Protein detail
LRP2
Low-density lipoprotein receptor-related protein 2 (LRP-2) (Glycoprotein 330) (gp330) (Megalin)
Protein symbol LRP2 | UniProt ID | EVMP score 0.25 |
Frequency 1 | Transmembrane count 1 | Protein classification Disease related genesHuman disease related genesMetabolic proteinsPlasma proteinsPotential drug targetsPredicted intracellular proteinsPredicted membrane proteinsTransporters |
Basic Information
Protein Names
Low-density lipoprotein receptor-related protein 2 (LRP-2) (Glycoprotein 330) (gp330) (Megalin)
Protein Class
Disease related genesHuman disease related genesMetabolic proteinsPlasma proteinsPotential drug targetsPredicted intracellular proteinsPredicted membrane proteinsTransporters
Protein Function
- Transporters
- Predicted intracellular proteins
- Potential drug targets
- Disease related genes
- Human disease related genes:Congenital malformations:Other congenital malformations
Transmembrane
4424..4446; Helical
Transmembrane Count
1
Ensembl
Entrez Gene Symbol
Gene Synonym
DBSgp330
Gene Description
LDL receptor related protein 2
Chromosome
2
Position
169127109-169362534
Frequency
1
EVMP Score
0.25
Fluorescence & Localization
Tissue SpecificbrainCell SpecificAdrenal cortex cellsBlood Cell Specificnon-classical monocyte
Function & Pathway
Protein Function
- Transporters
- Predicted intracellular proteins
- Potential drug targets
- Disease related genes
- Human disease related genes:Congenital malformations:Other congenital malformations
Cellular Component
- GO:0005764 lysosome
- GO:0005765 lysosomal membrane
- GO:0005783 endoplasmic reticulum
- GO:0005794 Golgi apparatus
- GO:0005886 plasma membrane
- GO:0005905 clathrin-coated pit
- GO:0009897 external side of plasma membrane
- GO:0016324 apical plasma membrane
- GO:0030424 axon
- GO:0030425 dendrite
- GO:0030669 clathrin-coated endocytic vesicle membrane
- GO:0031526 brush border membrane
- GO:0031904 endosome lumen
- GO:0043235 receptor complex
- GO:0070062 extracellular exosome
Molecular Function
- GO:0005041 low-density lipoprotein particle receptor activity
- GO:0005509 calcium ion binding
- GO:0005515 protein binding
- GO:0017124 SH3 domain binding
- GO:0031994 insulin-like growth factor I binding
- GO:0038024 cargo receptor activity
- GO:0042562 hormone binding
- GO:0051087 protein-folding chaperone binding
- GO:0140318 protein transporter activity
Biological Process
KEGG
Reactome
- R-hsa-8856825 cargo recognition for clathrin mediated endocytosis
- R-hsa-8856828 clathrin mediated endocytosis
- R-hsa-196741 cobalamin cbl vitamin b12 transport and metabolism
- R-hsa-199991 membrane trafficking
- R-hsa-6806667 metabolism of fat soluble vitamins
- R-hsa-556833 metabolism of lipids
- R-hsa-8957322 metabolism of steroids
- R-hsa-196854 metabolism of vitamins and cofactors
- R-hsa-196849 metabolism of water soluble vitamins and cofactors
- R-hsa-9709957 sensory perception
- R-hsa-9758890 transport of rcbl within the body
- R-hsa-5653656 vesicle mediated transport
- R-hsa-2187338 visual phototransduction
- R-hsa-196791 vitamin d calciferol metabolism
Mediation Categories
Adhesion and uptake mediationFusion and delivery mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
57 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| receptor_regulator | receptor_regulator | OmniPath | Yes | No | No | Yes | No |
| growth_factor_binder | ligand_regulator | GO_Intercell | Yes | No | No | Yes | No |
| ligand_regulator | ligand_regulator | OmniPath | Yes | No | No | Yes | No |
| cell_adhesion | cell_adhesion | Cellinker | Yes | Yes | No | Yes | No |
| matrix_adhesion | matrix_adhesion | Cellinker | No | Yes | No | Yes | No |
| adhesion | adhesion | OmniPath | Yes | Yes | No | Yes | No |
| cell_adhesion | cell_adhesion | OmniPath | Yes | Yes | No | Yes | No |
| matrix_adhesion | matrix_adhesion | OmniPath | No | Yes | No | Yes | No |
| transmembrane | transmembrane | UniProt_location | No | No | No | Yes | No |
| transmembrane | transmembrane | UniProt_topology | No | No | No | Yes | No |
Regulatory Interaction Network
5 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| LRP2 | P98164 | SHH | Q15465 | Yes | Yes | No | WangSignaLink3 | SignaLink3:11964399SignaLink3:23331499 |
| CLUS | P10909 | LRP2 | P98164 | Yes | Yes | No | SIGNORHPRDHINTBioGRIDSPIKE_LC | BioGRID:7768901HPRD:7768901HINT:7768901BioGRID:17260971HINT:9228033HINT:17260971SPIKE_LC:16713569SIGNOR:32332780 |
| MMP2 | P08253 | LRP2 | P98164 | Yes | Yes | No | SIGNOR | SIGNOR:28659595 |
| TIMP2 | P16035 | LRP2 | P98164 | Yes | Yes | No | SIGNOR | SIGNOR:28659595 |
| LRP2 | P98164 | PTC1 | Q13635 | Yes | Yes | No | SIGNOR | SIGNOR:26872844 |
Protein Complex Composition
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| PRotein Organic Solvent Precipitation；Differential Ultracentrifugation | Mass spectrometry | 1 | 32384937 |
Sequence, Structure & Domains
Sequences
Length
4,655
Mass
521,958
Sequence
MDRGPAAVACTLLLALVACLAPASGQECDSAHFRCGSGHCIPADWRCDGTKDCSDDADEIGCAVVTCQQGYFKCQSEGQCIPNSWVCDQDQDCDDGSDERQDCSQSTCSSHQITCSNGQCIPSEYRCDHVRDCPDGADENDCQYPTCEQLTCDNGACYNTSQKCDWKVDCRDSSDEINCTEICLHNEFSCGNGECIPRAYVCDHDNDCQDGSDEHACNYPTCGGYQFTCPSGRCIYQNWVCDGEDDCKDNGDEDGCESGPHDVHKCSPREWSCPESGRCISIYKVCDGILDCPGREDENNTSTGKYCSMTLCSALNCQYQCHETPYGGACFCPPGYIINHNDSRTCVEFDDCQIWGICDQKCESRPGRHLCHCEEGYILERGQYCKANDSFGEASIIFSNGRDLLIGDIHGRSFRILVESQNRGVAVGVAFHYHLQRVFWTDTVQNKVFSVDINGLNIQEVLNVSVETPENLAVDWVNNKIYLVETKVNRIDMVNLDGSYRVTLITENLGHPRGIAVDPTVGYLFFSDWESLSGEPKLERAFMDGSNRKDLVKTKLGWPAGVTLDMISKRVYWVDSRFDYIETVTYDGIQRKTVVHGGSLIPHPFGVSLFEGQVFFTDWTKMAVLKANKFTETNPQVYYQASLRPYGVTVYHSLRQPYATNPCKDNNGGCEQVCVLSHRTDNDGLGFRCKCTFGFQLDTDERHCIAVQNFLIFSSQVAIRGIPFTLSTQEDVMVPVSGNPSFFVGIDFDAQDSTIFFSDMSKHMIFKQKIDGTGREILAANRVENVESLAFDWISKNLYWTDSHYKSISVMRLADKTRRTVVQYLNNPRSVVVHPFAGYLFFTDWFRPAKIMRAWSDGSHLLPVINTTLGWPNGLAIDWAASRLYWVDAYFDKIEHSTFDGLDRRRLGHIEQMTHPFGLAIFGEHLFFTDWRLGAIIRVRKADGGEMTVIRSGIAYILHLKSYDVNIQTGSNACNQPTHPNGDCSHFCFPVPNFQRVCGCPYGMRLASNHLTCEGDPTNEPPTEQCGLFSFPCKNGRCVPNYYLCDGVDDCHDNSDEQLCGTLNNTCSSSAFTCGHGECIPAHWRCDKRNDCVDGSDEHNCPTHAPASCLDTQYTCDNHQCISKNWVCDTDNDCGDGSDEKNCNSTETCQPSQFNCPNHRCIDLSFVCDGDKDCVDGSDEVGCVLNCTASQFKCASGDKCIGVTNRCDGVFDCSDNSDEAGCPTRPPGMCHSDEFQCQEDGICIPNFWECDGHPDCLYGSDEHNACVPKTCPSSYFHCDNGNCIHRAWLCDRDNDCGDMSDEKDCPTQPFRCPSWQWQCLGHNICVNLSVVCDGIFDCPNGTDESPLCNGNSCSDFNGGCTHECVQEPFGAKCLCPLGFLLANDSKTCEDIDECDILGSCSQHCYNMRGSFRCSCDTGYMLESDGRTCKVTASESLLLLVASQNKIIADSVTSQVHNIYSLVENGSYIVAVDFDSISGRIFWSDATQGKTWSAFQNGTDRRVVFDSSIILTETIAIDWVGRNLYWTDYALETIEVSKIDGSHRTVLISKNLTNPRGLALDPRMNEHLLFWSDWGHHPRIERASMDGSMRTVIVQDKIFWPCGLTIDYPNRLLYFMDSYLDYMDFCDYNGHHRRQVIASDLIIRHPYALTLFEDSVYWTDRATRRVMRANKWHGGNQSVVMYNIQWPLGIVAVHPSKQPNSVNPCAFSRCSHLCLLSSQGPHFYSCVCPSGWSLSPDLLNCLRDDQPFLITVRQHIIFGISLNPEVKSNDAMVPIAGIQNGLDVEFDDAEQYIYWVENPGEIHRVKTDGTNRTVFASISMVGPSMNLALDWISRNLYSTNPRTQSIEVLTLHGDIRYRKTLIANDGTALGVGFPIGITVDPARGKLYWSDQGTDSGVPAKIASANMDGTSVKTLFTGNLEHLECVTLDIEEQKLYWAVTGRGVIERGNVDGTDRMILVHQLSHPWGIAVHDSFLYYTDEQYEVIERVDKATGANKIVLRDNVPNLRGLQVYHRRNAAESSNGCSNNMNACQQICLPVPGGLFSCACATGFKLNPDNRSCSPYNSFIVVSMLSAIRGFSLELSDHSETMVPVAGQGRNALHVDVDVSSGFIYWCDFSSSVASDNAIRRIKPDGSSLMNIVTHGIGENGVRGIAVDWVAGNLYFTNAFVSETLIEVLRINTTYRRVLLKVTVDMPRHIVVDPKNRYLFWADYGQRPKIERSFLDCTNRTVLVSEGIVTPRGLAVDRSDGYVYWVDDSLDIIARIRINGENSEVIRYGSRYPTPYGITVFENSIIWVDRNLKKIFQASKEPENTEPPTVIRDNINWLRDVTIFDKQVQPRSPAEVNNNPCLENNGGCSHLCFALPGLHTPKCDCAFGTLQSDGKNCAISTENFLIFALSNSLRSLHLDPENHSPPFQTINVERTVMSLDYDSVSDRIYFTQNLASGVGQISYATLSSGIHTPTVIASGIGTADGIAFDWITRRIYYSDYLNQMINSMAEDGSNRTVIARVPKPRAIVLDPCQGYLYWADWDTHAKIERATLGGNFRVPIVNSSLVMPSGLTLDYEEDLLYWVDASLQRIERSTLTGVDREVIVNAAVHAFGLTLYGQYIYWTDLYTQRIYRANKYDGSGQIAMTTNLLSQPRGINTVVKNQKQQCNNPCEQFNGGCSHICAPGPNGAECQCPHEGNWYLANNRKHCIVDNGERCGASSFTCSNGRCISEEWKCDNDNDCGDGSDEMESVCALHTCSPTAFTCANGRCVQYSYRCDYYNDCGDGSDEAGCLFRDCNATTEFMCNNRRCIPREFICNGVDNCHDNNTSDEKNCPDRTCQSGYTKCHNSNICIPRVYLCDGDNDCGDNSDENPTYCTTHTCSSSEFQCASGRCIPQHWYCDQETDCFDASDEPASCGHSERTCLADEFKCDGGRCIPSEWICDGDNDCGDMSDEDKRHQCQNQNCSDSEFLCVNDRPPDRRCIPQSWVCDGDVDCTDGYDENQNCTRRTCSENEFTCGYGLCIPKIFRCDRHNDCGDYSDERGCLYQTCQQNQFTCQNGRCISKTFVCDEDNDCGDGSDELMHLCHTPEPTCPPHEFKCDNGRCIEMMKLCNHLDDCLDNSDEKGCGINECHDPSISGCDHNCTDTLTSFYCSCRPGYKLMSDKRTCVDIDECTEMPFVCSQKCENVIGSYICKCAPGYLREPDGKTCRQNSNIEPYLIFSNRYYLRNLTIDGYFYSLILEGLDNVVALDFDRVEKRLYWIDTQRQVIERMFLNKTNKETIINHRLPAAESLAVDWVSRKLYWLDARLDGLFVSDLNGGHRRMLAQHCVDANNTFCFDNPRGLALHPQYGYLYWADWGHRAYIGRVGMDGTNKSVIISTKLEWPNGITIDYTNDLLYWADAHLGYIEYSDLEGHHRHTVYDGALPHPFAITIFEDTIYWTDWNTRTVEKGNKYDGSNRQTLVNTTHRPFDIHVYHPYRQPIVSNPCGTNNGGCSHLCLIKPGGKGFTCECPDDFRTLQLSGSTYCMPMCSSTQFLCANNEKCIPIWWKCDGQKDCSDGSDELALCPQRFCRLGQFQCSDGNCTSPQTLCNAHQNCPDGSDEDRLLCENHHCDSNEWQCANKRCIPESWQCDTFNDCEDNSDEDSSHCASRTCRPGQFRCANGRCIPQAWKCDVDNDCGDHSDEPIEECMSSAHLCDNFTEFSCKTNYRCIPKWAVCNGVDDCRDNSDEQGCEERTCHPVGDFRCKNHHCIPLRWQCDGQNDCGDNSDEENCAPRECTESEFRCVNQQCIPSRWICDHYNDCGDNSDERDCEMRTCHPEYFQCTSGHCVHSELKCDGSADCLDASDEADCPTRFPDGAYCQATMFECKNHVCIPPYWKCDGDDDCGDGSDEELHLCLDVPCNSPNRFRCDNNRCIYSHEVCNGVDDCGDGTDETEEHCRKPTPKPCTEYEYKCGNGHCIPHDNVCDDADDCGDWSDELGCNKGKERTCAENICEQNCTQLNEGGFICSCTAGFETNVFDRTSCLDINECEQFGTCPQHCRNTKGSYECVCADGFTSMSDRPGKRCAAEGSSPLLLLPDNVRIRKYNLSSERFSEYLQDEEYIQAVDYDWDPKDIGLSVVYYTVRGEGSRFGAIKRAYIPNFESGRNNLVQEVDLKLKYVMQPDGIAVDWVGRHIYWSDVKNKRIEVAKLDGRYRKWLISTDLDQPAAIAVNPKLGLMFWTDWGKEPKIESAWMNGEDRNILVFEDLGWPTGLSIDYLNNDRIYWSDFKEDVIETIKYDGTDRRVIAKEAMNPYSLDIFEDQLYWISKEKGEVWKQNKFGQGKKEKTLVVNPWLTQVRIFHQLRYNKSVPNLCKQICSHLCLLRPGGYSCACPQGSSFIEGSTTECDAAIELPINLPPPCRCMHGGNCYFDETDLPKCKCPSGYTGKYCEMAFSKGISPGTTAVAVLLTILLIVVIGALAIAGFFHYRRTGSLLPALPKLPSLSSLVKPSENGNGVTFRSGADLNMDIGVSGFGPETAIDRSMAMSEDFVMEMGKQPIIFENPMYSARDSAVKVVQPIQVTVSENVDNKNYGSPINPSEIVPETNPTSPAADGTQVTKWNLFKRKSKQTTNFENPIYAQMENEQKESVAATPPPSPSLPAKPKPPSRRDPTPTYSATEDTFKDTANLVKEDSEV
3D Structural Models
Helix
1138..1141
Beta Strand
1111..1115; 1121..1123; 1129..1131; 1133..1136
3D Structure
Electron microscopy (1); NMR spectroscopy (1)
Domain & Motif Annotations
Compositional Bias
4565..4574; Polar residues; 4612..4624; Pro residues
Repeat
436..478; LDL-receptor class B 1; 479..521; LDL-receptor class B 2; 522..568; LDL-receptor class B 3; 569..613; LDL-receptor class B 4; 753..795; LDL-receptor class B 5; 796..837; LDL-receptor class B 6; 838..881; LDL-receptor class B 7; 882..925; LDL-receptor class B 8; 1478..1520; LDL-receptor class B 9; 1521..1563; LDL-receptor class B 10; 1566..1609; LDL-receptor class B 11; 1610..1654; LDL-receptor class B 12; 1655..1695; LDL-receptor class B 13; 1790..1832; LDL-receptor class B 14; 1833..1882; LDL-receptor class B 15; 1883..1930; LDL-receptor class B 16; 1931..1972; LDL-receptor class B 17; 1973..2013; LDL-receptor class B 18; 2107..2156; LDL-receptor class B 19; 2157..2201; LDL-receptor class B 20; 2202..2245; LDL-receptor class B 21; 2246..2289; LDL-receptor class B 22; 2431..2477; LDL-receptor class B 23; 2478..2518; LDL-receptor class B 24; 2519..2562; LDL-receptor class B 25; 2563..2604; LDL-receptor class B 26; 2605..2646; LDL-receptor class B 27; 3239..3281; LDL-receptor class B 28; 3282..3324; LDL-receptor class B 29; 3333..3376; LDL-receptor class B 30; 3377..3419; LDL-receptor class B 31; 3420..3460; LDL-receptor class B 32; 4154..4196; LDL-receptor class B 33; 4197..4240; LDL-receptor class B 34; 4242..4283; LDL-receptor class B 35
Motif
4453..4462; SH3-binding; 4456..4461; PxLPxI/L motif 1; mediates interaction with ANKRA2; 4459..4464; PxLPxI/L motif 2; mediates interaction with ANKRA2; 4521..4526; Endocytosis signal; 4595..4598; NPXY motif; 4598..4601; SH2-binding; 4611..4622; SH3-binding
Domain (CC)
Two overlapping PxLPxI/L motifs mediate interaction with ankyrin repeats of ANKRA2..; DOMAIN: The cytoplasmic domain is required for sorting to the apical cell membrane.
Domain (FT)
27..63; LDL-receptor class A 1; 66..104; LDL-receptor class A 2; 107..143; LDL-receptor class A 3; 146..180; LDL-receptor class A 4; 182..218; LDL-receptor class A 5; 221..257; LDL-receptor class A 6; 265..308; LDL-receptor class A 7; 1025..1061; LDL-receptor class A 8; 1066..1102; LDL-receptor class A 9; 1108..1144; LDL-receptor class A 10; 1148..1184; LDL-receptor class A 11; 1186..1223; LDL-receptor class A 12; 1229..1267; LDL-receptor class A 13; 1270..1306; LDL-receptor class A 14; 1304..1349; LDL-receptor class A 15; 1390..1429; EGF-like 1; calcium-binding; 1700..1741; EGF-like 2; 2699..2737; LDL-receptor class A 16; 2740..2776; LDL-receptor class A 17; 2779..2818; LDL-receptor class A 18; 2821..2860; LDL-receptor class A 19; 2863..2900; LDL-receptor class A 20; 2905..2944; LDL-receptor class A 21; 2947..2989; LDL-receptor class A 22; 2992..3028; LDL-receptor class A 23; 3031..3069; LDL-receptor class A 24; 3074..3110; LDL-receptor class A 25; 3110..3151; EGF-like 3; 3152..3192; EGF-like 4; calcium-binding; 3511..3549; LDL-receptor class A 26; 3552..3590; LDL-receptor class A 27; 3593..3631; LDL-receptor class A 28; 3634..3672; LDL-receptor class A 29; 3677..3715; LDL-receptor class A 30; 3718..3755; LDL-receptor class A 31; 3758..3794; LDL-receptor class A 32; 3797..3833; LDL-receptor class A 33; 3841..3879; LDL-receptor class A 34; 3882..3921; LDL-receptor class A 35; 3927..3963; LDL-receptor class A 36; 4007..4048; EGF-like 5; calcium-binding; 4377..4411; EGF-like 6
Region
4550..4574; Disordered; 4589..4602; Interaction with DAB2; 4601..4655; Disordered
Protein Families
LDLR family
Sequence Similarities
Belongs to the LDLR family.