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Q91ZX7 (LRP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prolow-density lipoprotein receptor-related protein 1

Short name=LRP-1
Alternative name(s):
Alpha-2-macroglobulin receptor
Short name=A2MR
CD_antigen=CD91
Gene names
Name:Lrp1
Synonyms:A2mr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length4545 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission. Ref.3 Ref.6 Ref.11

Functions as a receptor for Vibrio cholerae cholix toxin and for Pseudomonas aeruginosa exotoxin A. Ref.3 Ref.6 Ref.11

Subunit structure

Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a non-covalently attached 515-kDa N-terminal subunit. 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 By similarity. Intracellular domain interacts with MAFB. Can weakly interact (via NPXY motif) with DAB2 (via PID domain); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif. Interacts with bacterial exotoxins. Ref.4 Ref.5

Subcellular location

Low-density lipoprotein receptor-related protein 1 85 kDa subunit: Cell membrane; Single-pass type I membrane protein By similarity. Membranecoated pit By similarity.

Low-density lipoprotein receptor-related protein 1 515 kDa subunit: Cell membrane; Peripheral membrane protein; Extracellular side By similarity. Membranecoated pit By similarity.

Low-density lipoprotein receptor-related protein 1 intracellular domain: Cytoplasm By similarity. Nucleus By similarity. Note: After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus By similarity.

Post-translational modification

Phosphorylated on serine and threonine residues By similarity.

Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1 By similarity.

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 By similarity. UniProtKB Q07954

Disruption phenotype

Death during early embryogenesis around 14 dpc. Ref.6

Sequence similarities

Belongs to the LDLR family.

Contains 22 EGF-like domains.

Contains 31 LDL-receptor class A domains.

Contains 34 LDL-receptor class B repeats.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Coated pit
Cytoplasm
Membrane
Nucleus
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionDevelopmental protein
Receptor
   PTMAcetylation
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

aorta morphogenesis

Inferred from mutant phenotype PubMed 19742316. Source: BHF-UCL

apoptotic cell clearance

Inferred from mutant phenotype PubMed 15647754. Source: MGI

beta-amyloid clearance

Inferred from mutant phenotype PubMed 19098903. Source: BHF-UCL

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from mutant phenotype PubMed 17920016. Source: MGI

lipoprotein metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of Wnt signaling pathway

Inferred from direct assay PubMed 16207730. Source: MGI

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of platelet-derived growth factor receptor-beta signaling pathway

Inferred from mutant phenotype PubMed 19742316. Source: BHF-UCL

negative regulation of smooth muscle cell migration

Inferred from mutant phenotype PubMed 19742316. Source: BHF-UCL

positive regulation of cholesterol efflux

Inferred from mutant phenotype PubMed 19718435. Source: BHF-UCL

positive regulation of lipid transport

Inferred from mutant phenotype PubMed 19718435. Source: BHF-UCL

positive regulation of protein transport

Inferred from electronic annotation. Source: Ensembl

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

receptor-mediated endocytosis

Inferred from direct assay PubMed 21795536. Source: MGI

regulation of actin cytoskeleton organization

Inferred from mutant phenotype PubMed 19742316. Source: BHF-UCL

regulation of cholesterol transport

Inferred from mutant phenotype PubMed 19718435. Source: BHF-UCL

regulation of phospholipase A2 activity

Inferred from mutant phenotype PubMed 19718435. Source: BHF-UCL

   Cellular_componentclathrin-coated vesicle

Inferred from electronic annotation. Source: Ensembl

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from direct assay PubMed 3266596. Source: UniProtKB

lysosomal membrane

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 15082773. Source: MGI

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from sequence orthology PubMed 19047013. Source: MGI

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 3266596. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10827173PubMed 19455133. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 45454526Prolow-density lipoprotein receptor-related protein 1
PRO_0000273273
Chain20 – ?39443925Low-density lipoprotein receptor-related protein 1 515 kDa subunit
PRO_0000302753
Chain?3945 – 4545601Low-density lipoprotein receptor-related protein 1 85 kDa subunit
PRO_0000302754
Chain?4442 – 4545104Low-density lipoprotein receptor-related protein 1 intracellular domain
PRO_0000302755

