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Entry version 170 (12 Aug 2020)
Sequence version 1 (01 Oct 1996)
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Protein

Low-density lipoprotein receptor-related protein 2

Gene

Lrp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Multiligand endocytic receptor. Acts together with CUBN to mediate endocytosis of high-density lipoproteins (By similarity). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (PubMed:7544804, PubMed:19202329). In the kidney, mediates the tubular uptake and clearance of leptin (By similarity). Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (PubMed:17324488). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (By similarity). Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells (PubMed:17462596). Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP (By similarity). Mediates renal uptake of metallothionein-bound heavy metals (PubMed:15126248). Together with CUBN, mediates renal reabsorption of myoglobin (PubMed:12724130). Mediates renal uptake and subsequent lysosomal degradation of APOM (PubMed:16099815). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (By similarity). Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (By similarity). Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (PubMed:28659595). Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (PubMed:11964399, PubMed:16801528). Also mediates ShhN transcytosis (PubMed:16801528). In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon (By similarity). Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH (By similarity). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (By similarity). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (By similarity). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (PubMed:18466341). Involved in neurite branching (By similarity). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (By similarity). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (By similarity). Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG (PubMed:16143106). Mediates endocytosis of angiotensin-2 (PubMed:15467006). Also mediates endocytosis of angiotensin 1-7 (PubMed:16380466). Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation (By similarity). Required for embryonic heart development (By similarity). Required for normal hearing, possibly through interaction with estrogen in the inner ear (PubMed:17846082).By similarity15 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1127Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1130CalciumBy similarity1
Metal bindingi1132Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1134CalciumBy similarity1
Metal bindingi1140CalciumBy similarity1
Metal bindingi1141CalciumBy similarity1
Metal bindingi1206Calcium; via carbonyl oxygen1 Publication1
Metal bindingi1209Calcium1 Publication1
Metal bindingi1211Calcium; via carbonyl oxygen1 Publication1
Metal bindingi1213Calcium1 Publication1
Metal bindingi1219Calcium1 Publication1
Metal bindingi1220Calcium1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionReceptor
Biological processEndocytosis, Hearing, Neurogenesis, Transport
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-196791, Vitamin D (calciferol) metabolism
R-RNO-8856825, Cargo recognition for clathrin-mediated endocytosis
R-RNO-8856828, Clathrin-mediated endocytosis
R-RNO-975634, Retinoid metabolism and transport

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 2
Short name:
LRP-2
Alternative name(s):
Glycoprotein 3301 Publication
Short name:
gp3301 Publication
Megalin
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Lrp2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
68407, Lrp2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini26 – 4425ExtracellularSequence analysisAdd BLAST4400
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei4426 – 4446HelicalSequence analysisAdd BLAST21
Topological domaini4447 – 4660CytoplasmicSequence analysisAdd BLAST214

Keywords - Cellular componenti

Cell membrane, Cell projection, Coated pit, Endosome, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi4527Y → C: Reduced interaction with ARH and dynein. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001732226 – 4660Low-density lipoprotein receptor-related protein 2Add BLAST4635

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi28 ↔ 40PROSITE-ProRule annotation
Disulfide bondi35 ↔ 53PROSITE-ProRule annotation
Disulfide bondi47 ↔ 62PROSITE-ProRule annotation
Disulfide bondi67 ↔ 80PROSITE-ProRule annotation
Disulfide bondi74 ↔ 93PROSITE-ProRule annotation
Disulfide bondi87 ↔ 103PROSITE-ProRule annotation
Disulfide bondi108 ↔ 120PROSITE-ProRule annotation
Disulfide bondi115 ↔ 133PROSITE-ProRule annotation
Disulfide bondi127 ↔ 142PROSITE-ProRule annotation
Disulfide bondi142 ↔ 157PROSITE-ProRule annotation
Disulfide bondi152 ↔ 170PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi159N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi164 ↔ 179PROSITE-ProRule annotation
Glycosylationi178N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi183 ↔ 195PROSITE-ProRule annotation
Disulfide bondi190 ↔ 208PROSITE-ProRule annotation
Disulfide bondi202 ↔ 217PROSITE-ProRule annotation
Disulfide bondi222 ↔ 234PROSITE-ProRule annotation
Disulfide bondi229 ↔ 247PROSITE-ProRule annotation
Disulfide bondi241 ↔ 256PROSITE-ProRule annotation
Glycosylationi259N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi265 ↔ 278PROSITE-ProRule annotation
Disulfide bondi272 ↔ 291PROSITE-ProRule annotation
Disulfide bondi285 ↔ 306PROSITE-ProRule annotation
Glycosylationi299N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi340N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi351 ↔ 361PROSITE-ProRule annotation
Disulfide bondi357 ↔ 370PROSITE-ProRule annotation
Glycosylationi462N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi657N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi865N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1025 ↔ 1037PROSITE-ProRule annotation
Disulfide bondi1032 ↔ 1050PROSITE-ProRule annotation
Disulfide bondi1044 ↔ 1059PROSITE-ProRule annotation
Glycosylationi1063N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1066 ↔ 1079PROSITE-ProRule annotation
Disulfide bondi1073 ↔ 1092PROSITE-ProRule annotation
Disulfide bondi1086 ↔ 1101PROSITE-ProRule annotation
Disulfide bondi1110 ↔ 1122PROSITE-ProRule annotation
Disulfide bondi1117 ↔ 1135PROSITE-ProRule annotation
Disulfide bondi1129 ↔ 1144PROSITE-ProRule annotation
Disulfide bondi1150 ↔ 1162PROSITE-ProRule annotation
Disulfide bondi1157 ↔ 1175PROSITE-ProRule annotation
Disulfide bondi1169 ↔ 1184PROSITE-ProRule annotation
Glycosylationi1187N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1188 ↔ 1201PROSITE-ProRule annotation1 Publication
Disulfide bondi1195 ↔ 1214PROSITE-ProRule annotation1 Publication
Disulfide bondi1208 ↔ 1223PROSITE-ProRule annotation1 Publication
Disulfide bondi1231 ↔ 1244PROSITE-ProRule annotation
Disulfide bondi1238 ↔ 1257PROSITE-ProRule annotation
Disulfide bondi1251 ↔ 1267PROSITE-ProRule annotation
Disulfide bondi1272 ↔ 1284PROSITE-ProRule annotation
Disulfide bondi1279 ↔ 1297PROSITE-ProRule annotation
Disulfide bondi1291 ↔ 1306PROSITE-ProRule annotation
Disulfide bondi1313 ↔ 1326PROSITE-ProRule annotation
Disulfide bondi1320 ↔ 1339PROSITE-ProRule annotation
Glycosylationi1328N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1333 ↔ 1349PROSITE-ProRule annotation
Glycosylationi1341N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1354 ↔ 1365PROSITE-ProRule annotation
Disulfide bondi1361 ↔ 1374PROSITE-ProRule annotation
Disulfide bondi1376 ↔ 1389PROSITE-ProRule annotation
Glycosylationi1384N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1395 ↔ 1405PROSITE-ProRule annotation
Disulfide bondi1401 ↔ 1414PROSITE-ProRule annotation
Disulfide bondi1416 ↔ 1429PROSITE-ProRule annotation
Glycosylationi1451N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1497N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1551N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1676N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1733N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1811N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2134N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2178N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2225N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2396N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2488N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2548N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2701 ↔ 2713PROSITE-ProRule annotation
Disulfide bondi2708 ↔ 2726PROSITE-ProRule annotation
Disulfide bondi2720 ↔ 2737PROSITE-ProRule annotation
Disulfide bondi2742 ↔ 2754PROSITE-ProRule annotation
Disulfide bondi2749 ↔ 2767PROSITE-ProRule annotation
Disulfide bondi2761 ↔ 2776PROSITE-ProRule annotation
Disulfide bondi2781 ↔ 2794PROSITE-ProRule annotation
Glycosylationi2782N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2789 ↔ 2807PROSITE-ProRule annotation
Disulfide bondi2801 ↔ 2818PROSITE-ProRule annotation
Glycosylationi2810N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2823 ↔ 2836PROSITE-ProRule annotation
Disulfide bondi2830 ↔ 2849PROSITE-ProRule annotation
Disulfide bondi2843 ↔ 2860PROSITE-ProRule annotation
Disulfide bondi2865 ↔ 2878PROSITE-ProRule annotation
Disulfide bondi2872 ↔ 2891PROSITE-ProRule annotation
Disulfide bondi2885 ↔ 2901PROSITE-ProRule annotation
Disulfide bondi2908 ↔ 2920PROSITE-ProRule annotation
Disulfide bondi2915 ↔ 2933PROSITE-ProRule annotation
Disulfide bondi2927 ↔ 2945PROSITE-ProRule annotation
Glycosylationi2949N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2950 ↔ 2967PROSITE-ProRule annotation
Disulfide bondi2957 ↔ 2980PROSITE-ProRule annotation
Disulfide bondi2974 ↔ 2990PROSITE-ProRule annotation
Glycosylationi2989N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2995 ↔ 3007PROSITE-ProRule annotation
Disulfide bondi3002 ↔ 3020PROSITE-ProRule annotation
Disulfide bondi3014 ↔ 3029PROSITE-ProRule annotation
Disulfide bondi3034 ↔ 3046PROSITE-ProRule annotation
Disulfide bondi3041 ↔ 3059PROSITE-ProRule annotation
Disulfide bondi3053 ↔ 3070PROSITE-ProRule annotation
Disulfide bondi3077 ↔ 3089PROSITE-ProRule annotation
Disulfide bondi3084 ↔ 3102PROSITE-ProRule annotation
Disulfide bondi3096 ↔ 3111PROSITE-ProRule annotation
Disulfide bondi3116 ↔ 3128PROSITE-ProRule annotation
Disulfide bondi3124 ↔ 3137PROSITE-ProRule annotation
Glycosylationi3127N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3139 ↔ 3152PROSITE-ProRule annotation
Disulfide bondi3158 ↔ 3169PROSITE-ProRule annotation
Disulfide bondi3165 ↔ 3178PROSITE-ProRule annotation
Disulfide bondi3180 ↔ 3193PROSITE-ProRule annotation
Glycosylationi3213N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3259N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3317N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3357N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3448N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3514 ↔ 3527PROSITE-ProRule annotation
Disulfide bondi3521 ↔ 3540PROSITE-ProRule annotation
Disulfide bondi3534 ↔ 3550PROSITE-ProRule annotation
Disulfide bondi3555 ↔ 3567PROSITE-ProRule annotation
Disulfide bondi3562 ↔ 3580PROSITE-ProRule annotation
Glycosylationi3566N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3574 ↔ 3591PROSITE-ProRule annotation
Disulfide bondi3596 ↔ 3608PROSITE-ProRule annotation
Disulfide bondi3603 ↔ 3621PROSITE-ProRule annotation
Disulfide bondi3615 ↔ 3632PROSITE-ProRule annotation
Disulfide bondi3637 ↔ 3649PROSITE-ProRule annotation
Disulfide bondi3644 ↔ 3662PROSITE-ProRule annotation
Disulfide bondi3656 ↔ 3673PROSITE-ProRule annotation
Disulfide bondi3680 ↔ 3694PROSITE-ProRule annotation
Glycosylationi3682N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3688 ↔ 3707PROSITE-ProRule annotation
Disulfide bondi3701 ↔ 3716PROSITE-ProRule annotation
Disulfide bondi3721 ↔ 3734PROSITE-ProRule annotation
Disulfide bondi3729 ↔ 3747PROSITE-ProRule annotation
Disulfide bondi3741 ↔ 3756PROSITE-ProRule annotation
Disulfide bondi3761 ↔ 3773PROSITE-ProRule annotation
Disulfide bondi3768 ↔ 3786PROSITE-ProRule annotation
Disulfide bondi3780 ↔ 3795PROSITE-ProRule annotation
Disulfide bondi3800 ↔ 3812PROSITE-ProRule annotation
Disulfide bondi3807 ↔ 3825PROSITE-ProRule annotation
Disulfide bondi3819 ↔ 3834PROSITE-ProRule annotation
Glycosylationi3840N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3844 ↔ 3856PROSITE-ProRule annotation
Disulfide bondi3851 ↔ 3869PROSITE-ProRule annotation
Disulfide bondi3863 ↔ 3880PROSITE-ProRule annotation
Disulfide bondi3885 ↔ 3898PROSITE-ProRule annotation
Disulfide bondi3893 ↔ 3911PROSITE-ProRule annotation
Disulfide bondi3905 ↔ 3922PROSITE-ProRule annotation
Disulfide bondi3930 ↔ 3942PROSITE-ProRule annotation
Disulfide bondi3937 ↔ 3955PROSITE-ProRule annotation
Disulfide bondi3949 ↔ 3964PROSITE-ProRule annotation
Glycosylationi3969N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3972 ↔ 3981PROSITE-ProRule annotation
Disulfide bondi3977 ↔ 3991PROSITE-ProRule annotation
Glycosylationi3980N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4013 ↔ 4023PROSITE-ProRule annotation
Disulfide bondi4019 ↔ 4032PROSITE-ProRule annotation
Disulfide bondi4034 ↔ 4049PROSITE-ProRule annotation
Glycosylationi4070N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi4329N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4383 ↔ 4391PROSITE-ProRule annotation
Disulfide bondi4385 ↔ 4401PROSITE-ProRule annotation
Disulfide bondi4403 ↔ 4412PROSITE-ProRule annotation
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei4464PhosphoserineCombined sources1
Modified residuei4467PhosphoserineBy similarity1
Modified residuei4577PhosphoserineCombined sources1
Modified residuei4624PhosphoserineCombined sources1
Modified residuei4637PhosphothreonineBy similarity1
Modified residuei4658PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

A fraction undergoes proteolytic cleavage of the extracellular domain at the cell membrane to generate a cytoplasmic tail fragment. This is internalized into the early endosome from where it trafficks in an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment (ERC). In the ERC, it is further cleaved by gamma-secretase to release a fragment which translocates to the nucleus and mediates transcriptional repression.1 Publication
N-glycosylation is required for ligand binding.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P98158

PRoteomics IDEntifications database

More...
PRIDEi
P98158

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
344, 25 N-Linked glycans

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P98158, 42 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P98158

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P98158

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P98158

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

In the inner ear, expressed in the lumen of the endolymphatic sac where it localizes to macrophage-like cells as well as to mitochondria-rich and ribosome-rich epithelial cells (at protein level) (PubMed:17063000). In the inner ear, expressed in marginal cells of the stria vascularis, epithelial cells at the spiral prominence, epithelial cells of Reissner's membrane facing the cochlear duct, and Kolliker's organ (at protein level) (PubMed:19202329). Expressed in the choroid plexus epithelium in the brain (at protein level) (PubMed:17324488). In the brain, also expressed in astrocytes (at protein level) (PubMed:18466341). Expression also detected in epithelial cells of the kidney glomerulus and proximal tubule, lung, epididymis and yolk sac (PubMed:7510321).5 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In the brain, expression is high after birth and gradually decreases from postnatal day 4 until the end of the first postnatal week.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds plasminogen, extracellular matrix components, plasminogen activator-plasminogen activator inhibitor type I complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin, CLU/clusterin and calcium.

Forms a multimeric complex together with LRPAP1 (PubMed:1400426).

Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (PubMed:22649097).

Interacts with LRP2BP.

Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif (By similarity).

Interacts with MB (PubMed:12724130).

Interacts with BMP4 (By similarity).

Interacts with the Sonic hedgehog protein N-product which is the active product of SHH (By similarity).

Interacts with CST3 in a calcium-dependent manner (PubMed:17462596).

Interacts with the vitamin-D binding protein GC/DBP (By similarity).

Interacts with sex hormone-binding protein SHBG (PubMed:16143106).

Interacts with angiotensin-2 (By similarity).

Also interacts with angiotensin 1-7 (By similarity).

Interacts with APOM (By similarity).

Interacts with selenoprotein SEPP1 (By similarity).

Interacts with LEP (PubMed:17324488).

Interacts with ALB (PubMed:18466341).

Interacts with the antiapoptotic protein BIRC5/survivin (By similarity).

Interacts with matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (PubMed:28659595). In neurons, forms a trimeric complex with APP and APPB1/FE65 (By similarity).

Interacts with LDLRAP1/ARH; mediates trafficking of LRP2 to the endocytic recycling compartment (PubMed:23836931). Does not interact with beta-amyloid protein 40 alone but interacts with the complex composed of beta-amyloid protein 40 and CLU/APOJ (By similarity).

Interacts with MDK (By similarity).

By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
247894, 2 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P98158

Database of interacting proteins

More...
DIPi
DIP-44866N

Protein interaction database and analysis system

More...
IntActi
P98158, 6 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000066394

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

14660
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P98158

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P98158

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini27 – 63LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST37
Domaini66 – 104LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST39
Domaini107 – 143LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST37
Domaini141 – 180LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST40
Domaini182 – 218LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST37
Domaini221 – 257LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST37
Domaini264 – 307LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST44
Domaini347 – 382EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati435 – 477LDL-receptor class B 1PROSITE-ProRule annotationAdd BLAST43
Repeati478 – 520LDL-receptor class B 2PROSITE-ProRule annotationAdd BLAST43
Repeati521 – 567LDL-receptor class B 3PROSITE-ProRule annotationAdd BLAST47
Repeati568 – 612LDL-receptor class B 4PROSITE-ProRule annotationAdd BLAST45
Repeati752 – 794LDL-receptor class B 5PROSITE-ProRule annotationAdd BLAST43
Repeati795 – 836LDL-receptor class B 6PROSITE-ProRule annotationAdd BLAST42
Repeati837 – 880LDL-receptor class B 7PROSITE-ProRule annotationAdd BLAST44
Repeati881 – 924LDL-receptor class B 8PROSITE-ProRule annotationAdd BLAST44
Domaini1024 – 1060LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST37
Domaini1065 – 1102LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST38
Domaini1109 – 1145LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST37
Domaini1149 – 1185LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST37
Domaini1187 – 1224LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST38
Domaini1230 – 1268LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST39
Domaini1271 – 1307LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST37
Domaini1312 – 1350LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST39
Domaini1350 – 1390EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini1391 – 1430EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Repeati1479 – 1521LDL-receptor class B 9PROSITE-ProRule annotationAdd BLAST43
Repeati1522 – 1564LDL-receptor class B 10PROSITE-ProRule annotationAdd BLAST43
Repeati1567 – 1610LDL-receptor class B 11PROSITE-ProRule annotationAdd BLAST44
Repeati1611 – 1655LDL-receptor class B 12PROSITE-ProRule annotationAdd BLAST45
Repeati1656 – 1696LDL-receptor class B 13PROSITE-ProRule annotationAdd BLAST41
Repeati1791 – 1833LDL-receptor class B 14PROSITE-ProRule annotationAdd BLAST43
Repeati1834 – 1883LDL-receptor class B 15PROSITE-ProRule annotationAdd BLAST50
Repeati1884 – 1931LDL-receptor class B 16PROSITE-ProRule annotationAdd BLAST48
Repeati1932 – 1973LDL-receptor class B 17PROSITE-ProRule annotationAdd BLAST42
Repeati1974 – 2014LDL-receptor class B 18PROSITE-ProRule annotationAdd BLAST41
Repeati2108 – 2157LDL-receptor class B 19PROSITE-ProRule annotationAdd BLAST50
Repeati2158 – 2202LDL-receptor class B 20PROSITE-ProRule annotationAdd BLAST45
Repeati2203 – 2246LDL-receptor class B 21PROSITE-ProRule annotationAdd BLAST44
Repeati2247 – 2290LDL-receptor class B 22PROSITE-ProRule annotationAdd BLAST44
Repeati2432 – 2478LDL-receptor class B 23PROSITE-ProRule annotationAdd BLAST47
Repeati2479 – 2519LDL-receptor class B 24PROSITE-ProRule annotationAdd BLAST41
Repeati2520 – 2563LDL-receptor class B 25PROSITE-ProRule annotationAdd BLAST44
Repeati2564 – 2605LDL-receptor class B 26PROSITE-ProRule annotationAdd BLAST42
Repeati2606 – 2647LDL-receptor class B 27PROSITE-ProRule annotationAdd BLAST42
Domaini2700 – 2738LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST39
Domaini2741 – 2777LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST37
Domaini2780 – 2819LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST40
Domaini2822 – 2861LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST40
Domaini2864 – 2902LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST39
Domaini2907 – 2946LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST40
Domaini2949 – 2991LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST43
Domaini2994 – 3030LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST37
Domaini3033 – 3071LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST39
Domaini3076 – 3112LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST37
Domaini3112 – 3153EGF-like 4PROSITE-ProRule annotationAdd BLAST42
Domaini3154 – 3194EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3241 – 3283LDL-receptor class B 28PROSITE-ProRule annotationAdd BLAST43
Repeati3284 – 3326LDL-receptor class B 29PROSITE-ProRule annotationAdd BLAST43
Repeati3335 – 3378LDL-receptor class B 30PROSITE-ProRule annotationAdd BLAST44
Repeati3379 – 3421LDL-receptor class B 31PROSITE-ProRule annotationAdd BLAST43
Repeati3422 – 3462LDL-receptor class B 32PROSITE-ProRule annotationAdd BLAST41
Domaini3513 – 3551LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST39
Domaini3554 – 3592LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST39
Domaini3595 – 3633LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST39
Domaini3636 – 3674LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST39
Domaini3679 – 3717LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST39
Domaini3720 – 3757LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST38
Domaini3760 – 3796LDL-receptor class A 32PROSITE-ProRule annotationAdd BLAST37
Domaini3799 – 3835LDL-receptor class A 33PROSITE-ProRule annotationAdd BLAST37
Domaini3843 – 3881LDL-receptor class A 34PROSITE-ProRule annotationAdd BLAST39
Domaini3884 – 3923LDL-receptor class A 35PROSITE-ProRule annotationAdd BLAST40
Domaini3929 – 3965LDL-receptor class A 36PROSITE-ProRule annotationAdd BLAST37
Domaini3968 – 4003EGF-like 6PROSITE-ProRule annotationAdd BLAST36
Domaini4009 – 4050EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Repeati4156 – 4198LDL-receptor class B 33PROSITE-ProRule annotationAdd BLAST43
Repeati4199 – 4242LDL-receptor class B 34PROSITE-ProRule annotationAdd BLAST44
Repeati4244 – 4285LDL-receptor class B 35PROSITE-ProRule annotationAdd BLAST42
Domaini4379 – 4413EGF-like 8PROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni4597 – 4610Interaction with DAB2By similarityAdd BLAST14

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi4454 – 4463SH3-bindingSequence analysis10
Motifi4457 – 4462PxLPxI/L motif 1; mediates interaction with ANKRA21 Publication6
Motifi4460 – 4465PxLPxI/L motif 2; mediates interaction with ANKRA21 Publication6
Motifi4522 – 4527Endocytosis signalSequence analysis6
Motifi4603 – 4606NPXY motif4
Motifi4606 – 4609SH2-bindingSequence analysis4
Motifi4619 – 4630SH3-bindingSequence analysisAdd BLAST12

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Two overlapping PxLPxI/L motifs mediate interaction with ankyrin repeats of ANKRA2.1 Publication
The cytoplasmic domain is required for sorting to the apical cell membrane.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the LDLR family.Curated

Keywords - Domaini

EGF-like domain, Repeat, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1215, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P98158

KEGG Orthology (KO)

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KOi
K06233

Database of Orthologous Groups

More...
OrthoDBi
1606at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P98158

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00112, LDLa, 36 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.120.10.30, 8 hits
4.10.400.10, 36 hits

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...
IDEALi
IID50221

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011042, 6-blade_b-propeller_TolB-like
IPR026823, cEGF
IPR001881, EGF-like_Ca-bd_dom
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR036055, LDL_receptor-like_sf
IPR023415, LDLR_class-A_CS
IPR000033, LDLR_classB_rpt
IPR002172, LDrepeatLR_classA_rpt

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12662, cEGF, 2 hits
PF07645, EGF_CA, 1 hit
PF00057, Ldl_recept_a, 35 hits
PF00058, Ldl_recept_b, 14 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00261, LDLRECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00181, EGF, 22 hits
SM00179, EGF_CA, 9 hits
SM00192, LDLa, 36 hits
SM00135, LY, 36 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57184, SSF57184, 2 hits
SSF57424, SSF57424, 35 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00010, ASX_HYDROXYL, 4 hits
PS00022, EGF_1, 1 hit
PS01186, EGF_2, 8 hits
PS50026, EGF_3, 8 hits
PS01187, EGF_CA, 3 hits
PS01209, LDLRA_1, 31 hits
PS50068, LDLRA_2, 36 hits
PS51120, LDLRB, 35 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P98158-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MERGAAAAAW MLLLAIAACL EPVSSQECGS GNFRCDNGYC IPASWRCDGT
60 70 80 90 100
RDCLDDTDEI GCPPRSCESG LFLCPAEGTC IPSSWVCDED KDCSDGADEQ
110 120 130 140 150
QNCAGTTCSA QQMTCSNGQC IPSEYRCDHV SDCPDGSDER NCHYPTCDQL
160 170 180 190 200
TCANGACYNT SQRCDQKVDC RDSSDEANCT TLCSQKEFEC GSGECILRAY
210 220 230 240 250
VCDHDNDCED NSDERNCNYD TCGGHQFTCS NGQCINQNWV CDGDDDCQDS
260 270 280 290 300
GDEDGCESNQ SHHRCYPREW ACPGSGRCIS IDKVCDGVPD CPEGDDENNV
310 320 330 340 350
TSGRTCGMGV CSVLNCEYQC HQTPFGGECF CPPGHIINSN DSRTCIDFDD
360 370 380 390 400
CQIWGICDQK CENRQGRHQC LCEEGYILER GQHCKSSDSF SAASVIFSNG
410 420 430 440 450
RDLLVGDLHG RNFRILAESK NRGMVMGVDF HYQKHRVFWT DPMQEKVFST
460 470 480 490 500
DINGLNTQEI LNVSVDTPEN LAVDWINNKL YLVETKVNRI DVVNLEGNQR
510 520 530 540 550
VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA FMDGSNRKDL
560 570 580 590 600
VTTKVGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV
610 620 630 640 650
PHPFGISLFE EHVFFTDWTK MAVMKASKFT ETNPQVYHQS SLRPHGVTVY
660 670 680 690 700
HALRQPNATN PCGSNNGGCA QVCVLSHRTD NGGLGYRCKC EFGFELDDDE
710 720 730 740 750
HRCVAVKNFL LFSSKTAVRG IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ
760 770 780 790 800
HSTVFYSDLS KDIIYKQKID GTGKEVITAN RLESVECLTF DWISRNLYWT
810 820 830 840 850
DGGLKSVTVL RLADKSRRQI ISNLNNPRSI VVHPTAGYMF LSDWFRPAKI
860 870 880 890 900
MRAWSDGSHL MPIVNTSLGW PNGLAIDWSA SRLYWVDAFF DKIEHSTLDG
910 920 930 940 950
LDRKRLGHVD QMTHPFGLTV FKDNVFITDW RLGAIIRVRK SDGGDMTVIR
960 970 980 990 1000
RGISSVMHVK AYDADLQTGS NYCSQTTHAN GDCSHFCFPV PNFQRVCGCP
1010 1020 1030 1040 1050
YGMKLQRDQM TCEGDPAREP PTQQCGSLSF PCNNGKCVPS FFRCDGVDDC
1060 1070 1080 1090 1100
HDNSDEHQCG VFNNTCSPSA FACVRGGQCI PGQWHCDRQN DCLDGSDEQN
1110 1120 1130 1140 1150
CPTHATSSTC PSTSFTCDNH VCIPKDWVCD TDNDCSDGSD EKNCQASGTC
1160 1170 1180 1190 1200
QPTQFRCPDH RCISPLYVCD GDKDCADGSD EAGCVLNCTS AQFKCADGSS
1210 1220 1230 1240 1250
CINSRYRCDG VYDCRDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE
1260 1270 1280 1290 1300
CDGHPDCIHG SDEHTGCVPK TCSPTHFLCD NGNCIYKAWI CDGDNDCRDM
1310 1320 1330 1340 1350
SDEKDCPTQP FHCPSTQWQC PGYSTCINLS ALCDGVFDCP NGTDESPLCN
1360 1370 1380 1390 1400
QDSCSHFNGG CTHQCMQGPF GATCLCPLGY QLANDTKTCE DINECDIPGF
1410 1420 1430 1440 1450
CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTGSENPLLV VASRDKIIVD
1460 1470 1480 1490 1500
NITAHTHNLY SLVQDVSFVV ALDFDSVTGR VFWSDLLQGK TWSVFQNGTD
1510 1520 1530 1540 1550
KRVVHDSGLS VTEMIAVDWI GRNLYWTDYA LETIEVSKID GSHRTVLISK
1560 1570 1580 1590 1600
NVTKPRGLAL DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW
1610 1620 1630 1640 1650
PCGLSIDYPN RLIYFMDAYL DYIEFCDYDG HNRRQVIASD LVLHHPHALT
1660 1670 1680 1690 1700
LFEDFVYWTD RGTRQVMQAN KWHGGNQSVV MYSVHQPLGI TAIHPSRQPP
1710 1720 1730 1740 1750
SRNPCASASC SHLCLLSAQA PRHYSCACPS GWNLSDDSVN CVRGDQPFLM
1760 1770 1780 1790 1800
SVRDNIIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG
1810 1820 1830 1840 1850
EIHRVKTDGS NRTVFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT
1860 1870 1880 1890 1900
LKGDTRYGKT LIANDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK
1910 1920 1930 1940 1950
IASANMDGTS LKILFTGNLQ HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD
1960 1970 1980 1990 2000
GTERMILVHH LAHPWGLVVY GSFLYYSDEQ YEVIERVDKS SGNNKVVLRD
2010 2020 2030 2040 2050
NVPYLRGLRV YHRRNAADSS NGCSNNPNAC QQICLPVPGG MFSCACASGF
2060 2070 2080 2090 2100
KLSPDGRSCS PYNSFMVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH
2110 2120 2130 2140 2150
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP DGSNFTNVVT YGIGANGIRG
2160 2170 2180 2190 2200
VALDWAAGNL YFTNAFVYET LIEVLRINTT YRRVLLKVSV DMPRHIIVDP
2210 2220 2230 2240 2250
KHRYLFWADY GQKPKIERSF LDCTNRTVLV SEGIVTPRGL AMDHDTGYIY
2260 2270 2280 2290 2300
WVDDSLDLIA RIHLDGGESQ VVRYGSRYPT PYGITVFGES IIWVDRNLKK
2310 2320 2330 2340 2350
VFQASKQPGN TDPPVVIRDK INLLRDVTIF DEHAQPLSPA ELNNNPCLQS
2360 2370 2380 2390 2400
NGGCSHFCFA LPELPTPRCG CAFGTLGNDG KSCATSQEDF LIYSLNNSLR
2410 2420 2430 2440 2450
SLHFDPRDHS LPFQVISVAG TAIALDYDRR NNRIFFTQKL NSLRGQISYV
2460 2470 2480 2490 2500
SLYSGSSSPT VLLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN
2510 2520 2530 2540 2550
RAVIARVSKP RAIVLDPCRG YMYWTDWGTN AKIERATLGG NFRVPIVNTS
2560 2570 2580 2590 2600
LVWPNGLALD LETDLLYWAD ASLQKIERST LTGTNREVVV STAFHSFGLT
2610 2620 2630 2640 2650
VYGQYIYWTD LYTRKIYRAN KYDGSDLVAM TTRLPTQPSG ISTVVKTQRQ
2660 2670 2680 2690 2700
QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGNWYLANDN KYCVVDTGTR
2710 2720 2730 2740 2750
CNQLQFTCLN GHCINQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCG
2760 2770 2780 2790 2800
NGRCVPYHYR CDYYNDCGDN SDEAGCLFRN CNSTTEFTCS NGRCIPLSYV
2810 2820 2830 2840 2850
CNGINNCHDN DTSDEKNCPP HTCPPDFTKC QTTNICVPRA FLCDGDNDCG
2860 2870 2880 2890 2900
DGSDENPIYC ASHTCRSNEF QCLSPQRCIP SYWFCDGEAD CADGSDEPDT
2910 2920 2930 2940 2950
CGHSVNTCRA SQFQCDNGRC ISGNWVCDGD NDCGDMSDED QRHHCELQNC
2960 2970 2980 2990 3000
SSTQFTCVNS RPPNRRCIPQ YWVCDGDADC SDALDELQNC TMRTCSAGEF
3010 3020 3030 3040 3050
SCANGRCVRQ SFRCDRRNDC GDYSDERGCS YPPCHANQFT CQNGRCIPRF
3060 3070 3080 3090 3100
FVCDEDNDCG DGSDEQEHLC HTPEPTCPLH QFRCDNGHCI EMGRVCNHVD
3110 3120 3130 3140 3150
DCSDNSDEKG CGINECLDSS ISRCDHNCTD TITSFYCSCL PGYKLMSDKR
3160 3170 3180 3190 3200
SCVDIDECKE SPQLCSQKCE NVVGSYICKC APGYIREPDG KSCRQNSNIE
3210 3220 3230 3240 3250
PYLIFSNRYY IRNLTTDGSS YSLILQGLGN VVALDFDRVE KRLYWIDAEK
3260 3270 3280 3290 3300
QIIERMFLNK TNRETIINHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD
3310 3320 3330 3340 3350
LEGRHRKMIA QHCVDANNTF CFEHPRGIVL HPQRGHVYWA DWGVHAYIGR
3360 3370 3380 3390 3400
IGMDGTNKSV IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH
3410 3420 3430 3440 3450
RHTVYDGSLP HPFALTIFED TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT
3460 3470 3480 3490 3500
HKPFDIHVYH PYRQPIMSNP CGTNNGGCSH LCLIKAGGRG FTCACPDDFQ
3510 3520 3530 3540 3550
TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC SDGSDEPDLC
3560 3570 3580 3590 3600
PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCESNE
3610 3620 3630 3640 3650
WQCANKRCIP QSWQCDSVND CLDNSDEDTS HCASRTCRPG QFKCNNGRCI
3660 3670 3680 3690 3700
PQSWKCDVDN DCGDYSDEPI DECTTAAYNC DNHTEFSCKT NYRCIPQWAV
3710 3720 3730 3740 3750
CNGFDDCRDN SDEQGCESVP CHPSGDFRCA NHHCIPLRWK CDGTDDCGDN
3760 3770 3780 3790 3800
SDEENCVPRE CSESEFRCAD QQCIPSRWVC DQENDCGDNS DERDCEMKTC
3810 3820 3830 3840 3850
HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN GTYCPAAMFE
3860 3870 3880 3890 3900
CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNIPCESPQR FRCDNSRCVY
3910 3920 3930 3940 3950
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCISQHYVCD
3960 3970 3980 3990 4000
NVNDCGDLSD ETGCNLGDNR TCAENICEQN CTQLSSGGFI CSCRPGFKPS
4010 4020 4030 4040 4050
TSDKNSCQDI NECEEFGICP QSCRNSKGSY ECFCVDGFKS MSTHYGERCA
4060 4070 4080 4090 4100
ADGSPPLLLL PENVRIRKYN TSSEKFSEYL EEEEHIQTID YDWDPEHIGL
4110 4120 4130 4140 4150
SVVYYTVLAQ GSQFGAIKRA YIPNFESGSN NPIREVDLGL KYLMQPDGLA
4160 4170 4180 4190 4200
VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL
4210 4220 4230 4240 4250
MFWTDQGKQP KIESAWMNGE HRSVLVSENL GWPNGLSIDY LNDDRVYWSD
4260 4270 4280 4290 4300
SKEDVIEAIK YDGTDRRLII NEAMKPFSLD IFEDKLYWVA KEKGEVWRQN
4310 4320 4330 4340 4350
KFGKENKEKV LVVNPWLTQV RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG
4360 4370 4380 4390 4400
YSCACPQGSD FVTGSTVQCD AASELPVTMP PPCRCMHGGN CYFDENELPK
4410 4420 4430 4440 4450
CKCSSGYSGE YCEVGLSRGI PPGTTMAVLL TFVIVIIVGA LVLVGLFHYR
4460 4470 4480 4490 4500
KTGSLLPTLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI
4510 4520 4530 4540 4550
IDRSMAMNEH FVMEVGKQPV IFENPMYAAK DNTSKVALAV QGPSTGAQVT
4560 4570 4580 4590 4600
VPENVENQNY GRPIDPSEIV PEPKPASPGA DEIQGKKWNI FKRKPKQTTN
4610 4620 4630 4640 4650
FENPIYAEMD SEVKDAVAVA PPPSPSLPAK ASKRNLTPGY TATEDTFKDT
4660
ANLVKEDSDV
Length:4,660
Mass (Da):519,276
Last modified:October 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE2A0CFD23D0923C3
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K9W7A0A0G2K9W7_RAT
Low-density lipoprotein receptor-re...
Lrp2 rCG_26871
4,660Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L34049 mRNA Translation: AAA51369.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T42737

