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UniProtKB - Q07954 (LRP1_HUMAN)

Protein

Prolow-density lipoprotein receptor-related protein 1

Gene

LRP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 (PubMed:11907044, PubMed:12888553, PubMed:12713657). Acts as an alpha-2-macroglobulin receptor (PubMed:26142438).4 Publications
(Microbial infection) Functions as a receptor for Pseudomonas aeruginosa exotoxin A.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi871Calcium 1; via carbonyl oxygen1
Metal bindingi874Calcium 11
Metal bindingi876Calcium 1; via carbonyl oxygen1
Metal bindingi878Calcium 11
Metal bindingi884Calcium 11
Metal bindingi885Calcium 11
Metal bindingi1032Calcium 2; via carbonyl oxygen1
Metal bindingi1035Calcium 21
Metal bindingi1037Calcium 2; via carbonyl oxygen1
Metal bindingi1039Calcium 21
Metal bindingi1045Calcium 21
Metal bindingi1046Calcium 21
Metal bindingi1080Calcium 3; via carbonyl oxygen1
Metal bindingi1083Calcium 31
Metal bindingi1085Calcium 3; via carbonyl oxygen1
Metal bindingi1087Calcium 31
Metal bindingi1093Calcium 31
Metal bindingi1094Calcium 31

GO - Molecular functioni

  • alpha-2 macroglobulin receptor activity Source: UniProtKB
  • apolipoprotein binding Source: UniProtKB
  • apolipoprotein receptor activity Source: ARUK-UCL
  • calcium ion binding Source: UniProtKB
  • clathrin heavy chain binding Source: ARUK-UCL
  • heparan sulfate proteoglycan binding Source: ARUK-UCL
  • lipoprotein particle receptor binding Source: BHF-UCL
  • lipoprotein transporter activity Source: UniProtKB
  • low-density lipoprotein particle receptor activity Source: ARUK-UCL
  • protease binding Source: Ensembl
  • protein-containing complex binding Source: BHF-UCL
  • RNA binding Source: UniProtKB
  • scavenger receptor activity Source: ARUK-UCL
  • signaling receptor activity Source: ProtInc
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDevelopmental protein, Receptor
Biological processEndocytosis
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-2168880 Scavenging of heme from plasma
R-HSA-975634 Retinoid metabolism and transport
SIGNORiQ07954

Names & Taxonomyi

Protein namesi
Recommended name:
Prolow-density lipoprotein receptor-related protein 1
Short 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:
Low-density lipoprotein receptor-related protein 1 85 kDa subunit
Short name:
LRP-85
Low-density lipoprotein receptor-related protein 1 515 kDa subunit
Short name:
LRP-515
Low-density lipoprotein receptor-related protein 1 intracellular domain
Short name:
LRPICD
Gene namesi
Name:LRP1
Synonyms:A2MR, APR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000123384.13
HGNCiHGNC:6692 LRP1
MIMi107770 gene
neXtProtiNX_Q07954

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 4419ExtracellularSequence analysisAdd BLAST4400
Transmembranei4420 – 4444HelicalSequence analysisAdd BLAST25
Topological domaini4445 – 4544CytoplasmicSequence analysisAdd BLAST100

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Keratosis pilaris atrophicans (KPA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA group of rare genodermatoses characterized by keratotic follicular papules, variable degrees of inflammation, and secondary atrophic scarring. Most cases are associated with an atopic diathesis and keratosis pilaris on the extensor extremities. KPA is comprised of three distinct clinical subtypes: keratosis pilaris atrophicans faciei, atrophoderma vermiculatum, and keratosis follicularis spinulosa decalvans. Affected individuals may present with features overlapping the 3 subtypes.
See also OMIM:604093
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0779821245K → R in KPA; reduced alpha-2 macroglobulin receptor activity; reduced protein abundance. 1 PublicationCorresponds to variant dbSNP:rs483353013EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4460T → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4517; A-4520 and A-4523. 1 Publication1
Mutagenesisi4470 – 4473NPTY → APTA: No effect on tyrosine phosphorylation. 1 Publication4
Mutagenesisi4470N → A: No effect on interaction with GULP1. 1 Publication1
Mutagenesisi4472T → A: No detectable effect on phosphorylation. 1 Publication1
Mutagenesisi4504 – 4507NPVY → APVA: Loss of tyrosine phosphorylation. Abolishes interaction with SHC1 and GULP1. 1 Publication4
Mutagenesisi4504N → A: Loss of interaction with GULP1. 1 Publication1
Mutagenesisi4517S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4520 and A-4523. 1 Publication1
Mutagenesisi4520S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4523. 1 Publication1
Mutagenesisi4523S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4520. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4035
MalaCardsiLRP1
MIMi604093 phenotype
OpenTargetsiENSG00000123384
Orphaneti79100 Atrophoderma vermiculata
2340 Keratosis follicularis spinulosa decalvans
PharmGKBiPA233

