UniProtKB - Q07954 (LRP1_HUMAN)
Prolow-density lipoprotein receptor-related protein 1
LRP1
Functioni
Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells (PubMed:11907044, PubMed:12713657).
Required for early embryonic development (By similarity).
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. Acts as an LRPAP1 alpha-2-macroglobulin receptor (PubMed:26142438, PubMed:1702392).
Acts as TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as its subsequent spread (PubMed:32296178).
May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (PubMed:12888553).
By similarity6 Publications(Microbial infection) Functions as a receptor for Pseudomonas aeruginosa exotoxin A.
1 PublicationSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 871 | Calcium 1; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 874 | Calcium 11 Publication | 1 | |
Metal bindingi | 876 | Calcium 1; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 878 | Calcium 11 Publication | 1 | |
Metal bindingi | 884 | Calcium 11 Publication | 1 | |
Metal bindingi | 885 | Calcium 11 Publication | 1 | |
Metal bindingi | 1032 | Calcium 2; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 1035 | Calcium 21 Publication | 1 | |
Metal bindingi | 1037 | Calcium 2; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 1039 | Calcium 21 Publication | 1 | |
Metal bindingi | 1045 | Calcium 21 Publication | 1 | |
Metal bindingi | 1046 | Calcium 21 Publication | 1 | |
Metal bindingi | 1080 | Calcium 3; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 1083 | Calcium 31 Publication | 1 | |
Metal bindingi | 1085 | Calcium 3; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 1087 | Calcium 31 Publication | 1 | |
Metal bindingi | 1093 | Calcium 31 Publication | 1 | |
Metal bindingi | 1094 | Calcium 31 Publication | 1 |
GO - Molecular functioni
- alpha-2 macroglobulin receptor activity Source: UniProtKB
- amyloid-beta binding Source: ARUK-UCL
- apolipoprotein binding Source: UniProtKB
- apolipoprotein receptor activity Source: ARUK-UCL
- calcium ion binding Source: UniProtKB
- cargo receptor activity Source: ARUK-UCL
- clathrin heavy chain binding Source: ARUK-UCL
- heparan sulfate proteoglycan binding Source: ARUK-UCL
- lipoprotein particle receptor binding Source: BHF-UCL
- low-density lipoprotein particle receptor activity Source: ARUK-UCL
- protein-containing complex binding Source: BHF-UCL
- RNA binding Source: UniProtKB
- scavenger receptor activity Source: ARUK-UCL
- signaling receptor activity Source: ProtInc
GO - Biological processi
- amyloid-beta clearance Source: BHF-UCL
- amyloid-beta clearance by cellular catabolic process Source: ARUK-UCL
- amyloid-beta clearance by transcytosis Source: ARUK-UCL
- aorta morphogenesis Source: BHF-UCL
- apoptotic cell clearance Source: BHF-UCL
- astrocyte activation involved in immune response Source: ARUK-UCL
- cellular response to amyloid-beta Source: ARUK-UCL
- enzyme linked receptor protein signaling pathway Source: BHF-UCL
- lipid metabolic process Source: ARUK-UCL
- lipoprotein transport Source: UniProtKB
- lysosomal transport Source: UniProtKB
- negative regulation of gene expression Source: BHF-UCL
- negative regulation of metallopeptidase activity Source: ARUK-UCL
- negative regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
- negative regulation of platelet-derived growth factor receptor-beta signaling pathway Source: BHF-UCL
- negative regulation of SMAD protein signal transduction Source: BHF-UCL
- negative regulation of smooth muscle cell migration Source: BHF-UCL
- negative regulation of Wnt signaling pathway Source: BHF-UCL
- phagocytosis Source: ARUK-UCL
- positive regulation of amyloid-beta clearance Source: ARUK-UCL
- positive regulation of cell death Source: ARUK-UCL
- positive regulation of cholesterol efflux Source: BHF-UCL
- positive regulation of endocytosis Source: ARUK-UCL
- positive regulation of lipid transport Source: BHF-UCL
- positive regulation of lysosomal protein catabolic process Source: ARUK-UCL
- positive regulation of protein binding Source: ARUK-UCL
- positive regulation of protein localization to plasma membrane Source: ARUK-UCL
- positive regulation of transcytosis Source: ARUK-UCL
- receptor internalization Source: ComplexPortal
- receptor-mediated endocytosis Source: ARUK-UCL
- regulation of actin cytoskeleton organization Source: BHF-UCL
- regulation of cholesterol transport Source: BHF-UCL
- regulation of extracellular matrix disassembly Source: ParkinsonsUK-UCL
- regulation of phospholipase A2 activity Source: BHF-UCL
- retinoid metabolic process Source: Reactome
- transcytosis Source: ARUK-UCL
- transport across blood-brain barrier Source: ARUK-UCL
Keywordsi
Molecular function | Developmental protein, Receptor |
Biological process | Endocytosis |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
PathwayCommonsi | Q07954 |
Reactomei | R-HSA-2168880, Scavenging of heme from plasma R-HSA-975634, Retinoid metabolism and transport |
SignaLinki | Q07954 |
SIGNORi | Q07954 |
Protein family/group databases
TCDBi | 9.B.87.1.16, the selenoprotein p receptor (selp-receptor) family |
Names & Taxonomyi
Protein namesi | Recommended name: Prolow-density lipoprotein receptor-related protein 1CuratedShort name: LRP-1 Alternative name(s): Alpha-2-macroglobulin receptor1 Publication Short name: A2MR Apolipoprotein E receptor Short name: APOER CD_antigen: CD91 Cleaved into the following 3 chains: |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:6692, LRP1 |
MIMi | 107770, gene |
neXtProti | NX_Q07954 |
VEuPathDBi | HostDB:ENSG00000123384 |
Subcellular locationi
Plasma membrane
Other locations
Plasma membrane
Other locations
Cytoskeleton
- microtubule organizing center By similarity
Golgi apparatus
- Golgi outpost By similarity
Note: Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation.By similarity
Cytoskeleton
- cytoskeleton Source: UniProtKB-SubCell
Endosome
- early endosome Source: ARUK-UCL
Golgi apparatus
- Golgi apparatus Source: UniProtKB-KW
Lysosome
- lysosomal membrane Source: UniProtKB
Nucleus
- nucleus Source: UniProtKB-SubCell
Plasma Membrane
- basolateral plasma membrane Source: ARUK-UCL
- clathrin-coated pit Source: UniProtKB-KW
- integral component of plasma membrane Source: UniProtKB
- low-density lipoprotein receptor complex Source: ComplexPortal
- plasma membrane Source: GO_Central
- plasma membrane protein complex Source: ARUK-UCL
Other locations
- endocytic vesicle membrane Source: Reactome
- focal adhesion Source: UniProtKB
- membrane Source: ARUK-UCL
- receptor complex Source: MGI
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 20 – 4419 | ExtracellularSequence analysisAdd BLAST | 4400 | |
Transmembranei | 4420 – 4444 | HelicalSequence analysisAdd BLAST | 25 | |
Topological domaini | 4445 – 4544 | CytoplasmicSequence analysisAdd BLAST | 100 |
Keywords - Cellular componenti
Cell membrane, Coated pit, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, NucleusPathology & Biotechi
Involvement in diseasei
Keratosis pilaris atrophicans (KPA)1 Publication
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_077982 | 1245 | K → R in KPA; reduced alpha-2 macroglobulin receptor activity; reduced protein abundance. 1 PublicationCorresponds to variant dbSNP:rs483353013EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 4460 | T → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4517; A-4520 and A-4523. 1 Publication | 1 | |
Mutagenesisi | 4470 – 4473 | NPTY → APTA: No effect on tyrosine phosphorylation. 1 Publication | 4 | |
Mutagenesisi | 4470 | N → A: No effect on interaction with GULP1. 1 Publication | 1 | |
Mutagenesisi | 4472 | T → A: No detectable effect on phosphorylation. 1 Publication | 1 | |
Mutagenesisi | 4504 – 4507 | NPVY → APVA: Loss of tyrosine phosphorylation. Abolishes interaction with SHC1 and GULP1. 1 Publication | 4 | |
Mutagenesisi | 4504 | N → A: Loss of interaction with GULP1. 1 Publication | 1 | |
Mutagenesisi | 4517 | S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4520 and A-4523. 1 Publication | 1 | |
Mutagenesisi | 4520 | S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4523. 1 Publication | 1 | |
Mutagenesisi | 4523 | S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4520. 1 Publication | 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNETi | 4035 |
MalaCardsi | LRP1 |
MIMi | 604093, phenotype |
OpenTargetsi | ENSG00000123384 |
Orphaneti | 79100, Atrophoderma vermiculata 2340, Keratosis follicularis spinulosa decalvans |
PharmGKBi | PA233 |
Miscellaneous databases
Pharosi | Q07954, Tbio |
Chemistry databases
ChEMBLi | CHEMBL4630884 |
DrugBanki | DB00025, Antihemophilic factor, human recombinant DB00100, Coagulation Factor IX (Recombinant) DB13152, Coagulation Factor IX Human DB06245, Lanoteplase DB13998, Lonoctocog alfa DB13999, Moroctocog alfa DB00031, Tenecteplase |
Genetic variation databases
BioMutai | LRP1 |
DMDMi | 317373384 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 19 | Sequence analysisAdd BLAST | 19 | |
ChainiPRO_0000017317 | 20 – 4544 | Prolow-density lipoprotein receptor-related protein 1Add BLAST | 4525 | |
ChainiPRO_0000302750 | 20 – ?3943 | Low-density lipoprotein receptor-related protein 1 515 kDa subunitAdd BLAST | 3924 | |
ChainiPRO_0000302751 | ?3944 – 4544 | Low-density lipoprotein receptor-related protein 1 85 kDa subunitAdd BLAST | 601 | |
ChainiPRO_0000302752 | ?4441 – 4544 | Low-density lipoprotein receptor-related protein 1 intracellular domainAdd BLAST | 104 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 27 ↔ 40 | By similarity | ||
Disulfide bondi | 34 ↔ 53 | By similarity | ||
