IED Industry Enzyme Database

Detail Information for IndEnz0002004665
IED ID IndEnz0002004665
Enzyme Type ID protease004665
Protein Name Low-density lipoprotein receptor
LDL receptor
Gene Name Ldlr
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MSTADLMRRWVIALLLAAAGVAAEDSCSRNEFQCRDGKCIASKWVCDGSPECPDGSDESPETCMSVTCQSNQFSCGGRVSRCIPDSWRCDGQVDCENDSDEQGCPPKTCSQDDFRCQDGKCISPQFVCDGDRDCLDGSDEAHCQATTCGPAHFRCNSSICIPSLWACDGDVDCVDGSDEWPQNCQGRDTASKGVSSPCSSLEFHCGSSECIHRSWVCDGEADCKDKSDEEHCAVATCRPDEFQCADGSCIHGSRQCDREHDCKDMSDELGCVNVTQCDGPNKFKCHSGECISLDKVCDSARDCQDWSDEPIKECKTNECLDNNGGCSHICKDLKIGSECLCPSGFRLVDLHRCEDIDECQEPDTCSQLCVNLEGSYKCECQAGFHMDPHTRVCKAVGSIGYLLFTNRHEVRKMTLDRSEYTSLLPNLKNVVALDTEVTNNRIYWSDLSQKKIYSALMDQAPNLSYDTIISEDLHAPDGLAVDWIHRNIYWTDSVPGSVSVADTKGVKRRTLFQEAGSRPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIHSLVTENIQWPNGITLDLSSGRLYWVDSKLHSISSIDVNGGNRKTILEDENRLAHPFSLAIYEDKVYWTDVINEAIFSANRLTGSDVNLVAENLLSPEDIVLFHKVTQPRGVNWCETTALLPNGGCQYLCLPAPQIGPHSPKFTCACPDGMLLAKDMRSCLTEVDTVLTTQGTSAVRPVVTASATRPPKHSEDLSAPSTPRQPVDTPGLSTVASVTVSHQVQGDMAGRGNEEQPHGMRFLSIFFPIALVALLVLGAVLLWRNWRLKNINSINFDNPVYQKTTEDELHICRSQDGYTYPSRQMVSLEDDVA
Enzyme Length 862
Uniprot Accession Number P35951
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:0000250|UniProtKB:P01130}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (1); Disulfide bond (29); Domain (10); Glycosylation (3); Modified residue (3); Motif (1); Region (3); Repeat (6); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Cell membrane;Cholesterol metabolism;Coated pit;Disulfide bond;EGF-like domain;Endocytosis;Endosome;Glycoprotein;Golgi apparatus;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
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01130}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:11247302}. Golgi apparatus {ECO:0000250|UniProtKB:P01130}. Early endosome {ECO:0000250|UniProtKB:P01130}. Late endosome {ECO:0000250|UniProtKB:P01130}. Lysosome {ECO:0000250|UniProtKB:P01130}. Note=Rapidly endocytosed upon ligand binding. {ECO:0000269|PubMed:12169628}.
Modified Residue MOD_RES 725; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P35952; MOD_RES 733; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P35952; MOD_RES 735; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35952
Post Translational Modification PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P01130}.; PTM: Ubiquitinated by MYLIP leading to degradation. {ECO:0000250|UniProtKB:P01130}.
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000250|UniProtKB:P01131
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10024503; 10049716; 10094927; 10195942; 10224158; 10323773; 10359814; 10380922; 10383427; 10395289; 10428071; 10428823; 10441168; 10446074; 10488949; 10511293; 10516643; 10518564; 10521476; 10529267; 10559025; 10575007; 10591674; 10640811; 10681404; 10683382; 10712395; 10712397; 10712412; 10712437; 10727439; 10737683; 10760479; 10760605; 10764675; 10765504; 10777503; 10811610; 10827173; 10858435; 10861012; 10866061; 10878506; 10884286; 10884299; 10891640; 10946016; 10953027; 10974047; 10978255; 11024044; 11060341; 11076954; 11090066; 11092755; 11093949; 11108739; 11120757; 11138930; 11160132; 11161810; 11181749; 11207293; 11208732; 11248083; 11248122; 11249874; 11344083; 11369802; 11375415; 11387232; 11390420; 11394880; 11397709; 11433351; 11438740; 11445560; 11451755; 11457878; 11457895; 11483626; 11483628; 11493760; 11502098; 11520791; 11530237; 11546779; 11581143; 11590219; 11592107; 11597927; 11602498; 11606787; 11687507; 11719520; 11739102; 11747355; 11786527; 11884290; 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8349823; 8464923; 8550828; 8617867; 8631787; 8636110; 8654360; 8656070; 8662221; 8662771; 8672141; 8692976; 8696940; 8798151; 8798405; 8827514; 8940032; 8941642; 8969230; 8994037; 9109446; 9160753; 9162757; 9199434; 9242189; 9244438; 9326295; 9344654; 9409199; 9409260; 9417056; 9435307; 9449704; 9466986; 9539774; 9545490; 9598833; 9614153; 9616220; 9643345; 9651338; 9664080; 9701246; 9726247; 9734366; 9756870; 9788969; 9804809;
Motif MOTIF 825..830; /note=NPXY motif; /evidence=ECO:0000250|UniProtKB:P01130
Gene Encoded By
Mass 94,947
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda