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Entry version 161 (10 Apr 2019)
Sequence version 2 (10 May 2004)
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Protein

Low-density lipoprotein receptor-related protein 8

Gene

Lrp8

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

Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation (PubMed:12695510). May also function as an endocytic receptor. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (PubMed:18174160). Together with its ligand, apolipoprotein E (apoE), may indirectly play a role in the suppression of the innate immune response by controlling the survival of myeloid-derived suppressor cells (PubMed:29336888).3 Publications

<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
LigandCalcium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-432142 Platelet sensitization by LDL
R-MMU-975634 Retinoid metabolism and transport

Protein family/group databases

Transport Classification Database

More...
TCDBi
9.B.87.1.9 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 8
Short name:
LRP-8
Alternative name(s):
Apolipoprotein E receptor 2
<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:Lrp8
Synonyms:Apoer2
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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 4

Organism-specific databases

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

More...
MGIi
MGI:1340044 Lrp8

<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_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 domaini29 – 858ExtracellularSequence analysisAdd BLAST830
<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>Transmembranei859 – 881HelicalSequence analysisAdd BLAST23
Topological domaini882 – 996CytoplasmicSequence analysisAdd BLAST115

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

<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

Does not affect endocytosis of SEPP1 in the kidney proximal tubule (PubMed:18174160). Targeted disruption of LRP8 and VLVLR together results in a phenotype virtually indistinguishable from that seen in "reeler" and "scrambler" mice. Subtle effects of VLDLR deletion are found mainly in the cerebellum, whereas lack of LRP8 predominantly affects the positioning of the neurons in the neocortex. Besides brain formation defects, LRP8-deficient mice also exhibit male infertility.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi61D → N: Lower affinity for RAP. Abolishes binding to Reelin. 1 Publication1
Mutagenesisi102E → Q: Same affinity for RAP. Same affinity for Reelin. 1 Publication1
Mutagenesisi145E → Q: Same affinity for RAP. Lower affinity for Reelin. 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 – 28Sequence analysisAdd BLAST28
<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_000001733329 – 996Low-density lipoprotein receptor-related protein 8Add BLAST968

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 bondi41 ↔ 53By similarity
Disulfide bondi48 ↔ 66By similarity
Disulfide bondi60 ↔ 75By similarity
Disulfide bondi80 ↔ 92By similarity
Disulfide bondi87 ↔ 105By similarity
Disulfide bondi99 ↔ 116By similarity
Disulfide bondi121 ↔ 135By similarity
Disulfide bondi128 ↔ 148By similarity
Disulfide bondi142 ↔ 157By similarity
Disulfide bondi161 ↔ 173By similarity
Disulfide bondi168 ↔ 186By similarity
<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>Glycosylationi170N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi180 ↔ 195By similarity
Disulfide bondi200 ↔ 213By similarity
Disulfide bondi207 ↔ 226By similarity
Disulfide bondi220 ↔ 237By similarity
Disulfide bondi251 ↔ 264By similarity
Disulfide bondi259 ↔ 277By similarity
Disulfide bondi271 ↔ 286By similarity
Disulfide bondi291 ↔ 303By similarity
Disulfide bondi298 ↔ 316By similarity
Disulfide bondi310 ↔ 325By similarity
Disulfide bondi331 ↔ 344By similarity
Disulfide bondi339 ↔ 357By similarity
Disulfide bondi351 ↔ 368By similarity
Disulfide bondi373 ↔ 384By similarity
Disulfide bondi380 ↔ 393By similarity
Disulfide bondi395 ↔ 407By similarity
Disulfide bondi413 ↔ 423By similarity
Disulfide bondi419 ↔ 432By similarity
Disulfide bondi434 ↔ 447By similarity
Glycosylationi551N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi805N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi840N-linked (GlcNAc...) asparagineSequence analysis1

<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

O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain.1 Publication
Undergoes sequential, furin and gamma-secretase dependent, proteolytic processing, resulting in the extracellular release of the entire ligand-binding domain as a soluble polypeptide and in the intracellular domain (ICD) release into the cytoplasm. The gamma-secretase-dependent proteolytical processing occurs after the bulk of the extracellular domain has been shed, in a furin-dependent manner, in alternatively spliced isoforms carrying the furin cleavage site. Hypoglycosylation (mainly hypo-O-glycosylation) leads to increased extracellular cleavage, which in turn results in accelerating release of the intracellular domain (ICD) by the gamma-secretase. The resulting receptor fragment is able to inhibit Reelin signaling and in particular the Reelin-induced DAB1 phosphorylation.2 Publications
Tyrosine phosphorylated upon apoE binding.By similarity
Ubiquitinated by MYLIP leading to degradation.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q924X6

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q924X6

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

More...
PhosphoSitePlusi
Q924X6

<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

Expressed in neurons throughout the brain, with strong expression in pyramidal neurons of the hippocampus, granule cells of the dentate gyrus, cortical neurons and Purkinje cells of the cerebellum. Also expressed in the epithelium of the choroid plexus and of the blood vessels (apical expression), as well as in the epididymis.1 Publication

<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

Expressed from 12 dpc to 16 dpc. Mice which are deficient in LRP8 have neuronal migration defect.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000028613 Expressed in 186 organ(s), highest expression level in brain blood vessel

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q924X6 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q924X6 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

Reelin associates with two or more receptor molecules. Interacts with DAB1 and JNK-interacting proteins. Interacts with SNX17. Interacts with PCSK9 (By similarity).By similarity

<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

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q924X6

Database of interacting proteins

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DIPi
DIP-33284N

Protein interaction database and analysis system

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IntActi
Q924X6, 9 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000102343

<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

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ProteinModelPortali
Q924X6

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

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SMRi
Q924X6

Database of comparative protein structure models

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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>Domaini40 – 76LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST37
Domaini79 – 117LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST39
Domaini120 – 158LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST39
Domaini160 – 196LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST37
Domaini199 – 238LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST40
Domaini250 – 287LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST38
Domaini290 – 326LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST37
Domaini330 – 369LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST40
Domaini364 – 408EGF-like 1PROSITE-ProRule annotationAdd BLAST45
Domaini409 – 448EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
<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>Repeati495 – 541LDL-receptor class B 1Add BLAST47
Repeati542 – 584LDL-receptor class B 2Add BLAST43
Repeati585 – 628LDL-receptor class B 3Add BLAST44
Repeati629 – 671LDL-receptor class B 4Add BLAST43
Repeati672 – 714LDL-receptor class B 5Add BLAST43

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>Regioni773 – 831Clustered O-linked oligosaccharidesAdd BLAST59

<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

The cytoplasmic domain is involved in the binding of DAB1 and in the recruitment of JNK-interacting proteins. Isoforms, which lack part of the cytoplasmic domain, are unable to recruit members of the family of JNK interacting proteins (JIP) to the cytoplasmic tail.

<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, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154819

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000115656

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG006250

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q924X6

Database of Orthologous Groups

More...
OrthoDBi
359795at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q924X6

Family and domain databases

Conserved Domains Database

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CDDi
cd00112 LDLa, 7 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.120.10.30, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
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
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
PF07645 EGF_CA, 1 hit
PF00057 Ldl_recept_a, 8 hits
PF00058 Ldl_recept_b, 5 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00261 LDLRECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00181 EGF, 4 hits
SM00179 EGF_CA, 2 hits
SM00192 LDLa, 8 hits
SM00135 LY, 5 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57424 SSF57424, 8 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00010 ASX_HYDROXYL, 2 hits
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 2 hits
PS01187 EGF_CA, 1 hit
PS01209 LDLRA_1, 8 hits
PS50068 LDLRA_2, 8 hits
PS51120 LDLRB, 5 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>Sequences (3+)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 describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q924X6-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MGRPELGALR PLALLLLLLL QLQHLSAADP LPGGQGPVKE CEEDQFRCRN
60 70 80 90 100
ERCIPLVWRC DEDNDCSDNS DEDDCPKRTC ADSDFTCDNG HCIPERWKCD
110 120 130 140 150
GEEECPDGSD ESKATCSSEE CPAEKLSCGP TSHKCVPASW RCDGEKDCEG
160 170 180 190 200
GADEAGCPTL CAPHEFQCSN RSCLASVFVC DGDDDCGDGS DERGCSDPAC
210 220 230 240 250
PPREFRCGGG GTCIPERWVC DRQFDCEDRS DEAAELCGRA GQGTTATPAA
260 270 280 290 300
CAPTAQFTCR SGECIHLGWR CDGDRDCKDK SDEADCSPGP CRENEFQCGD
310 320 330 340 350
GTCVLAIKRC NQERDCPDGS DEAGCLQEST CEGPRRFQCK SGECVDGGKV
360 370 380 390 400
CDDQRDCRDW SDEPQKVCGL NECLHNNGGC SHICTDLKIG FECTCPAGFQ
410 420 430 440 450
LLDQKTCGDI DECQDPDACS QICVNYKGYF KCECHPGYEM DTLTKNCKAV
460 470 480 490 500
AGKSPSLIFT NRHEVRRIDL VKRDYSRLIP MLKNVVALDV EVATNRIYWC
510 520 530 540 550
DLSYRKIYSA HMDKASIPDE QVVLIDEQLH SPEGLAVDWV HKHIYWTDSG
560 570 580 590 600
NKTISVATTD GRRRCTLFSR ELSEPRAIAV DPLRGFMYWS DWGFQAKIEK
610 620 630 640 650
AGLNGADRQT LVSDNIEWPN GITLDLLSQR LYWVDSKLHQ LSSIDFNGGN
660 670 680 690 700
RKMLIFSTDF LSHPFGVAVF EDKVFWTDLE NEAIFSANRL NGLEIAILAE
710 720 730 740 750
NLNNPHDIVI FHELKQPKAA DACDLSAQPN GGCEYLCLPA PQISSHSPKY
760 770 780 790 800
TCACPDTMWL GPDMKRCYRA PQSTSTTTLA SAMTRTVPAT TRAPGTTIHD
810 820 830 840 850
PTYQNHSTET PSQTAAAPHS VNVPRAPSTS PSTPSPATSN HSQHYGNEGS
860 870 880 890 900
QMGSTVTAAV IGVIVPIVVI ALLCMSGYLI WRNWKRKNTK SMNFDNPVYR
910 920 930 940 950
KTTEEEEEDE LHIGRTAQIG HVYPAAISNY DRPLWAEPCL GETRDLEDPA
960 970 980 990
PALKELFVLP GEPRSQLHQL PKNPLSELPV VKCKRVALSL EDDGLP
Length:996
Mass (Da):109,818
Last modified:May 10, 2004 - v2
<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:iBA1AF0132A964EBA
GO
Isoform 2 (identifier: Q924X6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     160-285: Missing.

Note: No experimental confirmation available.
Show »
Length:870
Mass (Da):96,351
Checksum:i3531262B7C9D6446
GO
Isoform 3 (identifier: Q924X6-5)
Also known as: ApoER2delta4-6,8-F
Sequence is not available
Note: Contains a 18 aa insert in the extracellular part which carries a furin cleavage site.
Length:
Mass (Da):

<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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1AXJ3B1AXJ3_MOUSE
Low-density lipoprotein receptor-re...
Lrp8
870Annotation score:

Annotation score:3 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>
B1AXJ4B1AXJ4_MOUSE
Low-density lipoprotein receptor-re...
Lrp8
955Annotation score:

Annotation score:2 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>
B1AXJ5B1AXJ5_MOUSE
Low-density lipoprotein receptor-re...
Lrp8
896Annotation score:

Annotation score:2 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>
B1AXJ6B1AXJ6_MOUSE
Low-density lipoprotein receptor-re...
Lrp8
694Annotation score:

Annotation score:2 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>
F6YZZ8F6YZZ8_MOUSE
Low-density lipoprotein receptor-re...
Lrp8
699Annotation score:

Annotation score:2 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 conflicti32P → L in BAB46965 (PubMed:9685741).Curated1
Sequence conflicti286 – 287CS → SA (PubMed:11294845).Curated2
Sequence conflicti610T → P in CAC38356 (PubMed:11294845).Curated1
Sequence conflicti672 – 673DK → VQ in CAC38356 (PubMed:11294845).Curated2
Sequence conflicti715 – 716KQ → NE in CAC38356 (PubMed:11294845).Curated2
Sequence conflicti750Y → F in CAC38356 (PubMed:11294845).Curated1
Sequence conflicti766R → K in CAC38356 (PubMed:11294845).Curated1
Sequence conflicti802T → A in CAC38356 (PubMed:11294845).Curated1
Sequence conflicti815 – 817AAA → VAV in CAC38356 (PubMed:11294845).Curated3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_010309160 – 285Missing in isoform 2. 1 PublicationAdd BLAST126

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
D85463 mRNA Translation: BAB46965.1
AJ312058 mRNA Translation: CAC38356.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS51255.1 [Q924X6-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
JE0237

NCBI Reference Sequences

More...
RefSeqi
XP_011238759.1, XM_011240457.2 [Q924X6-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.442134

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000143601; ENSMUSP00000115854; ENSMUSG00000028613 [Q924X6-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
16975

Keywords - Coding sequence diversityi

Alternative splicing

<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
D85463 mRNA Translation: BAB46965.1
AJ312058 mRNA Translation: CAC38356.1
CCDSiCCDS51255.1 [Q924X6-2]
PIRiJE0237
RefSeqiXP_011238759.1, XM_011240457.2 [Q924X6-1]
UniGeneiMm.442134

3D structure databases

ProteinModelPortaliQ924X6
SMRiQ924X6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiQ924X6
DIPiDIP-33284N
IntActiQ924X6, 9 interactors
STRINGi10090.ENSMUSP00000102343

Protein family/group databases

TCDBi9.B.87.1.9 the selenoprotein p receptor (selp-receptor) family

PTM databases

iPTMnetiQ924X6
PhosphoSitePlusiQ924X6

Proteomic databases

PRIDEiQ924X6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000143601; ENSMUSP00000115854; ENSMUSG00000028613 [Q924X6-1]
GeneIDi16975

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7804
MGIiMGI:1340044 Lrp8

Phylogenomic databases

GeneTreeiENSGT00940000154819
HOGENOMiHOG000115656
HOVERGENiHBG006250
InParanoidiQ924X6
OrthoDBi359795at2759
PhylomeDBiQ924X6

Enzyme and pathway databases

ReactomeiR-MMU-432142 Platelet sensitization by LDL
R-MMU-975634 Retinoid metabolism and transport

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q924X6

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028613 Expressed in 186 organ(s), highest expression level in brain blood vessel
ExpressionAtlasiQ924X6 baseline and differential
GenevisibleiQ924X6 MM

Family and domain databases

CDDicd00112 LDLa, 7 hits
Gene3Di2.120.10.30, 1 hit
InterProiView protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
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
IPR036055 LDL_receptor-like_sf
IPR023415 LDLR_class-A_CS
IPR000033 LDLR_classB_rpt
IPR002172 LDrepeatLR_classA_rpt
PfamiView protein in Pfam
PF07645 EGF_CA, 1 hit
PF00057 Ldl_recept_a, 8 hits
PF00058 Ldl_recept_b, 5 hits
PRINTSiPR00261 LDLRECEPTOR
SMARTiView protein in SMART
SM00181 EGF, 4 hits
SM00179 EGF_CA, 2 hits
SM00192 LDLa, 8 hits
SM00135 LY, 5 hits
SUPFAMiSSF57424 SSF57424, 8 hits
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 2 hits
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 2 hits
PS01187 EGF_CA, 1 hit
PS01209 LDLRA_1, 8 hits
PS50068 LDLRA_2, 8 hits
PS51120 LDLRB, 5 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 nameiLRP8_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: Q924X6
Secondary accession number(s): Q8CAK9, Q8CDF5, Q921B6
<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: May 10, 2004
Last sequence update: May 10, 2004
Last modified: April 10, 2019
This is version 161 of the entry and version 2 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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