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0LDLR_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLDLR
DescriptionLow-density lipoprotein receptor precursor (ldl receptor).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005886 plasma membrane (TAS)
0008034 lipoprotein binding (TAS)
0005041 low-density lipoprotein receptor activity (TAS)
0004888 transmembrane receptor activity (TAS)
0006897 endocytosis (TAS)
0006629 lipid metabolism (TAS)
0006493 protein amino acid O-linked glycosylation (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 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
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
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:-22.7695503234863 
Location:146-184IPR002172:Ldl_recept_a 
Evalue:-20.9586067199707 
Location:195-231IPR002172:Ldl_recept_a 
Evalue:-20.2676067352295 
Location:25-63IPR002172:Ldl_recept_a 
Evalue:-19.017728805542 
Location:234-270IPR002172:Ldl_recept_a 
Evalue:-18.8860569000244 
Location:66-104IPR002172:Ldl_recept_a 
Evalue:-18.8860569000244 
Location:107-143IPR002172:Ldl_recept_a 
Evalue:-17.5376014709473 
Location:274-313IPR000033:Ldl_recept_b 
Evalue:-16.4202156066895 
Location:439-484IPR000033:Ldl_recept_b 
Evalue:-15.5686359405518 
Location:486-527IPR000033:Ldl_recept_b 
Evalue:-15.0915145874023 
Location:529-571IPR000033:Ldl_recept_b 
Evalue:-14.1938199996948 
Location:573-616IPR001881:EGF_CA 
Evalue:-9.11350927482752 
Location:354-393IPR006209:EGF 
Evalue:-7.74472761154175 
Location:318-352IPR000033:Ldl_recept_b 
Evalue:-7.58502674102783 
Location:617-657IPR006209:EGF 
Evalue:-2.39793992042541 
Location:667-711IPR013032:EGF_1 
Evalue:0 
Location:0-0
SequencesProtein: LDLR_HUMAN (860 aa)
mRNA: AB209409 NM_000527
Local Annotation
Synapse Ontology
the clathrin located in the surface of the endocytotic intermediate.
sdb:0115 clathrin-coated pit  (Evidence:keywords)
Microglias, one kind of glias in CNS, are responsible for removing most of the waste and cellular debris from the CNS
sdb:0267 removing metabolic mass  (Evidence:keywords)
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 54 residues, 11061131-11061291Exon2: 43 residues, 11071898-11072021Exon3: 43 residues, 11074339-11074462Exon4: 129 residues, 11076895-11077276Exon5: 43 residues, 11078240-11078363Exon6: 43 residues, 11079067-11079190Exon7: 42 residues, 11082327-11082447Exon8: 44 residues, 11083189-11083315Exon9: 59 residues, 11084953-11085125Exon10: 78 residues, 11085210-11085438Exon11: 41 residues, 11087769-11087888Exon12: 48 residues, 11088534-11088674Exon13: 49 residues, 11091767-11091909Exon14: 53 residues, 11092045-11092198Exon15: 59 residues, 11094849-11095020Exon16: 28 residues, 11099683-11099761Exon17: 54 residues, 11101188-11101346Exon18: 846 residues, 11102956-11105490Exon19: 2 residues, -Jump to LDLR_HUMANExon1: 47 residues, 11061153-11061291Exon2: 43 residues, 11071898-11072021Exon3: 43 residues, 11074339-11074462Exon4: 129 residues, 11076895-11077276Exon5: 43 residues, 11078240-11078363Exon6: 43 residues, 11079067-11079190Exon7: 42 residues, 11082327-11082447Exon8: 44 residues, 11083189-11083315Exon9: 59 residues, 11084953-11085125Exon10: 78 residues, 11085210-11085438Exon11: 41 residues, 11087769-11087888Exon12: 48 residues, 11088534-11088674Exon13: 49 residues, 11091767-11091909Exon14: 53 residues, 11092045-11092198Exon15: 59 residues, 11094849-11095020Exon16: 28 residues, 11099683-11099761Exon17: 54 residues, 11101188-11101346Exon18: 177 residues, 11102962-11103488Exon19: 2 residues, -Jump to LDLR_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4364 10305453-10311300 ~-6K 17970(ICAM3)(-)Loci: 4365 10544347-10558991 ~-15K 17988(AP1M2)(-)Loci: 3088 10689754-10803579 ~-114K 18002(DNM2)(+)Loci: 3089 10843252-10894447 ~-51K 18009(CARM1)(+)Loci: 3090 11061131-11105490 ~-44K 18013(LDLR)(+)Loci: 4366 11296093-11311321 ~-15K 18027(RAB3D)(-)Loci: 4363 9825394-9908070 ~-83K 17941(OLFM2)(-)Link out to UCSC