Regions

Topological domain20 – 44244405Extracellular Potential
Transmembrane4425 – 444521Helical; Potential
Topological domain4446 – 4545100Cytoplasmic Potential
Domain26 – 6742LDL-receptor class A 1
Domain71 – 11141LDL-receptor class A 2
Domain112 – 15039EGF-like 1
Domain151 – 19040EGF-like 2; calcium-binding Potential
Repeat293 – 33543LDL-receptor class B 1
Repeat336 – 37944LDL-receptor class B 2
Repeat380 – 42344LDL-receptor class B 3
Domain475 – 52147EGF-like 3
Repeat572 – 61443LDL-receptor class B 4
Repeat615 – 66046LDL-receptor class B 5
Repeat661 – 71151LDL-receptor class B 6
Repeat712 – 75544LDL-receptor class B 7
Domain804 – 84441EGF-like 4
Domain853 – 89341LDL-receptor class A 3
Domain894 – 93441LDL-receptor class A 4
Domain935 – 97440LDL-receptor class A 5
Domain975 – 101440LDL-receptor class A 6
Domain1014 – 105441LDL-receptor class A 7
Domain1061 – 110040LDL-receptor class A 8
Domain1103 – 114341LDL-receptor class A 9
Domain1144 – 118340LDL-receptor class A 10
Domain1184 – 122340EGF-like 5
Domain1224 – 126340EGF-like 6
Repeat1310 – 135647LDL-receptor class B 8
Repeat1357 – 139943LDL-receptor class B 9
Repeat1400 – 144647LDL-receptor class B 10
Repeat1447 – 149145LDL-receptor class B 11
Repeat1492 – 153241LDL-receptor class B 12
Domain1537 – 158044EGF-like 7
Repeat1628 – 167043LDL-receptor class B 13
Repeat1671 – 171444LDL-receptor class B 14
Repeat1715 – 175440LDL-receptor class B 15
Repeat1755 – 179945LDL-receptor class B 16
Domain1847 – 188842EGF-like 8
Repeat1935 – 197743LDL-receptor class B 17
Repeat1978 – 202043LDL-receptor class B 18
Repeat2021 – 206444LDL-receptor class B 19
Repeat2065 – 210844LDL-receptor class B 20
Domain2156 – 219641EGF-like 9
Repeat2254 – 229542LDL-receptor class B 21
Repeat2296 – 234449LDL-receptor class B 22
Repeat2345 – 238945LDL-receptor class B 23
Repeat2390 – 243243LDL-receptor class B 24
Repeat2433 – 247442LDL-receptor class B 25
Domain2479 – 251941EGF-like 10
Domain2523 – 256442LDL-receptor class A 11
Domain2565 – 260339LDL-receptor class A 12
Domain2604 – 264239LDL-receptor class A 13
Domain2643 – 269149LDL-receptor class A 14
Domain2695 – 273339LDL-receptor class A 15
Domain2733 – 277240LDL-receptor class A 16
Domain2773 – 281543LDL-receptor class A 17
Domain2817 – 285640LDL-receptor class A 18
Domain2857 – 290044LDL-receptor class A 19
Domain2903 – 294139LDL-receptor class A 20
Domain2942 – 298241EGF-like 11
Domain2983 – 302341EGF-like 12; calcium-binding Potential
Repeat3070 – 311445LDL-receptor class B 26
Repeat3115 – 315743LDL-receptor class B 27
Repeat3158 – 320144LDL-receptor class B 28
Repeat3202 – 324443LDL-receptor class B 29
Repeat3245 – 328541LDL-receptor class B 30
Domain3291 – 333242EGF-like 13
Domain3333 – 337240LDL-receptor class A 21
Domain3373 – 341139LDL-receptor class A 22
Domain3412 – 345140LDL-receptor class A 23
Domain3452 – 349241LDL-receptor class A 24
Domain3493 – 353442LDL-receptor class A 25
Domain3535 – 357339LDL-receptor class A 26
Domain3574 – 361239LDL-receptor class A 27
Domain3612 – 365039LDL-receptor class A 28
Domain3653 – 369341LDL-receptor class A 29
Domain3694 – 373441LDL-receptor class A 30
Domain3740 – 377940LDL-receptor class A 31
Domain3782 – 382443EGF-like 14
Domain3825 – 386238EGF-like 15
Repeat3913 – 395543LDL-receptor class B 31
Repeat3971 – 401343LDL-receptor class B 32
Repeat4014 – 405744LDL-receptor class B 33
Repeat4058 – 410245LDL-receptor class B 34
Domain4148 – 418437EGF-like 16
Domain4197 – 423337EGF-like 17
Domain4233 – 426937EGF-like 18
Domain4269 – 430537EGF-like 19
Domain4305 – 434137EGF-like 20
Domain4341 – 437636EGF-like 21
Domain4374 – 441037EGF-like 22
Region4446 – 4545100Interaction with MAFB Ref.5
Motif3941 – 39444Recognition site for proteolytical processing Potential
Motif4503 – 45086NPXY motif

Sites

Metal binding8721Calcium 1; via carbonyl oxygen By similarity
Metal binding8751Calcium 1 By similarity
Metal binding8771Calcium 1; via carbonyl oxygen By similarity
Metal binding8791Calcium 1 By similarity
Metal binding8851Calcium 1 By similarity
Metal binding8861Calcium 1 By similarity
Metal binding10331Calcium 2; via carbonyl oxygen By similarity
Metal binding10361Calcium 2 By similarity
Metal binding10381Calcium 2; via carbonyl oxygen By similarity
Metal binding10401Calcium 2 By similarity
Metal binding10461Calcium 2 By similarity
Metal binding10471Calcium 2 By similarity
Metal binding10811Calcium 3; via carbonyl oxygen By similarity
Metal binding10841Calcium 3 By similarity
Metal binding10861Calcium 3; via carbonyl oxygen By similarity
Metal binding10881Calcium 3 By similarity
Metal binding10941Calcium 3 By similarity
Metal binding10951Calcium 3 By similarity

Amino acid modifications

Modified residue20101N6-acetyllysine Ref.12
Modified residue45081Phosphotyrosine By similarity
Modified residue45241Phosphoserine Ref.8
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Glycosylation3581N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Ref.10
Glycosylation7301N-linked (GlcNAc...) Ref.9
Glycosylation9291N-linked (GlcNAc...) Potential
Glycosylation10511N-linked (GlcNAc...) Potential
Glycosylation11551N-linked (GlcNAc...) Potential
Glycosylation11561N-linked (GlcNAc...) Potential
Glycosylation11961N-linked (GlcNAc...) Potential
Glycosylation12191N-linked (GlcNAc...) Potential
Glycosylation15121N-linked (GlcNAc...) Potential
Glycosylation15591N-linked (GlcNAc...) Potential
Glycosylation15761N-linked (GlcNAc...) Potential
Glycosylation16171N-linked (GlcNAc...) Potential
Glycosylation16461N-linked (GlcNAc...) Potential
Glycosylation17241N-linked (GlcNAc...) Potential
Glycosylation17341N-linked (GlcNAc...) Potential
Glycosylation17641N-linked (GlcNAc...) Potential
Glycosylation18261N-linked (GlcNAc...) Potential
Glycosylation19341N-linked (GlcNAc...) Potential
Glycosylation19961N-linked (GlcNAc...) Potential
Glycosylation20491N-linked (GlcNAc...) Potential
Glycosylation21181N-linked (GlcNAc...) Potential
Glycosylation21281N-linked (GlcNAc...) Ref.9
Glycosylation24731N-linked (GlcNAc...) Potential
Glycosylation25031N-linked (GlcNAc...) Potential
Glycosylation25221N-linked (GlcNAc...) Potential
Glycosylation26021N-linked (GlcNAc...) Potential
Glycosylation26211N-linked (GlcNAc...) Potential
Glycosylation26391N-linked (GlcNAc...) Potential
Glycosylation28161N-linked (GlcNAc...) Potential
Glycosylation29061N-linked (GlcNAc...) Potential
Glycosylation30491N-linked (GlcNAc...) Ref.9
Glycosylation30901N-linked (GlcNAc...) Potential
Glycosylation32651N-linked (GlcNAc...) Potential
Glycosylation33341N-linked (GlcNAc...) Potential
Glycosylation34891N-linked (GlcNAc...) Potential
Glycosylation36631N-linked (GlcNAc...) Potential
Glycosylation37891N-linked (GlcNAc...) Potential
Glycosylation38401N-linked (GlcNAc...) Potential
Glycosylation39541N-linked (GlcNAc...) Potential
Glycosylation40761N-linked (GlcNAc...) Potential
Glycosylation41261N-linked (GlcNAc...) Potential
Glycosylation41801N-linked (GlcNAc...) Potential
Glycosylation42791N-linked (GlcNAc...) Potential
Glycosylation42801N-linked (GlcNAc...) Potential
Glycosylation43651N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 41 By similarity UniProtKB P01130
Disulfide bond35 ↔ 54 By similarity UniProtKB P01130
Disulfide bond48 ↔ 65 By similarity UniProtKB P01130
Disulfide bond73 ↔ 86 By similarity UniProtKB P01130
Disulfide bond80 ↔ 99 By similarity UniProtKB P01130
Disulfide bond93 ↔ 109 By similarity UniProtKB P01130
Disulfide bond116 ↔ 125 By similarity UniProtKB P01130
Disulfide bond121 ↔ 134 By similarity UniProtKB P01130
Disulfide bond136 ↔ 149 By similarity UniProtKB P01130
Disulfide bond155 ↔ 165 By similarity UniProtKB P01130
Disulfide bond161 ↔ 174 By similarity UniProtKB P01130
Disulfide bond176 ↔ 189 By similarity UniProtKB P01130
Disulfide bond479 ↔ 494 By similarity UniProtKB P01130
Disulfide bond490 ↔ 505 By similarity UniProtKB P01130
Disulfide bond507 ↔ 520 By similarity UniProtKB P01130
Disulfide bond808 ↔ 819 By similarity UniProtKB P01130
Disulfide bond815 ↔ 828 By similarity UniProtKB P01130
Disulfide bond830 ↔ 843 By similarity UniProtKB P01130
Disulfide bond855 ↔ 867 By similarity UniProtKB Q07954
Disulfide bond862 ↔ 880 By similarity UniProtKB Q07954
Disulfide bond874 ↔ 891 By similarity UniProtKB Q07954
Disulfide bond896 ↔ 908 By similarity UniProtKB P01130
Disulfide bond903 ↔ 921 By similarity UniProtKB P01130
Disulfide bond915 ↔ 932 By similarity UniProtKB P01130
Disulfide bond937 ↔ 949 By similarity UniProtKB P01130
Disulfide bond944 ↔ 962 By similarity UniProtKB P01130
Disulfide bond956 ↔ 972 By similarity UniProtKB P01130
Disulfide bond977 ↔ 990 By similarity UniProtKB P01130
Disulfide bond985 ↔ 1003 By similarity UniProtKB P01130
Disulfide bond997 ↔ 1012 By similarity UniProtKB P01130
Disulfide bond1016 ↔ 1028 By similarity UniProtKB P01130
Disulfide bond1023 ↔ 1041 By similarity UniProtKB P01130
Disulfide bond1035 ↔ 1052 By similarity UniProtKB P01130
Disulfide bond1063 ↔ 1076 By similarity UniProtKB Q07954
Disulfide bond1070 ↔ 1089 By similarity UniProtKB Q07954
Disulfide bond1083 ↔ 1098 By similarity UniProtKB Q07954
Disulfide bond1105 ↔ 1119 By similarity UniProtKB P01130
Disulfide bond1113 ↔ 1132 By similarity UniProtKB P01130
Disulfide bond1126 ↔ 1141 By similarity UniProtKB P01130
Disulfide bond1146 ↔ 1160 By similarity UniProtKB P01130
Disulfide bond1153 ↔ 1173 By similarity UniProtKB P01130
Disulfide bond1167 ↔ 1183 By similarity UniProtKB P01130
Disulfide bond1186 ↔ 1197 By similarity UniProtKB P01130
Disulfide bond1193 ↔ 1207 By similarity UniProtKB P01130
Disulfide bond1209 ↔ 1222 By similarity UniProtKB P01130
Disulfide bond1228 ↔ 1238 By similarity UniProtKB P01130
Disulfide bond1234 ↔ 1247 By similarity UniProtKB P01130
Disulfide bond1249 ↔ 1262 By similarity UniProtKB P01130
Disulfide bond1541 ↔ 1554 By similarity UniProtKB P01130
Disulfide bond1550 ↔ 1564 By similarity UniProtKB P01130
Disulfide bond1566 ↔ 1579 By similarity UniProtKB P01130
Disulfide bond1851 ↔ 1862 By similarity UniProtKB P01130
Disulfide bond1858 ↔ 1872 By similarity UniProtKB P01130
Disulfide bond1874 ↔ 1887 By similarity UniProtKB P01130
Disulfide bond2160 ↔ 2171 By similarity UniProtKB P01130
Disulfide bond2167 ↔ 2181 By similarity UniProtKB P01130
Disulfide bond2183 ↔ 2195 By similarity UniProtKB P01130
Disulfide bond2483 ↔ 2494 By similarity UniProtKB P01130
Disulfide bond2490 ↔ 2504 By similarity UniProtKB P01130
Disulfide bond2506 ↔ 2518 By similarity UniProtKB P01130
Disulfide bond2525 ↔ 2538 By similarity UniProtKB P01130
Disulfide bond2533 ↔ 2551 By similarity UniProtKB P01130
Disulfide bond2545 ↔ 2562 By similarity UniProtKB P01130
Disulfide bond2567 ↔ 2579 By similarity UniProtKB P01130
Disulfide bond2574 ↔ 2592 By similarity UniProtKB P01130
Disulfide bond2586 ↔ 2601 By similarity UniProtKB P01130
Disulfide bond2606 ↔ 2618 By similarity UniProtKB P01130
Disulfide bond2613 ↔ 2631 By similarity UniProtKB P01130
Disulfide bond2625 ↔ 2640 By similarity UniProtKB P01130
Disulfide bond2645 ↔ 2667 By similarity UniProtKB P01130
Disulfide bond2661 ↔ 2680 By similarity UniProtKB P01130
Disulfide bond2674 ↔ 2689 By similarity UniProtKB P01130
Disulfide bond2697 ↔ 2709 By similarity UniProtKB P01130
Disulfide bond2704 ↔ 2722 By similarity UniProtKB P01130
Disulfide bond2716 ↔ 2731 By similarity UniProtKB P01130
Disulfide bond2735 ↔ 2747 By similarity UniProtKB P01130
Disulfide bond2742 ↔ 2760 By similarity UniProtKB P01130
Disulfide bond2754 ↔ 2770 By similarity UniProtKB P01130
Disulfide bond2775 ↔ 2788 By similarity UniProtKB P01130
Disulfide bond2782 ↔ 2801 By similarity UniProtKB P01130
Disulfide bond2795 ↔ 2813 By similarity UniProtKB P01130
Disulfide bond2819 ↔ 2831 By similarity UniProtKB P01130
Disulfide bond2826 ↔ 2844 By similarity UniProtKB P01130
Disulfide bond2838 ↔ 2854 By similarity UniProtKB P01130
Disulfide bond2859 ↔ 2871 By similarity UniProtKB P01130
Disulfide bond2866 ↔ 2885 By similarity UniProtKB P01130
Disulfide bond2879 ↔ 2898 By similarity UniProtKB P01130
Disulfide bond2905 ↔ 2918 By similarity UniProtKB P01130
Disulfide bond2913 ↔ 2931 By similarity UniProtKB P01130
Disulfide bond2925 ↔ 2940 By similarity UniProtKB P01130
Disulfide bond2945 ↔ 2957 By similarity UniProtKB P01130
Disulfide bond2953 ↔ 2966 By similarity UniProtKB P01130
Disulfide bond2968 ↔ 2981 By similarity UniProtKB P01130
Disulfide bond2987 ↔ 2997 By similarity UniProtKB P01130
Disulfide bond2993 ↔ 3006 By similarity UniProtKB P01130
Disulfide bond3008 ↔ 3022 By similarity UniProtKB P01130
Disulfide bond3295 ↔ 3306 By similarity UniProtKB P01130
Disulfide bond3302 ↔ 3316 By similarity UniProtKB P01130
Disulfide bond3318 ↔ 3331 By similarity UniProtKB P01130
Disulfide bond3335 ↔ 3347 By similarity UniProtKB P01130
Disulfide bond3342 ↔ 3360 By similarity UniProtKB P01130
Disulfide bond3354 ↔ 3370 By similarity UniProtKB P01130
Disulfide bond3375 ↔ 3387 By similarity UniProtKB P01130
Disulfide bond3382 ↔ 3400 By similarity UniProtKB P01130
Disulfide bond3394 ↔ 3409 By similarity UniProtKB P01130
Disulfide bond3414 ↔ 3427 By similarity UniProtKB P01130
Disulfide bond3421 ↔ 3440 By similarity UniProtKB P01130
Disulfide bond3434 ↔ 3449 By similarity UniProtKB P01130
Disulfide bond3454 ↔ 3467 By similarity UniProtKB P01130
Disulfide bond3461 ↔ 3480 By similarity UniProtKB P01130
Disulfide bond3474 ↔ 3490 By similarity UniProtKB P01130
Disulfide bond3495 ↔ 3508 By similarity UniProtKB P01130
Disulfide bond3502 ↔ 3521 By similarity UniProtKB P01130
Disulfide bond3515 ↔ 3532 By similarity UniProtKB P01130
Disulfide bond3537 ↔ 3549 By similarity UniProtKB P01130
Disulfide bond3544 ↔ 3562 By similarity UniProtKB P01130
Disulfide bond3556 ↔ 3571 By similarity UniProtKB P01130
Disulfide bond3576 ↔ 3588 By similarity UniProtKB P01130
Disulfide bond3583 ↔ 3601 By similarity UniProtKB P01130
Disulfide bond3595 ↔ 3610 By similarity UniProtKB P01130
Disulfide bond3614 ↔ 3626 By similarity UniProtKB P01130
Disulfide bond3621 ↔ 3639 By similarity UniProtKB P01130
Disulfide bond3633 ↔ 3648 By similarity UniProtKB P01130
Disulfide bond3655 ↔ 3667 By similarity UniProtKB P01130
Disulfide bond3662 ↔ 3680 By similarity UniProtKB P01130
Disulfide bond3674 ↔ 3691 By similarity UniProtKB P01130
Disulfide bond3696 ↔ 3710 By similarity UniProtKB P01130
Disulfide bond3704 ↔ 3723 By similarity UniProtKB P01130
Disulfide bond3717 ↔ 3732 By similarity UniProtKB P01130
Disulfide bond3742 ↔ 3755 By similarity UniProtKB P01130
Disulfide bond3750 ↔ 3768 By similarity UniProtKB P01130
Disulfide bond3762 ↔ 3777 By similarity UniProtKB P01130
Disulfide bond3786 ↔ 3799 By similarity UniProtKB P01130
Disulfide bond3793 ↔ 3808 By similarity UniProtKB P01130
Disulfide bond3810 ↔ 3823 By similarity UniProtKB P01130
Disulfide bond3829 ↔ 3839 By similarity UniProtKB P01130
Disulfide bond3835 ↔ 3848 By similarity UniProtKB P01130
Disulfide bond3850 ↔ 3861 By similarity UniProtKB P01130
Disulfide bond4152 ↔ 4161 By similarity UniProtKB P01130
Disulfide bond4157 ↔ 4170 By similarity UniProtKB P01130
Disulfide bond4172 ↔ 4183 By similarity UniProtKB P01130
Disulfide bond4201 ↔ 4211 By similarity UniProtKB P01130
Disulfide bond4205 ↔ 4221 By similarity UniProtKB P01130
Disulfide bond4223 ↔ 4232 By similarity UniProtKB P01130
Disulfide bond4237 ↔ 4247 By similarity UniProtKB P01130
Disulfide bond4241 ↔ 4257 By similarity UniProtKB P01130
Disulfide bond4259 ↔ 4268 By similarity UniProtKB P01130
Disulfide bond4273 ↔ 4283 By similarity UniProtKB P01130
Disulfide bond4277 ↔ 4293 By similarity UniProtKB P01130
Disulfide bond4295 ↔ 4304 By similarity UniProtKB P01130
Disulfide bond4309 ↔ 4319 By similarity UniProtKB P01130
Disulfide bond4313 ↔ 4329 By similarity UniProtKB P01130
Disulfide bond4331 ↔ 4340 By similarity UniProtKB P01130
Disulfide bond4345 ↔ 4353 By similarity UniProtKB P01130
Disulfide bond4348 ↔ 4364 By similarity UniProtKB P01130
Disulfide bond4366 ↔ 4375 By similarity UniProtKB P01130
Disulfide bond4378 ↔ 4388 By similarity UniProtKB P01130
Disulfide bond4382 ↔ 4398 By similarity UniProtKB P01130
Disulfide bond4400 ↔ 4409 By similarity UniProtKB P01130

