Q91ZX7 · LRP1_MOUSE
- ProteinProlow-density lipoprotein receptor-related protein 1
- GeneLrp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids4545 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development (PubMed:1423604).
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 alpha-2-macroglobulin receptor (By similarity).
Acts as a TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as its subsequent spread (PubMed:32296178).
May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (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 alpha-2-macroglobulin receptor (By similarity).
Acts as a TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as its subsequent spread (PubMed:32296178).
May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (By similarity).
(Microbial infection) Functions as a receptor for Vibrio cholerae cholix toxin and for Pseudomonas aeruginosa exotoxin A.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 872 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 875 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 877 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 879 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 885 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 886 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1033 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 1036 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1038 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1040 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1046 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1047 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1081 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 1084 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1086 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1088 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1094 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1095 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E |
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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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProlow-density lipoprotein receptor-related protein 1
- Short namesLRP-1
- Alternative names
- Cleaved into 3 chains
- CD Antigen Name
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ91ZX7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation.
Low-density lipoprotein receptor-related protein 1 85 kDa subunit
Cell membrane ; Single-pass type I membrane protein
Low-density lipoprotein receptor-related protein 1 515 kDa subunit
Cell membrane ; Peripheral membrane protein
Low-density lipoprotein receptor-related protein 1 intracellular domain
Note: After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-4424 | Extracellular | ||||
Sequence: ATMDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCPPNEHSCLGTELCVPMSRLCNGIQDCMDGSDEGAHCRELRANCSRMGCQHHCVPTPSGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFTCGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANTQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVAGAPPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDTDGVTCLANPSYVPPPQCQPGEFACANNRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHSDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKSCEGVTHVCDPNVKFGCKDSARCISKAWVCDGDSDCEDNSDEENCEALACRPPSHPCANNTSVCLPPDKLCDGKDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGSDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTIHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGRGPCSHLCLINYNRTVSCACPHLMKLHKDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMANMDGSNHTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSELEVIDTMRSQLGKATALAIMGDKLWWADQVSEKMGTCNKADGSGSVVLRNSTTLVMHMKVYDESIQLEHEGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGHYPRIERSRLDGTERVVLVNVSISWPNGISVDYQGGKLYWCDARMDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGCKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGGGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSGRTTIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNELHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKYVGSDMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQEDFTCRAVNSSCRAQDEFECANGECISFSLTCDGVSHCKDKSDEKPSYCNSRRCKKTFRQCNNGRCVSNMLWCNGVDDCGDGSDEIPCNKTACGVGEFRCRDGSCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCENGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCTDGADESVTAGCLYNSTCDDREFMCQNRLCIPKHFVCDHDRDCADGSDESPECEYPTCGPNEFRCANGRCLSSRQWECDGENDCHDHSDEAPKNPHCTSPEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDGSDERGCHVNECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADLDECSTTFPCSQLCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSGRSIIVDTKITWPNGLTVDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGANKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGGDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFICPPNRPFRCKNDRVCLWIGRQCDGVDNCGDGTDEEDCEPPTAQNPHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASMCGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQTFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLINLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCTLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEYCHNGGTCAASPSGMPTCRCPTGFTGPKCTAQVCAGYCSNNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGFCENFGTCQMAADGSRQCRCTVYFEGPRCEVNKCSRCLQGACVVNKQTGDVTCNCTDGRVAPSCLTCIDHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEQVVSQQQPGHMAS | ||||||
Transmembrane | 4425-4445 | Helical | ||||
Sequence: ILIPLLLLLLLLLVAGVVFWY | ||||||
Topological domain | 4446-4545 | Cytoplasmic | ||||
Sequence: KRRVRGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Homozygous knockout is embryonic lethal, most probably occurring around the implantation stage (PubMed:1423604, PubMed:36067312).
Heterozygous mice do not show any overt phenotype (PubMed:1423604, PubMed:36067312).
However, they exhibit a reduction of the acetabular volumes, leading to defective coverage of the femoral heads (PubMed:36067312).
Heterozygous mice do not show any overt phenotype (PubMed:1423604, PubMed:36067312).
However, they exhibit a reduction of the acetabular volumes, leading to defective coverage of the femoral heads (PubMed:36067312).
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MLTPPLLLLLPLLSALVSG | ||||||
Chain | PRO_0000302753 | 20-?3944 | Low-density lipoprotein receptor-related protein 1 515 kDa subunit | |||
Sequence: ATMDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCPPNEHSCLGTELCVPMSRLCNGIQDCMDGSDEGAHCRELRANCSRMGCQHHCVPTPSGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFTCGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANTQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVAGAPPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDTDGVTCLANPSYVPPPQCQPGEFACANNRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHSDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKSCEGVTHVCDPNVKFGCKDSARCISKAWVCDGDSDCEDNSDEENCEALACRPPSHPCANNTSVCLPPDKLCDGKDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGSDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTIHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGRGPCSHLCLINYNRTVSCACPHLMKLHKDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMANMDGSNHTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSELEVIDTMRSQLGKATALAIMGDKLWWADQVSEKMGTCNKADGSGSVVLRNSTTLVMHMKVYDESIQLEHEGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGHYPRIERSRLDGTERVVLVNVSISWPNGISVDYQGGKLYWCDARMDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGCKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGGGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSGRTTIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNELHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKYVGSDMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQEDFTCRAVNSSCRAQDEFECANGECISFSLTCDGVSHCKDKSDEKPSYCNSRRCKKTFRQCNNGRCVSNMLWCNGVDDCGDGSDEIPCNKTACGVGEFRCRDGSCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCENGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCTDGADESVTAGCLYNSTCDDREFMCQNRLCIPKHFVCDHDRDCADGSDESPECEYPTCGPNEFRCANGRCLSSRQWECDGENDCHDHSDEAPKNPHCTSPEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDGSDERGCHVNECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADLDECSTTFPCSQLCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSGRSIIVDTKITWPNGLTVDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGANKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGGDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFICPPNRPFRCKNDRVCLWIGRQCDGVDNCGDGTDEEDCEPPTAQNPHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASMCGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQTFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRR | ||||||
Chain | PRO_0000273273 | 20-4545 | Prolow-density lipoprotein receptor-related protein 1 | |||
Sequence: ATMDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCPPNEHSCLGTELCVPMSRLCNGIQDCMDGSDEGAHCRELRANCSRMGCQHHCVPTPSGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFTCGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANTQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVAGAPPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDTDGVTCLANPSYVPPPQCQPGEFACANNRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHSDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKSCEGVTHVCDPNVKFGCKDSARCISKAWVCDGDSDCEDNSDEENCEALACRPPSHPCANNTSVCLPPDKLCDGKDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGSDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTIHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGRGPCSHLCLINYNRTVSCACPHLMKLHKDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMANMDGSNHTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSELEVIDTMRSQLGKATALAIMGDKLWWADQVSEKMGTCNKADGSGSVVLRNSTTLVMHMKVYDESIQLEHEGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGHYPRIERSRLDGTERVVLVNVSISWPNGISVDYQGGKLYWCDARMDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGCKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGGGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSGRTTIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNELHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKYVGSDMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQEDFTCRAVNSSCRAQDEFECANGECISFSLTCDGVSHCKDKSDEKPSYCNSRRCKKTFRQCNNGRCVSNMLWCNGVDDCGDGSDEIPCNKTACGVGEFRCRDGSCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCENGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCTDGADESVTAGCLYNSTCDDREFMCQNRLCIPKHFVCDHDRDCADGSDESPECEYPTCGPNEFRCANGRCLSSRQWECDGENDCHDHSDEAPKNPHCTSPEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDGSDERGCHVNECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADLDECSTTFPCSQLCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSGRSIIVDTKITWPNGLTVDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGANKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGGDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFICPPNRPFRCKNDRVCLWIGRQCDGVDNCGDGTDEEDCEPPTAQNPHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASMCGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQTFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLINLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCTLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEYCHNGGTCAASPSGMPTCRCPTGFTGPKCTAQVCAGYCSNNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGFCENFGTCQMAADGSRQCRCTVYFEGPRCEVNKCSRCLQGACVVNKQTGDVTCNCTDGRVAPSCLTCIDHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEQVVSQQQPGHMASILIPLLLLLLLLLVAGVVFWYKRRVRGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA | ||||||
Disulfide bond | 28↔41 | |||||
Sequence: CSPKQFACRDQITC | ||||||
Disulfide bond | 35↔54 | |||||
Sequence: CRDQITCISKGWRCDGERDC | ||||||
Disulfide bond | 48↔65 | |||||
Sequence: CDGERDCPDGSDEAPEIC | ||||||
Disulfide bond | 73↔86 | |||||
Sequence: CPPNEHSCLGTELC | ||||||
Disulfide bond | 80↔99 | |||||
Sequence: CLGTELCVPMSRLCNGIQDC | ||||||
Disulfide bond | 93↔109 | |||||
Sequence: CNGIQDCMDGSDEGAHC | ||||||
Glycosylation | 115 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 116↔125 | |||||
Sequence: CSRMGCQHHC | ||||||
Disulfide bond | 121↔134 | |||||
Sequence: CQHHCVPTPSGPTC | ||||||
Disulfide bond | 136↔149 | |||||
Sequence: CNSSFQLQADGKTC | ||||||
Glycosylation | 137 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 155↔165 | |||||
Sequence: CSVYGTCSQLC | ||||||
Disulfide bond | 161↔174 | |||||
Sequence: CSQLCTNTDGSFTC | ||||||
Disulfide bond | 176↔189 | |||||
Sequence: CVEGYLLQPDNRSC | ||||||
Glycosylation | 186 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 240 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 275 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 358 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 447 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 479↔494 | |||||
Sequence: CENDQYGKPGGCSDIC | ||||||
Disulfide bond | 490↔505 | |||||
Sequence: CSDICLLANSHKARTC | ||||||
Disulfide bond | 507↔520 | |||||
Sequence: CRSGFSLGSDGKSC | ||||||
Glycosylation | 730 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 808↔819 | |||||
Sequence: CRVNNGGCSSLC | ||||||
Disulfide bond | 815↔828 | |||||
Sequence: CSSLCLATPGSRQC | ||||||
Disulfide bond | 830↔843 | |||||
Sequence: CAEDQVLDTDGVTC | ||||||
Disulfide bond | 855↔867 | |||||
Sequence: CQPGEFACANNRC | ||||||
Disulfide bond | 862↔880 | |||||
Sequence: CANNRCIQERWKCDGDNDC | ||||||
Disulfide bond | 874↔891 | |||||
Sequence: CDGDNDCLDNSDEAPALC | ||||||
Disulfide bond | 896↔908 | |||||
Sequence: CPSDRFKCENNRC | ||||||
Disulfide bond | 903↔921 | |||||
Sequence: CENNRCIPNRWLCDGDNDC | ||||||
Disulfide bond | 915↔932 | |||||
Sequence: CDGDNDCGNSEDESNATC | ||||||
Glycosylation | 929 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 937↔949 | |||||
Sequence: CPPNQFSCASGRC | ||||||
Disulfide bond | 944↔962 | |||||
Sequence: CASGRCIPISWTCDLDDDC | ||||||
Disulfide bond | 956↔972 | |||||
Sequence: CDLDDDCGDRSDESASC | ||||||
Disulfide bond | 977↔990 | |||||
Sequence: CFPLTQFTCNNGRC | ||||||
Disulfide bond | 985↔1003 | |||||
Sequence: CNNGRCININWRCDNDNDC | ||||||
Disulfide bond | 997↔1012 | |||||
Sequence: CDNDNDCGDNSDEAGC | ||||||
Disulfide bond | 1016↔1028 | |||||
Sequence: CSSTQFKCNSGRC | ||||||
Disulfide bond | 1023↔1041 | |||||
Sequence: CNSGRCIPEHWTCDGDNDC | ||||||
Disulfide bond | 1035↔1052 | |||||
Sequence: CDGDNDCGDYSDETHANC | ||||||
Glycosylation | 1051 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1063↔1076 | |||||
Sequence: CHSDEFQCRLDGLC | ||||||
Disulfide bond | 1070↔1089 | |||||
Sequence: CRLDGLCIPLRWRCDGDTDC | ||||||
Disulfide bond | 1083↔1098 | |||||
Sequence: CDGDTDCMDSSDEKSC | ||||||
Disulfide bond | 1105↔1119 | |||||
Sequence: CDPNVKFGCKDSARC | ||||||
Disulfide bond | 1113↔1132 | |||||
Sequence: CKDSARCISKAWVCDGDSDC | ||||||
Disulfide bond | 1126↔1141 | |||||
Sequence: CDGDSDCEDNSDEENC | ||||||
Disulfide bond | 1146↔1160 | |||||
Sequence: CRPPSHPCANNTSVC | ||||||
Disulfide bond | 1153↔1173 | |||||
Sequence: CANNTSVCLPPDKLCDGKDDC | ||||||
Glycosylation | 1155 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1156 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1167↔1183 | |||||
Sequence: CDGKDDCGDGSDEGELC | ||||||
Disulfide bond | 1186↔1197 | |||||
Sequence: CSLNNGGCSHNC | ||||||
Disulfide bond | 1193↔1207 | |||||
Sequence: CSHNCSVAPGEGIVC | ||||||
Glycosylation | 1196 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1209↔1222 | |||||
Sequence: CPLGMELGSDNHTC | ||||||
Glycosylation | 1219 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1228↔1238 | |||||
Sequence: CAKHLKCSQKC | ||||||
Disulfide bond | 1234↔1247 | |||||
Sequence: CSQKCDQNKFSVKC | ||||||
Disulfide bond | 1249↔1262 | |||||
Sequence: CYEGWVLEPDGESC | ||||||
Glycosylation | 1512 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1541↔1554 | |||||
Sequence: CEANGGRGPCSHLC | ||||||
Disulfide bond | 1550↔1564 | |||||
Sequence: CSHLCLINYNRTVSC | ||||||
Glycosylation | 1559 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1566↔1579 | |||||
Sequence: CPHLMKLHKDNTTC | ||||||
Glycosylation | 1576 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1617 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1646 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1724 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1734 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1764 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1826 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1851↔1862 | |||||
Sequence: CSVNNGDCSQLC | ||||||
Disulfide bond | 1858↔1872 | |||||
Sequence: CSQLCLPTSETTRSC | ||||||
Disulfide bond | 1874↔1887 | |||||
Sequence: CTAGYSLRSGQQAC | ||||||
Glycosylation | 1934 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1996 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 2010 | N6-acetyllysine | ||||
Sequence: K | ||||||
Glycosylation | 2049 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2118 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2128 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2160↔2171 | |||||
Sequence: CAVANGGCQQLC | ||||||
Disulfide bond | 2167↔2181 | |||||
Sequence: CQQLCLYRGGGQRAC | ||||||
Disulfide bond | 2183↔2195 | |||||
Sequence: CAHGMLAEDGASC | ||||||
Glycosylation | 2473 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2483↔2494 | |||||
Sequence: CRINNGGCQDLC | ||||||
Disulfide bond | 2490↔2504 | |||||
Sequence: CQDLCLLTHQGHVNC | ||||||
Glycosylation | 2503 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2506↔2518 | |||||
Sequence: CRGGRILQEDFTC | ||||||
Glycosylation | 2522 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2525↔2538 | |||||
Sequence: CRAQDEFECANGEC | ||||||
Disulfide bond | 2533↔2551 | |||||
Sequence: CANGECISFSLTCDGVSHC | ||||||
Disulfide bond | 2545↔2562 | |||||
Sequence: CDGVSHCKDKSDEKPSYC | ||||||
Disulfide bond | 2567↔2579 | |||||
Sequence: CKKTFRQCNNGRC | ||||||
Disulfide bond | 2574↔2592 | |||||
Sequence: CNNGRCVSNMLWCNGVDDC | ||||||
Disulfide bond | 2586↔2601 | |||||
Sequence: CNGVDDCGDGSDEIPC | ||||||
Glycosylation | 2602 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2606↔2618 | |||||
Sequence: CGVGEFRCRDGSC | ||||||
Disulfide bond | 2613↔2631 | |||||
Sequence: CRDGSCIGNSSRCNQFVDC | ||||||
Glycosylation | 2621 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2625↔2640 | |||||
Sequence: CNQFVDCEDASDEMNC | ||||||
Glycosylation | 2639 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2645↔2667 | |||||
Sequence: CSSYFRLGVKGVLFQPCERTSLC | ||||||
Disulfide bond | 2661↔2680 | |||||
Sequence: CERTSLCYAPSWVCDGANDC | ||||||
Disulfide bond | 2674↔2689 | |||||
Sequence: CDGANDCGDYSDERDC | ||||||
Disulfide bond | 2697↔2709 | |||||
Sequence: CPLNYFACPSGRC | ||||||
Disulfide bond | 2704↔2722 | |||||
Sequence: CPSGRCIPMSWTCDKEDDC | ||||||
Disulfide bond | 2716↔2731 | |||||
Sequence: CDKEDDCENGEDETHC | ||||||
Disulfide bond | 2735↔2747 | |||||
Sequence: CSEAQFECQNHRC | ||||||
Disulfide bond | 2742↔2760 | |||||
Sequence: CQNHRCISKQWLCDGSDDC | ||||||
Disulfide bond | 2754↔2770 | |||||
Sequence: CDGSDDCGDGSDEAAHC | ||||||
Disulfide bond | 2775↔2788 | |||||
Sequence: CGPSSFSCPGTHVC | ||||||
Disulfide bond | 2782↔2801 | |||||
Sequence: CPGTHVCVPERWLCDGDKDC | ||||||
Disulfide bond | 2795↔2813 | |||||
Sequence: CDGDKDCTDGADESVTAGC | ||||||
Glycosylation | 2816 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2819↔2831 | |||||
Sequence: CDDREFMCQNRLC | ||||||
Disulfide bond | 2826↔2844 | |||||
Sequence: CQNRLCIPKHFVCDHDRDC | ||||||
Disulfide bond | 2838↔2854 | |||||
Sequence: CDHDRDCADGSDESPEC | ||||||
Disulfide bond | 2859↔2871 | |||||
Sequence: CGPNEFRCANGRC | ||||||
Disulfide bond | 2866↔2885 | |||||
Sequence: CANGRCLSSRQWECDGENDC | ||||||
Disulfide bond | 2879↔2898 | |||||
Sequence: CDGENDCHDHSDEAPKNPHC | ||||||
Disulfide bond | 2905↔2918 | |||||
Sequence: CNASSQFLCSSGRC | ||||||
Glycosylation | 2906 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2913↔2931 | |||||
Sequence: CSSGRCVAEALLCNGQDDC | ||||||
Disulfide bond | 2925↔2940 | |||||
Sequence: CNGQDDCGDGSDERGC | ||||||
Disulfide bond | 2945↔2957 | |||||
Sequence: CLSRKLSGCSQDC | ||||||
Disulfide bond | 2953↔2966 | |||||
Sequence: CSQDCEDLKIGFKC | ||||||
Disulfide bond | 2968↔2981 | |||||
Sequence: CRPGFRLKDDGRTC | ||||||
Disulfide bond | 2987↔2997 | |||||
Sequence: CSTTFPCSQLC | ||||||
Disulfide bond | 2993↔3006 | |||||
Sequence: CSQLCINTHGSYKC | ||||||
Disulfide bond | 3008↔3022 | |||||
Sequence: CVEGYAPRGGDPHSC | ||||||
Glycosylation | 3049 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3090 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3265 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3295↔3306 | |||||
Sequence: CKVNNGGCSNLC | ||||||
Disulfide bond | 3302↔3316 | |||||
Sequence: CSNLCLLSPGGGHKC | ||||||
Disulfide bond | 3318↔3331 | |||||
Sequence: CPTNFYLGGDGRTC | ||||||
Glycosylation | 3334 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3335↔3347 | |||||
Sequence: CTASQFVCKNDKC | ||||||
Disulfide bond | 3342↔3360 | |||||
Sequence: CKNDKCIPFWWKCDTEDDC | ||||||
Disulfide bond | 3354↔3370 | |||||
Sequence: CDTEDDCGDHSDEPPDC | ||||||
Disulfide bond | 3375↔3387 | |||||
Sequence: CRPGQFQCSTGIC | ||||||
Disulfide bond | 3382↔3400 | |||||
Sequence: CSTGICTNPAFICDGDNDC | ||||||
Disulfide bond | 3394↔3409 | |||||
Sequence: CDGDNDCQDNSDEANC | ||||||
Disulfide bond | 3414↔3427 | |||||
Sequence: CLPSQFKCTNTNRC | ||||||
Disulfide bond | 3421↔3440 | |||||
Sequence: CTNTNRCIPGIFRCNGQDNC | ||||||
Disulfide bond | 3434↔3449 | |||||
Sequence: CNGQDNCGDGEDERDC | ||||||
Disulfide bond | 3454↔3467 | |||||
Sequence: CAPNQFQCSITKRC | ||||||
Disulfide bond | 3461↔3480 | |||||
Sequence: CSITKRCIPRVWVCDRDNDC | ||||||
Disulfide bond | 3474↔3490 | |||||
Sequence: CDRDNDCVDGSDEPANC | ||||||
Glycosylation | 3489 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3495↔3508 | |||||
Sequence: CGVDEFRCKDSGRC | ||||||
Disulfide bond | 3502↔3521 | |||||
Sequence: CKDSGRCIPARWKCDGEDDC | ||||||
Disulfide bond | 3515↔3532 | |||||
Sequence: CDGEDDCGDGSDEPKEEC | ||||||
Disulfide bond | 3537↔3549 | |||||
Sequence: CEPYQFRCKNNRC | ||||||
Disulfide bond | 3544↔3562 | |||||
Sequence: CKNNRCVPGRWQCDYDNDC | ||||||
Disulfide bond | 3556↔3571 | |||||
Sequence: CDYDNDCGDNSDEESC | ||||||
Disulfide bond | 3576↔3588 | |||||
Sequence: CSESEFSCANGRC | ||||||
Disulfide bond | 3583↔3601 | |||||
Sequence: CANGRCIAGRWKCDGDHDC | ||||||
Disulfide bond | 3595↔3610 | |||||
Sequence: CDGDHDCADGSDEKDC | ||||||
Disulfide bond | 3614↔3626 | |||||
Sequence: CDMDQFQCKSGHC | ||||||
Disulfide bond | 3621↔3639 | |||||
Sequence: CKSGHCIPLRWRCDADADC | ||||||
Disulfide bond | 3633↔3648 | |||||
Sequence: CDADADCMDGSDEEAC | ||||||
Disulfide bond | 3655↔3667 | |||||
Sequence: CPLDEFQCNNTLC | ||||||
Disulfide bond | 3662↔3680 | |||||
Sequence: CNNTLCKPLAWKCDGEDDC | ||||||
Glycosylation | 3663 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3674↔3691 | |||||
Sequence: CDGEDDCGDNSDENPEEC | ||||||
Disulfide bond | 3696↔3710 | |||||
Sequence: CPPNRPFRCKNDRVC | ||||||
Disulfide bond | 3704↔3723 | |||||
Sequence: CKNDRVCLWIGRQCDGVDNC | ||||||
Disulfide bond | 3717↔3732 | |||||
Sequence: CDGVDNCGDGTDEEDC | ||||||
Disulfide bond | 3742↔3755 | |||||
Sequence: CKDKKEFLCRNQRC | ||||||
Disulfide bond | 3750↔3768 | |||||
Sequence: CRNQRCLSSSLRCNMFDDC | ||||||
Disulfide bond | 3762↔3777 | |||||
Sequence: CNMFDDCGDGSDEEDC | ||||||
Disulfide bond | 3786↔3799 | |||||
Sequence: CATNASMCGDEARC | ||||||
Glycosylation | 3789 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3793↔3808 | |||||
Sequence: CGDEARCVRTEKAAYC | ||||||
Disulfide bond | 3810↔3823 | |||||
Sequence: CRSGFHTVPGQPGC | ||||||
Disulfide bond | 3829↔3839 | |||||
Sequence: CLRFGTCSQLC | ||||||
Disulfide bond | 3835↔3848 | |||||
Sequence: CSQLCNNTKGGHLC | ||||||
Glycosylation | 3840 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3850↔3861 | |||||
Sequence: CARNFMKTHNTC | ||||||
Chain | PRO_0000302754 | ?3945-4545 | Low-density lipoprotein receptor-related protein 1 85 kDa subunit | |||
Sequence: QIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLINLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCTLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEYCHNGGTCAASPSGMPTCRCPTGFTGPKCTAQVCAGYCSNNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGFCENFGTCQMAADGSRQCRCTVYFEGPRCEVNKCSRCLQGACVVNKQTGDVTCNCTDGRVAPSCLTCIDHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEQVVSQQQPGHMASILIPLLLLLLLLLVAGVVFWYKRRVRGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA | ||||||
Glycosylation | 3954 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4076 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4126 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 4152↔4161 | |||||
Sequence: CDRKKCEWLC | ||||||
Disulfide bond | 4157↔4170 | |||||
Sequence: CEWLCLLSPSGPVC | ||||||
Disulfide bond | 4172↔4183 | |||||
Sequence: CPNGKRLDNGTC | ||||||
Glycosylation | 4180 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 4201↔4211 | |||||
Sequence: CTLQCFNGGSC | ||||||
Disulfide bond | 4205↔4221 | |||||
Sequence: CFNGGSCFLNARRQPKC | ||||||
Disulfide bond | 4223↔4232 | |||||
Sequence: CQPRYTGDKC | ||||||
Disulfide bond | 4237↔4247 | |||||
Sequence: CWEYCHNGGTC | ||||||
Disulfide bond | 4241↔4257 | |||||
Sequence: CHNGGTCAASPSGMPTC | ||||||
Disulfide bond | 4259↔4268 | |||||
Sequence: CPTGFTGPKC | ||||||
Disulfide bond | 4273↔4283 | |||||
Sequence: CAGYCSNNSTC | ||||||
Disulfide bond | 4277↔4293 | |||||
Sequence: CSNNSTCTVNQGNQPQC | ||||||
Glycosylation | 4279 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4280 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 4295↔4304 | |||||
Sequence: CLPGFLGDRC | ||||||
Disulfide bond | 4309↔4319 | |||||
Sequence: CSGFCENFGTC | ||||||
Disulfide bond | 4313↔4329 | |||||
Sequence: CENFGTCQMAADGSRQC | ||||||
Disulfide bond | 4331↔4340 | |||||
Sequence: CTVYFEGPRC | ||||||
Disulfide bond | 4345↔4353 | |||||
Sequence: CSRCLQGAC | ||||||
Disulfide bond | 4348↔4364 | |||||
Sequence: CLQGACVVNKQTGDVTC | ||||||
Glycosylation | 4365 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 4366↔4375 | |||||
Sequence: CTDGRVAPSC | ||||||
Disulfide bond | 4378↔4388 | |||||
Sequence: CIDHCSNGGSC | ||||||
Disulfide bond | 4382↔4398 | |||||
Sequence: CSNGGSCTMNSKMMPEC | ||||||
Disulfide bond | 4400↔4409 | |||||
Sequence: CPPHMTGPRC | ||||||
Chain | PRO_0000302755 | ?4442-4545 | Low-density lipoprotein receptor-related protein 1 intracellular domain | |||
Sequence: VFWYKRRVRGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA | ||||||
Modified residue | 4461 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 4508 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 4518 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 4521 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 4524 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on serine and threonine residues.
Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1 (By similarity).
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 (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Highly expressed at 7.5 dpc in the trophoblast primary cells at the anti-mesometrial pole (at protein level). Also expressed in secondary trophoblast cells at the ectoplacental cone, although at lower levels (at protein level).
Interaction
Subunit
Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a non-covalently attached 515-kDa N-terminal subunit. Intracellular domain interacts with MAFB (PubMed:15135046).
Found in a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with SNX17, PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with SHC1, GULP1 and DAB1 (By similarity).
Can weakly interact (via NPXY motif) with DAB2 (via PID domain); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif (PubMed:11247302).
Interacts with MDK; promotes neuronal survival (PubMed:10772929).
Interacts with LRPAP1; this interaction is followed by rapid internalization. Interacts with uPA/PLAU and PAI1/SERPINE1, either individually or in complex with each other, leading to rapid endocytosis; this interaction is abolished in the presence of LRPAP1/RAP. Also interacts with tPA/PLAT alone or in complex with SERPINE1. Interacts with the urokinase receptor PLAUR; this interaction leads to PLAUR internalization and is impaired in the presence of SORL1. Interacts with PDGFB. Interacts with TAU/MAPT, leading to endocytosis; this interaction is reduced in the presence of LRPAP1/RAP (By similarity).
Found in a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with SNX17, PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with SHC1, GULP1 and DAB1 (By similarity).
Can weakly interact (via NPXY motif) with DAB2 (via PID domain); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif (PubMed:11247302).
Interacts with MDK; promotes neuronal survival (PubMed:10772929).
Interacts with LRPAP1; this interaction is followed by rapid internalization. Interacts with uPA/PLAU and PAI1/SERPINE1, either individually or in complex with each other, leading to rapid endocytosis; this interaction is abolished in the presence of LRPAP1/RAP. Also interacts with tPA/PLAT alone or in complex with SERPINE1. Interacts with the urokinase receptor PLAUR; this interaction leads to PLAUR internalization and is impaired in the presence of SORL1. Interacts with PDGFB. Interacts with TAU/MAPT, leading to endocytosis; this interaction is reduced in the presence of LRPAP1/RAP (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q91ZX7 | Dab1 P97318 | 2 | EBI-300955, EBI-81680 | |
BINARY | Q91ZX7 | Dlg4 Q62108 | 4 | EBI-300955, EBI-300895 | |
BINARY | Q91ZX7 | Lepr P48356 | 2 | EBI-300955, EBI-2257257 | |
BINARY | Q91ZX7 | Mapk8ip1 Q9WVI9 | 2 | EBI-300955, EBI-74515 | |
BINARY | Q91ZX7 | Mapk8ip2 Q9ERE9 | 2 | EBI-300955, EBI-74576 |
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for domain, repeat, motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 26-67 | LDL-receptor class A 1 | ||||
Sequence: KTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQ | ||||||
Domain | 71-111 | LDL-receptor class A 2 | ||||
Sequence: QRCPPNEHSCLGTELCVPMSRLCNGIQDCMDGSDEGAHCRE | ||||||
Domain | 112-150 | EGF-like 1 | ||||
Sequence: LRANCSRMGCQHHCVPTPSGPTCYCNSSFQLQADGKTCK | ||||||
Domain | 151-190 | EGF-like 2; calcium-binding | ||||
Sequence: DFDECSVYGTCSQLCTNTDGSFTCGCVEGYLLQPDNRSCK | ||||||
Repeat | 293-335 | LDL-receptor class B 1 | ||||
Sequence: GNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAM | ||||||
Repeat | 336-379 | LDL-receptor class B 2 | ||||
Sequence: GKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVS | ||||||
Repeat | 380-423 | LDL-receptor class B 3 | ||||
Sequence: RLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENY | ||||||
Domain | 475-521 | EGF-like 3 | ||||
Sequence: RSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCK | ||||||
Repeat | 572-614 | LDL-receptor class B 4 | ||||
Sequence: GFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMG | ||||||
Repeat | 615-660 | LDL-receptor class B 5 | ||||
Sequence: DNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLN | ||||||
Repeat | 661-711 | LDL-receptor class B 6 | ||||
Sequence: GWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPA | ||||||
Repeat | 712-755 | LDL-receptor class B 7 | ||||
Sequence: GRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNY | ||||||
Domain | 804-844 | EGF-like 4 | ||||
Sequence: GTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDTDGVTCL | ||||||
Domain | 853-893 | LDL-receptor class A 3 | ||||
Sequence: PQCQPGEFACANNRCIQERWKCDGDNDCLDNSDEAPALCHQ | ||||||
Domain | 894-934 | LDL-receptor class A 4 | ||||
Sequence: HTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSA | ||||||
Domain | 935-974 | LDL-receptor class A 5 | ||||
Sequence: RTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAY | ||||||
Domain | 975-1014 | LDL-receptor class A 6 | ||||
Sequence: PTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSH | ||||||
Domain | 1014-1054 | LDL-receptor class A 7 | ||||
Sequence: HSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTN | ||||||
Domain | 1061-1100 | LDL-receptor class A 8 | ||||
Sequence: GGCHSDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKSCEG | ||||||
Domain | 1103-1143 | LDL-receptor class A 9 | ||||
Sequence: HVCDPNVKFGCKDSARCISKAWVCDGDSDCEDNSDEENCEA | ||||||
Domain | 1144-1183 | LDL-receptor class A 10 | ||||
Sequence: LACRPPSHPCANNTSVCLPPDKLCDGKDDCGDGSDEGELC | ||||||
Domain | 1184-1223 | EGF-like 5 | ||||
Sequence: DQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGSDNHTCQ | ||||||
Domain | 1224-1263 | EGF-like 6 | ||||
Sequence: IQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCR | ||||||
Repeat | 1310-1356 | LDL-receptor class B 8 | ||||
Sequence: SALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIA | ||||||
Repeat | 1357-1399 | LDL-receptor class B 9 | ||||
Sequence: GNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRD | ||||||
Repeat | 1400-1446 | LDL-receptor class B 10 | ||||
Sequence: GILFWTDWDASLPRIEAASMSGAGRRTIHRETGSGGWPNGLTVDYLE | ||||||
Repeat | 1447-1491 | LDL-receptor class B 11 | ||||
Sequence: KRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGE | ||||||
Repeat | 1492-1532 | LDL-receptor class B 12 | ||||
Sequence: VYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPS | ||||||
Domain | 1537-1580 | EGF-like 7 | ||||
Sequence: APNPCEANGGRGPCSHLCLINYNRTVSCACPHLMKLHKDNTTCY | ||||||
Repeat | 1628-1670 | LDL-receptor class B 13 | ||||
Sequence: QRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVS | ||||||
Repeat | 1671-1714 | LDL-receptor class B 14 | ||||
Sequence: RNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLR | ||||||
Repeat | 1715-1754 | LDL-receptor class B 15 | ||||
Sequence: GKLYWTDGDNISMANMDGSNHTLLFSGQKGPVGLAIDFPE | ||||||
Repeat | 1755-1799 | LDL-receptor class B 16 | ||||
Sequence: SKLYWISSGNHTINRCNLDGSELEVIDTMRSQLGKATALAIMGDK | ||||||
Domain | 1847-1888 | EGF-like 8 | ||||
Sequence: GTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACE | ||||||
Repeat | 1935-1977 | LDL-receptor class B 17 | ||||
Sequence: DTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIA | ||||||
Repeat | 1978-2020 | LDL-receptor class B 18 | ||||
Sequence: GNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEK | ||||||
Repeat | 2021-2064 | LDL-receptor class B 19 | ||||
Sequence: GYLFWTEWGHYPRIERSRLDGTERVVLVNVSISWPNGISVDYQG | ||||||
Repeat | 2065-2108 | LDL-receptor class B 20 | ||||
Sequence: GKLYWCDARMDKIERIDLETGENREVVLSSNNMDMFSVSVFEDF | ||||||
Domain | 2156-2196 | EGF-like 9 | ||||
Sequence: GTNVCAVANGGCQQLCLYRGGGQRACACAHGMLAEDGASCR | ||||||
Repeat | 2254-2295 | LDL-receptor class B 21 | ||||
Sequence: NRIFFSDIHFGNIQQINDDGSGRTTIVENVGSVEGLAYHRGW | ||||||
Repeat | 2296-2344 | LDL-receptor class B 22 | ||||
Sequence: DTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQ | ||||||
Repeat | 2345-2389 | LDL-receptor class B 23 | ||||
Sequence: NLMFWTNWNELHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRA | ||||||
Repeat | 2390-2432 | LDL-receptor class B 24 | ||||
Sequence: EKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEH | ||||||
Repeat | 2433-2474 | LDL-receptor class B 25 | ||||
Sequence: IFWTDWVRRAVQRANKYVGSDMKLLRVDIPQQPMGIIAVAND | ||||||
Domain | 2479-2519 | EGF-like 10 | ||||
Sequence: ELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQEDFTCR | ||||||
Domain | 2523-2564 | LDL-receptor class A 11 | ||||
Sequence: SSCRAQDEFECANGECISFSLTCDGVSHCKDKSDEKPSYCNS | ||||||
Domain | 2565-2603 | LDL-receptor class A 12 | ||||
Sequence: RRCKKTFRQCNNGRCVSNMLWCNGVDDCGDGSDEIPCNK | ||||||
Domain | 2604-2642 | LDL-receptor class A 13 | ||||
Sequence: TACGVGEFRCRDGSCIGNSSRCNQFVDCEDASDEMNCSA | ||||||
Domain | 2643-2691 | LDL-receptor class A 14 | ||||
Sequence: TDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPG | ||||||
Domain | 2695-2733 | LDL-receptor class A 15 | ||||
Sequence: PRCPLNYFACPSGRCIPMSWTCDKEDDCENGEDETHCNK | ||||||
Domain | 2733-2772 | LDL-receptor class A 16 | ||||
Sequence: KFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEG | ||||||
Domain | 2773-2815 | LDL-receptor class A 17 | ||||
Sequence: KTCGPSSFSCPGTHVCVPERWLCDGDKDCTDGADESVTAGCLY | ||||||
Domain | 2817-2856 | LDL-receptor class A 18 | ||||
Sequence: STCDDREFMCQNRLCIPKHFVCDHDRDCADGSDESPECEY | ||||||
Domain | 2857-2900 | LDL-receptor class A 19 | ||||
Sequence: PTCGPNEFRCANGRCLSSRQWECDGENDCHDHSDEAPKNPHCTS | ||||||
Domain | 2903-2941 | LDL-receptor class A 20 | ||||
Sequence: HKCNASSQFLCSSGRCVAEALLCNGQDDCGDGSDERGCH | ||||||
Domain | 2942-2982 | EGF-like 11 | ||||
Sequence: VNECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCA | ||||||
Domain | 2983-3023 | EGF-like 12; calcium-binding | ||||
Sequence: DLDECSTTFPCSQLCINTHGSYKCLCVEGYAPRGGDPHSCK | ||||||
Repeat | 3070-3114 | LDL-receptor class B 26 | ||||
Sequence: QMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVG | ||||||
Repeat | 3115-3157 | LDL-receptor class B 27 | ||||
Sequence: GNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQN | ||||||
Repeat | 3158-3201 | LDL-receptor class B 28 | ||||
Sequence: GYLYWTDWGDHSLIGRIGMDGSGRSIIVDTKITWPNGLTVDYVT | ||||||
Repeat | 3202-3244 | LDL-receptor class B 29 | ||||
Sequence: ERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDY | ||||||
Repeat | 3245-3285 | LDL-receptor class B 30 | ||||
Sequence: VYWTDWETKSINRAHKTTGANKTLLISTLHRPMDLHVFHAL | ||||||
Domain | 3291-3332 | EGF-like 13 | ||||
Sequence: PNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGGDGRTCV | ||||||
Domain | 3333-3372 | LDL-receptor class A 21 | ||||
Sequence: SNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPE | ||||||
Domain | 3373-3411 | LDL-receptor class A 22 | ||||
Sequence: FKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDI | ||||||
Domain | 3412-3451 | LDL-receptor class A 23 | ||||
Sequence: HVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPE | ||||||
Domain | 3452-3492 | LDL-receptor class A 24 | ||||
Sequence: VTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQ | ||||||
Domain | 3493-3534 | LDL-receptor class A 25 | ||||
Sequence: MTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDE | ||||||
Domain | 3535-3573 | LDL-receptor class A 26 | ||||
Sequence: RTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTP | ||||||
Domain | 3574-3612 | LDL-receptor class A 27 | ||||
Sequence: RPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTP | ||||||
Domain | 3612-3650 | LDL-receptor class A 28 | ||||
Sequence: PRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGT | ||||||
Domain | 3653-3693 | LDL-receptor class A 29 | ||||
Sequence: RTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECAR | ||||||
Domain | 3694-3734 | LDL-receptor class A 30 | ||||
Sequence: FICPPNRPFRCKNDRVCLWIGRQCDGVDNCGDGTDEEDCEP | ||||||
Domain | 3740-3779 | LDL-receptor class A 31 | ||||
Sequence: PHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSI | ||||||
Domain | 3782-3824 | EGF-like 14 | ||||
Sequence: KLTSCATNASMCGDEARCVRTEKAAYCACRSGFHTVPGQPGCQ | ||||||
Domain | 3825-3862 | EGF-like 15 | ||||
Sequence: DINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCK | ||||||
Repeat | 3913-3955 | LDL-receptor class B 31 | ||||
Sequence: GRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNI | ||||||
Motif | 3941-3944 | Recognition site for proteolytical processing | ||||
Sequence: RHRR | ||||||
Repeat | 3971-4013 | LDL-receptor class B 32 | ||||
Sequence: GNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLR | ||||||
Repeat | 4014-4057 | LDL-receptor class B 33 | ||||
Sequence: GTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHN | ||||||
Repeat | 4058-4102 | LDL-receptor class B 34 | ||||
Sequence: ERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDY | ||||||
Domain | 4148-4184 | EGF-like 16 | ||||
Sequence: VTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCV | ||||||
Domain | 4197-4233 | EGF-like 17 | ||||
Sequence: RPGTCTLQCFNGGSCFLNARRQPKCRCQPRYTGDKCE | ||||||
Domain | 4233-4269 | EGF-like 18 | ||||
Sequence: ELDQCWEYCHNGGTCAASPSGMPTCRCPTGFTGPKCT | ||||||
Domain | 4269-4305 | EGF-like 19 | ||||
Sequence: TAQVCAGYCSNNSTCTVNQGNQPQCRCLPGFLGDRCQ | ||||||
Domain | 4305-4341 | EGF-like 20 | ||||
Sequence: QYRQCSGFCENFGTCQMAADGSRQCRCTVYFEGPRCE | ||||||
Domain | 4341-4376 | EGF-like 21 | ||||
Sequence: EVNKCSRCLQGACVVNKQTGDVTCNCTDGRVAPSCL | ||||||
Domain | 4374-4410 | EGF-like 22 | ||||
Sequence: SCLTCIDHCSNGGSCTMNSKMMPECQCPPHMTGPRCE | ||||||
Region | 4446-4545 | Interaction with MAFB | ||||
Sequence: KRRVRGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA | ||||||
Motif | 4503-4508 | NPXY motif | ||||
Sequence: FTNPVY |
Sequence similarities
Belongs to the LDLR family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length4,545
- Mass (Da)504,742
- Last updated2001-12-01 v1
- Checksum9904CF5DF5EE333E
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6XU19 | F6XU19_MOUSE | Lrp1 | 13 | ||
Q3U5J2 | Q3U5J2_MOUSE | Lrp1 | 743 | ||
A0A0R4J0I9 | A0A0R4J0I9_MOUSE | Lrp1 | 4545 | ||
D3Z5M3 | D3Z5M3_MOUSE | Lrp1 | 285 | ||
F6UAC8 | F6UAC8_MOUSE | Lrp1 | 98 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2642 | in Ref. 2; AAL09567 | ||||
Sequence: A → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X67469 EMBL· GenBank· DDBJ | CAA47817.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AF367720 EMBL· GenBank· DDBJ | AAL09566.1 EMBL· GenBank· DDBJ | mRNA | ||
AF369477 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369389 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369390 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369391 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369392 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369393 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369394 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369395 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369396 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369397 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369398 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369399 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369400 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369401 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369402 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369403 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369404 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369405 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369406 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369407 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369408 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369409 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369410 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369411 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369412 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369413 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369414 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369415 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369416 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369417 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369418 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369419 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369420 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369421 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369422 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369423 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369424 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369425 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369426 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369427 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369428 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369429 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369430 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369431 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369432 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369433 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369434 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369435 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369436 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369437 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369438 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369439 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369440 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369441 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369442 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369443 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369444 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369445 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369446 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369447 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369448 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369449 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369450 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369451 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369452 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369453 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369454 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369455 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369456 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369457 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369458 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369459 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369460 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369461 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369462 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369463 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369464 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369465 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369466 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369467 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369468 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369469 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369470 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369471 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369472 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369473 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369474 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369475 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF369476 EMBL· GenBank· DDBJ | AAL09567.1 EMBL· GenBank· DDBJ | Genomic DNA |