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Q91ZX7

- LRP1_MOUSE

UniProt

Q91ZX7 - LRP1_MOUSE

Protein

Prolow-density lipoprotein receptor-related protein 1

Gene

Lrp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 Vibrio cholerae cholix toxin and for Pseudomonas aeruginosa exotoxin A.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi872 – 8721Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi875 – 8751Calcium 1By similarity
    Metal bindingi877 – 8771Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi879 – 8791Calcium 1By similarity
    Metal bindingi885 – 8851Calcium 1By similarity
    Metal bindingi886 – 8861Calcium 1By similarity
    Metal bindingi1033 – 10331Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi1036 – 10361Calcium 2By similarity
    Metal bindingi1038 – 10381Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi1040 – 10401Calcium 2By similarity
    Metal bindingi1046 – 10461Calcium 2By similarity
    Metal bindingi1047 – 10471Calcium 2By similarity
    Metal bindingi1081 – 10811Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi1084 – 10841Calcium 3By similarity
    Metal bindingi1086 – 10861Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi1088 – 10881Calcium 3By similarity
    Metal bindingi1094 – 10941Calcium 3By similarity
    Metal bindingi1095 – 10951Calcium 3By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Molecular functioni

    Developmental protein, Receptor

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196575. Scavenging of heme from plasma.
    REACT_198569. Retinoid metabolism and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolow-density lipoprotein receptor-related protein 1
    Short name:
    LRP-1
    Alternative name(s):
    Alpha-2-macroglobulin receptor
    Short name:
    A2MR
    CD_antigen: CD91
    Cleaved into the following 3 chains:
    Gene namesi
    Name:Lrp1Imported
    Synonyms:A2mrImported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:96828. Lrp1.

    Subcellular locationi

    Chain 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

    GO - Cellular componenti

    1. clathrin-coated vesicle Source: Ensembl
    2. coated pit Source: UniProtKB-SubCell
    3. dendrite Source: Ensembl
    4. endosome Source: Ensembl
    5. integral component of plasma membrane Source: UniProtKB
    6. lysosomal membrane Source: Ensembl
    7. membrane Source: MGI
    8. neuronal cell body Source: Ensembl
    9. nucleus Source: UniProtKB-SubCell
    10. perinuclear region of cytoplasm Source: MGI
    11. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Death during early embryogenesis around 14 dpc.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 45454526Prolow-density lipoprotein receptor-related protein 1PRO_0000273273Add
    BLAST
    Chaini20 – ?39443925Low-density lipoprotein receptor-related protein 1 515 kDa subunitPRO_0000302753Add
    BLAST
    Chaini?3945 – 4545601Low-density lipoprotein receptor-related protein 1 85 kDa subunitPRO_0000302754Add
    BLAST
    Chaini?4442 – 4545104Low-density lipoprotein receptor-related protein 1 intracellular domainPRO_0000302755Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 41By similarity
    Disulfide bondi35 ↔ 54By similarity
    Disulfide bondi48 ↔ 65By similarity
    Disulfide bondi73 ↔ 86By similarity
    Disulfide bondi80 ↔ 99By similarity
    Disulfide bondi93 ↔ 109By similarity
    Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi116 ↔ 125By similarity
    Disulfide bondi121 ↔ 134By similarity
    Disulfide bondi136 ↔ 149By similarity
    Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi155 ↔ 165By similarity
    Disulfide bondi161 ↔ 174By similarity
    Disulfide bondi176 ↔ 189By similarity
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi447 – 4471N-linked (GlcNAc...)1 Publication
    Disulfide bondi479 ↔ 494By similarity
    Disulfide bondi490 ↔ 505By similarity
    Disulfide bondi507 ↔ 520By similarity
    Glycosylationi730 – 7301N-linked (GlcNAc...)1 Publication
    Disulfide bondi808 ↔ 819By similarity
    Disulfide bondi815 ↔ 828By similarity
    Disulfide bondi830 ↔ 843By similarity
    Disulfide bondi855 ↔ 867By similarity
    Disulfide bondi862 ↔ 880By similarity
    Disulfide bondi874 ↔ 891By similarity
    Disulfide bondi896 ↔ 908By similarity
    Disulfide bondi903 ↔ 921By similarity
    Disulfide bondi915 ↔ 932By similarity
    Glycosylationi929 – 9291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi937 ↔ 949By similarity
    Disulfide bondi944 ↔ 962By similarity
    Disulfide bondi956 ↔ 972By similarity
    Disulfide bondi977 ↔ 990By similarity
    Disulfide bondi985 ↔ 1003By similarity
    Disulfide bondi997 ↔ 1012By similarity
    Disulfide bondi1016 ↔ 1028By similarity
    Disulfide bondi1023 ↔ 1041By similarity
    Disulfide bondi1035 ↔ 1052By similarity
    Glycosylationi1051 – 10511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1063 ↔ 1076By similarity
    Disulfide bondi1070 ↔ 1089By similarity
    Disulfide bondi1083 ↔ 1098By similarity
    Disulfide bondi1105 ↔ 1119By similarity
    Disulfide bondi1113 ↔ 1132By similarity
    Disulfide bondi1126 ↔ 1141By similarity
    Disulfide bondi1146 ↔ 1160By similarity
    Disulfide bondi1153 ↔ 1173By similarity
    Glycosylationi1155 – 11551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1156 – 11561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1167 ↔ 1183By similarity
    Disulfide bondi1186 ↔ 1197By similarity
    Disulfide bondi1193 ↔ 1207By similarity
    Glycosylationi1196 – 11961N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1209 ↔ 1222By similarity
    Glycosylationi1219 – 12191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1228 ↔ 1238By similarity
    Disulfide bondi1234 ↔ 1247By similarity
    Disulfide bondi1249 ↔ 1262By similarity
    Glycosylationi1512 – 15121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1541 ↔ 1554By similarity
    Disulfide bondi1550 ↔ 1564By similarity
    Glycosylationi1559 – 15591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1566 ↔ 1579By similarity
    Glycosylationi1576 – 15761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1617 – 16171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1646 – 16461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1724 – 17241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1734 – 17341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1764 – 17641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1826 – 18261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1851 ↔ 1862By similarity
    Disulfide bondi1858 ↔ 1872By similarity
    Disulfide bondi1874 ↔ 1887By similarity
    Glycosylationi1934 – 19341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1996 – 19961N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2010 – 20101N6-acetyllysine1 Publication
    Glycosylationi2049 – 20491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2118 – 21181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2128 – 21281N-linked (GlcNAc...)1 Publication
    Disulfide bondi2160 ↔ 2171By similarity
    Disulfide bondi2167 ↔ 2181By similarity
    Disulfide bondi2183 ↔ 2195By similarity
    Glycosylationi2473 – 24731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2483 ↔ 2494By similarity
    Disulfide bondi2490 ↔ 2504By similarity
    Glycosylationi2503 – 25031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2506 ↔ 2518By similarity
    Glycosylationi2522 – 25221N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2525 ↔ 2538By similarity
    Disulfide bondi2533 ↔ 2551By similarity
    Disulfide bondi2545 ↔ 2562By similarity
    Disulfide bondi2567 ↔ 2579By similarity
    Disulfide bondi2574 ↔ 2592By similarity
    Disulfide bondi2586 ↔ 2601By similarity
    Glycosylationi2602 – 26021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2606 ↔ 2618By similarity
    Disulfide bondi2613 ↔ 2631By similarity
    Glycosylationi2621 – 26211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2625 ↔ 2640By similarity
    Glycosylationi2639 – 26391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2645 ↔ 2667By similarity
    Disulfide bondi2661 ↔ 2680By similarity
    Disulfide bondi2674 ↔ 2689By similarity
    Disulfide bondi2697 ↔ 2709By similarity
    Disulfide bondi2704 ↔ 2722By similarity
    Disulfide bondi2716 ↔ 2731By similarity
    Disulfide bondi2735 ↔ 2747By similarity
    Disulfide bondi2742 ↔ 2760By similarity
    Disulfide bondi2754 ↔ 2770By similarity
    Disulfide bondi2775 ↔ 2788By similarity
    Disulfide bondi2782 ↔ 2801By similarity
    Disulfide bondi2795 ↔ 2813By similarity
    Glycosylationi2816 – 28161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2819 ↔ 2831By similarity
    Disulfide bondi2826 ↔ 2844By similarity
    Disulfide bondi2838 ↔ 2854By similarity
    Disulfide bondi2859 ↔ 2871By similarity
    Disulfide bondi2866 ↔ 2885By similarity
    Disulfide bondi2879 ↔ 2898By similarity
    Disulfide bondi2905 ↔ 2918By similarity
    Glycosylationi2906 – 29061N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2913 ↔ 2931By similarity
    Disulfide bondi2925 ↔ 2940By similarity
    Disulfide bondi2945 ↔ 2957By similarity
    Disulfide bondi2953 ↔ 2966By similarity
    Disulfide bondi2968 ↔ 2981By similarity
    Disulfide bondi2987 ↔ 2997By similarity
    Disulfide bondi2993 ↔ 3006By similarity
    Disulfide bondi3008 ↔ 3022By similarity
    Glycosylationi3049 – 30491N-linked (GlcNAc...)1 Publication
    Glycosylationi3090 – 30901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3265 – 32651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3295 ↔ 3306By similarity
    Disulfide bondi3302 ↔ 3316By similarity
    Disulfide bondi3318 ↔ 3331By similarity
    Glycosylationi3334 – 33341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3335 ↔ 3347By similarity
    Disulfide bondi3342 ↔ 3360By similarity
    Disulfide bondi3354 ↔ 3370By similarity
    Disulfide bondi3375 ↔ 3387By similarity
    Disulfide bondi3382 ↔ 3400By similarity
    Disulfide bondi3394 ↔ 3409By similarity
    Disulfide bondi3414 ↔ 3427By similarity
    Disulfide bondi3421 ↔ 3440By similarity
    Disulfide bondi3434 ↔ 3449By similarity
    Disulfide bondi3454 ↔ 3467By similarity
    Disulfide bondi3461 ↔ 3480By similarity
    Disulfide bondi3474 ↔ 3490By similarity
    Glycosylationi3489 – 34891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3495 ↔ 3508By similarity
    Disulfide bondi3502 ↔ 3521By similarity
    Disulfide bondi3515 ↔ 3532By similarity
    Disulfide bondi3537 ↔ 3549By similarity
    Disulfide bondi3544 ↔ 3562By similarity
    Disulfide bondi3556 ↔ 3571By similarity
    Disulfide bondi3576 ↔ 3588By similarity
    Disulfide bondi3583 ↔ 3601By similarity
    Disulfide bondi3595 ↔ 3610By similarity
    Disulfide bondi3614 ↔ 3626By similarity
    Disulfide bondi3621 ↔ 3639By similarity
    Disulfide bondi3633 ↔ 3648By similarity
    Disulfide bondi3655 ↔ 3667By similarity
    Disulfide bondi3662 ↔ 3680By similarity
    Glycosylationi3663 – 36631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3674 ↔ 3691By similarity
    Disulfide bondi3696 ↔ 3710By similarity
    Disulfide bondi3704 ↔ 3723By similarity
    Disulfide bondi3717 ↔ 3732By similarity
    Disulfide bondi3742 ↔ 3755By similarity
    Disulfide bondi3750 ↔ 3768By similarity
    Disulfide bondi3762 ↔ 3777By similarity
    Disulfide bondi3786 ↔ 3799By similarity
    Glycosylationi3789 – 37891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3793 ↔ 3808By similarity
    Disulfide bondi3810 ↔ 3823By similarity
    Disulfide bondi3829 ↔ 3839By similarity
    Disulfide bondi3835 ↔ 3848By similarity
    Glycosylationi3840 – 38401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3850 ↔ 3861By similarity
    Glycosylationi3954 – 39541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4076 – 40761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4126 – 41261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4152 ↔ 4161By similarity
    Disulfide bondi4157 ↔ 4170By similarity
    Disulfide bondi4172 ↔ 4183By similarity
    Glycosylationi4180 – 41801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4201 ↔ 4211By similarity
    Disulfide bondi4205 ↔ 4221By similarity
    Disulfide bondi4223 ↔ 4232By similarity
    Disulfide bondi4237 ↔ 4247By similarity
    Disulfide bondi4241 ↔ 4257By similarity
    Disulfide bondi4259 ↔ 4268By similarity
    Disulfide bondi4273 ↔ 4283By similarity
    Disulfide bondi4277 ↔ 4293By similarity
    Glycosylationi4279 – 42791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4280 – 42801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4295 ↔ 4304By similarity
    Disulfide bondi4309 ↔ 4319By similarity
    Disulfide bondi4313 ↔ 4329By similarity
    Disulfide bondi4331 ↔ 4340By similarity
    Disulfide bondi4345 ↔ 4353By similarity
    Disulfide bondi4348 ↔ 4364By similarity
    Glycosylationi4365 – 43651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4366 ↔ 4375By similarity
    Disulfide bondi4378 ↔ 4388By similarity
    Disulfide bondi4382 ↔ 4398By similarity
    Disulfide bondi4400 ↔ 4409By similarity
    Modified residuei4508 – 45081PhosphotyrosineBy similarity
    Modified residuei4524 – 45241Phosphoserine1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ91ZX7.
    PaxDbiQ91ZX7.
    PRIDEiQ91ZX7.

    PTM databases

    PhosphoSiteiQ91ZX7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ91ZX7.
    BgeeiQ91ZX7.
    GenevestigatoriQ91ZX7.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dab1P973182EBI-300955,EBI-81680
    Dlg4Q621083EBI-300955,EBI-300895
    Mapk8ip1Q9WVI92EBI-300955,EBI-74515
    Mapk8ip2Q9ERE92EBI-300955,EBI-74576

    Protein-protein interaction databases

    BioGridi201201. 6 interactions.
    DIPiDIP-47785N.
    IntActiQ91ZX7. 13 interactions.
    MINTiMINT-1848960.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91ZX7.
    SMRiQ91ZX7. Positions 26-844, 851-1179, 1186-1567, 1585-2519, 2529-4412.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 44244405ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini4446 – 4545100CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4425 – 444521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 6742LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini71 – 11141LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini112 – 15039EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini151 – 19040EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati293 – 33543LDL-receptor class B 1Sequence AnalysisAdd
    BLAST
    Repeati336 – 37944LDL-receptor class B 2Sequence AnalysisAdd
    BLAST
    Repeati380 – 42344LDL-receptor class B 3Sequence AnalysisAdd
    BLAST
    Domaini475 – 52147EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati572 – 61443LDL-receptor class B 4Sequence AnalysisAdd
    BLAST
    Repeati615 – 66046LDL-receptor class B 5Sequence AnalysisAdd
    BLAST
    Repeati661 – 71151LDL-receptor class B 6Sequence AnalysisAdd
    BLAST
    Repeati712 – 75544LDL-receptor class B 7Sequence AnalysisAdd
    BLAST
    Domaini804 – 84441EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini853 – 89341LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini894 – 93441LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini935 – 97440LDL-receptor class A 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini975 – 101440LDL-receptor class A 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1014 – 105441LDL-receptor class A 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1061 – 110040LDL-receptor class A 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1103 – 114341LDL-receptor class A 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1144 – 118340LDL-receptor class A 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1184 – 122340EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1224 – 126340EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Repeati1310 – 135647LDL-receptor class B 8Sequence AnalysisAdd
    BLAST
    Repeati1357 – 139943LDL-receptor class B 9Sequence AnalysisAdd
    BLAST
    Repeati1400 – 144647LDL-receptor class B 10Sequence AnalysisAdd
    BLAST
    Repeati1447 – 149145LDL-receptor class B 11Sequence AnalysisAdd
    BLAST
    Repeati1492 – 153241LDL-receptor class B 12Sequence AnalysisAdd
    BLAST
    Domaini1537 – 158044EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Repeati1628 – 167043LDL-receptor class B 13Sequence AnalysisAdd
    BLAST
    Repeati1671 – 171444LDL-receptor class B 14Sequence AnalysisAdd
    BLAST
    Repeati1715 – 175440LDL-receptor class B 15Sequence AnalysisAdd
    BLAST
    Repeati1755 – 179945LDL-receptor class B 16Sequence AnalysisAdd
    BLAST
    Domaini1847 – 188842EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Repeati1935 – 197743LDL-receptor class B 17Sequence AnalysisAdd
    BLAST
    Repeati1978 – 202043LDL-receptor class B 18Sequence AnalysisAdd
    BLAST
    Repeati2021 – 206444LDL-receptor class B 19Sequence AnalysisAdd
    BLAST
    Repeati2065 – 210844LDL-receptor class B 20Sequence AnalysisAdd
    BLAST
    Domaini2156 – 219641EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Repeati2254 – 229542LDL-receptor class B 21Sequence AnalysisAdd
    BLAST
    Repeati2296 – 234449LDL-receptor class B 22Sequence AnalysisAdd
    BLAST
    Repeati2345 – 238945LDL-receptor class B 23Sequence AnalysisAdd
    BLAST
    Repeati2390 – 243243LDL-receptor class B 24Sequence AnalysisAdd
    BLAST
    Repeati2433 – 247442LDL-receptor class B 25Sequence AnalysisAdd
    BLAST
    Domaini2479 – 251941EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini2523 – 256442LDL-receptor class A 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini2565 – 260339LDL-receptor class A 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini2604 – 264239LDL-receptor class A 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini2643 – 269149LDL-receptor class A 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini2695 – 273339LDL-receptor class A 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini2733 – 277240LDL-receptor class A 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2773 – 281543LDL-receptor class A 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2817 – 285640LDL-receptor class A 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini2857 – 290044LDL-receptor class A 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini2903 – 294139LDL-receptor class A 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini2942 – 298241EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini2983 – 302341EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati3070 – 311445LDL-receptor class B 26Sequence AnalysisAdd
    BLAST
    Repeati3115 – 315743LDL-receptor class B 27Sequence AnalysisAdd
    BLAST
    Repeati3158 – 320144LDL-receptor class B 28Sequence AnalysisAdd
    BLAST
    Repeati3202 – 324443LDL-receptor class B 29Sequence AnalysisAdd
    BLAST
    Repeati3245 – 328541LDL-receptor class B 30Sequence AnalysisAdd
    BLAST
    Domaini3291 – 333242EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini3333 – 337240LDL-receptor class A 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini3373 – 341139LDL-receptor class A 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini3412 – 345140LDL-receptor class A 23PROSITE-ProRule annotationAdd
    BLAST
    Domaini3452 – 349241LDL-receptor class A 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini3493 – 353442LDL-receptor class A 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini3535 – 357339LDL-receptor class A 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini3574 – 361239LDL-receptor class A 27PROSITE-ProRule annotationAdd
    BLAST
    Domaini3612 – 365039LDL-receptor class A 28PROSITE-ProRule annotationAdd
    BLAST
    Domaini3653 – 369341LDL-receptor class A 29PROSITE-ProRule annotationAdd
    BLAST
    Domaini3694 – 373441LDL-receptor class A 30PROSITE-ProRule annotationAdd
    BLAST
    Domaini3740 – 377940LDL-receptor class A 31PROSITE-ProRule annotationAdd
    BLAST
    Domaini3782 – 382443EGF-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini3825 – 386238EGF-like 15PROSITE-ProRule annotationAdd
    BLAST
    Repeati3913 – 395543LDL-receptor class B 31Sequence AnalysisAdd
    BLAST
    Repeati3971 – 401343LDL-receptor class B 32Sequence AnalysisAdd
    BLAST
    Repeati4014 – 405744LDL-receptor class B 33Sequence AnalysisAdd
    BLAST
    Repeati4058 – 410245LDL-receptor class B 34Sequence AnalysisAdd
    BLAST
    Domaini4148 – 418437EGF-like 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini4197 – 423337EGF-like 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini4233 – 426937EGF-like 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini4269 – 430537EGF-like 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini4305 – 434137EGF-like 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini4341 – 437636EGF-like 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini4374 – 441037EGF-like 22PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4446 – 4545100Interaction with MAFB1 PublicationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi3941 – 39444Recognition site for proteolytical processingSequence Analysis
    Motifi4503 – 45086NPXY motif

    Sequence similaritiesi

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

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiNOG235850.
    GeneTreeiENSGT00750000117273.
    HOGENOMiHOG000230574.
    HOVERGENiHBG006292.
    InParanoidiQ91ZX7.
    KOiK04550.
    OrthoDBiEOG790FZT.
    PhylomeDBiQ91ZX7.
    TreeFamiTF315253.

    Family and domain databases

    Gene3Di2.120.10.30. 8 hits.
    4.10.400.10. 29 hits.
    InterProiIPR011042. 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]
    PfamiPF07645. EGF_CA. 2 hits.
    PF00057. Ldl_recept_a. 30 hits.
    PF00058. Ldl_recept_b. 16 hits.
    [Graphical view]
    PRINTSiPR00261. LDLRECEPTOR.
    SMARTiSM00181. EGF. 17 hits.
    SM00179. EGF_CA. 3 hits.
    SM00192. LDLa. 31 hits.
    SM00135. LY. 35 hits.
    SM00289. WR1. 4 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q91ZX7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTPPLLLLL PLLSALVSGA TMDAPKTCSP KQFACRDQIT CISKGWRCDG     50
    ERDCPDGSDE APEICPQSKA QRCPPNEHSC LGTELCVPMS RLCNGIQDCM 100
    DGSDEGAHCR ELRANCSRMG CQHHCVPTPS GPTCYCNSSF QLQADGKTCK 150
    DFDECSVYGT CSQLCTNTDG SFTCGCVEGY LLQPDNRSCK AKNEPVDRPP 200
    VLLIANSQNI LATYLSGAQV STITPTSTRQ TTAMDFSYAN ETVCWVHVGD 250
    SAAQTQLKCA RMPGLKGFVD EHTINISLSL HHVEQMAIDW LTGNFYFVDD 300
    IDDRIFVCNR NGDTCVTLLD LELYNPKGIA LDPAMGKVFF TDYGQIPKVE 350
    RCDMDGQNRT KLVDSKIVFP HGITLDLVSR LVYWADAYLD YIEVVDYEGK 400
    GRQTIIQGIL IEHLYGLTVF ENYLYATNSD NANTQQKTSV IRVNRFNSTE 450
    YQVVTRVDKG GALHIYHQRR QPRVRSHACE NDQYGKPGGC SDICLLANSH 500
    KARTCRCRSG FSLGSDGKSC KKPEHELFLV YGKGRPGIIR GMDMGAKVPD 550
    EHMIPIENLM NPRALDFHAE TGFIYFADTT SYLIGRQKID GTERETILKD 600
    GIHNVEGVAV DWMGDNLYWT DDGPKKTISV ARLEKAAQTR KTLIEGKMTH 650
    PRAIVVDPLN GWMYWTDWEE DPKDSRRGRL ERAWMDGSHR DIFVTSKTVL 700
    WPNGLSLDIP AGRLYWVDAF YDRIETILLN GTDRKIVYEG PELNHAFGLC 750
    HHGNYLFWTE YRSGSVYRLE RGVAGAPPTV TLLRSERPPI FEIRMYDAQQ 800
    QQVGTNKCRV NNGGCSSLCL ATPGSRQCAC AEDQVLDTDG VTCLANPSYV 850
    PPPQCQPGEF ACANNRCIQE RWKCDGDNDC LDNSDEAPAL CHQHTCPSDR 900
    FKCENNRCIP NRWLCDGDND CGNSEDESNA TCSARTCPPN QFSCASGRCI 950
    PISWTCDLDD DCGDRSDESA SCAYPTCFPL TQFTCNNGRC ININWRCDND 1000
    NDCGDNSDEA GCSHSCSSTQ FKCNSGRCIP EHWTCDGDND CGDYSDETHA 1050
    NCTNQATRPP GGCHSDEFQC RLDGLCIPLR WRCDGDTDCM DSSDEKSCEG 1100
    VTHVCDPNVK FGCKDSARCI SKAWVCDGDS DCEDNSDEEN CEALACRPPS 1150
    HPCANNTSVC LPPDKLCDGK DDCGDGSDEG ELCDQCSLNN GGCSHNCSVA 1200
    PGEGIVCSCP LGMELGSDNH TCQIQSYCAK HLKCSQKCDQ NKFSVKCSCY 1250
    EGWVLEPDGE SCRSLDPFKP FIIFSNRHEI RRIDLHKGDY SVLVPGLRNT 1300
    IALDFHLSQS ALYWTDVVED KIYRGKLLDN GALTSFEVVI QYGLATPEGL 1350
    AVDWIAGNIY WVESNLDQIE VAKLDGTLRT TLLAGDIEHP RAIALDPRDG 1400
    ILFWTDWDAS LPRIEAASMS GAGRRTIHRE TGSGGWPNGL TVDYLEKRIL 1450
    WIDARSDAIY SARYDGSGHM EVLRGHEFLS HPFAVTLYGG EVYWTDWRTN 1500
    TLAKANKWTG HNVTVVQRTN TQPFDLQVYH PSRQPMAPNP CEANGGRGPC 1550
    SHLCLINYNR TVSCACPHLM KLHKDNTTCY EFKKFLLYAR QMEIRGVDLD 1600
    APYYNYIISF TVPDIDNVTV LDYDAREQRV YWSDVRTQAI KRAFINGTGV 1650
    ETVVSADLPN AHGLAVDWVS RNLFWTSYDT NKKQINVARL DGSFKNAVVQ 1700
    GLEQPHGLVV HPLRGKLYWT DGDNISMANM DGSNHTLLFS GQKGPVGLAI 1750
    DFPESKLYWI SSGNHTINRC NLDGSELEVI DTMRSQLGKA TALAIMGDKL 1800
    WWADQVSEKM GTCNKADGSG SVVLRNSTTL VMHMKVYDES IQLEHEGTNP 1850
    CSVNNGDCSQ LCLPTSETTR SCMCTAGYSL RSGQQACEGV GSFLLYSVHE 1900
    GIRGIPLDPN DKSDALVPVS GTSLAVGIDF HAENDTIYWV DMGLSTISRA 1950
    KRDQTWREDV VTNGIGRVEG IAVDWIAGNI YWTDQGFDVI EVARLNGSFR 2000
    YVVISQGLDK PRAITVHPEK GYLFWTEWGH YPRIERSRLD GTERVVLVNV 2050
    SISWPNGISV DYQGGKLYWC DARMDKIERI DLETGENREV VLSSNNMDMF 2100
    SVSVFEDFIY WSDRTHANGS IKRGCKDNAT DSVPLRTGIG VQLKDIKVFN 2150
    RDRQKGTNVC AVANGGCQQL CLYRGGGQRA CACAHGMLAE DGASCREYAG 2200
    YLLYSERTIL KSIHLSDERN LNAPVQPFED PEHMKNVIAL AFDYRAGTSP 2250
    GTPNRIFFSD IHFGNIQQIN DDGSGRTTIV ENVGSVEGLA YHRGWDTLYW 2300
    TSYTTSTITR HTVDQTRPGA FERETVITMS GDDHPRAFVL DECQNLMFWT 2350
    NWNELHPSIM RAALSGANVL TLIEKDIRTP NGLAIDHRAE KLYFSDATLD 2400
    KIERCEYDGS HRYVILKSEP VHPFGLAVYG EHIFWTDWVR RAVQRANKYV 2450
    GSDMKLLRVD IPQQPMGIIA VANDTNSCEL SPCRINNGGC QDLCLLTHQG 2500
    HVNCSCRGGR ILQEDFTCRA VNSSCRAQDE FECANGECIS FSLTCDGVSH 2550
    CKDKSDEKPS YCNSRRCKKT FRQCNNGRCV SNMLWCNGVD DCGDGSDEIP 2600
    CNKTACGVGE FRCRDGSCIG NSSRCNQFVD CEDASDEMNC SATDCSSYFR 2650
    LGVKGVLFQP CERTSLCYAP SWVCDGANDC GDYSDERDCP GVKRPRCPLN 2700
    YFACPSGRCI PMSWTCDKED DCENGEDETH CNKFCSEAQF ECQNHRCISK 2750
    QWLCDGSDDC GDGSDEAAHC EGKTCGPSSF SCPGTHVCVP ERWLCDGDKD 2800
    CTDGADESVT AGCLYNSTCD DREFMCQNRL CIPKHFVCDH DRDCADGSDE 2850
    SPECEYPTCG PNEFRCANGR CLSSRQWECD GENDCHDHSD EAPKNPHCTS 2900
    PEHKCNASSQ FLCSSGRCVA EALLCNGQDD CGDGSDERGC HVNECLSRKL 2950
    SGCSQDCEDL KIGFKCRCRP GFRLKDDGRT CADLDECSTT FPCSQLCINT 3000
    HGSYKCLCVE GYAPRGGDPH SCKAVTDEEP FLIFANRYYL RKLNLDGSNY 3050
    TLLKQGLNNA VALDFDYREQ MIYWTDVTTQ GSMIRRMHLN GSNVQVLHRT 3100
    GLSNPDGLAV DWVGGNLYWC DKGRDTIEVS KLNGAYRTVL VSSGLREPRA 3150
    LVVDVQNGYL YWTDWGDHSL IGRIGMDGSG RSIIVDTKIT WPNGLTVDYV 3200
    TERIYWADAR EDYIEFASLD GSNRHVVLSQ DIPHIFALTL FEDYVYWTDW 3250
    ETKSINRAHK TTGANKTLLI STLHRPMDLH VFHALRQPDV PNHPCKVNNG 3300
    GCSNLCLLSP GGGHKCACPT NFYLGGDGRT CVSNCTASQF VCKNDKCIPF 3350
    WWKCDTEDDC GDHSDEPPDC PEFKCRPGQF QCSTGICTNP AFICDGDNDC 3400
    QDNSDEANCD IHVCLPSQFK CTNTNRCIPG IFRCNGQDNC GDGEDERDCP 3450
    EVTCAPNQFQ CSITKRCIPR VWVCDRDNDC VDGSDEPANC TQMTCGVDEF 3500
    RCKDSGRCIP ARWKCDGEDD CGDGSDEPKE ECDERTCEPY QFRCKNNRCV 3550
    PGRWQCDYDN DCGDNSDEES CTPRPCSESE FSCANGRCIA GRWKCDGDHD 3600
    CADGSDEKDC TPRCDMDQFQ CKSGHCIPLR WRCDADADCM DGSDEEACGT 3650
    GVRTCPLDEF QCNNTLCKPL AWKCDGEDDC GDNSDENPEE CARFICPPNR 3700
    PFRCKNDRVC LWIGRQCDGV DNCGDGTDEE DCEPPTAQNP HCKDKKEFLC 3750
    RNQRCLSSSL RCNMFDDCGD GSDEEDCSID PKLTSCATNA SMCGDEARCV 3800
    RTEKAAYCAC RSGFHTVPGQ PGCQDINECL RFGTCSQLCN NTKGGHLCSC 3850
    ARNFMKTHNT CKAEGSEYQV LYIADDNEIR SLFPGHPHSA YEQTFQGDES 3900
    VRIDAMDVHV KAGRVYWTNW HTGTISYRSL PPAAPPTTSN RHRRQIDRGV 3950
    THLNISGLKM PRGIAIDWVA GNVYWTDSGR DVIEVAQMKG ENRKTLISGM 4000
    IDEPHAIVVD PLRGTMYWSD WGNHPKIETA AMDGTLRETL VQDNIQWPTG 4050
    LAVDYHNERL YWADAKLSVI GSIRLNGTDP IVAADSKRGL SHPFSIDVFE 4100
    DYIYGVTYIN NRVFKIHKFG HSPLINLTGG LSHASDVVLY HQHKQPEVTN 4150
    PCDRKKCEWL CLLSPSGPVC TCPNGKRLDN GTCVPVPSPT PPPDAPRPGT 4200
    CTLQCFNGGS CFLNARRQPK CRCQPRYTGD KCELDQCWEY CHNGGTCAAS 4250
    PSGMPTCRCP TGFTGPKCTA QVCAGYCSNN STCTVNQGNQ PQCRCLPGFL 4300
    GDRCQYRQCS GFCENFGTCQ MAADGSRQCR CTVYFEGPRC EVNKCSRCLQ 4350
    GACVVNKQTG DVTCNCTDGR VAPSCLTCID HCSNGGSCTM NSKMMPECQC 4400
    PPHMTGPRCE EQVVSQQQPG HMASILIPLL LLLLLLLVAG VVFWYKRRVR 4450
    GAKGFQHQRM TNGAMNVEIG NPTYKMYEGG EPDDVGGLLD ADFALDPDKP 4500
    TNFTNPVYAT LYMGGHGSRH SLASTDEKRE LLGRGPEDEI GDPLA 4545
    Length:4,545
    Mass (Da):504,742
    Last modified:December 1, 2001 - v1
    Checksum:i9904CF5DF5EE333E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2642 – 26421A → T in AAL09567. (PubMed:12151109)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67469 mRNA. Translation: CAA47817.1. Sequence problems.
    AF367720 mRNA. Translation: AAL09566.1.
    AF369477
    , 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.
    CCDSiCCDS24245.1.
    PIRiS25111.
    RefSeqiNP_032538.2. NM_008512.2.
    UniGeneiMm.271854.

