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Protein

Prolow-density lipoprotein receptor-related protein 1

Gene

LRP1

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

Functioni

Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission.
Functions as a receptor for Pseudomonas aeruginosa exotoxin A.

Sites

Feature keyPosition(s)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

  • apolipoprotein binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • lipoprotein particle receptor binding Source: BHF-UCL
  • lipoprotein transporter activity Source: UniProtKB
  • low-density lipoprotein receptor activity Source: Reactome
  • poly(A) RNA binding Source: UniProtKB
  • protein complex binding Source: BHF-UCL
  • receptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, 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 receptor
Short name:
A2MR
Apolipoprotein E receptor
Short name:
APOER
CD_antigen: CD91
Cleaved into the following 3 chains:
Gene namesi
Name:LRP1
Synonyms:A2MR, APR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:6692. LRP1.

Subcellular locationi

Low-density lipoprotein receptor-related protein 1 intracellular domain :
  • Cytoplasm
  • Nucleus

  • Note: After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus.

Topology

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

GO - Cellular componenti

  • clathrin-coated pit Source: UniProtKB-SubCell
  • clathrin-coated vesicle Source: Ensembl
  • cytoplasm Source: HPA
  • dendrite Source: Ensembl
  • endocytic vesicle membrane Source: Reactome
  • endosome Source: Ensembl
  • focal adhesion Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • nucleolus Source: HPA
  • plasma membrane Source: ParkinsonsUK-UCL
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

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

Organism-specific databases

DisGeNETi4035.
OpenTargetsiENSG00000123384.
PharmGKBiPA233.

Chemistry databases

DrugBankiDB00025. Antihemophilic Factor (Recombinant).
DB00100. Coagulation Factor IX.
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...)Sequence analysis1
Disulfide bondi115 ↔ 124By similarity
Disulfide bondi120 ↔ 133By similarity
Disulfide bondi135 ↔ 148By similarity
Glycosylationi136N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi154 ↔ 164By similarity
Disulfide bondi160 ↔ 173By similarity
Disulfide bondi175 ↔ 188By similarity
Glycosylationi185N-linked (GlcNAc...)Sequence analysis1
Glycosylationi239N-linked (GlcNAc...)Sequence analysis1
Glycosylationi274N-linked (GlcNAc...)Sequence analysis1
Glycosylationi357N-linked (GlcNAc...)Sequence analysis1
Glycosylationi446N-linked (GlcNAc...)2 Publications1
Disulfide bondi478 ↔ 493By similarity
Disulfide bondi489 ↔ 504By similarity
Disulfide bondi506 ↔ 519By similarity
Glycosylationi729N-linked (GlcNAc...) (complex)3 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...)Sequence 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...)Sequence 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...)Sequence analysis1
Glycosylationi1155N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1166 ↔ 1182By similarity
Disulfide bondi1185 ↔ 1196By similarity
Disulfide bondi1192 ↔ 1206By similarity
Glycosylationi1195N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1208 ↔ 1221By similarity
Glycosylationi1218N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1227 ↔ 1237By similarity
Disulfide bondi1233 ↔ 1246By similarity
Disulfide bondi1248 ↔ 1261By similarity
Glycosylationi1511N-linked (GlcNAc...) (complex)2 Publications1
Disulfide bondi1540 ↔ 1553By similarity
Disulfide bondi1549 ↔ 1563By similarity
Glycosylationi1558N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1565 ↔ 1578By similarity
Glycosylationi1575N-linked (GlcNAc...)1 Publication1
Glycosylationi1616N-linked (GlcNAc...)1 Publication1
Glycosylationi1645N-linked (GlcNAc...)1 Publication1
Glycosylationi1723N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1733N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1763N-linked (GlcNAc...)1 Publication1
Glycosylationi1825N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1850 ↔ 1861By similarity
Disulfide bondi1857 ↔ 1871By similarity
Disulfide bondi1873 ↔ 1886By similarity
Glycosylationi1933N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1995N-linked (GlcNAc...)Sequence analysis1
Modified residuei2009N6-acetyllysineBy similarity1
Glycosylationi2048N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2117N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2127N-linked (GlcNAc...)2 Publications1
Disulfide bondi2159 ↔ 2170By similarity
Disulfide bondi2166 ↔ 2180By similarity
Disulfide bondi2182 ↔ 2194By similarity
Glycosylationi2472N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2482 ↔ 2493By similarity
Disulfide bondi2489 ↔ 2503By similarity
Glycosylationi2502N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2505 ↔ 2517By similarity
Glycosylationi2521N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2524 ↔ 2537By similarity
Disulfide bondi2532 ↔ 2550By similarity
Glycosylationi2539N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2544 ↔ 2561By similarity
Disulfide bondi2566 ↔ 2578By similarity
Disulfide bondi2573 ↔ 2591By similarity
Disulfide bondi2585 ↔ 2600By similarity
Glycosylationi2601N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2605 ↔ 2617By similarity
Disulfide bondi2612 ↔ 2630By similarity
Glycosylationi2620N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2624 ↔ 2639By similarity
Glycosylationi2638N-linked (GlcNAc...)Sequence 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...)1 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...)Sequence 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...)2 Publications1
Glycosylationi3089N-linked (GlcNAc...)1 Publication1
Glycosylationi3264N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3294 ↔ 3305By similarity
Disulfide bondi3301 ↔ 3315By similarity
Disulfide bondi3317 ↔ 3330By similarity
Glycosylationi3333N-linked (GlcNAc...)Sequence 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...)1 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...)Sequence 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...)1 Publication1
Disulfide bondi3792 ↔ 3807By similarity
Disulfide bondi3809 ↔ 3822By similarity
Disulfide bondi3828 ↔ 3838By similarity
Disulfide bondi3834 ↔ 3847By similarity
Glycosylationi3839N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3849 ↔ 3860By similarity
Glycosylationi3953N-linked (GlcNAc...)1 Publication1
Glycosylationi4075N-linked (GlcNAc...)1 Publication1
Glycosylationi4125N-linked (GlcNAc...)1 Publication1
Disulfide bondi4151 ↔ 4160By similarity
Disulfide bondi4156 ↔ 4169By similarity
Disulfide bondi4171 ↔ 4182By similarity
Glycosylationi4179N-linked (GlcNAc...)Sequence 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...)Sequence analysis1
Glycosylationi4279N-linked (GlcNAc...)Sequence 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...)Sequence 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.

PTM databases

iPTMnetiQ07954.
PhosphoSitePlusiQ07954.

Expressioni

Tissue specificityi

Most abundant in liver, brain and lung.

Gene expression databases

BgeeiENSG00000123384.
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

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

GO - Molecular functioni

  • apolipoprotein binding Source: UniProtKB
  • lipoprotein particle receptor binding Source: BHF-UCL
  • protein complex binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110215. 110 interactors.
DIPiDIP-50613N.
IntActiQ07954. 23 interactors.
MINTiMINT-5004471.
STRINGi9606.ENSP00000243077.

Structurei

Secondary structure

14544
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni853 – 857Combined sources5
Beta strandi859 – 861Combined sources3
Turni862 – 864Combined sources3
Beta strandi865 – 867Combined sources3
Helixi869 – 871Combined sources3
Beta strandi874 – 876Combined sources3
Turni878 – 881Combined sources4
Beta strandi934 – 936Combined sources3
Beta strandi940 – 942Combined sources3
Turni944 – 946Combined sources3
Beta strandi948 – 950Combined sources3
Beta strandi953 – 956Combined sources4
Beta strandi958 – 961Combined sources4
Turni964 – 968Combined sources5
Turni969 – 971Combined sources3
Beta strandi974 – 976Combined sources3
Beta strandi978 – 983Combined sources6
Turni985 – 987Combined sources3
Beta strandi989 – 991Combined sources3
Beta strandi995 – 1000Combined sources6
Beta strandi1003 – 1007Combined sources5
Beta strandi1009 – 1011Combined sources3
Beta strandi1013 – 1015Combined sources3
Beta strandi1019 – 1021Combined sources3
Beta strandi1027 – 1029Combined sources3
Helixi1030 – 1032Combined sources3
Beta strandi1035 – 1037Combined sources3
Beta strandi1040 – 1043Combined sources4
Helixi1044 – 1046Combined sources3
Helixi1048 – 1051Combined sources4
Turni1070 – 1072Combined sources3
Helixi1078 – 1080Combined sources3
Beta strandi1081 – 1085Combined sources5
Beta strandi1088 – 1091Combined sources4
Turni1092 – 1096Combined sources5
Beta strandi2778 – 2781Combined sources4
Turni2782 – 2785Combined sources4
Beta strandi2786 – 2789Combined sources4
Turni2790 – 2794Combined sources5
Beta strandi2795 – 2797Combined sources3
Beta strandi2800 – 2803Combined sources4
Helixi2804 – 2806Combined sources3
Helixi2808 – 2810Combined sources3
Beta strandi2813 – 2816Combined sources4

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...

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
Contains 22 EGF-like domains.PROSITE-ProRule annotation
Contains 31 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 34 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000230574.
HOVERGENiHBG006292.
InParanoidiQ07954.
KOiK04550.
OMAiAYFEGPR.
OrthoDBiEOG091G000N.
PhylomeDBiQ07954.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 29 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
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_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF16472. DUF5050. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 29 hits.
PF00058. Ldl_recept_b. 12 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 26 hits.
SM00179. EGF_CA. 7 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 35 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 9 hits.
SSF57424. SSF57424. 30 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 2 hits.
PS01209. LDLRA_1. 27 hits.
PS50068. LDLRA_2. 31 hits.
PS51120. LDLRB. 34 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

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

« Hide

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

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

Note: No experimental confirmation available.
Show »
Length:292
Mass (Da):31,631
Checksum:i82C39315F1ECEE24
GO

Experimental Info

Feature keyPosition(s)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 rs2306691dbSNPEnsembl.1
Natural variantiVAR_014725217A → V.Corresponds to variant rs1800127dbSNPEnsembl.1
Natural variantiVAR_035994869E → K in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0291812059V → L.Corresponds to variant rs2229278dbSNPEnsembl.1
Natural variantiVAR_0475252080D → N.Corresponds to variant rs34577247dbSNPEnsembl.1
Natural variantiVAR_0475262900Q → P.3 PublicationsCorresponds to variant rs7397167dbSNPEnsembl.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 rs569866427dbSNPEnsembl.1
Natural variantiVAR_0475274536E → G.Corresponds to variant rs17357542dbSNPEnsembl.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

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. 110 interactors.
DIPiDIP-50613N.
IntActiQ07954. 23 interactors.
MINTiMINT-5004471.
STRINGi9606.ENSP00000243077.

Chemistry databases

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

PTM databases

iPTMnetiQ07954.
PhosphoSitePlusiQ07954.

Polymorphism and mutation databases

BioMutaiLRP1.
DMDMi317373384.

Proteomic databases

EPDiQ07954.
MaxQBiQ07954.
PaxDbiQ07954.
PeptideAtlasiQ07954.
PRIDEiQ07954.

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.
GeneCardsiLRP1.
HGNCiHGNC:6692. LRP1.
HPAiCAB018621.
HPA004182.
HPA022903.
MIMi107770. gene.
neXtProtiNX_Q07954.
OpenTargetsiENSG00000123384.
PharmGKBiPA233.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000230574.
HOVERGENiHBG006292.
InParanoidiQ07954.
KOiK04550.
OMAiAYFEGPR.
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.
PROiQ07954.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000123384.
CleanExiHS_LRP1.
ExpressionAtlasiQ07954. baseline and differential.
GenevisibleiQ07954. HS.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 29 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
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_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF16472. DUF5050. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 29 hits.
PF00058. Ldl_recept_b. 12 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 26 hits.
SM00179. EGF_CA. 7 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 35 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 9 hits.
SSF57424. SSF57424. 30 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 2 hits.
PS01209. LDLRA_1. 27 hits.
PS50068. LDLRA_2. 31 hits.
PS51120. LDLRB. 34 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLRP1_HUMAN
AccessioniPrimary (citable) accession number: Q07954
Secondary accession number(s): Q2PP12, Q86SW0, Q8IVG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 188 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.