P20063 · LDLR_RABIT

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
Molecular Functionlipoprotein particle binding
Molecular Functionlow-density lipoprotein particle receptor activity
Biological Processcholesterol homeostasis
Biological Processcholesterol metabolic process
Biological Processreceptor-mediated endocytosis involved in cholesterol transport

Keywords

Names & Taxonomy

Protein names

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

Gene names

    • Name
      LDLR

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus

Accessions

  • Primary accession
    P20063

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 domain1-765Extracellular
Transmembrane766-787Helical
Topological domain788-837Cytoplasmic

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
ChainPRO_00001910771-837Low-density lipoprotein receptor
Disulfide bond14↔26
Disulfide bond21↔39
Disulfide bond33↔50
Disulfide bond55↔69
Disulfide bond62↔82
Disulfide bond76↔91
Disulfide bond96↔108
Disulfide bond103↔121
Disulfide bond115↔130
Disulfide bond135↔147
Disulfide bond142↔160
Glycosylation143N-linked (GlcNAc...) asparagine
Disulfide bond154↔171
Disulfide bond184↔196
Disulfide bond191↔209
Disulfide bond203↔218
Disulfide bond223↔235
Disulfide bond230↔248
Disulfide bond242↔257
Glycosylation259N-linked (GlcNAc...) asparagine
Disulfide bond263↔276
Disulfide bond271↔289
Disulfide bond283↔300
Disulfide bond305↔316
Disulfide bond312↔325
Disulfide bond327↔339
Disulfide bond345↔355
Disulfide bond351↔364
Disulfide bond366↔379
Glycosylation644N-linked (GlcNAc...) asparagine
Disulfide bond654↔668
Disulfide bond664↔683
Disulfide bond685↔698
Modified residue720Phosphothreonine
Modified residue722Phosphoserine

Post-translational modification

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

Keywords

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
Domain12-52LDL-receptor class A 1
Domain53-93LDL-receptor class A 2
Domain94-132LDL-receptor class A 3
Domain133-173LDL-receptor class A 4
Domain182-220LDL-receptor class A 5
Domain221-259LDL-receptor class A 6
Domain261-300LDL-receptor class A 7
Domain301-340EGF-like 1
Domain341-380EGF-like 2; calcium-binding
Repeat384-425LDL-receptor class B 1
Repeat426-472LDL-receptor class B 2
Repeat473-515LDL-receptor class B 3
Repeat516-559LDL-receptor class B 4
Repeat560-602LDL-receptor class B 5
Repeat603-645LDL-receptor class B 6
Domain650-699EGF-like 3
Region709-731Disordered
Region788-837Required for MYLIP-triggered down-regulation of LDLR
Motif800-805NPXY 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
    Fragment
  • Length
    837
  • Mass (Da)
    91,407
  • Last updated
    1991-02-01 v1
  • Checksum
    ED8D231E234400A9
LLAAAAGAAAGDKCGRNEFQCRNGKCISYKWVCDGSSECQDGSDEWEQTCMSLTCKSDDFSCGGRLNRCIPGHWKCDGQQDCEDGSDELGCAPKTCSQDEFRCAEGACISRLFACDGEPDCPDGSDEASCAPSTCGPAHFRCNSSSCVPALWACDGEPDCDDGSDEWPARCGARPSPQPGRGPCSRHEFHCGSGECVHASWRCDGDADCRDGSDERDCAAATCRPDEFQCSDGTCIHGSRQCDQQQDCGDMSDEVGCVNVTLCEGPDKFKCHSGECISLDKVCNSARDCQDWSDEPIKECATNECMRGNGGCSHTCFDLRIGHECHCPKGYRLVDQRRCEDINECEDPDICSQLCVNLAGSYKCECRAGFQLDPHSQACKAVDSIAYLFFTNRHEVRKMTLDRSEYTSLIANLKNVVALDAEVASNRIYWSDLSQRKIYSAQIDGAHGFPAYDTVISSDLQAPDGLAVDWIHGHIYWTDSVLGTVSVADTRGFRRKTLFRQEGSKPRAIVVDPAHGFMYWTDWGVPAKIEKGGLNGVDVYSLVTEDIQWPNGITLDLSSGRLYWVDSKLHSISSIDVNGGNRKTVLEDEQRLAHPFSLAIFEDKVFWTDVINEAIFSANRLTGSDVHLVAENLLSPEDIVLFHNLTQPRGVNWCEKTALPNGGCQYLCLPAPQINSHSPKFTCACPDGTLLAADMRSCRTEADVILSTQRASTAARPQLTGSPAGTTQEPLTEPTLSTLETATTSQQALHNADGRGSEGTPRSVGALSVVLPIALLGLLCLGALVLWKNWRLRSVHSINFDNPVYQKTTEDEVHICRSQDGYTYPSRQMVSLEDDVA

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M11501
EMBL· GenBank· DDBJ
AAA31383.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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