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UniProtKB - A2ARV4 (LRP2_MOUSE)

Protein

Low-density lipoprotein receptor-related protein 2

Gene

Lrp2

Organism
Mus musculus (Mouse)
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 (PubMed:10766831). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and clearance of leptin (PubMed:22841573). Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (PubMed:24825475). 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 (PubMed:10052453). Mediates renal uptake of metallothionein-bound heavy metals (By similarity). Together with CUBN, mediates renal reabsorption of myoglobin (By similarity). Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (PubMed:18174160). Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (PubMed:23825075). 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 (By similarity). Also mediates ShhN transcytosis (By similarity). 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 (PubMed:15623804). 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 (PubMed:22340494). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (PubMed:24639464). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (PubMed:20460439). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity). Involved in neurite branching (PubMed:20637285). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (PubMed:22354480). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (PubMed:26439398). 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 (By similarity). Also mediates endocytosis of angiotensin 1-7 (By similarity). 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 (PubMed:26822476). Required for normal hearing, possibly through interaction with estrogen in the inner ear (PubMed:17846082).By similarity19 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 oxygenBy similarity1
Metal bindingi1209CalciumBy similarity1
Metal bindingi1211Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1213CalciumBy similarity1
Metal bindingi1219CalciumBy similarity1
Metal bindingi1220CalciumBy similarity1

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Protein family/group databases

Transport Classification Database

More...TCDBi		9.B.87.1.1 the selenoprotein p receptor (selp-receptor) family

<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_and_taxonomy_section">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 330
Short name:
gp330
Megalin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Chromosome 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:95794 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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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_location_section">'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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Severe facial dysgenesis and impaired forebrain development around mid-gestation, absence of Shh expression and decreased cell proliferation in the ventral neural tube, and aberrant expression of morphogens Fgf8 and Bmp4 (PubMed:15623804). Reduced expression of homeobox protein Six3 at E8.0 in the prospective forebrain and impaired Shh expression at the ventral midline with resulting midline formation defects and holoprosencephaly (PubMed:22340494). At E9.5, loss of Shh in the ventral anterior diencephalon and increased Bmp4 expression in the dorsal forebrain (PubMed:22340494). Increased Bmp4 expression and impaired proliferation of neural precursor cells in the subependymal zone of the brain which results in decreased numbers of neuroblasts reaching the olfactory bulb (PubMed:20460439). Compound heterozygotes display enlarged and exophthalmic eyes with thinning of the retina (PubMed:26439398). Severe cardiovascular abnormalities including aortic arch anomalies, persistent truncus arteriosus with coronary artery anomalies, ventricular septal defects, overriding of the tricuspid valve, marked thinning of the ventricular myocardium, and abnormal positioning of the neural crest cells and second heart field (PubMed:26822476). Impaired endocytosis of folate bound to the folate receptor FOLR1, reduced folate levels in embryos and impaired closure of the rostral neural tube (PubMed:24639464). High lethality at and after birth with survivors showing profound hearing loss, elevated lipofuscin granule levels and irregular apical surfaces in marginal cells of the stria vascularis, complete loss of potassium ion channel KCQN1 in basal and midbasal cochlear turns, and reduced estrogen uptake in the stria vascularis (PubMed:17846082). Survivors also display severe vitamin D deficiency and bone formation defects (PubMed:10052453). Failure of the vaginal cavity to open after birth in females and impaired testis descent in males with the left testis poorly developed and severely retarded in size (PubMed:16143106). Conditional knockout in the kidney results in reduced expression of CUBN in kidney cells and little or no uptake of myoglobin (PubMed:12724130). It also results in reduced uptake of Cst3 by kidney proximal tubule cells (PubMed:17462596). In addition, it causes pronounced urinary excretion of Apom, Birc5/survivin, and Mmp2 together with Timp1 (PubMed:16099815, PubMed:23825075, PubMed:28659595).14 Publications

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000030984526 – 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 bondi147 ↔ 157PROSITE-ProRule annotation
Disulfide bondi152 ↔ 170PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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
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
Glycosylationi387N-linked (GlcNAc...) asparagine1 Publication1
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 annotation
Disulfide bondi1195 ↔ 1214PROSITE-ProRule annotation
Disulfide bondi1208 ↔ 1223PROSITE-ProRule annotation
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
Glycosylationi2131N-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
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 residuei4467PhosphoserineCombined sources1
Modified residuei4577PhosphoserineCombined sources1
Modified residuei4624PhosphoserineBy similarity1
Modified residuei4637PhosphothreonineCombined sources1
Modified residuei4658PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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.By similarity
N-glycosylation is required for ligand binding. Contains core-fucosylated N-glycans in kidney proximal convoluted tubules (PCTs) and hybrid-type N-glycans in proximal straight tubules (PSTs). Interacts with ligands in a glycoform-dependent manner. Retinol-binding protein and the vitamin D carrier GC/DBP are endocytosed primarily by PCTs, albumin is endocytosed equally by PCTs and PSTs, and the aminoglycoside kanamycin is endocytosed primarily by PSTs.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		A2ARV4

MaxQB - The MaxQuant DataBase

More...MaxQBi		A2ARV4

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

More...PaxDbi		A2ARV4

PeptideAtlas

More...PeptideAtlasi		A2ARV4

PRoteomics IDEntifications database

More...PRIDEi		A2ARV4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		A2ARV4

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

More...PhosphoSitePlusi		A2ARV4

<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, strongly expressed in the marginal cells of the stria vascularis (at protein level) (PubMed:17846082). In the female reproductive tract, expressed on the luminal side of the uterine epithelium (at protein level) (PubMed:16143106). In the adult brain, expressed in ependymal cells of the lateral ventricles where expression is restricted to the ependyma that faces the stem cell niche (at protein level) (PubMed:20460439). Expressed in neurons throughout the brain including in the hippocampus, limbic cortices and cerebellum (at protein level) (PubMed:20637285). In the developing optic nerve, expressed exclusively in astrocytes at E14.5, E16.5 and E18.5 (at protein level) (PubMed:22354480).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 developing optic nerve, more strongly expressed at E14.5 and E16.5 than at E18.5 (at protein level) (PubMed:22354480). In the embryo, expression is detected from E7.5 on the apical side of the developing neural plate and persists throughout later stages of development (PubMed:22340494). After neural tube closure at E9.5, becomes progressively restricted to the midline region (PubMed:22340494). During the estrus cycle, expression is highest in metestrus II and diestrus (PubMed:16143106).3 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated in the kidney by cannabinoids, such as endocannabinoid anandamide and synthetic cannabinoid HU-210.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000027070 Expressed in 154 organ(s), highest expression level in kidney

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		A2ARV4 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		A2ARV4 MM

<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_section">'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_section">'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 (By similarity). Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (By similarity). Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif (PubMed:11247302). Interacts with MB (By similarity). Interacts with BMP4 (PubMed:15623804). Interacts with the Sonic hedgehog protein N-product which is the active product of SHH (PubMed:11964399). Interacts with CST3 in a calcium-dependent manner (By similarity). Interacts with the vitamin-D binding protein GC/DBP (PubMed:10052453). Interacts with sex hormone-binding protein SHBG (By similarity). Interacts with angiotensin-2 (PubMed:15467006). Also interacts with angiotensin 1-7 (PubMed:16380466). Interacts with APOM (PubMed:16099815). Interacts with selenoprotein SEPP1 (PubMed:18174160). Interacts with LEP (By similarity). Interacts with ALB (By similarity). Interacts with the antiapoptotic protein BIRC5/survivin (By similarity). Interacts with matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity). In neurons, forms a trimeric complex with APP and APPB1/FE65 (PubMed:20637285). Interacts with LDLRAP1/ARH; mediates trafficking of LRP2 to the endocytic recycling compartment (By similarity). 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).By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		200005, 5 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		A2ARV4

Protein interaction database and analysis system

More...IntActi		A2ARV4, 11 interactors

Molecular INTeraction database

More...MINTi		A2ARV4

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000079752

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		A2ARV4

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

More...SMRi		A2ARV4

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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_and_domains_section">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
Domaini146 – 180LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST35
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
<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 1PROSITE-ProRule annotationAdd BLAST41
Domaini1391 – 1430EGF-like 2; 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
Repeati2291 – 2333LDL-receptor class B 23PROSITE-ProRule annotationAdd BLAST43
Repeati2432 – 2478LDL-receptor class B 24PROSITE-ProRule annotationAdd BLAST47
Repeati2479 – 2519LDL-receptor class B 25PROSITE-ProRule annotationAdd BLAST41
Repeati2520 – 2563LDL-receptor class B 26PROSITE-ProRule annotationAdd BLAST44
Repeati2564 – 2605LDL-receptor class B 27PROSITE-ProRule annotationAdd BLAST42
Repeati2606 – 2647LDL-receptor class B 28PROSITE-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 3PROSITE-ProRule annotationAdd BLAST42
Domaini3154 – 3194EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3241 – 3283LDL-receptor class B 29PROSITE-ProRule annotationAdd BLAST43
Repeati3284 – 3326LDL-receptor class B 30PROSITE-ProRule annotationAdd BLAST43
Repeati3335 – 3378LDL-receptor class B 31PROSITE-ProRule annotationAdd BLAST44
Repeati3379 – 3421LDL-receptor class B 32PROSITE-ProRule annotationAdd BLAST43
Repeati3422 – 3462LDL-receptor class B 33PROSITE-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
Domaini4009 – 4050EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Repeati4156 – 4198LDL-receptor class B 34PROSITE-ProRule annotationAdd BLAST43
Repeati4199 – 4242LDL-receptor class B 35PROSITE-ProRule annotationAdd BLAST44
Repeati4244 – 4285LDL-receptor class B 36PROSITE-ProRule annotationAdd BLAST42
Domaini4379 – 4413EGF-like 6PROSITE-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 ANKRA2By similarity6
Motifi4460 – 4465PxLPxI/L motif 2; mediates interaction with ANKRA2By similarity6
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.By similarity
The cytoplasmic domain is required for sorting to the apical cell membrane.By similarity

<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
ENOG410XP34 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157232

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000230574

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG097941

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		A2ARV4

KEGG Orthology (KO)

More...KOi		K06233

Database of Orthologous Groups

More...OrthoDBi		1606at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		A2ARV4

TreeFam database of animal gene trees

More...TreeFami		TF315253

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

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, 34 hits
PF00058 Ldl_recept_b, 17 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, 25 hits
SM00179 EGF_CA, 9 hits
SM00192 LDLa, 36 hits
SM00135 LY, 37 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, 6 hits
PS01187 EGF_CA, 3 hits
PS01209 LDLRA_1, 31 hits
PS50068 LDLRA_2, 36 hits
PS51120 LDLRB, 36 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 2 potential isoforms that are computationally mapped.Show allAlign All

A2ARV4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MERGAAAAAW MLLLAIAACL APVSGQECGS GNFRCDNGYC IPASWRCDGT 
        60         70         80         90        100
RDCLDDTDEI GCPPRSCGSG FFLCPAEGTC IPSSWVCDQD KDCSDGADEQ 
       110        120        130        140        150
QNCPGTTCSS QQLTCSNGQC VPIEYRCDHV SDCPDGSDER NCYYPTCDQL 
       160        170        180        190        200
TCANGACYNT SQKCDHKVDC RDSSDEANCT TLCSQKEFQC GSGECILRAY 
       210        220        230        240        250
VCDHDNDCED NSDEHNCNYD TCGGHQFTCS NGQCINQNWV CDGDDDCQDS 
       260        270        280        290        300
GDEDGCESNQ RHHTCYPREW ACPGSGRCIS MDKVCDGVPD CPEGEDENNA 
       310        320        330        340        350
TSGRYCGTGL CSILNCEYQC HQTPYGGECF CPPGHIINSN DSRTCIDFDD 
       360        370        380        390        400
CQIWGICDQK CESRQGRHQC LCEEGYILER GQHCKSNDSF SAASIIFSNG 
       410        420        430        440        450
RDLLVGDLHG RNFRILAESK NRGIVMGVDF HYQKHRVFWT DPMQAKVFST 
       460        470        480        490        500
DINGLNTQEI LNVSIDAPEN LAVDWINNKL YLVETRVNRI DVVNLEGNQR 
       510        520        530        540        550
VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA FMDGSNRKDL 
       560        570        580        590        600
VTTKLGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV 
       610        620        630        640        650
PHPFGISLFE EHVFFTDWTK MAVMKANKFT DTNPQVYHQS SLTPFGVTVY 
       660        670        680        690        700
HALRQPNATN PCGNNNGGCA QICVLSHRTD NGGLGYRCKC EFGFELDADE 
       710        720        730        740        750
HHCVAVKNFL LFSSQTAVRG IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ 
       760        770        780        790        800
HSTIFYSDLS KNIIYQQKID GTGKEVITAN RLQNVECLSF DWISRNLYWT 
       810        820        830        840        850
DGGSKSVTVM KLADKSRRQI ISNLNNPRSI VVHPAAGYMF LSDWFRPAKI 
       860        870        880        890        900
MRAWSDGSHL MPIVNTSLGW PNGLAIDWST SRLYWVDAFF DKIEHSNLDG 
       910        920        930        940        950
LDRKRLGHVD QMTHPFGLTV FKDNVFLTDW RLGAIIRVRK SDGGDMTVVR 
       960        970        980        990       1000
RGISSIMHVK AYDADLQTGT NYCSQTTHPN GDCSHFCFPV PNFQRVCGCP 
      1010       1020       1030       1040       1050
YGMKLQRDQM TCEGDPAREP PTQQCGSSSF PCNNGKCVPS IFRCDGVDDC 
      1060       1070       1080       1090       1100
HDNSDEHQCG ALNNTCSSSA FTCVHGGQCI PGQWRCDKQN DCLDGSDEQN 
      1110       1120       1130       1140       1150
CPTRSPSSTC PPTSFTCDNH MCIPKEWVCD TDNDCSDGSD EKNCQASGTC 
      1160       1170       1180       1190       1200
HPTQFRCPDH RCISPLYVCD GDKDCVDGSD EAGCVLNCTS SQFKCADGSS 
      1210       1220       1230       1240       1250
CINSRYRCDG VYDCKDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE 
      1260       1270       1280       1290       1300
CDGHPDCIQG SDEHNGCVPK TCSPSHFLCD NGNCIYNSWV CDGDNDCRDM 
      1310       1320       1330       1340       1350
SDEKDCPTQP FHCPSSQWQC PGYSICVNLS ALCDGVFDCP NGTDESPLCN 
      1360       1370       1380       1390       1400
QDSCLHFNGG CTHRCIQGPF GATCVCPIGY QLANDTKTCE DVNECDIPGF 
      1410       1420       1430       1440       1450
CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTASENLLLV VASRDKIIMD 
      1460       1470       1480       1490       1500
NITAHTHNIY SLVQDVSFVV ALDFDSVTGR VFWSDLLEGK TWSAFQNGTD 
      1510       1520       1530       1540       1550
KRVVHDSGLS LTEMIAVDWI GRNIYWTDYT LETIEVSKID GSHRTVLISK 
      1560       1570       1580       1590       1600
NVTKPRGLAL DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW 
      1610       1620       1630       1640       1650
PCGLSIDYPN RLIYFMDAYL DYIEFCDYDG QNRRQVIASD LVLHHPHALT 
      1660       1670       1680       1690       1700
LFEDSVFWTD RGTHQVMQAN KWHGRNQSVV MYSVPQPLGI IAIHPSRQPS 
      1710       1720       1730       1740       1750
SPNPCASATC SHLCLLSAQE PRHYSCACPS GWNLSDDSVN CVRGDQPFLI 
      1760       1770       1780       1790       1800
SVRENVIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG 
      1810       1820       1830       1840       1850
EIHRVKTDGS NRTAFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT 
      1860       1870       1880       1890       1900
LRGDTRYGKT LITNDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK 
      1910       1920       1930       1940       1950
IASANMDGTS LKILFTGNME HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD 
      1960       1970       1980       1990       2000
GTERMILVHH LAHPWGLVVH GSFLYYSDEQ YEVIERVDKS SGSNKVVFRD 
      2010       2020       2030       2040       2050
NIPYLRGLRV YHHRNAADSS NGCSNNPNAC QQICLPVPGG MFSCACASGF 
      2060       2070       2080       2090       2100
KLSPDGRSCS PYNSFIVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH 
      2110       2120       2130       2140       2150
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP NGSNFTNIVT YGIGANGIRG 
      2160       2170       2180       2190       2200
VAVDWVAGNL YFTNAFVYET LIEVIRINTT YRRVLLKVSV DMPRHIVVDP 
      2210       2220       2230       2240       2250
KHRYLFWADY GQKPKIERSF LDCTNRTVLV SEGIVTPRGL AVDHDTGYIY 
      2260       2270       2280       2290       2300
WVDDSLDIIA RIHRDGGESQ VVRYGSRYPT PYGITVFGES IIWVDRNLRK 
      2310       2320       2330       2340       2350
VFQASKQPGN TDPPTVIRDS INLLRDVTIF DEHVQPLSPA ELNNNPCLQS 
      2360       2370       2380       2390       2400
NGGCSHFCFA LPELPTPKCG CAFGTLEDDG KNCATSREDF LIYSLNNSLR 
      2410       2420       2430       2440       2450
SLHFDPQDHN LPFQAISVEG MAIALDYDRR NNRIFFTQKL NPIRGQISYV 
      2460       2470       2480       2490       2500
NLYSGASSPT ILLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN 
      2510       2520       2530       2540       2550
RAVIARVSKP RAIVLDPCRG YMYWTDWGTN AKIERATLGG NFRVPIVNTS 
      2560       2570       2580       2590       2600
LVWPNGLTLD LETDLLYWAD ASLQKIERST LTGSNREVVI STAFHSFGLT 
      2610       2620       2630       2640       2650
VYGQYIYWTD FYTKKIYRAN KYDGSDLIAM TTRLPTQPSG ISTVVKTQQQ 
      2660       2670       2680       2690       2700
QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGSWYLANDN KYCVVDTGAR 
      2710       2720       2730       2740       2750
CNQFQFTCLN GRCISQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCA 
      2760       2770       2780       2790       2800
NGRCVPYHYR CDFYNDCGDN SDEAGCLFRS CNSTTEFTCS NGRCIPLSYV 
      2810       2820       2830       2840       2850
CNGINNCHDN DTSDEKNCPP ITCQPDFAKC QTTNICVPRA FLCDGDNDCG 
      2860       2870       2880       2890       2900
DGSDENPIYC ASHTCRSNEF QCVSPHRCIP SYWFCDGEAD CVDSSDEPDT 
      2910       2920       2930       2940       2950
CGHSLNSCSA NQFHCDNGRC ISSSWVCDGD NDCGDMSDED QRHHCELQNC 
      2960       2970       2980       2990       3000
SSTEFTCINS RPPNRRCIPQ HWVCDGDADC ADALDELQNC TMRACSTGEF 
      3010       3020       3030       3040       3050
SCANGRCIRQ SFRCDRRNDC GDYSDERGCS YPPCRDDQFT CQNGQCITKL 
      3060       3070       3080       3090       3100
YVCDEDNDCG DGSDEQEHLC HTPEPTCPPH QFRCDNGHCI EMGTVCNHVD 
      3110       3120       3130       3140       3150
DCSDNSDEKG CGINECQDSS ISHCDHNCTD TITSFYCSCL PGYKLMSDKR 
      3160       3170       3180       3190       3200
TCVDIDECKE TPQLCSQKCE NVIGSYICKC APGYIREPDG KSCRQNSNIE 
      3210       3220       3230       3240       3250
PYLVFSNRYY IRNLTIDGTS YSLILQGLGN VVALDFDRVE ERLYWIDAEK 
      3260       3270       3280       3290       3300
QIIERMFLNK TNQETIISHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD 
      3310       3320       3330       3340       3350
LEGRQRKMLA QHCVDANNTF CFENPRGIVL HPQRGYVYWA DWGDHAYIAR 
      3360       3370       3380       3390       3400
IGMDGTNKTV IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH 
      3410       3420       3430       3440       3450
RHTVYDGTLP HPFALTIFED TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT 
      3460       3470       3480       3490       3500
HKPFDIHVLH PYRQPIMSNP CATNNGGCSH LCLIKAGGRG FTCECPDDFQ 
      3510       3520       3530       3540       3550
TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC SDGSDESDLC 
      3560       3570       3580       3590       3600
PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCEANE 
      3610       3620       3630       3640       3650
WQCANKRCIP EYWQCDSVDD CLDNSDEDPS HCASRTCRPG QFKCNNGRCI 
      3660       3670       3680       3690       3700
PQSWKCDVDN DCGDYSDEPI HECMTAAYNC DNHTEFSCKT NYRCIPQWAV 
      3710       3720       3730       3740       3750
CNGFDDCRDN SDEQGCESVP CHPSGDFRCG NHHCIPLRWK CDGIDDCGDN 
      3760       3770       3780       3790       3800
SDEESCVPRE CTESEFRCAD QQCIPSRWVC DQENDCGDNS DERDCEMKTC 
      3810       3820       3830       3840       3850
HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN GTYCPAAMFE 
      3860       3870       3880       3890       3900
CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNVPCESPQR FRCDNSRCIY 
      3910       3920       3930       3940       3950
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCVSQHYVCD 
      3960       3970       3980       3990       4000
NVDDCGDLSD ETGCNLGENR TCAEKICEQN CTQLSNGGFI CSCRPGFKPS 
      4010       4020       4030       4040       4050
TLDKNSCQDI NECEEFGICP QSCRNSKGSY ECFCVDGFKS MSTHYGERCA 
      4060       4070       4080       4090       4100
ADGSPPLLLL PENVRIRKYN ISSEKFSEYL EEEEHIQAID YDWDPEGIGL 
      4110       4120       4130       4140       4150
SVVYYTVLSQ GSQFGAIKRA YLPDFESGSN NPVREVDLGL KYLMQPDGLA 
      4160       4170       4180       4190       4200
VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL 
      4210       4220       4230       4240       4250
MFWTDQGKQP KIESAWMNGE HRSVLASANL GWPNGLSIDY LNGDRIYWSD 
      4260       4270       4280       4290       4300
SKEDVIESIK YDGTDRRLII NDAMKPFSLD IFEDQLYWVA KEKGEVWRQN 
      4310       4320       4330       4340       4350
KFGKGNKEKL LVVNPWLTQV RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG 
      4360       4370       4380       4390       4400
YSCACPQGSD FVTGSTVECD AASELPITMP SPCRCMHGGS CYFDENDLPK 
      4410       4420       4430       4440       4450
CKCSSGYSGE YCEIGLSRGI PPGTTMALLL TFAMVIIVGA LVLVGFFHYR 
      4460       4470       4480       4490       4500
KTGSLLPSLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI 
      4510       4520       4530       4540       4550
IDRSMAMNEQ FVMEVGKQPV IFENPMYAAK DSTSKVGLAV QGPSVSSQVT 
      4560       4570       4580       4590       4600
VPENVENQNY GRSIDPSEIV PEPKPASPGA DETQGTKWNI FKRKPKQTTN 
      4610       4620       4630       4640       4650
FENPIYAEMD TEQKEAVAVA PPPSPSLPAK ASKRSSTPGY TATEDTFKDT 
      4660
ANLVKEDSDV
Length:4,660
Mass (Da):519,208
Last modified:February 20, 2007 - 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:i4CF399C24DF2FAA4
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2ARV5A2ARV5_MOUSE
Low-density lipoprotein receptor-re...
Lrp2
1,363Annotation 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>
Q3V346Q3V346_MOUSE
Low-density lipoprotein receptor-re...
Lrp2
426Annotation score:

Annotation score:4 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti4198L → F in CAA69877 (Ref. 3) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AL845489 Genomic DNA No translation available.
AK166702 mRNA Translation: BAE38957.1
Y08566 mRNA Translation: CAA69877.1
AF197160 mRNA Translation: AAF61488.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS38135.1

NCBI Reference Sequences

More...RefSeqi		NP_001074557.1, NM_001081088.1

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.23847

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000080953; ENSMUSP00000079752; ENSMUSG00000027070

Database of genes from NCBI RefSeq genomes

More...GeneIDi		14725

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:14725

UCSC genome browser

More...UCSCi		uc008jyc.1 mouse

<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
AL845489 Genomic DNA No translation available.
AK166702 mRNA Translation: BAE38957.1
Y08566 mRNA Translation: CAA69877.1
AF197160 mRNA Translation: AAF61488.1
CCDSiCCDS38135.1
RefSeqiNP_001074557.1, NM_001081088.1
UniGeneiMm.23847

3D structure databases

ProteinModelPortaliA2ARV4
SMRiA2ARV4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200005, 5 interactors
CORUMiA2ARV4
IntActiA2ARV4, 11 interactors
MINTiA2ARV4
STRINGi10090.ENSMUSP00000079752

Protein family/group databases

TCDBi9.B.87.1.1 the selenoprotein p receptor (selp-receptor) family

PTM databases

iPTMnetiA2ARV4
PhosphoSitePlusiA2ARV4

Proteomic databases

jPOSTiA2ARV4
MaxQBiA2ARV4
PaxDbiA2ARV4
PeptideAtlasiA2ARV4
PRIDEiA2ARV4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000080953; ENSMUSP00000079752; ENSMUSG00000027070
GeneIDi14725
KEGGimmu:14725
UCSCiuc008jyc.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4036
MGIiMGI:95794 Lrp2

Phylogenomic databases

eggNOGiKOG1215 Eukaryota
ENOG410XP34 LUCA
GeneTreeiENSGT00940000157232
HOGENOMiHOG000230574
HOVERGENiHBG097941
InParanoidiA2ARV4
KOiK06233
OrthoDBi1606at2759
PhylomeDBiA2ARV4
TreeFamiTF315253

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...PROi		PR:A2ARV4

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000027070 Expressed in 154 organ(s), highest expression level in kidney
ExpressionAtlasiA2ARV4 baseline and differential
GenevisibleiA2ARV4 MM

Family and domain databases

CDDicd00112 LDLa, 36 hits
Gene3Di2.120.10.30, 8 hits
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, 34 hits
PF00058 Ldl_recept_b, 17 hits
PRINTSiPR00261 LDLRECEPTOR
SMARTiView protein in SMART
SM00181 EGF, 25 hits
SM00179 EGF_CA, 9 hits
SM00192 LDLa, 36 hits
SM00135 LY, 37 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, 6 hits
PS01187 EGF_CA, 3 hits
PS01209 LDLRA_1, 31 hits
PS50068 LDLRA_2, 36 hits
PS51120 LDLRB, 36 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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_MOUSE
<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: A2ARV4
Secondary accession number(s): P70215, Q3TL35, Q9JLB3
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: February 20, 2007
Last modified: January 16, 2019
This is version 118 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

Complete proteome, Reference proteome

Documents

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