Chemistry databases

DrugBankiDB00025 Antihemophilic Factor (Recombinant)
DB00100 Coagulation Factor IX (Recombinant)
DB00031 Tenecteplase

Polymorphism and mutation databases

BioMutaiLRP1
DMDMi317373384

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001731720 – 4544Prolow-density lipoprotein receptor-related protein 1Add BLAST4525
ChainiPRO_000030275020 – ?3943Low-density lipoprotein receptor-related protein 1 515 kDa subunitAdd BLAST3924
ChainiPRO_0000302751?3944 – 4544Low-density lipoprotein receptor-related protein 1 85 kDa subunitAdd BLAST601
ChainiPRO_0000302752?4441 – 4544Low-density lipoprotein receptor-related protein 1 intracellular domainAdd BLAST104

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 40By similarity
Disulfide bondi34 ↔ 53By similarity
Disulfide bondi47 ↔ 64By similarity
Disulfide bondi72 ↔ 85By similarity
Disulfide bondi79 ↔ 98By similarity
Disulfide bondi92 ↔ 108By similarity
Glycosylationi114N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi115 ↔ 124By similarity
Disulfide bondi120 ↔ 133By similarity
Disulfide bondi135 ↔ 148By similarity
Glycosylationi136N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi154 ↔ 164By similarity
Disulfide bondi160 ↔ 173By similarity
Disulfide bondi175 ↔ 188By similarity
Glycosylationi185N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi239N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi274N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi357N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi446N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi478 ↔ 493By similarity
Disulfide bondi489 ↔ 504By similarity
Disulfide bondi506 ↔ 519By similarity
Glycosylationi729N-linked (GlcNAc...) (complex) asparagine3 Publications1
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
Glycosylationi928N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi1050N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi1154N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1155N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1166 ↔ 1182By similarity
Disulfide bondi1185 ↔ 1196By similarity
Disulfide bondi1192 ↔ 1206By similarity
Glycosylationi1195N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1208 ↔ 1221By similarity
Glycosylationi1218N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1227 ↔ 1237By similarity
Disulfide bondi1233 ↔ 1246By similarity
Disulfide bondi1248 ↔ 1261By similarity
Glycosylationi1511N-linked (GlcNAc...) (complex) asparagine2 Publications1
Disulfide bondi1540 ↔ 1553By similarity
Disulfide bondi1549 ↔ 1563By similarity
Glycosylationi1558N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1565 ↔ 1578By similarity
Glycosylationi1575N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1616N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1645N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1723N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1733N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1763N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1825N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1850 ↔ 1861By similarity
Disulfide bondi1857 ↔ 1871By similarity
Disulfide bondi1873 ↔ 1886By similarity
Glycosylationi1933N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1995N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei2009N6-acetyllysineBy similarity1
Glycosylationi2048N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2117N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2127N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi2159 ↔ 2170By similarity
Disulfide bondi2166 ↔ 2180By similarity
Disulfide bondi2182 ↔ 2194By similarity
Glycosylationi2472N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2482 ↔ 2493By similarity
Disulfide bondi2489 ↔ 2503By similarity
Glycosylationi2502N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2505 ↔ 2517By similarity
Glycosylationi2521N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2524 ↔ 2537By similarity
Disulfide bondi2532 ↔ 2550By similarity
Glycosylationi2539N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2544 ↔ 2561By similarity
Disulfide bondi2566 ↔ 2578By similarity
Disulfide bondi2573 ↔ 2591By similarity
Disulfide bondi2585 ↔ 2600By similarity
Glycosylationi2601N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2605 ↔ 2617By similarity
Disulfide bondi2612 ↔ 2630By similarity
Glycosylationi2620N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2624 ↔ 2639By similarity
Glycosylationi2638N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi2815N-linked (GlcNAc...) asparagine1 Publication1
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
Glycosylationi2905N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi3048N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi3089N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi3264N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3294 ↔ 3305By similarity
Disulfide bondi3301 ↔ 3315By similarity
Disulfide bondi3317 ↔ 3330By similarity
Glycosylationi3333N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi3488N-linked (GlcNAc...) asparagine1 Publication1
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
Glycosylationi3662N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi3788N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi3792 ↔ 3807By similarity
Disulfide bondi3809 ↔ 3822By similarity
Disulfide bondi3828 ↔ 3838By similarity
Disulfide bondi3834 ↔ 3847By similarity
Glycosylationi3839N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3849 ↔ 3860By similarity
Glycosylationi3953N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi4075N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi4125N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi4151 ↔ 4160By similarity
Disulfide bondi4156 ↔ 4169By similarity
Disulfide bondi4171 ↔ 4182By similarity
Glycosylationi4179N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi4278N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi4279N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4294 ↔ 4303By similarity
Disulfide bondi4308 ↔ 4318By similarity
Disulfide bondi4312 ↔ 4328By similarity
Disulfide bondi4330 ↔ 4339By similarity
Disulfide bondi4344 ↔ 4352By similarity
Disulfide bondi4347 ↔ 4363By similarity
Glycosylationi4364N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4365 ↔ 4374By similarity
Disulfide bondi4377 ↔ 4387By similarity
Disulfide bondi4381 ↔ 4397By similarity
Disulfide bondi4399 ↔ 4408By similarity
Modified residuei4460Phosphothreonine1 Publication1
Modified residuei4507Phosphotyrosine1 Publication1
Modified residuei4517Phosphoserine1 Publication1
Modified residuei4520PhosphoserineCombined sources1
Modified residuei4523Phosphoserine1 Publication1

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

EPDiQ07954
MaxQBiQ07954
PaxDbiQ07954
PeptideAtlasiQ07954
PRIDEiQ07954
ProteomicsDBi58559

PTM databases

CarbonylDBiQ07954
GlyConnecti1638
iPTMnetiQ07954
PhosphoSitePlusiQ07954

Expressioni

Tissue specificityi

Most abundant in liver, brain and lung.

Gene expression databases

BgeeiENSG00000123384 Expressed in 230 organ(s), highest expression level in thoracic aorta
CleanExiHS_LRP1
ExpressionAtlasiQ07954 baseline and differential
GenevisibleiQ07954 HS

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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi110215, 123 interactors
CORUMiQ07954
DIPiDIP-50613N
ELMiQ07954
IntActiQ07954, 26 interactors
MINTiQ07954
STRINGi9606.ENSP00000243077

Structurei

Secondary structure

14544
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ07954
SMRiQ07954
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07954

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 66LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST42
Domaini70 – 110LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST41
Domaini111 – 149EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini150 – 189EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Repeati292 – 334LDL-receptor class B 1Add BLAST43
Repeati335 – 378LDL-receptor class B 2Add BLAST44
Repeati379 – 422LDL-receptor class B 3Add BLAST44
Domaini474 – 520EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Repeati571 – 613LDL-receptor class B 4Add BLAST43
Repeati614 – 659LDL-receptor class B 5Add BLAST46
Repeati660 – 710LDL-receptor class B 6Add BLAST51
Repeati711 – 754LDL-receptor class B 7Add BLAST44
Domaini803 – 843EGF-like 4PROSITE-ProRule annotationAdd BLAST41
Domaini852 – 892LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST41
Domaini893 – 933LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST41
Domaini934 – 973LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST40
Domaini974 – 1013LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST40
Domaini1013 – 1053LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST41
Domaini1060 – 1099LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST40
Domaini1102 – 1142LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST41
Domaini1143 – 1182LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST40
Domaini1183 – 1222EGF-like 5PROSITE-ProRule annotationAdd BLAST40
Domaini1223 – 1262EGF-like 6PROSITE-ProRule annotationAdd BLAST40
Repeati1309 – 1355LDL-receptor class B 8Add BLAST47
Repeati1356 – 1398LDL-receptor class B 9Add BLAST43
Repeati1399 – 1445LDL-receptor class B 10Add BLAST47
Repeati1446 – 1490LDL-receptor class B 11Add BLAST45
Repeati1491 – 1531LDL-receptor class B 12Add BLAST41
Domaini1536 – 1579EGF-like 7PROSITE-ProRule annotationAdd BLAST44
Repeati1627 – 1669LDL-receptor class B 13Add BLAST43
Repeati1670 – 1713LDL-receptor class B 14Add BLAST44
Repeati1714 – 1753LDL-receptor class B 15Add BLAST40
Repeati1754 – 1798LDL-receptor class B 16Add BLAST45
Domaini1846 – 1887EGF-like 8PROSITE-ProRule annotationAdd BLAST42
Repeati1934 – 1976LDL-receptor class B 17Add BLAST43
Repeati1977 – 2019LDL-receptor class B 18Add BLAST43
Repeati2020 – 2063LDL-receptor class B 19Add BLAST44
Repeati2064 – 2107LDL-receptor class B 20Add BLAST44
Domaini2155 – 2195EGF-like 9PROSITE-ProRule annotationAdd BLAST41
Repeati2253 – 2294LDL-receptor class B 21Add BLAST42
Repeati2295 – 2343LDL-receptor class B 22Add BLAST49
Repeati2344 – 2388LDL-receptor class B 23Add BLAST45
Repeati2389 – 2431LDL-receptor class B 24Add BLAST43
Repeati2432 – 2473LDL-receptor class B 25Add BLAST42
Domaini2478 – 2518EGF-like 10PROSITE-ProRule annotationAdd BLAST41
Domaini2522 – 2563LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST42
Domaini2564 – 2602LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST39
Domaini2603 – 2641LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST39
Domaini2642 – 2690LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST49
Domaini2694 – 2732LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST39
Domaini2732 – 2771LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST40
Domaini2772 – 2814LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST43
Domaini2816 – 2855LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST40
Domaini2856 – 2899LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST44
Domaini2902 – 2940LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST39
Domaini2941 – 2981EGF-like 11PROSITE-ProRule annotationAdd BLAST41
Domaini2982 – 3022EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3069 – 3113LDL-receptor class B 26Add BLAST45
Repeati3114 – 3156LDL-receptor class B 27Add BLAST43
Repeati3157 – 3200LDL-receptor class B 28Add BLAST44
Repeati3201 – 3243LDL-receptor class B 29Add BLAST43
Repeati3244 – 3284LDL-receptor class B 30Add BLAST41
Domaini3290 – 3331EGF-like 13PROSITE-ProRule annotationAdd BLAST42
Domaini3332 – 3371LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST40
Domaini3372 – 3410LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST39
Domaini3411 – 3450LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST40
Domaini3451 – 3491LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST41
Domaini3492 – 3533LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST42
Domaini3534 – 3572LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST39
Domaini3573 – 3611LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST39
Domaini3611 – 3649LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST39
Domaini3652 – 3692LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST41
Domaini3693 – 3733LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST41
Domaini3739 – 3778LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST40
Domaini3781 – 3823EGF-like 14PROSITE-ProRule annotationAdd BLAST43
Domaini3824 – 3861EGF-like 15PROSITE-ProRule annotationAdd BLAST38
Repeati3912 – 3954LDL-receptor class B 31Add BLAST43
Repeati3970 – 4012LDL-receptor class B 32Add BLAST43
Repeati4013 – 4056LDL-receptor class B 33Add BLAST44
Repeati4057 – 4101LDL-receptor class B 34Add BLAST45
Domaini4147 – 4183EGF-like 16PROSITE-ProRule annotationAdd BLAST37
Domaini4196 – 4232EGF-like 17PROSITE-ProRule annotationAdd BLAST37
Domaini4232 – 4268EGF-like 18PROSITE-ProRule annotationAdd BLAST37
Domaini4268 – 4304EGF-like 19PROSITE-ProRule annotationAdd BLAST37
Domaini4304 – 4340EGF-like 20PROSITE-ProRule annotationAdd BLAST37
Domaini4340 – 4375EGF-like 21PROSITE-ProRule annotationAdd BLAST36
Domaini4373 – 4409EGF-like 22PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4445 – 4544Interaction with MAFBBy similarityAdd BLAST100

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi3940 – 3943Recognition site for proteolytical processingSequence analysis4
Motifi4502 – 4507NPXY motif6

Sequence similaritiesi

Belongs to the LDLR family.Curated

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG1215 Eukaryota
ENOG410XP34 LUCA
GeneTreeiENSGT00760000118968
HOGENOMiHOG000230574
HOVERGENiHBG066902
InParanoidiQ07954
KOiK04550
OMAiTSKATCD
OrthoDBiEOG091G000N
PhylomeDBiQ07954
TreeFamiTF315253

Family and domain databases

CDDicd00112 LDLa, 31 hits
Gene3Di2.120.10.30, 8 hits
InterProiView protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR026823 cEGF
IPR032485 DUF5050
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
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
PfamiView 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
PRINTSiPR00261 LDLRECEPTOR
SMARTiView protein in SMART
SM00181 EGF, 26 hits
SM00179 EGF_CA, 7 hits
SM00192 LDLa, 31 hits
SM00135 LY, 35 hits
SUPFAMiSSF57184 SSF57184, 4 hits
SSF57424 SSF57424, 30 hits
PROSITEiView 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

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. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q6PJ72Q6PJ72_HUMAN
LRP1 protein
LRP1
439Annotation score:
Q7Z7K9Q7Z7K9_HUMAN
LRP1 protein
LRP1
296Annotation score:
H0YJ88H0YJ88_HUMAN
Prolow-density lipoprotein receptor...
LRP1
183Annotation score:
H0YJI8H0YJI8_HUMAN
Prolow-density lipoprotein receptor...
LRP1
139Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti685D → G AA sequence (PubMed:1698775).Curated1
Sequence conflicti1743G → S AA sequence (PubMed:1698775).Curated1
Sequence conflicti2871 – 2872LS → IA AA sequence (PubMed:1698775).Curated2
Sequence conflicti3036R → M AA sequence (PubMed:1698775).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021885166N → D. Corresponds to variant dbSNP:rs2306691Ensembl.1
Natural variantiVAR_014725217A → V. Corresponds to variant dbSNP:rs1800127Ensembl.1
Natural variantiVAR_035994869E → K in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1207947902Ensembl.1
Natural variantiVAR_0779821245K → R in KPA; reduced alpha-2 macroglobulin receptor activity; reduced protein abundance. 1 PublicationCorresponds to variant dbSNP:rs483353013EnsemblClinVar.1
Natural variantiVAR_0291812059V → L. Corresponds to variant dbSNP:rs2229278Ensembl.1
Natural variantiVAR_0475252080D → N. Corresponds to variant dbSNP:rs34577247Ensembl.1
Natural variantiVAR_0475262900Q → P3 PublicationsCorresponds to variant dbSNP:rs7397167Ensembl.1
Natural variantiVAR_0693883258H → Q Found in a patient with severe mental retardation, seizures, stereotypic behavior, high pain threshold and sleep disturbances. 1 Publication1
Natural variantiVAR_0359953760R → H in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs569866427Ensembl.1
Natural variantiVAR_0475274536E → G. Corresponds to variant dbSNP:rs17357542Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056919281 – 292HVEQM…DWLTG → LCVFSKSQQEMG in isoform 2. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_056920293 – 4544Missing in isoform 2. 1 PublicationAdd BLAST4252

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
CCDSiCCDS8932.1 [Q07954-1]
PIRiS02392
RefSeqiNP_002323.2, NM_002332.2 [Q07954-1]
UniGeneiHs.162757

Genome annotation databases

EnsembliENST00000243077; ENSP00000243077; ENSG00000123384 [Q07954-1]
ENST00000338962; ENSP00000341264; ENSG00000123384 [Q07954-2]
GeneIDi4035
KEGGihsa:4035
UCSCiuc001snd.4 human [Q07954-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar 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
CCDSiCCDS8932.1 [Q07954-1]
PIRiS02392
RefSeqiNP_002323.2, NM_002332.2 [Q07954-1]
UniGeneiHs.162757

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110215, 123 interactors
CORUMiQ07954
DIPiDIP-50613N
ELMiQ07954
IntActiQ07954, 26 interactors
MINTiQ07954
STRINGi9606.ENSP00000243077

Chemistry databases

DrugBankiDB00025 Antihemophilic Factor (Recombinant)
DB00100 Coagulation Factor IX (Recombinant)
DB00031 Tenecteplase

PTM databases

CarbonylDBiQ07954
GlyConnecti1638
iPTMnetiQ07954
PhosphoSitePlusiQ07954

Polymorphism and mutation databases

BioMutaiLRP1
DMDMi317373384

Proteomic databases

EPDiQ07954
MaxQBiQ07954
PaxDbiQ07954
PeptideAtlasiQ07954
PRIDEiQ07954
ProteomicsDBi58559

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000243077; ENSP00000243077; ENSG00000123384 [Q07954-1]
ENST00000338962; ENSP00000341264; ENSG00000123384 [Q07954-2]
GeneIDi4035
KEGGihsa:4035
UCSCiuc001snd.4 human [Q07954-1]

Organism-specific databases

CTDi4035
DisGeNETi4035
EuPathDBiHostDB:ENSG00000123384.13
GeneCardsiLRP1
HGNCiHGNC:6692 LRP1
HPAiCAB018621
HPA004182
HPA022903
MalaCardsiLRP1
MIMi107770 gene
604093 phenotype
neXtProtiNX_Q07954
OpenTargetsiENSG00000123384
Orphaneti79100 Atrophoderma vermiculata
2340 Keratosis follicularis spinulosa decalvans
PharmGKBiPA233
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1215 Eukaryota
ENOG410XP34 LUCA
GeneTreeiENSGT00760000118968
HOGENOMiHOG000230574
HOVERGENiHBG066902
InParanoidiQ07954
KOiK04550
OMAiTSKATCD
OrthoDBiEOG091G000N
PhylomeDBiQ07954
TreeFamiTF315253

Enzyme and pathway databases

ReactomeiR-HSA-2168880 Scavenging of heme from plasma
R-HSA-975634 Retinoid metabolism and transport
SIGNORiQ07954

Miscellaneous databases

ChiTaRSiLRP1 human
EvolutionaryTraceiQ07954
GeneWikiiLRP1
GenomeRNAii4035
PROiPR:Q07954
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000123384 Expressed in 230 organ(s), highest expression level in thoracic aorta
CleanExiHS_LRP1
ExpressionAtlasiQ07954 baseline and differential
GenevisibleiQ07954 HS

Family and domain databases

CDDicd00112 LDLa, 31 hits
Gene3Di2.120.10.30, 8 hits
InterProiView protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR026823 cEGF
IPR032485 DUF5050
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
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
PfamiView 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
PRINTSiPR00261 LDLRECEPTOR
SMARTiView protein in SMART
SM00181 EGF, 26 hits
SM00179 EGF_CA, 7 hits
SM00192 LDLa, 31 hits
SM00135 LY, 35 hits
SUPFAMiSSF57184 SSF57184, 4 hits
SSF57424 SSF57424, 30 hits
PROSITEiView 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
ProtoNetiSearch...

Entry informationi

Entry nameiLRP1_HUMAN
AccessioniPrimary (citable) accession number: Q07954
Secondary accession number(s): Q2PP12, Q86SW0, Q8IVG8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: November 7, 2018
This is version 207 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  7. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
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