P35950 · LDLR_CRIGR

Function

function

Binds low density lipoprotein /LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Forms a ternary complex with PGRMC1 and TMEM97 receptors which increases LDLR-mediated LDL internalization.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell surface
Cellular Componentclathrin-coated pit
Cellular Componentearly endosome
Cellular ComponentGolgi apparatus
Cellular Componentlate endosome
Cellular Componentlow-density lipoprotein particle
Cellular Componentlysosome
Cellular Componentplasma membrane
Molecular Functioncalcium ion binding
Biological Processcholesterol metabolic process
Biological Processendocytosis
Biological Processlipid transport

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Low-density lipoprotein receptor
  • Short names
    LDL receptor

Gene names

    • Name
      LDLR
    • Synonyms
      LDLA
    • ORF names
      I79_005860

Organism names

Accessions

  • Primary accession
    P35950
  • Secondary accessions
    • G3H6A6

Proteomes

Subcellular Location

Cell membrane
; Single-pass type I membrane protein
Golgi apparatus
Early endosome
Late endosome
Lysosome
Note: Rapidly endocytosed upon ligand binding.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain22-782Extracellular
Transmembrane783-804Helical
Topological domain805-862Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_000001731122-862Low-density lipoprotein receptor
Disulfide bond27↔39
Disulfide bond34↔52
Disulfide bond46↔63
Disulfide bond68↔82
Disulfide bond75↔95
Disulfide bond89↔104
Glycosylation97N-linked (GlcNAc...) asparagine
Disulfide bond109↔121
Disulfide bond116↔134
Disulfide bond128↔143
Disulfide bond148↔160
Disulfide bond155↔173
Disulfide bond167↔184
Disulfide bond198↔210
Disulfide bond205↔223
Disulfide bond217↔232
Disulfide bond237↔249
Disulfide bond244↔262
Disulfide bond256↔271
Glycosylation273N-linked (GlcNAc...) asparagine
Disulfide bond277↔290
Disulfide bond285↔303
Disulfide bond297↔314
Disulfide bond319↔330
Disulfide bond326↔339
Disulfide bond341↔353
Disulfide bond359↔369
Disulfide bond365↔378
Disulfide bond380↔393
Glycosylation657N-linked (GlcNAc...) asparagine
Disulfide bond667↔681
Disulfide bond677↔696
Disulfide bond698↔711
Modified residue724Phosphothreonine
Modified residue732Phosphothreonine

Post-translational modification

N- and O-glycosylated.
Ubiquitinated by MYLIP leading to degradation.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif (By similarity).
Interacts (via NPXY motif) with LDLRAP1 (via PID domain). Interacts with ARRB1. Interacts with SNX17. Interacts with the full-length immature form of PCSK9 (via C-terminus) (By similarity).
Interacts with PGRMC1 and TMEM97; the interaction increases LDL internalization (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, repeat, region, motif.

TypeIDPosition(s)Description
Domain25-65LDL-receptor class A 1
Domain66-106LDL-receptor class A 2
Domain107-145LDL-receptor class A 3
Domain146-186LDL-receptor class A 4
Domain196-234LDL-receptor class A 5
Domain235-273LDL-receptor class A 6
Domain275-314LDL-receptor class A 7
Domain315-354EGF-like 1
Domain355-394EGF-like 2; calcium-binding
Repeat398-439LDL-receptor class B 1
Repeat440-485LDL-receptor class B 2
Repeat486-528LDL-receptor class B 3
Repeat529-572LDL-receptor class B 4
Repeat573-615LDL-receptor class B 5
Repeat616-658LDL-receptor class B 6
Domain663-712EGF-like 3
Region721-765Clustered O-linked oligosaccharides
Region729-760Disordered
Region805-862Required for MYLIP-triggered down-regulation of LDLR
Motif817-822NPXY motif

Domain

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.

Sequence similarities

Belongs to the LDLR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    862
  • Mass (Da)
    95,236
  • Last updated
    2012-02-22 v2
  • Checksum
    7B0DD369C4E33402
MSTADLRLRWAIALLLAAAGAAAEDTCDRNEFRCRDGKCIASKWVCDGSPECPDGSDESSETCMSVTCQSKEFSCGGRVSRCIPNSWRCDGQTDCENGSDEQGCAPKTCSQDEFRCQDGKCISQKFVCDQDQDCVDGSDEAHCQAATCGPAHFRCNSSACIPSLWACDGDDDCEDGSDEWPQNCGGRDTAAAWSSSPCSSLEFHCGSSECIHRSWVCDGSADCKDKSDEEHCVTATCRPDEFQCADGTCIHGSRQCDREYDCKDMSDELGCINVTQCDGPNKFKCHSGECIALDKVCDSMRDCRDWSDEPIKDCRTNECLDNNGGCSHVCKDLKIGYECLCPNGFQLVDQHRCEDIDECQEPDTCDQLCVNLEGSYKCECRAGFHMDPHTRVCKAVGSVAYLLFTNRHEVRKMTLDRSEYTSLIPNLKNVVALDTEVANNRIYWSDLSQGKIYSALMDQAPTLSYDTIISGDLQAPDGLAVDWIHGNIYWTDSVPGSVSVADTKGIRRRTLFQEKGSRPRDIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTEDIQWPNGITLDIPSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKQLAHPFSLAIYEDKVFWTDVINEAIFSANRLTGSDVNLVAENLLSPEDIVLFHNITQPRGVNWCERTALPNGGCQYLCLPAPQINPHSPKFTCACPDGMLLAKDMRSCLTEVAPVLTTQGTSTIRPEITAGAEGLPKHKEDQSASSTSRQPALSTVESVTMSHQVQGDRRNEERPQGVGVLSITLPIALVILLVFGAILLWRNWRLRNINSINFDNPVYQKTTEDELHICRSQDGYSYPSVSMPFCGREEAASKLKDRS

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict158-159in Ref. 2; AAA51449
Sequence conflict710in Ref. 2; AAA51449
Sequence conflict738in Ref. 2; AAA51449

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JH000173
EMBL· GenBank· DDBJ
EGV96177.1
EMBL· GenBank· DDBJ
Genomic DNA
M94387
EMBL· GenBank· DDBJ
AAA51449.1
EMBL· GenBank· DDBJ
Genomic DNA
M13877
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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