P20063 · LDLR_RABIT
- ProteinLow-density lipoprotein receptor
- GeneLDLR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids837 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | clathrin-coated pit | |
Cellular Component | early endosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | late endosome | |
Cellular Component | low-density lipoprotein particle | |
Cellular Component | lysosome | |
Cellular Component | plasma membrane | |
Molecular Function | calcium ion binding | |
Molecular Function | lipoprotein particle binding | |
Molecular Function | low-density lipoprotein particle receptor activity | |
Biological Process | cholesterol homeostasis | |
Biological Process | cholesterol metabolic process | |
Biological Process | receptor-mediated endocytosis involved in cholesterol transport |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameLow-density lipoprotein receptor
- Short namesLDL receptor
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionP20063
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: Rapidly endocytosed upon ligand binding.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-765 | Extracellular | ||||
Sequence: LLAAAAGAAAGDKCGRNEFQCRNGKCISYKWVCDGSSECQDGSDEWEQTCMSLTCKSDDFSCGGRLNRCIPGHWKCDGQQDCEDGSDELGCAPKTCSQDEFRCAEGACISRLFACDGEPDCPDGSDEASCAPSTCGPAHFRCNSSSCVPALWACDGEPDCDDGSDEWPARCGARPSPQPGRGPCSRHEFHCGSGECVHASWRCDGDADCRDGSDERDCAAATCRPDEFQCSDGTCIHGSRQCDQQQDCGDMSDEVGCVNVTLCEGPDKFKCHSGECISLDKVCNSARDCQDWSDEPIKECATNECMRGNGGCSHTCFDLRIGHECHCPKGYRLVDQRRCEDINECEDPDICSQLCVNLAGSYKCECRAGFQLDPHSQACKAVDSIAYLFFTNRHEVRKMTLDRSEYTSLIANLKNVVALDAEVASNRIYWSDLSQRKIYSAQIDGAHGFPAYDTVISSDLQAPDGLAVDWIHGHIYWTDSVLGTVSVADTRGFRRKTLFRQEGSKPRAIVVDPAHGFMYWTDWGVPAKIEKGGLNGVDVYSLVTEDIQWPNGITLDLSSGRLYWVDSKLHSISSIDVNGGNRKTVLEDEQRLAHPFSLAIFEDKVFWTDVINEAIFSANRLTGSDVHLVAENLLSPEDIVLFHNLTQPRGVNWCEKTALPNGGCQYLCLPAPQINSHSPKFTCACPDGTLLAADMRSCRTEADVILSTQRASTAARPQLTGSPAGTTQEPLTEPTLSTLETATTSQQALHNADGRGSEGTPRSVG | ||||||
Transmembrane | 766-787 | Helical | ||||
Sequence: ALSVVLPIALLGLLCLGALVLW | ||||||
Topological domain | 788-837 | Cytoplasmic | ||||
Sequence: KNWRLRSVHSINFDNPVYQKTTEDEVHICRSQDGYTYPSRQMVSLEDDVA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000191077 | 1-837 | Low-density lipoprotein receptor | |||
Sequence: LLAAAAGAAAGDKCGRNEFQCRNGKCISYKWVCDGSSECQDGSDEWEQTCMSLTCKSDDFSCGGRLNRCIPGHWKCDGQQDCEDGSDELGCAPKTCSQDEFRCAEGACISRLFACDGEPDCPDGSDEASCAPSTCGPAHFRCNSSSCVPALWACDGEPDCDDGSDEWPARCGARPSPQPGRGPCSRHEFHCGSGECVHASWRCDGDADCRDGSDERDCAAATCRPDEFQCSDGTCIHGSRQCDQQQDCGDMSDEVGCVNVTLCEGPDKFKCHSGECISLDKVCNSARDCQDWSDEPIKECATNECMRGNGGCSHTCFDLRIGHECHCPKGYRLVDQRRCEDINECEDPDICSQLCVNLAGSYKCECRAGFQLDPHSQACKAVDSIAYLFFTNRHEVRKMTLDRSEYTSLIANLKNVVALDAEVASNRIYWSDLSQRKIYSAQIDGAHGFPAYDTVISSDLQAPDGLAVDWIHGHIYWTDSVLGTVSVADTRGFRRKTLFRQEGSKPRAIVVDPAHGFMYWTDWGVPAKIEKGGLNGVDVYSLVTEDIQWPNGITLDLSSGRLYWVDSKLHSISSIDVNGGNRKTVLEDEQRLAHPFSLAIFEDKVFWTDVINEAIFSANRLTGSDVHLVAENLLSPEDIVLFHNLTQPRGVNWCEKTALPNGGCQYLCLPAPQINSHSPKFTCACPDGTLLAADMRSCRTEADVILSTQRASTAARPQLTGSPAGTTQEPLTEPTLSTLETATTSQQALHNADGRGSEGTPRSVGALSVVLPIALLGLLCLGALVLWKNWRLRSVHSINFDNPVYQKTTEDEVHICRSQDGYTYPSRQMVSLEDDVA | ||||||
Disulfide bond | 14↔26 | |||||
Sequence: CGRNEFQCRNGKC | ||||||
Disulfide bond | 21↔39 | |||||
Sequence: CRNGKCISYKWVCDGSSEC | ||||||
Disulfide bond | 33↔50 | |||||
Sequence: CDGSSECQDGSDEWEQTC | ||||||
Disulfide bond | 55↔69 | |||||
Sequence: CKSDDFSCGGRLNRC | ||||||
Disulfide bond | 62↔82 | |||||
Sequence: CGGRLNRCIPGHWKCDGQQDC | ||||||
Disulfide bond | 76↔91 | |||||
Sequence: CDGQQDCEDGSDELGC | ||||||
Disulfide bond | 96↔108 | |||||
Sequence: CSQDEFRCAEGAC | ||||||
Disulfide bond | 103↔121 | |||||
Sequence: CAEGACISRLFACDGEPDC | ||||||
Disulfide bond | 115↔130 | |||||
Sequence: CDGEPDCPDGSDEASC | ||||||
Disulfide bond | 135↔147 | |||||
Sequence: CGPAHFRCNSSSC | ||||||
Disulfide bond | 142↔160 | |||||
Sequence: CNSSSCVPALWACDGEPDC | ||||||
Glycosylation | 143 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 154↔171 | |||||
Sequence: CDGEPDCDDGSDEWPARC | ||||||
Disulfide bond | 184↔196 | |||||
Sequence: CSRHEFHCGSGEC | ||||||
Disulfide bond | 191↔209 | |||||
Sequence: CGSGECVHASWRCDGDADC | ||||||
Disulfide bond | 203↔218 | |||||
Sequence: CDGDADCRDGSDERDC | ||||||
Disulfide bond | 223↔235 | |||||
Sequence: CRPDEFQCSDGTC | ||||||
Disulfide bond | 230↔248 | |||||
Sequence: CSDGTCIHGSRQCDQQQDC | ||||||
Disulfide bond | 242↔257 | |||||
Sequence: CDQQQDCGDMSDEVGC | ||||||
Glycosylation | 259 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 263↔276 | |||||
Sequence: CEGPDKFKCHSGEC | ||||||
Disulfide bond | 271↔289 | |||||
Sequence: CHSGECISLDKVCNSARDC | ||||||
Disulfide bond | 283↔300 | |||||
Sequence: CNSARDCQDWSDEPIKEC | ||||||
Disulfide bond | 305↔316 | |||||
Sequence: CMRGNGGCSHTC | ||||||
Disulfide bond | 312↔325 | |||||
Sequence: CSHTCFDLRIGHEC | ||||||
Disulfide bond | 327↔339 | |||||
Sequence: CPKGYRLVDQRRC | ||||||
Disulfide bond | 345↔355 | |||||
Sequence: CEDPDICSQLC | ||||||
Disulfide bond | 351↔364 | |||||
Sequence: CSQLCVNLAGSYKC | ||||||
Disulfide bond | 366↔379 | |||||
Sequence: CRAGFQLDPHSQAC | ||||||
Glycosylation | 644 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 654↔668 | |||||
Sequence: CEKTALPNGGCQYLC | ||||||
Disulfide bond | 664↔683 | |||||
Sequence: CQYLCLPAPQINSHSPKFTC | ||||||
Disulfide bond | 685↔698 | |||||
Sequence: CPDGTLLAADMRSC | ||||||
Modified residue | 720 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 722 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
N- and O-glycosylated.
Ubiquitinated by MYLIP leading to degradation.
Keywords
- PTM
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-52 | LDL-receptor class A 1 | ||||
Sequence: DKCGRNEFQCRNGKCISYKWVCDGSSECQDGSDEWEQTCMS | ||||||
Domain | 53-93 | LDL-receptor class A 2 | ||||
Sequence: LTCKSDDFSCGGRLNRCIPGHWKCDGQQDCEDGSDELGCAP | ||||||
Domain | 94-132 | LDL-receptor class A 3 | ||||
Sequence: KTCSQDEFRCAEGACISRLFACDGEPDCPDGSDEASCAP | ||||||
Domain | 133-173 | LDL-receptor class A 4 | ||||
Sequence: STCGPAHFRCNSSSCVPALWACDGEPDCDDGSDEWPARCGA | ||||||
Domain | 182-220 | LDL-receptor class A 5 | ||||
Sequence: GPCSRHEFHCGSGECVHASWRCDGDADCRDGSDERDCAA | ||||||
Domain | 221-259 | LDL-receptor class A 6 | ||||
Sequence: ATCRPDEFQCSDGTCIHGSRQCDQQQDCGDMSDEVGCVN | ||||||
Domain | 261-300 | LDL-receptor class A 7 | ||||
Sequence: TLCEGPDKFKCHSGECISLDKVCNSARDCQDWSDEPIKEC | ||||||
Domain | 301-340 | EGF-like 1 | ||||
Sequence: ATNECMRGNGGCSHTCFDLRIGHECHCPKGYRLVDQRRCE | ||||||
Domain | 341-380 | EGF-like 2; calcium-binding | ||||
Sequence: DINECEDPDICSQLCVNLAGSYKCECRAGFQLDPHSQACK | ||||||
Repeat | 384-425 | LDL-receptor class B 1 | ||||
Sequence: SIAYLFFTNRHEVRKMTLDRSEYTSLIANLKNVVALDAEVAS | ||||||
Repeat | 426-472 | LDL-receptor class B 2 | ||||
Sequence: NRIYWSDLSQRKIYSAQIDGAHGFPAYDTVISSDLQAPDGLAVDWIH | ||||||
Repeat | 473-515 | LDL-receptor class B 3 | ||||
Sequence: GHIYWTDSVLGTVSVADTRGFRRKTLFRQEGSKPRAIVVDPAH | ||||||
Repeat | 516-559 | LDL-receptor class B 4 | ||||
Sequence: GFMYWTDWGVPAKIEKGGLNGVDVYSLVTEDIQWPNGITLDLSS | ||||||
Repeat | 560-602 | LDL-receptor class B 5 | ||||
Sequence: GRLYWVDSKLHSISSIDVNGGNRKTVLEDEQRLAHPFSLAIFE | ||||||
Repeat | 603-645 | LDL-receptor class B 6 | ||||
Sequence: DKVFWTDVINEAIFSANRLTGSDVHLVAENLLSPEDIVLFHNL | ||||||
Domain | 650-699 | EGF-like 3 | ||||
Sequence: GVNWCEKTALPNGGCQYLCLPAPQINSHSPKFTCACPDGTLLAADMRSCR | ||||||
Region | 709-731 | Disordered | ||||
Sequence: QRASTAARPQLTGSPAGTTQEPL | ||||||
Region | 788-837 | Required for MYLIP-triggered down-regulation of LDLR | ||||
Sequence: KNWRLRSVHSINFDNPVYQKTTEDEVHICRSQDGYTYPSRQMVSLEDDVA | ||||||
Motif | 800-805 | NPXY motif | ||||
Sequence: FDNPVY |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length837
- Mass (Da)91,407
- Last updated1991-02-01 v1
- ChecksumED8D231E234400A9
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: L |
Keywords
- Technical term