NCBI Reference Sequences

More...
RefSeqi
NP_110454.1, NM_030827.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29216

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:29216

UCSC genome browser

More...
UCSCi
RGD:68407, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34049 mRNA Translation: AAA51369.1
PIRiT42737
RefSeqiNP_110454.1, NM_030827.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I1PNMR-A1185-1229[»]
3V2OX-ray1.89B4448-4466[»]
3V2XX-ray1.85B4455-4465[»]
SMRiP98158
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi247894, 2 interactors
CORUMiP98158
DIPiDIP-44866N
IntActiP98158, 6 interactors
STRINGi10116.ENSRNOP00000066394

PTM databases

GlyConnecti344, 25 N-Linked glycans
GlyGeniP98158, 42 sites
iPTMnetiP98158
PhosphoSitePlusiP98158
UniCarbKBiP98158

Proteomic databases

PaxDbiP98158
PRIDEiP98158

Genome annotation databases

GeneIDi29216
KEGGirno:29216
UCSCiRGD:68407, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4036
RGDi68407, Lrp2

Phylogenomic databases

eggNOGiKOG1215, Eukaryota
InParanoidiP98158
KOiK06233
OrthoDBi1606at2759
PhylomeDBiP98158

Enzyme and pathway databases

ReactomeiR-RNO-196791, Vitamin D (calciferol) metabolism
R-RNO-8856825, Cargo recognition for clathrin-mediated endocytosis
R-RNO-8856828, Clathrin-mediated endocytosis
R-RNO-975634, Retinoid metabolism and transport

Miscellaneous databases

EvolutionaryTraceiP98158

Protein Ontology

More...
PROi
PR:P98158

Family and domain databases

CDDicd00112, LDLa, 36 hits
Gene3Di2.120.10.30, 8 hits
4.10.400.10, 36 hits
IDEALiIID50221
InterProiView protein in InterPro
IPR011042, 6-blade_b-propeller_TolB-like
IPR026823, cEGF
IPR001881, EGF-like_Ca-bd_dom
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR036055, LDL_receptor-like_sf
IPR023415, LDLR_class-A_CS
IPR000033, LDLR_classB_rpt
IPR002172, LDrepeatLR_classA_rpt
PfamiView protein in Pfam
PF12662, cEGF, 2 hits
PF07645, EGF_CA, 1 hit
PF00057, Ldl_recept_a, 35 hits
PF00058, Ldl_recept_b, 14 hits
PRINTSiPR00261, LDLRECEPTOR
SMARTiView protein in SMART
SM00181, EGF, 22 hits
SM00179, EGF_CA, 9 hits
SM00192, LDLa, 36 hits
SM00135, LY, 36 hits
SUPFAMiSSF57184, SSF57184, 2 hits
SSF57424, SSF57424, 35 hits
PROSITEiView protein in PROSITE
PS00010, ASX_HYDROXYL, 4 hits
PS00022, EGF_1, 1 hit
PS01186, EGF_2, 8 hits
PS50026, EGF_3, 8 hits
PS01187, EGF_CA, 3 hits
PS01209, LDLRA_1, 31 hits
PS50068, LDLRA_2, 36 hits
PS51120, LDLRB, 35 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLRP2_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P98158
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: August 12, 2020
This is version 170 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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