| IED ID | IndEnz0002007877 |
| Enzyme Type ID | protease007877 |
| Protein Name |
Low-density lipoprotein receptor LDL receptor |
| Gene Name | LDLR |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA |
| Enzyme Length | 860 |
| Uniprot Accession Number | P01130 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Binds 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. {ECO:0000269|PubMed:3005267, ECO:0000269|PubMed:6091915}.; FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus in hepatocytes, but not through a direct interaction with viral proteins. {ECO:0000269|PubMed:10535997, ECO:0000269|PubMed:12615904}.; FUNCTION: (Microbial infection) Acts as a receptor for Vesicular stomatitis virus. {ECO:0000269|PubMed:23589850}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, may function as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells. {ECO:0000269|PubMed:11100124}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (7); Beta strand (72); Chain (1); Compositional bias (1); Disulfide bond (30); Domain (10); Erroneous initiation (1); Glycosylation (5); Helix (17); Modified residue (1); Motif (1); Mutagenesis (10); Natural variant (195); Region (3); Repeat (6); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (22) |
| Keywords | 3D-structure;Alternative splicing;Cell membrane;Cholesterol metabolism;Coated pit;Direct protein sequencing;Disease variant;Disulfide bond;EGF-like domain;Endocytosis;Endosome;Glycoprotein;Golgi apparatus;Host cell receptor for virus entry;Host-virus interaction;LDL;Lipid metabolism;Lipid transport;Lysosome;Membrane;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Steroid metabolism;Sterol metabolism;Transmembrane;Transmembrane helix;Transport;Ubl conjugation |
| Interact With | P04114; P02649; P02749; Itself; P30533; Q9H2K0; Q8NBP7; Q8NBP7-1; Q08117-2; D3ZAR1; P0DTC2 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17461796, ECO:0000269|PubMed:19520913}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit {ECO:0000303|PubMed:6091915}. Golgi apparatus {ECO:0000269|PubMed:17461796}. Early endosome {ECO:0000269|PubMed:17461796}. Late endosome {ECO:0000269|PubMed:17461796}. Lysosome {ECO:0000269|PubMed:17461796}. Note=Rapidly endocytosed upon ligand binding. {ECO:0000269|PubMed:3104336}. |
| Modified Residue | MOD_RES 724; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P35952 |
| Post Translational Modification | PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:3005267}.; PTM: Ubiquitinated by MYLIP leading to degradation. {ECO:0000269|PubMed:19520913}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000250|UniProtKB:P01131 |
| Structure 3D | NMR spectroscopy (13); X-ray crystallography (19) |
| Cross Reference PDB | 1AJJ; 1D2J; 1F5Y; 1F8Z; 1HJ7; 1HZ8; 1I0U; 1IJQ; 1LDL; 1LDR; 1N7D; 1XFE; 2FCW; 2KRI; 2LGP; 2M7P; 2MG9; 2W2M; 2W2N; 2W2O; 2W2P; 2W2Q; 3BPS; 3GCW; 3GCX; 3M0C; 3P5B; 3P5C; 3SO6; 4NE9; 5OY9; 5OYL; |
| Mapped Pubmed ID | 10535736; 10542231; 10559861; 10559924; 10625686; 10699424; 10704205; 10766823; 10914685; 10981718; 11060341; 11082044; 11231140; 11239472; 11247302; 11317192; 11327878; 11373616; 11435110; 11470803; 11478865; 11517213; 11532990; 11577110; 11859771; 11860839; 11889126; 12057195; 12209363; 12234931; 12451172; 12464675; 12901493; 12944396; 12952949; 12975003; 1361731; 14622578; 14622579; 14624402; 15166224; 15252009; 15260957; 15318165; 15494314; 15502812; 15502813; 15649145; 15703209; 15728179; 15823280; 15895077; 16103228; 16179341; 16215232; 16257961; 16326391; 16410077; 16459141; 16516836; 16630895; 1673111; 1674215; 16770077; 16798879; 16837242; 16903783; 16927291; 17018281; 17158794; 17170699; 17452316; 17512409; 17517690; 17540576; 17609109; 17681954; 17765681; 17962812; 17978091; 18093523; 18193043; 18193044; 18250299; 18388313; 18660489; 18660751; 18790740; 18981233; 19001363; 19060906; 19060910; 19060911; 19092055; 19198609; 19224862; 19296720; 19336370; 19458185; 19536138; 19575674; 19603039; 1968060; 19696796; 1981179; 20033059; 20059951; 20223219; 20231386; 20428113; 20448150; 20826345; 20946875; 2115402; 21187331; 21278753; 21316588; 21445324; 21482805; 21613550; 21779028; 21841790; 21927000; 21927001; 21962517; 21988832; 22081141; 22091758; 22099461; 221835; 22190034; 22233676; 22505844; 22764087; 23297414; 23536704; 23823722; 23861397; 23891661; 23926099; 24186068; 24440079; 24447298; 24581490; 24789820; 24966051; 25107275; 25341920; 25613181; 25915661; 26042225; 26496610; 26526611; 2722848; 2901393; 29531262; 6146630; 7634533; 7820934; 7877694; 8096495; 8099307; 8100826; 8218110; 8300609; 8524399; 8552632; 8589690; 8773610; 8829662; 9003506; 9092476; 9100026; 9427626; 9428629; 9633944; 9635431; 9736607; |
| Motif | MOTIF 823..828; /note=NPXY motif; /evidence=ECO:0000269|PubMed:22509010 |
| Gene Encoded By | |
| Mass | 95,376 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |