| IED ID | IndEnz0002002956 |
| Enzyme Type ID | protease002956 |
| Protein Name |
Prolow-density lipoprotein receptor-related protein 1 LRP-1 Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit LRP-85 ; Low-density lipoprotein receptor-related protein 1 515 kDa subunit LRP-515 ; Low-density lipoprotein receptor-related protein 1 intracellular domain LRPICD |
| Gene Name | Lrp1 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MLTPPLLLLLPLLSALVAGATMDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCPPNEHSCLGTELCVPMSRLCNGIQDCMDGSDEGAHCRELRVNCSRMGCQHHCVPTPSGPTCYCNNSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFTCGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPSLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANTQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVAGAQPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDADGVTCLANPSYVPPPQCQPGEFACANNRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHSDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKGCEGVTHVCDPNVKFGCKDSARCISKAWVCDGDSDCEDNSDEENCEALACRPPSHPCANNTSVCLSPDKLCDGKDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGPDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTIHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGRGPCSHLCLINYNRTVSCACPHLMKLHNDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMVNMDGSNRTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSELEVIDTMRSQLGKATALAIMGDKLWWADQVSEKMGTCNKADGSGSVVLRNSTTLVMHMKVYDESIQLEHEGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGHYPRIERSRLDGTERVVLVNVSISWPNGISVDYQGGKLYWCDARMDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGCKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGGGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSGRTTIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNELHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKYVGSDMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQEDFTCRAMNSSCRAQDEFECANGECISFSLTCDGVSHCKDKSDEKPSYCNSRRCKKTFRQCNNGRCVSNMLWCNGVDDCGDGSDEIPCNKTACGVGEFRCRDGSCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCENGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCADGADESISAGCLYNSTCDDREFMCQNRLCIPKHFVCDHDRDCADGSDESPECEYPTCGPNEFRCANGRCLSSRQWECDGENDCHDHSDEAPKNPHCTSPEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDGSDERGCHVNECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADVDECSTTFPCSQLCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYRGQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSGRSIIVDTKITWPNGLTVDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGANKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGGDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECTRFQCPPNRPFRCKNDRVCLWIGRQCDGTDNCGDGTDEEDCEPPTAQNPHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASMCGDEARCVRTEKAAYCACRPGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQAFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAVDSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLINLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCTLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEYCHNGGTCAASPSGMPTCRCPTGFTGPRCTQQVCAGYCANNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGFCENFGTCQMAADGSRQCRCTVYFEGTRCEVNKCSRCLQGACVVNKQTGDVTCNCTDGRVAPSCLTCIDHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEQVVSQQQPGHMTSILIPLLLLLLLLLVAGVVFWYKRRVRGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA |
| Enzyme Length | 4545 |
| Uniprot Accession Number | G3V928 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells (By similarity). Required for early embryonic development (By similarity). Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. Acts as an LRPAP1 alpha-2-macroglobulin receptor. Acts as TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as its subsequent spread. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (By similarity). {ECO:0000250|UniProtKB:Q07954, ECO:0000250|UniProtKB:Q91ZX7}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (4); Disulfide bond (108); Domain (37); Glycosylation (49); Metal binding (18); Modified residue (6); Region (1); Repeat (44); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Acetylation;Calcium;Cell membrane;Coated pit;Cytoplasm;Cytoskeleton;Developmental protein;Disulfide bond;EGF-like domain;Endocytosis;Glycoprotein;Golgi apparatus;Membrane;Metal-binding;Nucleus;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein 1 85 kDa subunit]: Cell membrane {ECO:0000250|UniProtKB:Q07954}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q07954}. Membrane, coated pit {ECO:0000250|UniProtKB:Q07954}.; SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein 1 515 kDa subunit]: Cell membrane {ECO:0000250|UniProtKB:Q07954}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q07954}; Extracellular side {ECO:0000250|UniProtKB:Q07954}. Membrane, coated pit {ECO:0000250|UniProtKB:Q07954}.; SUBCELLULAR LOCATION: Golgi outpost {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:31522887}. Note=Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation. {ECO:0000269|PubMed:31522887}.; SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein 1 intracellular domain]: Cytoplasm {ECO:0000250|UniProtKB:Q07954}. Nucleus {ECO:0000250|UniProtKB:Q07954}. Note=After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus. {ECO:0000250|UniProtKB:Q07954}. |
| Modified Residue | MOD_RES 2010; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q91ZX7; MOD_RES 4461; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q07954; MOD_RES 4508; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:Q07954; MOD_RES 4518; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q07954; MOD_RES 4521; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q07954; MOD_RES 4524; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q91ZX7 |
| Post Translational Modification | PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515) that remains non-covalently associated. Gamma-secretase-dependent cleavage of LRP-85 releases the intracellular domain from the membrane. {ECO:0000250|UniProtKB:Q07954}.; PTM: Phosphorylated on serine and threonine residues. {ECO:0000250|UniProtKB:Q07954}.; PTM: Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1. {ECO:0000250|UniProtKB:Q07954}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10514495; 10778874; 11100124; 12153398; 14623925; 14701798; 15178744; 16190982; 16303771; 16979164; 17065459; 17314289; 18285446; 18321860; 19299462; 19864425; 20197276; 20488202; 20940000; 21040802; 21290408; 22454363; 22674573; 22889684; 23132925; 23867460; 24086544; 24865476; 26506094; 26598525; 26656067; 29115637; 8626514; 8930375; 9046007; |
| Motif | |
| Gene Encoded By | |
| Mass | 504,889 |
| Kinetics | |
| Metal Binding | METAL 872; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 875; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 877; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 879; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 885; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 886; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1033; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1036; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1038; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1040; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1046; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1047; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1081; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1084; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1086; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1088; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1094; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q07954; METAL 1095; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q07954 |
| Rhea ID | |
| Cross Reference Brenda |