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0LRP8_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLRP8
DescriptionLow-density lipoprotein receptor-related protein 8 precursor (apolipoprotein e receptor 2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (IC)
0005886 plasma membrane (NAS)
0030227 apolipoprotein E receptor activity (IDA)
0008034 lipoprotein binding (IC)
0004888 transmembrane receptor activity (TAS)
0019221 cytokine and chemokine mediated signaling p... (NAS)
0006897 endocytosis (IDA)
0006629 lipid metabolism (NAS)
0006508 proteolysis and peptidolysis (NAS)
0007165 signal transduction (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Low density lipoprotein (LDL) is the major cholesterol-carrying lipoprotein of plasma. The receptor protein binds LDL and transports it into cells by endocytosis. In order to be internalised.he receptor-ligand complex must first cluster into clathrin-coated pits. Seven successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein .The LDL-receptor class A domain contains 6 disulphide-bound cysteines and a highly conserved cluster of negatively charged amino acids.f which many are clustered on one face of the module . A schematic representation of this domain is shown here:In LDL-receptors the class A domains form the binding site for LDL and calcium . The acidic residues between the fourth and sixth cysteines are important for high-affinity binding of positively charged sequences in LDLRs ligands . The repeat has been shown to consist of a beta-hairpin structure followed by a series of beta turns. In the absence of calcium.DL-A domains are unstructured; the bound calcium ion imparts structural integrity.Following these repeats is a 350 residue domain that resembles part of the epidermal growth factor (EGF) precursor .Similar domains have been found (see references in ) in several extracellular and membrane proteins (see examples).Numerous familial hypercholestorolemia mutations of the LDL receptor alter the calcium coordinating residue of LDL-A domains or other crucial scaffolding residues.
  IPR002172:Low density lipoprotein-receptor, class A
The low-density lipoprotein receptor (LDLR) regulates cholesterol homeostasis in mammalian cells. LDLR binds cholesterol-carrying LDL.ssociates with clathrin-coated pits.nd is internalized into acidic endosomes where it separates from its ligand. The ligand is degraded in lysosomes.hile the receptor returns to the cell surface . The LDLR has several domains. The ligand-binding domain contains seven LDL receptor class A repeats.ach with three disulfide bonds and a coordinated Ca2+ ion. The second conserved region contains two EGF repeats.ollowed by six YWTD or LDL receptor class B repeats and another EGF repeat . This conserved region is critical for ligand release and recycling of the receptor . The structure of the six YWTD repeats of LDL receptor have been solved . The six YWTD repeats together fold into a six-bladed beta-propeller. Each blade of the propeller consists of four antiparallel beta-strands; the innermost strand of each blade is labeled 1 and the outermost strand.. The sequence repeats are offset with respect to the blades of the propeller.uch that any given 40-residue YWTD repeat spans strands 24 of one propeller blade and strand 1 of the subsequent blade. This offset ensures circularization of the propeller because the last strand of the final sequence repeat acts as an innermost strand 1 of the blade that harbors strands 24 from the first sequence repeat. The repeat is found in a variety of proteins that include.itellogenin receptor from Drosophila melanogaster.ow-density lipoprotein (LDL) receptor .reproepidermal growth factor.nd nidogen (entactin).
  IPR000033:Low-density lipoprotein receptor, YWTD repeat
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown .o be present in a large number of membrane-bound and extracellular.ostly animal.roteins. Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains . Calcium-binding may be crucial for numerous protein-protein interactions.For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. The first.hird and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated (see aspartic acid and asparagine hydroxylation site) . A conserved aromatic residue.s well as the second conserved negative residue.re thought to be involved in stabilizing the calcium-binding site.As in non-calcium binding EGF-like domains.here are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes .
  IPR001881:EGF-like calcium-binding
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.
  IPR006209:EGF-like
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown .o be present in a large number of membrane-bound and extracellular.ostly animal.roteins. Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains . Calcium-binding may be crucial for numerous protein-protein interactions.For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. The first.hird and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated (see aspartic acid and asparagine hydroxylation site) . A conserved aromatic residue.s well as the second conserved negative residue.re thought to be involved in stabilizing the calcium-binding site.As in non-calcium binding EGF-like domains.here are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes .
  IPR013091:EGF calcium-binding
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
IPR002172:Ldl_recept_a 
Evalue:-18 
Location:165-201IPR002172:Ldl_recept_a 
Evalue:-17.508638381958 
Location:257-294IPR002172:Ldl_recept_a 
Evalue:-17.3372421264648 
Location:84-122IPR000033:Ldl_recept_b 
Evalue:-15.5528421401978 
Location:552-594IPR000033:Ldl_recept_b 
Evalue:-15.4948501586914 
Location:509-550IPR002172:Ldl_recept_a 
Evalue:-15.4202165603638 
Location:45-81IPR002172:Ldl_recept_a 
Evalue:-14.6989698410034 
Location:297-333IPR002172:Ldl_recept_a 
Evalue:-14.4948501586914 
Location:204-245IPR000033:Ldl_recept_b 
Evalue:-12.3979396820068 
Location:596-639IPR000033:Ldl_recept_b 
Evalue:-10.7695512771606 
Location:462-507IPR002172:Ldl_recept_a 
Evalue:-9.04575729370117 
Location:125-163IPR001881:EGF_CA 
Evalue:-8.74472749489669 
Location:376-415IPR000033:Ldl_recept_b 
Evalue:-8.6777811050415 
Location:640-680IPR006209:EGF 
Evalue:-7.50863838195801 
Location:340-374IPR013032:EGF_1 
Evalue:0 
Location:0-0IPR006210:EGF 
Evalue:1.17609125905568 
Location:689-735
SequencesProtein: LRP8_HUMAN (963 aa)
mRNA: D50678 NM_004631
Local Annotation
Synapse Ontology
microtubules of the presynaptic compartment function as the tracks for the intense traffic of organelles from cell body to axon terminals and vice versa. It is generally excluded from the presynaptic vesicle cluster.Microtubules do not directly regulate synapse morphology or function
sdb:0087 microtubules  (Evidence:keywords)
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 505 residues, 53483804-53485316Exon2: 61 residues, 53487639-53487816Exon3: 59 residues, 53488949-53489122Exon4: 25 residues, 53493376-53493445Exon5: 77 residues, 53495499-53495724Exon6: 53 residues, 53496578-53496731Exon7: 49 residues, 53498723-53498865Exon8: 48 residues, 53500327-53500467Exon9: 41 residues, 53500705-53500824Exon10: 78 residues, 53502428-53502656Exon11: 59 residues, 53504732-53504905Exon12: 44 residues, 53509285-53509413Exon13: 42 residues, 53509486-53509606Exon14: 43 residues, 53513890-53514013Exon15: 131 residues, 53514951-53515338Exon16: 45 residues, 53518846-53518975Exon17: 43 residues, 53527826-53527949Exon18: 42 residues, 53565132-53565252Exon19: 77 residues, 53566048-53566274Exon20: 2 residues, -Jump to LRP8_HUMANExon1: 505 residues, 53483804-53485316Exon2: 61 residues, 53487639-53487816Exon3: 59 residues, 53488949-53489122Exon4: 25 residues, 53493376-53493445Exon5: 77 residues, 53495499-53495724Exon6: 53 residues, 53496578-53496731Exon7: 49 residues, 53498723-53498865Exon8: 48 residues, 53500327-53500467Exon9: 41 residues, 53500705-53500824Exon10: 78 residues, 53502428-53502656Exon11: 60 residues, 53504732-53504907Exon12: 44 residues, 53509287-53509413Exon13: 42 residues, 53509486-53509606Exon14: 43 residues, 53513890-53514013Exon15: 131 residues, 53514951-53515338Exon16: 45 residues, 53518846-53518975Exon17: 43 residues, 53527826-53527949Exon18: 42 residues, 53565132-53565252Exon19: 90 residues, 53566048-53566314Exon20: 2 residues, -Jump to LRP8_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2519 53434688-53452455 ~-18K 1515(CPT2)(+)Loci: 3804 53483804-53566314 ~-83K 1520(LRP8)(-)Loci: 2518 53165535-53289870 ~-124K 1506(SCP2)(+)Link out to UCSC