Disulfide bondi | 47 ↔ 64 | By similarity | ||
Disulfide bondi | 72 ↔ 85 | By similarity | ||
Disulfide bondi | 79 ↔ 98 | By similarity | ||
Disulfide bondi | 92 ↔ 108 | By similarity | ||
Glycosylationi | 114 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 115 ↔ 124 | By similarity | ||
Disulfide bondi | 120 ↔ 133 | By similarity | ||
Disulfide bondi | 135 ↔ 148 | By similarity | ||
Glycosylationi | 136 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 154 ↔ 164 | By similarity | ||
Disulfide bondi | 160 ↔ 173 | By similarity | ||
Disulfide bondi | 175 ↔ 188 | By similarity | ||
Glycosylationi | 185 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 239 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 274 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 357 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 446 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Disulfide bondi | 478 ↔ 493 | By similarity | ||
Disulfide bondi | 489 ↔ 504 | By similarity | ||
Disulfide bondi | 506 ↔ 519 | By similarity | ||
Glycosylationi | 729 | N-linked (GlcNAc...) (complex) asparagine3 Publications | 1 | |
Disulfide bondi | 807 ↔ 818 | By similarity | ||
Disulfide bondi | 814 ↔ 827 | By similarity | ||
Disulfide bondi | 829 ↔ 842 | By similarity | ||
Disulfide bondi | 854 ↔ 866 | |||
Disulfide bondi | 861 ↔ 879 | |||
Disulfide bondi | 873 ↔ 890 | |||
Disulfide bondi | 895 ↔ 907 | By similarity | ||
Disulfide bondi | 902 ↔ 920 | By similarity | ||
Disulfide bondi | 914 ↔ 931 | By similarity | ||
Glycosylationi | 928 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 936 ↔ 948 | |||
Disulfide bondi | 943 ↔ 961 | |||
Disulfide bondi | 955 ↔ 971 | |||
Disulfide bondi | 976 ↔ 989 | |||
Disulfide bondi | 984 ↔ 1002 | |||
Disulfide bondi | 996 ↔ 1011 | |||
Disulfide bondi | 1015 ↔ 1027 | |||
Disulfide bondi | 1022 ↔ 1040 | |||
Disulfide bondi | 1034 ↔ 1051 | |||
Glycosylationi | 1050 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1062 ↔ 1075 | |||
Disulfide bondi | 1069 ↔ 1088 | |||
Disulfide bondi | 1082 ↔ 1097 | |||
Disulfide bondi | 1104 ↔ 1118 | By similarity | ||
Disulfide bondi | 1112 ↔ 1131 | By similarity | ||
Disulfide bondi | 1125 ↔ 1140 | By similarity | ||
Disulfide bondi | 1145 ↔ 1159 | By similarity | ||
Disulfide bondi | 1152 ↔ 1172 | By similarity | ||
Glycosylationi | 1154 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1155 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1166 ↔ 1182 | By similarity | ||
Disulfide bondi | 1185 ↔ 1196 | By similarity | ||
Disulfide bondi | 1192 ↔ 1206 | By similarity | ||
Glycosylationi | 1195 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1208 ↔ 1221 | By similarity | ||
Glycosylationi | 1218 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1227 ↔ 1237 | By similarity | ||
Disulfide bondi | 1233 ↔ 1246 | By similarity | ||
Disulfide bondi | 1248 ↔ 1261 | By similarity | ||
Glycosylationi | 1511 | N-linked (GlcNAc...) (complex) asparagine2 Publications | 1 | |
Disulfide bondi | 1540 ↔ 1553 | By similarity | ||
Disulfide bondi | 1549 ↔ 1563 | By similarity | ||
Glycosylationi | 1558 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1565 ↔ 1578 | By similarity | ||
Glycosylationi | 1575 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 1616 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 1645 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 1723 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1733 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1763 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 1825 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1850 ↔ 1861 | By similarity | ||
Disulfide bondi | 1857 ↔ 1871 | By similarity | ||
Disulfide bondi | 1873 ↔ 1886 | By similarity | ||
Glycosylationi | 1933 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1995 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 2009 | N6-acetyllysineBy similarity | 1 | |
Glycosylationi | 2048 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2117 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2127 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Disulfide bondi | 2159 ↔ 2170 | By similarity | ||
Disulfide bondi | 2166 ↔ 2180 | By similarity | ||
Disulfide bondi | 2182 ↔ 2194 | By similarity | ||
Glycosylationi | 2472 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2482 ↔ 2493 | By similarity | ||
Disulfide bondi | 2489 ↔ 2503 | By similarity | ||
Glycosylationi | 2502 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2505 ↔ 2517 | By similarity | ||
Glycosylationi | 2521 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2524 ↔ 2537 | By similarity | ||
Disulfide bondi | 2532 ↔ 2550 | By similarity | ||
Glycosylationi | 2539 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2544 ↔ 2561 | By similarity | ||
Disulfide bondi | 2566 ↔ 2578 | By similarity | ||
Disulfide bondi | 2573 ↔ 2591 | By similarity | ||
Disulfide bondi | 2585 ↔ 2600 | By similarity | ||
Glycosylationi | 2601 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2605 ↔ 2617 | By similarity | ||
Disulfide bondi | 2612 ↔ 2630 | By similarity | ||
Glycosylationi | 2620 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2624 ↔ 2639 | By similarity | ||
Glycosylationi | 2638 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2644 ↔ 2666 | By similarity | ||
Disulfide bondi | 2660 ↔ 2679 | By similarity | ||
Disulfide bondi | 2673 ↔ 2688 | By similarity | ||
Disulfide bondi | 2696 ↔ 2708 | By similarity | ||
Disulfide bondi | 2703 ↔ 2721 | By similarity | ||
Disulfide bondi | 2715 ↔ 2730 | By similarity | ||
Disulfide bondi | 2734 ↔ 2746 | By similarity | ||
Disulfide bondi | 2741 ↔ 2759 | By similarity | ||
Disulfide bondi | 2753 ↔ 2769 | By similarity | ||
Disulfide bondi | 2774 ↔ 2787 | By similarity | ||
Disulfide bondi | 2781 ↔ 2800 | By similarity | ||
Disulfide bondi | 2794 ↔ 2812 | By similarity | ||
Glycosylationi | 2815 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 2818 ↔ 2830 | By similarity | ||
Disulfide bondi | 2825 ↔ 2843 | By similarity | ||
Disulfide bondi | 2837 ↔ 2853 | By similarity | ||
Disulfide bondi | 2858 ↔ 2870 | By similarity | ||
Disulfide bondi | 2865 ↔ 2884 | By similarity | ||
Disulfide bondi | 2878 ↔ 2897 | By similarity | ||
Disulfide bondi | 2904 ↔ 2917 | By similarity | ||
Glycosylationi | 2905 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2912 ↔ 2930 | By similarity | ||
Disulfide bondi | 2924 ↔ 2939 | By similarity | ||
Disulfide bondi | 2944 ↔ 2956 | By similarity | ||
Disulfide bondi | 2952 ↔ 2965 | By similarity | ||
Disulfide bondi | 2967 ↔ 2980 | By similarity | ||
Disulfide bondi | 2986 ↔ 2996 | By similarity | ||
Disulfide bondi | 2992 ↔ 3005 | By similarity | ||
Disulfide bondi | 3007 ↔ 3021 | By similarity | ||
Glycosylationi | 3048 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Glycosylationi | 3089 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 3264 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3294 ↔ 3305 | By similarity | ||
Disulfide bondi | 3301 ↔ 3315 | By similarity | ||
Disulfide bondi | 3317 ↔ 3330 | By similarity | ||
Glycosylationi | 3333 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3334 ↔ 3346 | By similarity | ||
Disulfide bondi | 3341 ↔ 3359 | By similarity | ||
Disulfide bondi | 3353 ↔ 3369 | By similarity | ||
Disulfide bondi | 3374 ↔ 3386 | By similarity | ||
Disulfide bondi | 3381 ↔ 3399 | By similarity | ||
Disulfide bondi | 3393 ↔ 3408 | By similarity | ||
Disulfide bondi | 3413 ↔ 3426 | By similarity | ||
Disulfide bondi | 3420 ↔ 3439 | By similarity | ||
Disulfide bondi | 3433 ↔ 3448 | By similarity | ||
Disulfide bondi | 3453 ↔ 3466 | By similarity | ||
Disulfide bondi | 3460 ↔ 3479 | By similarity | ||
Disulfide bondi | 3473 ↔ 3489 | By similarity | ||
Glycosylationi | 3488 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 3494 ↔ 3507 | By similarity | ||
Disulfide bondi | 3501 ↔ 3520 | By similarity | ||
Disulfide bondi | 3514 ↔ 3531 | By similarity | ||
Disulfide bondi | 3536 ↔ 3548 | By similarity | ||
Disulfide bondi | 3543 ↔ 3561 | By similarity | ||
Disulfide bondi | 3555 ↔ 3570 | By similarity | ||
Disulfide bondi | 3575 ↔ 3587 | By similarity | ||
Disulfide bondi | 3582 ↔ 3600 | By similarity | ||
Disulfide bondi | 3594 ↔ 3609 | By similarity | ||
Disulfide bondi | 3613 ↔ 3625 | By similarity | ||
Disulfide bondi | 3620 ↔ 3638 | By similarity | ||
Disulfide bondi | 3632 ↔ 3647 | By similarity | ||
Disulfide bondi | 3654 ↔ 3666 | By similarity | ||
Disulfide bondi | 3661 ↔ 3679 | By similarity | ||
Glycosylationi | 3662 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3673 ↔ 3690 | By similarity | ||
Disulfide bondi | 3695 ↔ 3709 | By similarity | ||
Disulfide bondi | 3703 ↔ 3722 | By similarity | ||
Disulfide bondi | 3716 ↔ 3731 | By similarity | ||
Disulfide bondi | 3741 ↔ 3754 | By similarity | ||
Disulfide bondi | 3749 ↔ 3767 | By similarity | ||
Disulfide bondi | 3761 ↔ 3776 | By similarity | ||
Disulfide bondi | 3785 ↔ 3798 | By similarity | ||
Glycosylationi | 3788 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 3792 ↔ 3807 | By similarity | ||
Disulfide bondi | 3809 ↔ 3822 | By similarity | ||
Disulfide bondi | 3828 ↔ 3838 | By similarity | ||
Disulfide bondi | 3834 ↔ 3847 | By similarity | ||
Glycosylationi | 3839 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3849 ↔ 3860 | By similarity | ||
Glycosylationi | 3953 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 4075 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 4125 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 4151 ↔ 4160 | By similarity | ||
Disulfide bondi | 4156 ↔ 4169 | By similarity | ||
Disulfide bondi | 4171 ↔ 4182 | By similarity | ||
Glycosylationi | 4179 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 4200 ↔ 4210 | By similarity | ||
Disulfide bondi | 4204 ↔ 4220 | By similarity | ||
Disulfide bondi | 4222 ↔ 4231 | By similarity | ||
Disulfide bondi | 4236 ↔ 4246 | By similarity | ||
Disulfide bondi | 4240 ↔ 4256 | By similarity | ||
Disulfide bondi | 4258 ↔ 4267 | By similarity | ||
Disulfide bondi | 4272 ↔ 4282 | By similarity | ||
Disulfide bondi | 4276 ↔ 4292 | By similarity | ||
Glycosylationi | 4278 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 4279 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 4294 ↔ 4303 | By similarity | ||
Disulfide bondi | 4308 ↔ 4318 | By similarity | ||
Disulfide bondi | 4312 ↔ 4328 | By similarity | ||
Disulfide bondi | 4330 ↔ 4339 | By similarity | ||
Disulfide bondi | 4344 ↔ 4352 | By similarity | ||
Disulfide bondi | 4347 ↔ 4363 | By similarity | ||
Glycosylationi | 4364 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 4365 ↔ 4374 | By similarity | ||
Disulfide bondi | 4377 ↔ 4387 | By similarity | ||
Disulfide bondi | 4381 ↔ 4397 | By similarity | ||
Disulfide bondi | 4399 ↔ 4408 | By similarity | ||
Modified residuei | 4460 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 4507 | Phosphotyrosine1 Publication | 1 | |
Modified residuei | 4517 | Phosphoserine1 Publication | 1 | |
Modified residuei | 4520 | PhosphoserineCombined sources | 1 | |
Modified residuei | 4523 | Phosphoserine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
CPTACi | CPTAC-1617 CPTAC-2222 CPTAC-2223 |
EPDi | Q07954 |
jPOSTi | Q07954 |
MassIVEi | Q07954 |
MaxQBi | Q07954 |
PaxDbi | Q07954 |
PeptideAtlasi | Q07954 |
PRIDEi | Q07954 |
ProteomicsDBi | 58559 [Q07954-1] 69639 |
PTM databases
CarbonylDBi | Q07954 |
GlyConnecti | 1638, 61 N-Linked glycans (38 sites), 1 O-Linked glycan (1 site) |
GlyGeni | Q07954, 74 sites, 62 N-linked glycans (36 sites), 3 O-linked glycans (13 sites) |
iPTMneti | Q07954 |
MetOSitei | Q07954 |
PhosphoSitePlusi | Q07954 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000123384, Expressed in stromal cell of endometrium and 241 other tissues |
ExpressionAtlasi | Q07954, baseline and differential |
Genevisiblei | Q07954, HS |
Organism-specific databases
HPAi | ENSG00000123384, Tissue enhanced (adipose) |
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 (PubMed:17124247).
Interacts with SNX17, PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with SHC1, GULP1 and DAB1. Can weakly interact (via NPXY motif) with DAB2 (via PID domain); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif.
Interacts with MDK; promotes neuronal survival (PubMed:10772929).
Interacts with LRPAP1; this interaction is followed by rapid internalization (PubMed:15053742, PubMed:32296178, PubMed:16938309).
Interacts with uPA/PLAU and PAI1/SERPINE1, either individually or in complex with each other, leading to rapid endocytosis; this interaction is abolished in the presence of LRPAP1/RAP (PubMed:15053742).
Also interacts with tPA/PLAT alone or in complex with SERPINE1 (PubMed:15053742).
Interacts with the urokinase receptor PLAUR; this interaction leads to PLAUR internalization and is impaired in the presence of SORL1 (PubMed:14764453).
Interacts with PDGFB (PubMed:15053742).
Interacts with TAU/MAPT, leading to endocytosis; this interaction is reduced in the presence of LRPAP1/RAP (PubMed:32296178).
By similarity10 Publications(Microbial infection) Interacts with bacterial exotoxins.
1 PublicationBinary interactionsi
Q07954
Isoform 2 [Q07954-2]
GO - Molecular functioni
- apolipoprotein binding Source: UniProtKB
- clathrin heavy chain binding Source: ARUK-UCL
- heparan sulfate proteoglycan binding Source: ARUK-UCL
- lipoprotein particle receptor binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 110215, 218 interactors |
ComplexPortali | CPX-4310, Prolow-density lipoprotein receptor-related protein 1 complex |
CORUMi | Q07954 |
DIPi | DIP-50613N |
ELMi | Q07954 |
IntActi | Q07954, 91 interactors |
MINTi | Q07954 |
STRINGi | 9606.ENSP00000243077 |
Miscellaneous databases
RNActi | Q07954, protein |
Structurei
Secondary structure
3D structure databases
SMRi | Q07954 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q07954 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 25 – 66 | LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 70 – 110 | LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 111 – 149 | EGF-like 1PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 150 – 189 | EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 40 | |
Repeati | 292 – 334 | LDL-receptor class B 1Add BLAST | 43 | |
Repeati | 335 – 378 | LDL-receptor class B 2Add BLAST | 44 | |
Repeati | 379 – 422 | LDL-receptor class B 3Add BLAST | 44 | |
Domaini | 474 – 520 | EGF-like 3PROSITE-ProRule annotationAdd BLAST | 47 | |
Repeati | 571 – 613 | LDL-receptor class B 4Add BLAST | 43 | |
Repeati | 614 – 659 | LDL-receptor class B 5Add BLAST | 46 | |
Repeati | 660 – 710 | LDL-receptor class B 6Add BLAST | 51 | |
Repeati | 711 – 754 | LDL-receptor class B 7Add BLAST | 44 | |
Domaini | 803 – 843 | EGF-like 4PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 852 – 892 | LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 893 – 933 | LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 934 – 973 | LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 974 – 1013 | LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1013 – 1053 | LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 1060 – 1099 | LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1102 – 1142 | LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 1143 – 1182 | LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1183 – 1222 | EGF-like 5PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1223 – 1262 | EGF-like 6PROSITE-ProRule annotationAdd BLAST | 40 | |
Repeati | 1309 – 1355 | LDL-receptor class B 8Add BLAST | 47 | |
Repeati | 1356 – 1398 | LDL-receptor class B 9Add BLAST | 43 | |
Repeati | 1399 – 1445 | LDL-receptor class B 10Add BLAST | 47 | |
Repeati | 1446 – 1490 | LDL-receptor class B 11Add BLAST | 45 | |
Repeati | 1491 – 1531 | LDL-receptor class B 12Add BLAST | 41 | |
Domaini | 1536 – 1579 | EGF-like 7PROSITE-ProRule annotationAdd BLAST | 44 | |
Repeati | 1627 – 1669 | LDL-receptor class B 13Add BLAST | 43 | |
Repeati | 1670 – 1713 | LDL-receptor class B 14Add BLAST | 44 | |
Repeati | 1714 – 1753 | LDL-receptor class B 15Add BLAST | 40 | |
Repeati | 1754 – 1798 | LDL-receptor class B 16Add BLAST | 45 | |
Domaini | 1846 – 1887 | EGF-like 8PROSITE-ProRule annotationAdd BLAST | 42 | |
Repeati | 1934 – 1976 | LDL-receptor class B 17Add BLAST | 43 | |
Repeati | 1977 – 2019 | LDL-receptor class B 18Add BLAST | 43 | |
Repeati | 2020 – 2063 | LDL-receptor class B 19Add BLAST | 44 | |
Repeati | 2064 – 2107 | LDL-receptor class B 20Add BLAST | 44 | |
Domaini | 2155 – 2195 | EGF-like 9PROSITE-ProRule annotationAdd BLAST | 41 | |
Repeati | 2253 – 2294 | LDL-receptor class B 21Add BLAST | 42 | |
Repeati | 2295 – 2343 | LDL-receptor class B 22Add BLAST | 49 | |
Repeati | 2344 – 2388 | LDL-receptor class B 23Add BLAST | 45 | |
Repeati | 2389 – 2431 | LDL-receptor class B 24Add BLAST | 43 | |
Repeati | 2432 – 2473 | LDL-receptor class B 25Add BLAST | 42 | |
Domaini | 2478 – 2518 | EGF-like 10PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 2522 – 2563 | LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 2564 – 2602 | LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 2603 – 2641 | LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 2642 – 2690 | LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST | 49 | |
Domaini | 2694 – 2732 | LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 2732 – 2771 | LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 2772 – 2814 | LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST | 43 | |
Domaini | 2816 – 2855 | LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 2856 – 2899 | LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST | 44 | |
Domaini | 2902 – 2940 | LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 2941 – 2981 | EGF-like 11PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 2982 – 3022 | EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 41 | |
Repeati | 3069 – 3113 | LDL-receptor class B 26Add BLAST | 45 | |
Repeati | 3114 – 3156 | LDL-receptor class B 27Add BLAST | 43 | |
Repeati | 3157 – 3200 | LDL-receptor class B 28Add BLAST | 44 | |
Repeati | 3201 – 3243 | LDL-receptor class B 29Add BLAST | 43 | |
Repeati | 3244 – 3284 | LDL-receptor class B 30Add BLAST | 41 | |
Domaini | 3290 – 3331 | EGF-like 13PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 3332 – 3371 | LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 3372 – 3410 | LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3411 – 3450 | LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 3451 – 3491 | LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 3492 – 3533 | LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 3534 – 3572 | LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3573 – 3611 | LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3611 – 3649 | LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3652 – 3692 | LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 3693 – 3733 | LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 3739 – 3778 | LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 3781 – 3823 | EGF-like 14PROSITE-ProRule annotationAdd BLAST | 43 | |
Domaini | 3824 – 3861 | EGF-like 15PROSITE-ProRule annotationAdd BLAST | 38 | |
Repeati | 3912 – 3954 | LDL-receptor class B 31Add BLAST | 43 | |
Repeati | 3970 – 4012 | LDL-receptor class B 32Add BLAST | 43 | |
Repeati | 4013 – 4056 | LDL-receptor class B 33Add BLAST | 44 | |
Repeati | 4057 – 4101 | LDL-receptor class B 34Add BLAST | 45 | |
Domaini | 4147 – 4183 | EGF-like 16PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 4196 – 4232 | EGF-like 17PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 4232 – 4268 | EGF-like 18PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 4268 – 4304 | EGF-like 19PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 4304 – 4340 | EGF-like 20PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 4340 – 4375 | EGF-like 21PROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 4373 – 4409 | EGF-like 22PROSITE-ProRule annotationAdd BLAST | 37 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 4445 – 4544 | Interaction with MAFBBy similarityAdd BLAST | 100 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 3940 – 3943 | Recognition site for proteolytical processingSequence analysis | 4 | |
Motifi | 4502 – 4507 | NPXY motif | 6 |
Sequence similaritiesi
Keywords - Domaini
EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1215, Eukaryota |
GeneTreei | ENSGT00940000157899 |
HOGENOMi | CLU_000085_1_0_1 |
InParanoidi | Q07954 |
OMAi | CEYDGTR |
OrthoDBi | 1606at2759 |
PhylomeDBi | Q07954 |
TreeFami | TF315253 |
Family and domain databases
CDDi | cd00112, LDLa, 31 hits |
Gene3Di | 2.120.10.30, 8 hits 4.10.400.10, 30 hits |
InterProi | View protein in InterPro IPR011042, 6-blade_b-propeller_TolB-like IPR026823, cEGF IPR032485, DUF5050 IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR009030, Growth_fac_rcpt_cys_sf IPR036055, LDL_receptor-like_sf IPR023415, LDLR_class-A_CS IPR000033, LDLR_classB_rpt IPR002172, LDrepeatLR_classA_rpt |
Pfami | View protein in Pfam PF12662, cEGF, 1 hit PF16472, DUF5050, 1 hit PF07645, EGF_CA, 2 hits PF00057, Ldl_recept_a, 29 hits PF00058, Ldl_recept_b, 12 hits |
PRINTSi | PR00261, LDLRECEPTOR |
SMARTi | View protein in SMART SM00181, EGF, 26 hits SM00179, EGF_CA, 7 hits SM00192, LDLa, 31 hits SM00135, LY, 35 hits |
SUPFAMi | SSF57184, SSF57184, 4 hits SSF57424, SSF57424, 30 hits |
PROSITEi | View protein in 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 |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketQ6PJ72 | Q6PJ72_HUMAN | LRP1 protein | LRP1 | 439 | Annotation score: | ||
Q7Z7K9 | Q7Z7K9_HUMAN | LRP1 protein | LRP1 | 296 | Annotation score: | ||
H0YJ88 | H0YJ88_HUMAN | Prolow-density lipoprotein receptor... | LRP1 | 183 | Annotation score: | ||
H0YJI8 | H0YJI8_HUMAN | Prolow-density lipoprotein receptor... | LRP1 | 139 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 685 | D → G AA sequence (PubMed:1698775).Curated | 1 | |
Sequence conflicti | 1743 | G → S AA sequence (PubMed:1698775).Curated | 1 | |
Sequence conflicti | 2871 – 2872 | LS → IA AA sequence (PubMed:1698775).Curated | 2 | |
Sequence conflicti | 3036 | R → M AA sequence (PubMed:1698775).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_021885 | 166 | N → D. Corresponds to variant dbSNP:rs2306691Ensembl. | 1 | |
Natural variantiVAR_014725 | 217 | A → V. Corresponds to variant dbSNP:rs1800127Ensembl. | 1 | |
Natural variantiVAR_035994 | 869 | E → K in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1207947902Ensembl. | 1 | |
Natural variantiVAR_077982 | 1245 | K → R in KPA; reduced alpha-2 macroglobulin receptor activity; reduced protein abundance. 1 PublicationCorresponds to variant dbSNP:rs483353013EnsemblClinVar. | 1 | |
Natural variantiVAR_029181 | 2059 | V → L. Corresponds to variant dbSNP:rs2229278Ensembl. | 1 | |
Natural variantiVAR_047525 | 2080 | D → N. Corresponds to variant dbSNP:rs34577247Ensembl. | 1 | |
Natural variantiVAR_047526 | 2900 | Q → P3 PublicationsCorresponds to variant dbSNP:rs7397167Ensembl. | 1 | |
Natural variantiVAR_069388 | 3258 | H → Q Found in a patient with severe mental retardation, seizures, stereotypic behavior, high pain threshold and sleep disturbances. 1 PublicationCorresponds to variant dbSNP:rs1565750061EnsemblClinVar. | 1 | |
Natural variantiVAR_035995 | 3760 | R → H in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs569866427Ensembl. | 1 | |
Natural variantiVAR_047527 | 4536 | E → G. Corresponds to variant dbSNP:rs17357542Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_056919 | 281 – 292 | HVEQM…DWLTG → LCVFSKSQQEMG in isoform 2. 1 PublicationAdd BLAST | 12 | |
Alternative sequenceiVSP_056920 | 293 – 4544 | Missing in isoform 2. 1 PublicationAdd BLAST | 4252 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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 [Q07954-1] |
PIRi | S02392 |
RefSeqi | NP_002323.2, NM_002332.2 [Q07954-1] |
Genome annotation databases
Ensembli | ENST00000243077.8; ENSP00000243077.3; ENSG00000123384.14 ENST00000338962.8; ENSP00000341264.4; ENSG00000123384.14 [Q07954-2] |
GeneIDi | 4035 |
KEGGi | hsa:4035 |
MANE-Selecti | ENST00000243077.8; ENSP00000243077.3; NM_002332.3; NP_002323.2 |
UCSCi | uc001snd.4, human [Q07954-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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 [Q07954-1] |
PIRi | S02392 |
RefSeqi | NP_002323.2, NM_002332.2 [Q07954-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
SMRi | Q07954 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 110215, 218 interactors |
ComplexPortali | CPX-4310, Prolow-density lipoprotein receptor-related protein 1 complex |
CORUMi | Q07954 |
DIPi | DIP-50613N |
ELMi | Q07954 |
IntActi | Q07954, 91 interactors |
MINTi | Q07954 |
STRINGi | 9606.ENSP00000243077 |
Chemistry databases
ChEMBLi | CHEMBL4630884 |
DrugBanki | DB00025, Antihemophilic factor, human recombinant DB00100, Coagulation Factor IX (Recombinant) DB13152, Coagulation Factor IX Human DB06245, Lanoteplase DB13998, Lonoctocog alfa DB13999, Moroctocog alfa DB00031, Tenecteplase |
Protein family/group databases
TCDBi | 9.B.87.1.16, the selenoprotein p receptor (selp-receptor) family |
PTM databases
CarbonylDBi | Q07954 |
GlyConnecti | 1638, 61 N-Linked glycans (38 sites), 1 O-Linked glycan (1 site) |
GlyGeni | Q07954, 74 sites, 62 N-linked glycans (36 sites), 3 O-linked glycans (13 sites) |
iPTMneti | Q07954 |
MetOSitei | Q07954 |
PhosphoSitePlusi | Q07954 |
Genetic variation databases
BioMutai | LRP1 |
DMDMi | 317373384 |
Proteomic databases
CPTACi | CPTAC-1617 CPTAC-2222 CPTAC-2223 |
EPDi | Q07954 |
jPOSTi | Q07954 |
MassIVEi | Q07954 |
MaxQBi | Q07954 |
PaxDbi | Q07954 |
PeptideAtlasi | Q07954 |
PRIDEi | Q07954 |
ProteomicsDBi | 58559 [Q07954-1] 69639 |
Protocols and materials databases
Antibodypediai | 4353, 1116 antibodies from 40 providers |
DNASUi | 4035 |
Genome annotation databases
Ensembli | ENST00000243077.8; ENSP00000243077.3; ENSG00000123384.14 ENST00000338962.8; ENSP00000341264.4; ENSG00000123384.14 [Q07954-2] |
GeneIDi | 4035 |
KEGGi | hsa:4035 |
MANE-Selecti | ENST00000243077.8; ENSP00000243077.3; NM_002332.3; NP_002323.2 |
UCSCi | uc001snd.4, human [Q07954-1] |
Organism-specific databases
CTDi | 4035 |
DisGeNETi | 4035 |
GeneCardsi | LRP1 |
HGNCi | HGNC:6692, LRP1 |
HPAi | ENSG00000123384, Tissue enhanced (adipose) |
MalaCardsi | LRP1 |
MIMi | 107770, gene 604093, phenotype |
neXtProti | NX_Q07954 |
OpenTargetsi | ENSG00000123384 |
Orphaneti | 79100, Atrophoderma vermiculata 2340, Keratosis follicularis spinulosa decalvans |
PharmGKBi | PA233 |
VEuPathDBi | HostDB:ENSG00000123384 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1215, Eukaryota |
GeneTreei | ENSGT00940000157899 |
HOGENOMi | CLU_000085_1_0_1 |
InParanoidi | Q07954 |
OMAi | CEYDGTR |
OrthoDBi | 1606at2759 |
PhylomeDBi | Q07954 |
TreeFami | TF315253 |
Enzyme and pathway databases
PathwayCommonsi | Q07954 |
Reactomei | R-HSA-2168880, Scavenging of heme from plasma R-HSA-975634, Retinoid metabolism and transport |
SignaLinki | Q07954 |
SIGNORi | Q07954 |
Miscellaneous databases
BioGRID-ORCSi | 4035, 16 hits in 1075 CRISPR screens |
ChiTaRSi | LRP1, human |
EvolutionaryTracei | Q07954 |
GeneWikii | LRP1 |
GenomeRNAii | 4035 |
Pharosi | Q07954, Tbio |
PROi | PR:Q07954 |
RNActi | Q07954, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000123384, Expressed in stromal cell of endometrium and 241 other tissues |
ExpressionAtlasi | Q07954, baseline and differential |
Genevisiblei | Q07954, HS |
Family and domain databases
CDDi | cd00112, LDLa, 31 hits |
Gene3Di | 2.120.10.30, 8 hits 4.10.400.10, 30 hits |
InterProi | View protein in InterPro IPR011042, 6-blade_b-propeller_TolB-like IPR026823, cEGF IPR032485, DUF5050 IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR009030, Growth_fac_rcpt_cys_sf IPR036055, LDL_receptor-like_sf IPR023415, LDLR_class-A_CS IPR000033, LDLR_classB_rpt IPR002172, LDrepeatLR_classA_rpt |
Pfami | View protein in Pfam PF12662, cEGF, 1 hit PF16472, DUF5050, 1 hit PF07645, EGF_CA, 2 hits PF00057, Ldl_recept_a, 29 hits PF00058, Ldl_recept_b, 12 hits |
PRINTSi | PR00261, LDLRECEPTOR |
SMARTi | View protein in SMART SM00181, EGF, 26 hits SM00179, EGF_CA, 7 hits SM00192, LDLa, 31 hits SM00135, LY, 35 hits |
SUPFAMi | SSF57184, SSF57184, 4 hits SSF57424, SSF57424, 30 hits |
PROSITEi | View protein in 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | LRP1_HUMAN | |
Accessioni | Q07954Primary (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: | May 25, 2022 | |
This is version 229 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human cell differentiation molecules
CD nomenclature of surface proteins of human leucocytes and list of entries - Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families