    Genome annotation databases

    EnsembliENSMUST00000049149; ENSMUSP00000044004; ENSMUSG00000040249.
    GeneIDi16971.
    KEGGimmu:16971.
    UCSCiuc007hjx.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67469 mRNA. Translation: CAA47817.1 . Sequence problems.
    AF367720 mRNA. Translation: AAL09566.1 .
    AF369477
    , 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 .
    CCDSi CCDS24245.1.
    PIRi S25111.
    RefSeqi NP_032538.2. NM_008512.2.
    UniGenei Mm.271854.

    3D structure databases

    ProteinModelPortali Q91ZX7.
    SMRi Q91ZX7. Positions 26-844, 851-1179, 1186-1567, 1585-2519, 2529-4412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201201. 6 interactions.
    DIPi DIP-47785N.
    IntActi Q91ZX7. 13 interactions.
    MINTi MINT-1848960.

    PTM databases

    PhosphoSitei Q91ZX7.

    Proteomic databases

    MaxQBi Q91ZX7.
    PaxDbi Q91ZX7.
    PRIDEi Q91ZX7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049149 ; ENSMUSP00000044004 ; ENSMUSG00000040249 .
    GeneIDi 16971.
    KEGGi mmu:16971.
    UCSCi uc007hjx.1. mouse.

    Organism-specific databases

    CTDi 4035.
    MGIi MGI:96828. Lrp1.

    Phylogenomic databases

    eggNOGi NOG235850.
    GeneTreei ENSGT00750000117273.
    HOGENOMi HOG000230574.
    HOVERGENi HBG006292.
    InParanoidi Q91ZX7.
    KOi K04550.
    OrthoDBi EOG790FZT.
    PhylomeDBi Q91ZX7.
    TreeFami TF315253.

    Enzyme and pathway databases

    Reactomei REACT_196575. Scavenging of heme from plasma.
    REACT_198569. Retinoid metabolism and transport.

    Miscellaneous databases

    NextBioi 291026.
    PROi Q91ZX7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91ZX7.
    Bgeei Q91ZX7.
    Genevestigatori Q91ZX7.

    Family and domain databases

    Gene3Di 2.120.10.30. 8 hits.
    4.10.400.10. 29 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    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 ]
    Pfami PF07645. EGF_CA. 2 hits.
    PF00057. Ldl_recept_a. 30 hits.
    PF00058. Ldl_recept_b. 16 hits.
    [Graphical view ]
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00181. EGF. 17 hits.
    SM00179. EGF_CA. 3 hits.
    SM00192. LDLa. 31 hits.
    SM00135. LY. 35 hits.
    SM00289. WR1. 4 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 9 hits.
    SSF57424. SSF57424. 30 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 3 hits.
    PS00022. EGF_1. 5 hits.
    PS01186. EGF_2. 8 hits.
    PS50026. EGF_3. 6 hits.
    PS01187. EGF_CA. 2 hits.
    PS01209. LDLRA_1. 27 hits.
    PS50068. LDLRA_2. 31 hits.
    PS51120. LDLRB. 34 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: LiverImported.
    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/JImported and CBAImported.
    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. "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].
    8. "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.
    9. "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.
    10. Cited for: FUNCTION AS A RECEPTOR FOR CHOLIX TOXIN.
    11. "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.

    Entry informationi

    Entry nameiLRP1_MOUSE
    AccessioniPrimary (citable) accession number: Q91ZX7
    Secondary accession number(s): Q61291, Q920Y4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3