Protein detail

LDLR

Low-density lipoprotein receptor (LDL receptor)

Protein symbol
LDLR
UniProt ID
EVMP score
0.25
Frequency
3
Transmembrane count
1
Protein classification
Disease related genesHuman disease related genesMetabolic proteinsPlasma proteinsPredicted intracellular proteinsPredicted membrane proteins
Basic Information
Protein Names
Low-density lipoprotein receptor (LDL receptor)
Protein Class
Disease related genesHuman disease related genesMetabolic proteinsPlasma proteinsPredicted intracellular proteinsPredicted membrane proteins
Protein Function
  • Human disease related genes:Cardiovascular diseases:Vascular diseases
  • Human disease related genes:Congenital disorders of metabolism:Mitochondrial diseases
  • Predicted intracellular proteins
  • Human disease related genes:Congenital disorders of metabolism:Congenital disorders of lipid/glycolipid metabolism
  • Human disease related genes:Endocrine and metabolic diseases:Other endocrine and metabolic diseases
  • Disease related genes
Transmembrane
789..810; Helical
Transmembrane Count
1
Entrez Gene Symbol
Gene Synonym
LDLCQ2
Gene Description
Low density lipoprotein receptor
Chromosome
19
Position
11089462-11133820
Frequency
3
EVMP Score
0.25
Fluorescence & Localization
Tissue SpecifickidneyCell SpecificAdipocytesSingle-Nuclei Brain SpecificCGE interneuronBlood Cell SpecificneutrophilBlood Lineage Specificgranulocytes
Function & Pathway
Protein Function
  • Human disease related genes:Cardiovascular diseases:Vascular diseases
  • Human disease related genes:Congenital disorders of metabolism:Mitochondrial diseases
  • Predicted intracellular proteins
  • Human disease related genes:Congenital disorders of metabolism:Congenital disorders of lipid/glycolipid metabolism
  • Human disease related genes:Endocrine and metabolic diseases:Other endocrine and metabolic diseases
  • Disease related genes
Canonical Pathways
M72 Pid nectin pathway
Mediation Categories
Adhesion and uptake mediationFusion and delivery mediationImmune mediationMetabolism mediation
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

50 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
cell_adhesioncell_adhesionOmniPathYesYesNoYesNo
matrix_adhesionmatrix_adhesionOmniPathNoYesNoYesNo
transmembranetransmembraneUniProt_locationNoNoNoYesNo
transmembranetransmembraneUniProt_topologyNoNoNoYesNo
transmembranetransmembraneUniProt_keywordNoNoNoYesNo
transmembrane_predictedtransmembraneOmniPathNoNoNoYesNo
transmembranetransmembraneTopDBNoNoNoYesNo
transmembranetransmembraneOmniPathNoNoNoYesNo
plasma_membraneplasma_membraneUniProt_locationNoNoNoYesNo
plasma_membraneplasma_membraneCellinkerNoNoNoYesNo
Page 3 of 5PreviousNext

Regulatory Interaction Network

2 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
APOBP04114LDLRP01130YesYesNoiTALKKEGG-MEDICUSICELLNETSIGNORLit-BM-17HPMR_talklrHPRD_LRdbtalklrHPRDRamilowski2015_Baccin2019WangRamilowski2015HPMR_LRdbReactome_LRdbHPRD_talklrBaccin2019CellinkerSTRING_talklrEMBRACEFantom5_LRdbCellTalkDBHPMR_CellinkerconnectomeDB2020LRdbSIGNOR:11986215HPRD:12031600Cellinker:12031600LRdb:12Cellinker:15840700CellTalkDB:11327878Lit-BM-17:24447298LRdb:11327878connectomeDB2020:12031600connectomeDB2020:11327878Baccin2019:1132787812031600Cellinker:11327878ICELLNET:24447298
MYLIPQ8WY64LDLRP01130YesNoYesHINTSIGNORBioGRIDHINT:32727844HINT:21734303BioGRID:23382078BioGRID:26666640SIGNOR:30896554HINT:21685362

Protein Complex Composition

17 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
AP-1 adaptor complexAFTPHAP1G2AP1S1LDLRAP1SLC18A3SYNRGO75843P61966Q16572Q5SW96Q6ULP2Q9UMZ21:1:1:1:1:1CompleatCompleat:HC15101245117297337681575802510477754
HT_DM_Cluster170FAM43AFAM43BLDLRAP1PSMD9PTGES3STATHO00233P02808Q15185Q5SW96Q6ZT52Q8N2R81:1:1:1:1:1CompleatCompleat:HC84422036573
LDLR-PCSK9 complexLDLRPCSK9P01130Q8NBP71:2ComplexPortalPDBPDB:3m0cPDB:2w2nPDB:2w2oPDB:2w2qPDB:3p5bPDB:3gcxPDB:2w2mPDB:3bpsPDB:3p5cintact:EBI-10796271PDB:3gcwPDB:2w2pPDB:4ne92208114124440079147552921745231618250299
SYT1SYT2SYT5VLDLRO00445P21579P98155Q8N9I00:0:0:0hu.MAP2
LDLRAD4LEMD3SMAD2SMAD3SMAD9ZFYVE9O15165O15198O95405P84022Q15796Q9Y2U80:0:0:0:0:0hu.MAP2
FLCNLDLRAD4SMURF2WWC2O15165Q6AWC2Q8NFG4Q9HAU40:0:0:0hu.MAP
FLCNHECW1LDLRAD4SMURF2O15165Q76N89Q8NFG4Q9HAU40:0:0:0hu.MAP
FLCNLDLRAD4RBCK1SMURF2O15165Q8NFG4Q9BYM8Q9HAU40:0:0:0hu.MAP
LDLRP011302PDBPDB:1ijq
APOHLDLRP01130P027491:1PDBPDB:2kri
Page 1 of 2Next

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Size Exclusion ChromatographyMass spectrometry131414377
Sequence, Structure & Domains

Sequences

Length
860
Mass
95,376
Sequence
MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA
Alternative Products
Event=Alternative splicing; Named isoforms=6; Name=1; IsoId=P01130-1; Sequence=Displayed; Name=2; IsoId=P01130-2; Sequence=VSP_043053, VSP_043054; Name=3; IsoId=P01130-3; Sequence=VSP_055014, VSP_055015; Name=4; IsoId=P01130-4; Sequence=VSP_043595; Name=5; IsoId=P01130-5; Sequence=VSP_045525; Name=6; IsoId=P01130-6; Sequence=VSP_047413
Alternative Sequence
35..155; Missing (in isoform 6); 64..105; LSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCP -> S (in isoform 4); 105..272; Missing (in isoform 3); 106..232; Missing (in isoform 2); 273; V -> L (in isoform 3); 663..713; Missing (in isoform 2); 850..851; Missing (in isoform 5)

3D Structural Models

Turn
42..46; 60..62; 138..142; 156..158; 189..191; 205..207; 244..246; 293..296; 310..312; 348..350; 387..389; 436..439; 446..449; 483..486; 493..496; 526..529; 570..573; 580..583; 602..605; 623..626; 633..635; 826..829
Helix
56..58; 85..87; 99..101; 124..126; 143..147; 163..165; 177..179; 181..183; 212..214; 226..228; 251..253; 265..267; 317..319; 321..324; 357..359; 657..659; 673..676
Beta Strand
29..33; 35..37; 39..41; 47..49; 51..55; 65..67; 70..72; 77..79; 90..93; 95..97; 102..104; 113..115; 121..123; 129..131; 148..151; 152..154; 160..162; 168..170; 173..176; 201..204; 208..211; 217..219; 222..224; 241..243; 247..249; 254..258; 260..264; 268..270; 281..283; 289..292; 306..308; 326..330; 333..335; 337..339; 341..343; 345..347; 351..353; 363..369; 372..374; 376..378; 381..385; 392..394; 400..404; 406..413; 420..423; 427..435; 440..445; 450..455; 466..469; 478..482; 487..492; 497..502; 505..513; 519..525; 530..535; 537..539; 541..546; 552..556; 563..569; 574..579; 584..589; 596..600; 606..614; 617..622; 627..632; 640..643; 652..656; 668..672; 678..683; 693..697; 708..713; 821..824
3D Structure
Electron microscopy (4); NMR spectroscopy (13); X-ray crystallography (19)

Domain & Motif Annotations

Compositional Bias
734..744; Polar residues
Repeat
397..438; LDL-receptor class B 1; 439..485; LDL-receptor class B 2; 486..528; LDL-receptor class B 3; 529..572; LDL-receptor class B 4; 573..615; LDL-receptor class B 5; 616..658; LDL-receptor class B 6
Motif
823..828; NPXY motif
Domain (CC)
The NPXY motif mediates the interaction with the clathrin adapter DAB2 and with LDLRAP1 which are involved in receptor internalization. A few residues outside the motif also play a role in the interaction.
Domain (FT)
25..65; LDL-receptor class A 1; 66..106; LDL-receptor class A 2; 107..145; LDL-receptor class A 3; 146..186; LDL-receptor class A 4; 195..233; LDL-receptor class A 5; 234..272; LDL-receptor class A 6; 274..313; LDL-receptor class A 7; 314..353; EGF-like 1; 354..393; EGF-like 2; calcium-binding; 663..712; EGF-like 3
Region
146..233; Binding to Getah virus E1-E2 spike glycoproteins; 721..768; Clustered O-linked oligosaccharides; 734..755; Disordered; 811..860; Required for MYLIP-triggered down-regulation of LDLR
Protein Families
LDLR family
Sequence Similarities
Belongs to the LDLR family.
Clinical Relevance