Experimental info

Sequence conflict26421A → T in AAL09567. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q91ZX7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 9904CF5DF5EE333E

FASTA4,545504,742
        10         20         30         40         50         60 
MLTPPLLLLL PLLSALVSGA TMDAPKTCSP KQFACRDQIT CISKGWRCDG ERDCPDGSDE 

        70         80         90        100        110        120 
APEICPQSKA QRCPPNEHSC LGTELCVPMS RLCNGIQDCM DGSDEGAHCR ELRANCSRMG 

       130        140        150        160        170        180 
CQHHCVPTPS GPTCYCNSSF QLQADGKTCK DFDECSVYGT CSQLCTNTDG SFTCGCVEGY 

       190        200        210        220        230        240 
LLQPDNRSCK AKNEPVDRPP VLLIANSQNI LATYLSGAQV STITPTSTRQ TTAMDFSYAN 

       250        260        270        280        290        300 
ETVCWVHVGD SAAQTQLKCA RMPGLKGFVD EHTINISLSL HHVEQMAIDW LTGNFYFVDD 

       310        320        330        340        350        360 
IDDRIFVCNR NGDTCVTLLD LELYNPKGIA LDPAMGKVFF TDYGQIPKVE RCDMDGQNRT 

       370        380        390        400        410        420 
KLVDSKIVFP HGITLDLVSR LVYWADAYLD YIEVVDYEGK GRQTIIQGIL IEHLYGLTVF 

       430        440        450        460        470        480 
ENYLYATNSD NANTQQKTSV IRVNRFNSTE YQVVTRVDKG GALHIYHQRR QPRVRSHACE 

       490        500        510        520        530        540 
NDQYGKPGGC SDICLLANSH KARTCRCRSG FSLGSDGKSC KKPEHELFLV YGKGRPGIIR 

       550        560        570        580        590        600 
GMDMGAKVPD EHMIPIENLM NPRALDFHAE TGFIYFADTT SYLIGRQKID GTERETILKD 

       610        620        630        640        650        660 
GIHNVEGVAV DWMGDNLYWT DDGPKKTISV ARLEKAAQTR KTLIEGKMTH PRAIVVDPLN 

       670        680        690        700        710        720 
GWMYWTDWEE DPKDSRRGRL ERAWMDGSHR DIFVTSKTVL WPNGLSLDIP AGRLYWVDAF 

       730        740        750        760        770        780 
YDRIETILLN GTDRKIVYEG PELNHAFGLC HHGNYLFWTE YRSGSVYRLE RGVAGAPPTV 

       790        800        810        820        830        840 
TLLRSERPPI FEIRMYDAQQ QQVGTNKCRV NNGGCSSLCL ATPGSRQCAC AEDQVLDTDG 

       850        860        870        880        890        900 
VTCLANPSYV PPPQCQPGEF ACANNRCIQE RWKCDGDNDC LDNSDEAPAL CHQHTCPSDR 

       910        920        930        940        950        960 
FKCENNRCIP NRWLCDGDND CGNSEDESNA TCSARTCPPN QFSCASGRCI PISWTCDLDD 

       970        980        990       1000       1010       1020 
DCGDRSDESA SCAYPTCFPL TQFTCNNGRC ININWRCDND NDCGDNSDEA GCSHSCSSTQ 

      1030       1040       1050       1060       1070       1080 
FKCNSGRCIP EHWTCDGDND CGDYSDETHA NCTNQATRPP GGCHSDEFQC RLDGLCIPLR 

      1090       1100       1110       1120       1130       1140 
WRCDGDTDCM DSSDEKSCEG VTHVCDPNVK FGCKDSARCI SKAWVCDGDS DCEDNSDEEN 

      1150       1160       1170       1180       1190       1200 
CEALACRPPS HPCANNTSVC LPPDKLCDGK DDCGDGSDEG ELCDQCSLNN GGCSHNCSVA 

      1210       1220       1230       1240       1250       1260 
PGEGIVCSCP LGMELGSDNH TCQIQSYCAK HLKCSQKCDQ NKFSVKCSCY EGWVLEPDGE 

      1270       1280       1290       1300       1310       1320 
SCRSLDPFKP FIIFSNRHEI RRIDLHKGDY SVLVPGLRNT IALDFHLSQS ALYWTDVVED 

      1330       1340       1350       1360       1370       1380 
KIYRGKLLDN GALTSFEVVI QYGLATPEGL AVDWIAGNIY WVESNLDQIE VAKLDGTLRT 

      1390       1400       1410       1420       1430       1440 
TLLAGDIEHP RAIALDPRDG ILFWTDWDAS LPRIEAASMS GAGRRTIHRE TGSGGWPNGL 

      1450       1460       1470       1480       1490       1500 
TVDYLEKRIL WIDARSDAIY SARYDGSGHM EVLRGHEFLS HPFAVTLYGG EVYWTDWRTN 

      1510       1520       1530       1540       1550       1560 
TLAKANKWTG HNVTVVQRTN TQPFDLQVYH PSRQPMAPNP CEANGGRGPC SHLCLINYNR 

      1570       1580       1590       1600       1610       1620 
TVSCACPHLM KLHKDNTTCY EFKKFLLYAR QMEIRGVDLD APYYNYIISF TVPDIDNVTV 

      1630       1640       1650       1660       1670       1680 
LDYDAREQRV YWSDVRTQAI KRAFINGTGV ETVVSADLPN AHGLAVDWVS RNLFWTSYDT 

      1690       1700       1710       1720       1730       1740 
NKKQINVARL DGSFKNAVVQ GLEQPHGLVV HPLRGKLYWT DGDNISMANM DGSNHTLLFS 

      1750       1760       1770       1780       1790       1800 
GQKGPVGLAI DFPESKLYWI SSGNHTINRC NLDGSELEVI DTMRSQLGKA TALAIMGDKL 

      1810       1820       1830       1840       1850       1860 
WWADQVSEKM GTCNKADGSG SVVLRNSTTL VMHMKVYDES IQLEHEGTNP CSVNNGDCSQ 

      1870       1880       1890       1900       1910       1920 
LCLPTSETTR SCMCTAGYSL RSGQQACEGV GSFLLYSVHE GIRGIPLDPN DKSDALVPVS 

      1930       1940       1950       1960       1970       1980 
GTSLAVGIDF HAENDTIYWV DMGLSTISRA KRDQTWREDV VTNGIGRVEG IAVDWIAGNI 

      1990       2000       2010       2020       2030       2040 
YWTDQGFDVI EVARLNGSFR YVVISQGLDK PRAITVHPEK GYLFWTEWGH YPRIERSRLD 

      2050       2060       2070       2080       2090       2100 
GTERVVLVNV SISWPNGISV DYQGGKLYWC DARMDKIERI DLETGENREV VLSSNNMDMF 

      2110       2120       2130       2140       2150       2160 
SVSVFEDFIY WSDRTHANGS IKRGCKDNAT DSVPLRTGIG VQLKDIKVFN RDRQKGTNVC 

      2170       2180       2190       2200       2210       2220 
AVANGGCQQL CLYRGGGQRA CACAHGMLAE DGASCREYAG YLLYSERTIL KSIHLSDERN 

      2230       2240       2250       2260       2270       2280 
LNAPVQPFED PEHMKNVIAL AFDYRAGTSP GTPNRIFFSD IHFGNIQQIN DDGSGRTTIV 

      2290       2300       2310       2320       2330       2340 
ENVGSVEGLA YHRGWDTLYW TSYTTSTITR HTVDQTRPGA FERETVITMS GDDHPRAFVL 

      2350       2360       2370       2380       2390       2400 
DECQNLMFWT NWNELHPSIM RAALSGANVL TLIEKDIRTP NGLAIDHRAE KLYFSDATLD 

      2410       2420       2430       2440       2450       2460 
KIERCEYDGS HRYVILKSEP VHPFGLAVYG EHIFWTDWVR RAVQRANKYV GSDMKLLRVD 

      2470       2480       2490       2500       2510       2520 
IPQQPMGIIA VANDTNSCEL SPCRINNGGC QDLCLLTHQG HVNCSCRGGR ILQEDFTCRA 

      2530       2540       2550       2560       2570       2580 
VNSSCRAQDE FECANGECIS FSLTCDGVSH CKDKSDEKPS YCNSRRCKKT FRQCNNGRCV 

      2590       2600       2610       2620       2630       2640 
SNMLWCNGVD DCGDGSDEIP CNKTACGVGE FRCRDGSCIG NSSRCNQFVD CEDASDEMNC 

      2650       2660       2670       2680       2690       2700 
SATDCSSYFR LGVKGVLFQP CERTSLCYAP SWVCDGANDC GDYSDERDCP GVKRPRCPLN 

      2710       2720       2730       2740       2750       2760 
YFACPSGRCI PMSWTCDKED DCENGEDETH CNKFCSEAQF ECQNHRCISK QWLCDGSDDC 

      2770       2780       2790       2800       2810       2820 
GDGSDEAAHC EGKTCGPSSF SCPGTHVCVP ERWLCDGDKD CTDGADESVT AGCLYNSTCD 

      2830       2840       2850       2860       2870       2880 
DREFMCQNRL CIPKHFVCDH DRDCADGSDE SPECEYPTCG PNEFRCANGR CLSSRQWECD 

      2890       2900       2910       2920       2930       2940 
GENDCHDHSD EAPKNPHCTS PEHKCNASSQ FLCSSGRCVA EALLCNGQDD CGDGSDERGC 

      2950       2960       2970       2980       2990       3000 
HVNECLSRKL SGCSQDCEDL KIGFKCRCRP GFRLKDDGRT CADLDECSTT FPCSQLCINT 

      3010       3020       3030       3040       3050       3060 
HGSYKCLCVE GYAPRGGDPH SCKAVTDEEP FLIFANRYYL RKLNLDGSNY TLLKQGLNNA 

      3070       3080       3090       3100       3110       3120 
VALDFDYREQ MIYWTDVTTQ GSMIRRMHLN GSNVQVLHRT GLSNPDGLAV DWVGGNLYWC 

      3130       3140       3150       3160       3170       3180 
DKGRDTIEVS KLNGAYRTVL VSSGLREPRA LVVDVQNGYL YWTDWGDHSL IGRIGMDGSG 

      3190       3200       3210       3220       3230       3240 
RSIIVDTKIT WPNGLTVDYV TERIYWADAR EDYIEFASLD GSNRHVVLSQ DIPHIFALTL 

      3250       3260       3270       3280       3290       3300 
FEDYVYWTDW ETKSINRAHK TTGANKTLLI STLHRPMDLH VFHALRQPDV PNHPCKVNNG 

      3310       3320       3330       3340       3350       3360 
GCSNLCLLSP GGGHKCACPT NFYLGGDGRT CVSNCTASQF VCKNDKCIPF WWKCDTEDDC 

      3370       3380       3390       3400       3410       3420 
GDHSDEPPDC PEFKCRPGQF QCSTGICTNP AFICDGDNDC QDNSDEANCD IHVCLPSQFK 

      3430       3440       3450       3460       3470       3480 
CTNTNRCIPG IFRCNGQDNC GDGEDERDCP EVTCAPNQFQ CSITKRCIPR VWVCDRDNDC 

      3490       3500       3510       3520       3530       3540 
VDGSDEPANC TQMTCGVDEF RCKDSGRCIP ARWKCDGEDD CGDGSDEPKE ECDERTCEPY 

      3550       3560       3570       3580       3590       3600 
QFRCKNNRCV PGRWQCDYDN DCGDNSDEES CTPRPCSESE FSCANGRCIA GRWKCDGDHD 

      3610       3620       3630       3640       3650       3660 
CADGSDEKDC TPRCDMDQFQ CKSGHCIPLR WRCDADADCM DGSDEEACGT GVRTCPLDEF 

      3670       3680       3690       3700       3710       3720 
QCNNTLCKPL AWKCDGEDDC GDNSDENPEE CARFICPPNR PFRCKNDRVC LWIGRQCDGV 

      3730       3740       3750       3760       3770       3780 
DNCGDGTDEE DCEPPTAQNP HCKDKKEFLC RNQRCLSSSL RCNMFDDCGD GSDEEDCSID 

      3790       3800       3810       3820       3830       3840 
PKLTSCATNA SMCGDEARCV RTEKAAYCAC RSGFHTVPGQ PGCQDINECL RFGTCSQLCN 

      3850       3860       3870       3880       3890       3900 
NTKGGHLCSC ARNFMKTHNT CKAEGSEYQV LYIADDNEIR SLFPGHPHSA YEQTFQGDES 

      3910       3920       3930       3940       3950       3960 
VRIDAMDVHV KAGRVYWTNW HTGTISYRSL PPAAPPTTSN RHRRQIDRGV THLNISGLKM 

      3970       3980       3990       4000       4010       4020 
PRGIAIDWVA GNVYWTDSGR DVIEVAQMKG ENRKTLISGM IDEPHAIVVD PLRGTMYWSD 

      4030       4040       4050       4060       4070       4080 
WGNHPKIETA AMDGTLRETL VQDNIQWPTG LAVDYHNERL YWADAKLSVI GSIRLNGTDP 

      4090       4100       4110       4120       4130       4140 
IVAADSKRGL SHPFSIDVFE DYIYGVTYIN NRVFKIHKFG HSPLINLTGG LSHASDVVLY 

      4150       4160       4170       4180       4190       4200 
HQHKQPEVTN PCDRKKCEWL CLLSPSGPVC TCPNGKRLDN GTCVPVPSPT PPPDAPRPGT 

      4210       4220       4230       4240       4250       4260 
CTLQCFNGGS CFLNARRQPK CRCQPRYTGD KCELDQCWEY CHNGGTCAAS PSGMPTCRCP 

      4270       4280       4290       4300       4310       4320 
TGFTGPKCTA QVCAGYCSNN STCTVNQGNQ PQCRCLPGFL GDRCQYRQCS GFCENFGTCQ 

      4330       4340       4350       4360       4370       4380 
MAADGSRQCR CTVYFEGPRC EVNKCSRCLQ GACVVNKQTG DVTCNCTDGR VAPSCLTCID 

      4390       4400       4410       4420       4430       4440 
HCSNGGSCTM NSKMMPECQC PPHMTGPRCE EQVVSQQQPG HMASILIPLL LLLLLLLVAG 

      4450       4460       4470       4480       4490       4500 
VVFWYKRRVR GAKGFQHQRM TNGAMNVEIG NPTYKMYEGG EPDDVGGLLD ADFALDPDKP 

      4510       4520       4530       4540 
TNFTNPVYAT LYMGGHGSRH SLASTDEKRE LLGRGPEDEI GDPLA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of the murine alpha-2-macroglobulin receptor cDNA."
Van Leuven F., Stas L., Raymakers L., Overbergh L., De Strooper B., Hilliker C., Lorent K., Fias E., Umans L., Torrekens S., Serneels L., Moechars D., Van den Berghe H.
Biochim. Biophys. Acta 1173:71-74(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Functional expression of murine LRP1 requires correction of Lrp1 cDNA sequences."
Smeijers L., Willems S., Lauwers A., Thiry E., van Leuven F., Roebroek A.J.M.
Biochim. Biophys. Acta 1577:155-158(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/J and CBA.
[3]"The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A."
Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J., Strickland D.K., Saelinger C.B.
J. Biol. Chem. 267:12420-12423(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RECEPTOR FOR P.AERUGINOSA EXOA TOXIN.
[4]"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2."
Morris S.M., Cooper J.A.
Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
[5]"Low-density lipoprotein receptor-related protein interacts with MafB, a regulator of hindbrain development."
Petersen H.H., Hilpert J., Jacobsen C., Lauwers A., Roebroek A.J.M., Willnow T.E.
FEBS Lett. 565:23-27(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAFB.
[6]"LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation."
Herz J., Clouthier D.E., Hammer R.E.
Cell 71:411-421(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]Erratum
Herz J., Couthier D.E., Hammer R.E.
Cell 73:428-428(1993) [PubMed] [Europe PMC] [Abstract]
[8]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-730; ASN-2128 AND ASN-3049.
Tissue: Myoblast.
[10]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-447.
[11]"Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae."
Jorgensen R., Purdy A.E., Fieldhouse R.J., Kimber M.S., Bartlett D.H., Merrill A.R.
J. Biol. Chem. 283:10671-10678(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RECEPTOR FOR CHOLIX TOXIN.
[12]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2010, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67469 mRNA. Translation: CAA47817.1. Sequence problems.
AF367720 mRNA. Translation: AAL09566.1.
AF369477 expand/collapse EMBL AC list , AF369389, AF369390, AF369391, AF369392, AF369393, AF369394, AF369395, AF369396, AF369397, AF369398, AF369399, AF369400, AF369401, AF369402, AF369403, AF369404, AF369405, AF369406, AF369407, AF369408, AF369409, AF369410, AF369411, AF369412, AF369413, AF369414, AF369415, AF369416, AF369417, AF369418, AF369419, AF369420, AF369421, AF369422, AF369423, AF369424, AF369425, AF369426, AF369427, AF369428, AF369429, AF369430, AF369431, AF369432, AF369433, AF369434, AF369435, AF369436, AF369437, AF369438, AF369439, AF369440, AF369441, AF369442, AF369443, AF369444, AF369445, AF369446, AF369447, AF369448, AF369449, AF369450, AF369451, AF369452, AF369453, AF369454, AF369455, AF369456, AF369457, AF369458, AF369459, AF369460, AF369461, AF369462, AF369463, AF369464, AF369465, AF369466, AF369467, AF369468, AF369469, AF369470, AF369471, AF369472, AF369473, AF369474, AF369475, AF369476 Genomic DNA. Translation: AAL09567.1.
CCDSCCDS24245.1.
PIRS25111.
RefSeqNP_032538.2. NM_008512.2.
UniGeneMm.271854.

3D structure databases

ProteinModelPortalQ91ZX7.
SMRQ91ZX7. Positions 26-844, 851-1179, 1186-1567, 1585-2519, 2529-4412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201201. 6 interactions.
DIPDIP-47785N.
IntActQ91ZX7. 13 interactions.
MINTMINT-1848960.

PTM databases

PhosphoSiteQ91ZX7.

Proteomic databases

MaxQBQ91ZX7.
PaxDbQ91ZX7.
PRIDEQ91ZX7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049149; ENSMUSP00000044004; ENSMUSG00000040249.
GeneID16971.
KEGGmmu:16971.
UCSCuc007hjx.1. mouse.

Organism-specific databases

CTD4035.
MGIMGI:96828. Lrp1.

Phylogenomic databases

eggNOGNOG235850.
GeneTreeENSGT00750000117273.
HOGENOMHOG000230574.
HOVERGENHBG006292.
InParanoidQ91ZX7.
KOK04550.
OrthoDBEOG790FZT.
PhylomeDBQ91ZX7.
TreeFamTF315253.

Gene expression databases

ArrayExpressQ91ZX7.
BgeeQ91ZX7.
GenevestigatorQ91ZX7.

Family and domain databases

Gene3D2.120.10.30. 8 hits.
4.10.400.10. 29 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR006150. Cys_repeat_1.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamPF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00181. EGF. 17 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 35 hits.
SM00289. WR1. 4 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 9 hits.
SSF57424. SSF57424. 30 hits.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

NextBio291026.
PROQ91ZX7.
SOURCESearch...

Entry information

Entry nameLRP1_MOUSE
AccessionPrimary (citable) accession number: Q91ZX7
Secondary accession number(s): Q61291, Q920Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot