor class B 14Add
BLAST
Repeati1714 – 175340LDL-receptor class B 15Add
BLAST
Repeati1754 – 179845LDL-receptor class B 16Add
BLAST
Domaini1846 – 188742EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Repeati1934 – 197643LDL-receptor class B 17Add
BLAST
Repeati1977 – 201943LDL-receptor class B 18Add
BLAST
Repeati2020 – 206344LDL-receptor class B 19Add
BLAST
Repeati2064 – 210744LDL-receptor class B 20Add
BLAST
Domaini2155 – 219541EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Repeati2253 – 229442LDL-receptor class B 21Add
BLAST
Repeati2295 – 234349LDL-receptor class B 22Add
BLAST
Repeati2344 – 238845LDL-receptor class B 23Add
BLAST
Repeati2389 – 243143LDL-receptor class B 24Add
BLAST
Repeati2432 – 247342LDL-receptor class B 25Add
BLAST
Domaini2478 – 251841EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini2522 – 256342LDL-receptor class A 11PROSITE-ProRule annotationAdd
BLAST
Domaini2564 – 260239LDL-receptor class A 12PROSITE-ProRule annotationAdd
BLAST
Domaini2603 – 264139LDL-receptor class A 13PROSITE-ProRule annotationAdd
BLAST
Domaini2642 – 269049LDL-receptor class A 14PROSITE-ProRule annotationAdd
BLAST
Domaini2694 – 273239LDL-receptor class A 15PROSITE-ProRule annotationAdd
BLAST
Domaini2732 – 277140LDL-receptor class A 16PROSITE-ProRule annotationAdd
BLAST
Domaini2772 – 281443LDL-receptor class A 17PROSITE-ProRule annotationAdd
BLAST
Domaini2816 – 285540LDL-receptor class A 18PROSITE-ProRule annotationAdd
BLAST
Domaini2856 – 289944LDL-receptor class A 19PROSITE-ProRule annotationAdd
BLAST
Domaini2902 – 294039LDL-receptor class A 20PROSITE-ProRule annotationAdd
BLAST
Domaini2941 – 298141EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini2982 – 302241EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati3069 – 311345LDL-receptor class B 26Add
BLAST
Repeati3114 – 315643LDL-receptor class B 27Add
BLAST
Repeati3157 – 320044LDL-receptor class B 28Add
BLAST
Repeati3201 – 324343LDL-receptor class B 29Add
BLAST
Repeati3244 – 328441LDL-receptor class B 30Add
BLAST
Domaini3290 – 333142EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini3332 – 337140LDL-receptor class A 21PROSITE-ProRule annotationAdd
BLAST
Domaini3372 – 341039LDL-receptor class A 22PROSITE-ProRule annotationAdd
BLAST
Domaini3411 – 345040LDL-receptor class A 23PROSITE-ProRule annotationAdd
BLAST
Domaini3451 – 349141LDL-receptor class A 24PROSITE-ProRule annotationAdd
BLAST
Domaini3492 – 353342LDL-receptor class A 25PROSITE-ProRule annotationAdd
BLAST
Domaini3534 – 357239LDL-receptor class A 26PROSITE-ProRule annotationAdd
BLAST
Domaini3573 – 361139LDL-receptor class A 27PROSITE-ProRule annotationAdd
BLAST
Domaini3611 – 364939LDL-receptor class A 28PROSITE-ProRule annotationAdd
BLAST
Domaini3652 – 369241LDL-receptor class A 29PROSITE-ProRule annotationAdd
BLAST
Domaini3693 – 373341LDL-receptor class A 30PROSITE-ProRule annotationAdd
BLAST
Domaini3739 – 377840LDL-receptor class A 31PROSITE-ProRule annotationAdd
BLAST
Domaini3781 – 382343EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini3824 – 386138EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Repeati3912 – 395443LDL-receptor class B 31Add
BLAST
Repeati3970 – 401243LDL-receptor class B 32Add
BLAST
Repeati4013 – 405644LDL-receptor class B 33Add
BLAST
Repeati4057 – 410145LDL-receptor class B 34Add
BLAST
Domaini4147 – 418337EGF-like 16PROSITE-ProRule annotationAdd
BLAST
Domaini4196 – 423237EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini4232 – 426837EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini4268 – 430437EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini4304 – 434037EGF-like 20PROSITE-ProRule annotationAdd
BLAST
Domaini4340 – 437536EGF-like 21PROSITE-ProRule annotationAdd
BLAST
Domaini4373 – 440937EGF-like 22PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4445 – 4544100Interaction with MAFBBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3940 – 39434Recognition site for proteolytical processingSequence Analysis
Motifi4502 – 45076NPXY motif

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 22 EGF-like domains.PROSITE-ProRule annotation
Contains 31 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 34 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG235850.
GeneTreeiENSGT00760000119194.
HOGENOMiHOG000230574.
HOVERGENiHBG006292.
InParanoidiQ07954.
KOiK04550.
OMAiAYFEGPR.
OrthoDBiEOG790FZT.
PhylomeDBiQ07954.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 29 hits.
InterProiIPR011042. 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]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 18 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 35 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 9 hits.
SSF57424. SSF57424. 30 hits.
PROSITEiPS00010. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q07954-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLTPPLLLLL PLLSALVAAA IDAPKTCSPK QFACRDQITC ISKGWRCDGE
60 70 80 90 100
RDCPDGSDEA PEICPQSKAQ RCQPNEHNCL GTELCVPMSR LCNGVQDCMD
110 120 130 140 150
GSDEGPHCRE LQGNCSRLGC QHHCVPTLDG PTCYCNSSFQ LQADGKTCKD
160 170 180 190 200
FDECSVYGTC SQLCTNTDGS FICGCVEGYL LQPDNRSCKA KNEPVDRPPV
210 220 230 240 250
LLIANSQNIL ATYLSGAQVS TITPTSTRQT TAMDFSYANE TVCWVHVGDS
260 270 280 290 300
AAQTQLKCAR MPGLKGFVDE HTINISLSLH HVEQMAIDWL TGNFYFVDDI
310 320 330 340 350
DDRIFVCNRN GDTCVTLLDL ELYNPKGIAL DPAMGKVFFT DYGQIPKVER
360 370 380 390 400
CDMDGQNRTK LVDSKIVFPH GITLDLVSRL VYWADAYLDY IEVVDYEGKG
410 420 430 440 450
RQTIIQGILI EHLYGLTVFE NYLYATNSDN ANAQQKTSVI RVNRFNSTEY
460 470 480 490 500
QVVTRVDKGG ALHIYHQRRQ PRVRSHACEN DQYGKPGGCS DICLLANSHK
510 520 530 540 550
ARTCRCRSGF SLGSDGKSCK KPEHELFLVY GKGRPGIIRG MDMGAKVPDE
560 570 580 590 600
HMIPIENLMN PRALDFHAET GFIYFADTTS YLIGRQKIDG TERETILKDG
610 620 630 640 650
IHNVEGVAVD WMGDNLYWTD DGPKKTISVA RLEKAAQTRK TLIEGKMTHP
660 670 680 690 700
RAIVVDPLNG WMYWTDWEED PKDSRRGRLE RAWMDGSHRD IFVTSKTVLW
710 720 730 740 750
PNGLSLDIPA GRLYWVDAFY DRIETILLNG TDRKIVYEGP ELNHAFGLCH
760 770 780 790 800
HGNYLFWTEY RSGSVYRLER GVGGAPPTVT LLRSERPPIF EIRMYDAQQQ
810 820 830 840 850
QVGTNKCRVN NGGCSSLCLA TPGSRQCACA EDQVLDADGV TCLANPSYVP
860 870 880 890 900
PPQCQPGEFA CANSRCIQER WKCDGDNDCL DNSDEAPALC HQHTCPSDRF
910 920 930 940 950
KCENNRCIPN RWLCDGDNDC GNSEDESNAT CSARTCPPNQ FSCASGRCIP
960 970 980 990 1000
ISWTCDLDDD CGDRSDESAS CAYPTCFPLT QFTCNNGRCI NINWRCDNDN
1010 1020 1030 1040 1050
DCGDNSDEAG CSHSCSSTQF KCNSGRCIPE HWTCDGDNDC GDYSDETHAN
1060 1070 1080 1090 1100
CTNQATRPPG GCHTDEFQCR LDGLCIPLRW RCDGDTDCMD SSDEKSCEGV
1110 1120 1130 1140 1150
THVCDPSVKF GCKDSARCIS KAWVCDGDND CEDNSDEENC ESLACRPPSH
1160 1170 1180 1190 1200
PCANNTSVCL PPDKLCDGND DCGDGSDEGE LCDQCSLNNG GCSHNCSVAP
1210 1220 1230 1240 1250
GEGIVCSCPL GMELGPDNHT CQIQSYCAKH LKCSQKCDQN KFSVKCSCYE
1260 1270 1280 1290 1300
GWVLEPDGES CRSLDPFKPF IIFSNRHEIR RIDLHKGDYS VLVPGLRNTI
1310 1320 1330 1340 1350
ALDFHLSQSA LYWTDVVEDK IYRGKLLDNG ALTSFEVVIQ YGLATPEGLA
1360 1370 1380 1390 1400
VDWIAGNIYW VESNLDQIEV AKLDGTLRTT LLAGDIEHPR AIALDPRDGI
1410 1420 1430 1440 1450
LFWTDWDASL PRIEAASMSG AGRRTVHRET GSGGWPNGLT VDYLEKRILW
1460 1470 1480 1490 1500
IDARSDAIYS ARYDGSGHME VLRGHEFLSH PFAVTLYGGE VYWTDWRTNT
1510 1520 1530 1540 1550
LAKANKWTGH NVTVVQRTNT QPFDLQVYHP SRQPMAPNPC EANGGQGPCS
1560 1570 1580 1590 1600
HLCLINYNRT VSCACPHLMK LHKDNTTCYE FKKFLLYARQ MEIRGVDLDA
1610 1620 1630 1640 1650
PYYNYIISFT VPDIDNVTVL DYDAREQRVY WSDVRTQAIK RAFINGTGVE
1660 1670 1680 1690 1700
TVVSADLPNA HGLAVDWVSR NLFWTSYDTN KKQINVARLD GSFKNAVVQG
1710 1720 1730 1740 1750
LEQPHGLVVH PLRGKLYWTD GDNISMANMD GSNRTLLFSG QKGPVGLAID
1760 1770 1780 1790 1800
FPESKLYWIS SGNHTINRCN LDGSGLEVID AMRSQLGKAT ALAIMGDKLW
1810 1820 1830 1840 1850
WADQVSEKMG TCSKADGSGS VVLRNSTTLV MHMKVYDESI QLDHKGTNPC
1860 1870 1880 1890 1900
SVNNGDCSQL CLPTSETTRS CMCTAGYSLR SGQQACEGVG SFLLYSVHEG
1910 1920 1930 1940 1950
IRGIPLDPND KSDALVPVSG TSLAVGIDFH AENDTIYWVD MGLSTISRAK
1960 1970 1980 1990 2000
RDQTWREDVV TNGIGRVEGI AVDWIAGNIY WTDQGFDVIE VARLNGSFRY
2010 2020 2030 2040 2050
VVISQGLDKP RAITVHPEKG YLFWTEWGQY PRIERSRLDG TERVVLVNVS
2060 2070 2080 2090 2100
ISWPNGISVD YQDGKLYWCD ARTDKIERID LETGENREVV LSSNNMDMFS
2110 2120 2130 2140 2150
VSVFEDFIYW SDRTHANGSI KRGSKDNATD SVPLRTGIGV QLKDIKVFNR
2160 2170 2180 2190 2200
DRQKGTNVCA VANGGCQQLC LYRGRGQRAC ACAHGMLAED GASCREYAGY
2210 2220 2230 2240 2250
LLYSERTILK SIHLSDERNL NAPVQPFEDP EHMKNVIALA FDYRAGTSPG
2260 2270 2280 2290 2300
TPNRIFFSDI HFGNIQQIND DGSRRITIVE NVGSVEGLAY HRGWDTLYWT
2310 2320 2330 2340 2350
SYTTSTITRH TVDQTRPGAF ERETVITMSG DDHPRAFVLD ECQNLMFWTN
2360 2370 2380 2390 2400
WNEQHPSIMR AALSGANVLT LIEKDIRTPN GLAIDHRAEK LYFSDATLDK
2410 2420 2430 2440 2450
IERCEYDGSH RYVILKSEPV HPFGLAVYGE HIFWTDWVRR AVQRANKHVG
2460 2470 2480 2490 2500
SNMKLLRVDI PQQPMGIIAV ANDTNSCELS PCRINNGGCQ DLCLLTHQGH
2510 2520 2530 2540 2550
VNCSCRGGRI LQDDLTCRAV NSSCRAQDEF ECANGECINF SLTCDGVPHC
2560 2570 2580 2590 2600
KDKSDEKPSY CNSRRCKKTF RQCSNGRCVS NMLWCNGADD CGDGSDEIPC
2610 2620 2630 2640 2650
NKTACGVGEF RCRDGTCIGN SSRCNQFVDC EDASDEMNCS ATDCSSYFRL
2660 2670 2680 2690 2700
GVKGVLFQPC ERTSLCYAPS WVCDGANDCG DYSDERDCPG VKRPRCPLNY
2710 2720 2730 2740 2750
FACPSGRCIP MSWTCDKEDD CEHGEDETHC NKFCSEAQFE CQNHRCISKQ
2760 2770 2780 2790 2800
WLCDGSDDCG DGSDEAAHCE GKTCGPSSFS CPGTHVCVPE RWLCDGDKDC
2810 2820 2830 2840 2850
ADGADESIAA GCLYNSTCDD REFMCQNRQC IPKHFVCDHD RDCADGSDES
2860 2870 2880 2890 2900
PECEYPTCGP SEFRCANGRC LSSRQWECDG ENDCHDQSDE APKNPHCTSQ
2910 2920 2930 2940 2950
EHKCNASSQF LCSSGRCVAE ALLCNGQDDC GDSSDERGCH INECLSRKLS
2960 2970 2980 2990 3000
GCSQDCEDLK IGFKCRCRPG FRLKDDGRTC ADVDECSTTF PCSQRCINTH
3010 3020 3030 3040 3050
GSYKCLCVEG YAPRGGDPHS CKAVTDEEPF LIFANRYYLR KLNLDGSNYT
3060 3070 3080 3090 3100
LLKQGLNNAV ALDFDYREQM IYWTDVTTQG SMIRRMHLNG SNVQVLHRTG
3110 3120 3130 3140 3150
LSNPDGLAVD WVGGNLYWCD KGRDTIEVSK LNGAYRTVLV SSGLREPRAL
3160 3170 3180 3190 3200
VVDVQNGYLY WTDWGDHSLI GRIGMDGSSR SVIVDTKITW PNGLTLDYVT
3210 3220 3230 3240 3250
ERIYWADARE DYIEFASLDG SNRHVVLSQD IPHIFALTLF EDYVYWTDWE
3260 3270 3280 3290 3300
TKSINRAHKT TGTNKTLLIS TLHRPMDLHV FHALRQPDVP NHPCKVNNGG
3310 3320 3330 3340 3350
CSNLCLLSPG GGHKCACPTN FYLGSDGRTC VSNCTASQFV CKNDKCIPFW
3360 3370 3380 3390 3400
WKCDTEDDCG DHSDEPPDCP EFKCRPGQFQ CSTGICTNPA FICDGDNDCQ
3410 3420 3430 3440 3450
DNSDEANCDI HVCLPSQFKC TNTNRCIPGI FRCNGQDNCG DGEDERDCPE
3460 3470 3480 3490 3500
VTCAPNQFQC SITKRCIPRV WVCDRDNDCV DGSDEPANCT QMTCGVDEFR
3510 3520 3530 3540 3550
CKDSGRCIPA RWKCDGEDDC GDGSDEPKEE CDERTCEPYQ FRCKNNRCVP
3560 3570 3580 3590 3600
GRWQCDYDND CGDNSDEESC TPRPCSESEF SCANGRCIAG RWKCDGDHDC
3610 3620 3630 3640 3650
ADGSDEKDCT PRCDMDQFQC KSGHCIPLRW RCDADADCMD GSDEEACGTG
3660 3670 3680 3690 3700
VRTCPLDEFQ CNNTLCKPLA WKCDGEDDCG DNSDENPEEC ARFVCPPNRP
3710 3720 3730 3740 3750
FRCKNDRVCL WIGRQCDGTD NCGDGTDEED CEPPTAHTTH CKDKKEFLCR
3760 3770 3780 3790 3800
NQRCLSSSLR CNMFDDCGDG SDEEDCSIDP KLTSCATNAS ICGDEARCVR
3810 3820 3830 3840 3850
TEKAAYCACR SGFHTVPGQP GCQDINECLR FGTCSQLCNN TKGGHLCSCA
3860 3870 3880 3890 3900
RNFMKTHNTC KAEGSEYQVL YIADDNEIRS LFPGHPHSAY EQAFQGDESV
3910 3920 3930 3940 3950
RIDAMDVHVK AGRVYWTNWH TGTISYRSLP PAAPPTTSNR HRRQIDRGVT
3960 3970 3980 3990 4000
HLNISGLKMP RGIAIDWVAG NVYWTDSGRD VIEVAQMKGE NRKTLISGMI
4010 4020 4030 4040 4050
DEPHAIVVDP LRGTMYWSDW GNHPKIETAA MDGTLRETLV QDNIQWPTGL
4060 4070 4080 4090 4100
AVDYHNERLY WADAKLSVIG SIRLNGTDPI VAADSKRGLS HPFSIDVFED
4110 4120 4130 4140 4150
YIYGVTYINN RVFKIHKFGH SPLVNLTGGL SHASDVVLYH QHKQPEVTNP
4160 4170 4180 4190 4200
CDRKKCEWLC LLSPSGPVCT CPNGKRLDNG TCVPVPSPTP PPDAPRPGTC
4210 4220 4230 4240 4250
NLQCFNGGSC FLNARRQPKC RCQPRYTGDK CELDQCWEHC RNGGTCAASP
4260 4270 4280 4290 4300
SGMPTCRCPT GFTGPKCTQQ VCAGYCANNS TCTVNQGNQP QCRCLPGFLG
4310 4320 4330 4340 4350
DRCQYRQCSG YCENFGTCQM AADGSRQCRC TAYFEGSRCE VNKCSRCLEG
4360 4370 4380 4390 4400
ACVVNKQSGD VTCNCTDGRV APSCLTCVGH CSNGGSCTMN SKMMPECQCP
4410 4420 4430 4440 4450
PHMTGPRCEE HVFSQQQPGH IASILIPLLL LLLLVLVAGV VFWYKRRVQG
4460 4470 4480 4490 4500
AKGFQHQRMT NGAMNVEIGN PTYKMYEGGE PDDVGGLLDA DFALDPDKPT
4510 4520 4530 4540
NFTNPVYATL YMGGHGSRHS LASTDEKREL LGRGPEDEIG DPLA
Length:4,544
Mass (Da):504,606
Last modified:January 11, 2011 - v2
Checksum:i5A11CC02FAB127BE
GO
Isoform 2 (identifier: Q07954-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     281-292: HVEQMAIDWLTG → LCVFSKSQQEMG
     293-4544: Missing.

Note: No experimental confirmation available

Show »
Length:292
Mass (Da):31,631
Checksum:i82C39315F1ECEE24
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti685 – 6851D → G AA sequence (PubMed:1698775)Curated
Sequence conflicti1743 – 17431G → S AA sequence (PubMed:1698775)Curated
Sequence conflicti2871 – 28722LS → IA AA sequence (PubMed:1698775)Curated
Sequence conflicti3036 – 30361R → M AA sequence (PubMed:1698775)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti166 – 1661N → D.
Corresponds to variant rs2306691 [ dbSNP | Ensembl ].
VAR_021885
Natural varianti217 – 2171A → V.
Corresponds to variant rs1800127 [ dbSNP | Ensembl ].
VAR_014725
Natural varianti869 – 8691E → K in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035994
Natural varianti2059 – 20591V → L.
Corresponds to variant rs2229278 [ dbSNP | Ensembl ].
VAR_029181
Natural varianti2080 – 20801D → N.
Corresponds to variant rs34577247 [ dbSNP | Ensembl ].
VAR_047525
Natural varianti2900 – 29001Q → P.3 Publications
Corresponds to variant rs7397167 [ dbSNP | Ensembl ].
VAR_047526
Natural varianti3258 – 32581H → Q Found in a patient with severe mental retardation, seizures, stereotypic behavior, high pain threshold and sleep disturbances. 1 Publication
VAR_069388
Natural varianti3760 – 37601R → H in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035995
Natural varianti4536 – 45361E → G.
Corresponds to variant rs17357542 [ dbSNP | Ensembl ].
VAR_047527

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei281 – 29212HVEQM…DWLTG → LCVFSKSQQEMG in isoform 2. 1 PublicationVSP_056919Add
BLAST
Alternative sequencei293 – 45444252Missing in isoform 2. 1 PublicationVSP_056920Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
BC045107 mRNA. Translation: AAH45107.1.
X15424 Genomic DNA. Translation: CAA33464.1.
Y18524 Genomic DNA. Translation: CAD57169.1.
CCDSiCCDS8932.1.
PIRiS02392.
RefSeqiNP_002323.2. NM_002332.2.
UniGeneiHs.162757.

Genome annotation databases

EnsembliENST00000243077; ENSP00000243077; ENSG00000123384.
GeneIDi4035.
KEGGihsa:4035.
UCSCiuc001snd.3. human.

Polymorphism databases

DMDMi317373384.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
BC045107 mRNA. Translation: AAH45107.1 .
X15424 Genomic DNA. Translation: CAA33464.1 .
Y18524 Genomic DNA. Translation: CAD57169.1 .
CCDSi CCDS8932.1.
PIRi S02392.
RefSeqi NP_002323.2. NM_002332.2.
UniGenei Hs.162757.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CR8 NMR - A 1059-1100 [» ]
1D2L NMR - A 851-893 [» ]
1J8E X-ray 1.85 A 1011-1054 [» ]
2FYJ NMR - A 932-1013 [» ]
2FYL NMR - B 932-1013 [» ]
2KNX NMR - A 2770-2817 [» ]
2KNY NMR - A 2770-2817 [» ]
ProteinModelPortali Q07954.
SMRi Q07954. Positions 851-893, 932-1054, 1059-1100, 2770-2815, 2856-2896, 3571-3606.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110215. 54 interactions.
DIPi DIP-50613N.
IntActi Q07954. 18 interactions.
MINTi MINT-5004471.

Chemistry

DrugBanki DB00025. Antihemophilic Factor.
DB00100. Coagulation Factor IX.
DB00031. Tenecteplase.

PTM databases

PhosphoSitei Q07954.

Polymorphism databases

DMDMi 317373384.

Proteomic databases

MaxQBi Q07954.
PaxDbi Q07954.
PRIDEi Q07954.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000243077 ; ENSP00000243077 ; ENSG00000123384 .
GeneIDi 4035.
KEGGi hsa:4035.
UCSCi uc001snd.3. human.

Organism-specific databases

CTDi 4035.
GeneCardsi GC12P057497.
HGNCi HGNC:6692. LRP1.
HPAi CAB018621.
HPA004182.
HPA022903.
MIMi 107770. gene.
neXtProti NX_Q07954.
PharmGKBi PA233.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG235850.
GeneTreei ENSGT00760000119194.
HOGENOMi HOG000230574.
HOVERGENi HBG006292.
InParanoidi Q07954.
KOi K04550.
OMAi AYFEGPR.
OrthoDBi EOG790FZT.
PhylomeDBi Q07954.
TreeFami TF315253.

Enzyme and pathway databases

Reactomei REACT_160163. Scavenging of heme from plasma.
REACT_24968. Retinoid metabolism and transport.

Miscellaneous databases

ChiTaRSi LRP1. human.
EvolutionaryTracei Q07954.
GeneWikii LRP1.
GenomeRNAii 4035.
NextBioi 15806.
PROi Q07954.
SOURCEi Search...

Gene expression databases

Bgeei Q07954.
CleanExi HS_LRP1.
ExpressionAtlasi Q07954. baseline and differential.
Genevestigatori Q07954.

Family and domain databases

Gene3Di 2.120.10.30. 8 hits.
4.10.400.10. 29 hits.
InterProi IPR011042. 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 ]
Pfami PF12662. cEGF. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view ]
PRINTSi PR00261. LDLRECEPTOR.
SMARTi SM00181. EGF. 18 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 35 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 9 hits.
SSF57424. SSF57424. 30 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Skin.
  7. "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.
  8. Glaeser C.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
    Tissue: Blood.
  9. "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]
    Tissue: Placenta.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "LDL receptor-related proteins in neurodevelopment."
    May P., Herz J.
    Traffic 4:291-301(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. Cited for: GLYCOSYLATION AT ASN-729 AND ASN-1511.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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.
  26. "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.
  27. "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.
  28. "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.
  29. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-869 AND HIS-3760.
  30. Cited for: VARIANT GLN-3258.

Entry informationi

Entry nameiLRP1_HUMAN
AccessioniPrimary (citable) accession number: Q07954
Secondary accession number(s): Q2PP12, Q86SW0, Q8IVG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3