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Protein

Low-density lipoprotein receptor-related protein 2

Gene

LRP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts together with cubilin to mediate HDL endocytosis (By similarity). May participate in regulation of parathyroid-hormone and para-thyroid-hormone-related protein release.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1208CalciumBy similarity1
Metal bindingi1210Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1212CalciumBy similarity1
Metal bindingi1218CalciumBy similarity1
Metal bindingi1219CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

  • aorta development Source: Ensembl
  • cell proliferation Source: Ensembl
  • coronary vasculature development Source: Ensembl
  • endocytosis Source: ProtInc
  • forebrain development Source: Ensembl
  • lipid metabolic process Source: ProtInc
  • protein glycosylation Source: ProtInc
  • receptor-mediated endocytosis Source: ProtInc
  • retinoid metabolic process Source: Reactome
  • ventricular septum development Source: Ensembl
  • vitamin D metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000081479-MONOMER.
ReactomeiR-HSA-196791. Vitamin D (calciferol) metabolism.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-975634. Retinoid metabolism and transport.
SignaLinkiP98164.

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 2
Short name:
LRP-2
Alternative name(s):
Glycoprotein 330
Short name:
gp330
Megalin
Gene namesi
Name:LRP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6694. LRP2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 4423ExtracellularSequence analysisAdd BLAST4398
Transmembranei4424 – 4446HelicalSequence analysisAdd BLAST23
Topological domaini4447 – 4655CytoplasmicSequence analysisAdd BLAST209

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • brush border membrane Source: Ensembl
  • clathrin-coated pit Source: UniProtKB-SubCell
  • endocytic vesicle Source: Ensembl
  • endoplasmic reticulum Source: Ensembl
  • endosome Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: UniProtKB
  • lysosome Source: ProtInc
  • plasma membrane Source: Reactome
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane

Pathology & Biotechi

Involvement in diseasei

Donnai-Barrow syndrome (DBS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRare autosomal recessive disorder characterized by major malformations including agenesis of the corpus callosum, congenital diaphragmatic hernia, facial dysmorphology, ocular anomalies, sensorineural hearing loss and developmental delay. The FOAR syndrome was first described as comprising facial anomalies, ocular anomalies, sensorineural hearing loss, and proteinuria. DBS and FOAR were first described as distinct disorders but the classic distinguishing features between the 2 disorders were presence of proteinuria and absence of diaphragmatic hernia and corpus callosum anomalies in FOAR. Early reports noted that the 2 disorders shared many phenotypic features and may be identical. Although there is variability in the expression of some features (e.g., agenesis of the corpus callosum and proteinuria), DBS and FOAR are now considered to represent the same entity.
See also OMIM:222448
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0370132522Y → H in DBS. 1 PublicationCorresponds to variant rs80338747dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4036.
MalaCardsiLRP2.
MIMi222448. phenotype.
OpenTargetsiENSG00000081479.
Orphaneti2143. Donnai-Barrow syndrome.
PharmGKBiPA30452.

Chemistry databases

DrugBankiDB00798. Gentamicin.
DB00030. Insulin Regular.
DB00013. Urokinase.

Polymorphism and mutation databases

BioMutaiLRP2.
DMDMi160332309.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000001732126 – 4655Low-density lipoprotein receptor-related protein 2Add BLAST4630

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 40By similarity
Disulfide bondi35 ↔ 53By similarity
Disulfide bondi47 ↔ 62By similarity
Disulfide bondi67 ↔ 80By similarity
Disulfide bondi74 ↔ 93By similarity
Disulfide bondi87 ↔ 103By similarity
Disulfide bondi108 ↔ 120By similarity
Disulfide bondi115 ↔ 133By similarity
Disulfide bondi127 ↔ 142By similarity
Disulfide bondi147 ↔ 157By similarity
Disulfide bondi152 ↔ 170By similarity
Glycosylationi159N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi164 ↔ 179By similarity
Glycosylationi178N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi183 ↔ 195By similarity
Disulfide bondi190 ↔ 208By similarity
Disulfide bondi202 ↔ 217By similarity
Disulfide bondi222 ↔ 234By similarity
Disulfide bondi229 ↔ 247By similarity
Disulfide bondi241 ↔ 256By similarity
Disulfide bondi266 ↔ 279By similarity
Disulfide bondi273 ↔ 292By similarity
Disulfide bondi286 ↔ 307By similarity
Glycosylationi299N-linked (GlcNAc...)Sequence analysis1
Glycosylationi300N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi312 ↔ 321By similarity
Disulfide bondi317 ↔ 330By similarity
Disulfide bondi332 ↔ 346By similarity
Glycosylationi341N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi352 ↔ 362By similarity
Disulfide bondi358 ↔ 371By similarity
Disulfide bondi373 ↔ 385By similarity
Glycosylationi388N-linked (GlcNAc...)Sequence analysis1
Glycosylationi463N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi663 ↔ 674By similarity
Disulfide bondi670 ↔ 689By similarity
Disulfide bondi691 ↔ 704By similarity
Glycosylationi866N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi974 ↔ 988By similarity
Disulfide bondi984 ↔ 998By similarity
Disulfide bondi1000 ↔ 1013By similarity
Disulfide bondi1026 ↔ 1038By similarity
Disulfide bondi1033 ↔ 1051By similarity
Disulfide bondi1045 ↔ 1060By similarity
Glycosylationi1064N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1067 ↔ 1079By similarity
Disulfide bondi1074 ↔ 1092By similarity
Disulfide bondi1086 ↔ 1101By similarity
Disulfide bondi1109 ↔ 1121By similarity
Disulfide bondi1116 ↔ 1134By similarity
Disulfide bondi1128 ↔ 1143By similarity
Glycosylationi1144N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1149 ↔ 1161By similarity
Disulfide bondi1156 ↔ 1174By similarity
Disulfide bondi1168 ↔ 1183By similarity
Glycosylationi1186N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1187 ↔ 1200By similarity
Disulfide bondi1194 ↔ 1213By similarity
Disulfide bondi1207 ↔ 1222By similarity
Disulfide bondi1230 ↔ 1243By similarity
Disulfide bondi1237 ↔ 1256By similarity
Disulfide bondi1250 ↔ 1266By similarity
Disulfide bondi1271 ↔ 1283By similarity
Disulfide bondi1278 ↔ 1296By similarity
Disulfide bondi1290 ↔ 1305By similarity
Disulfide bondi1312 ↔ 1325By similarity
Disulfide bondi1319 ↔ 1338By similarity
Glycosylationi1327N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1332 ↔ 1348By similarity
Glycosylationi1340N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1353 ↔ 1364By similarity
Disulfide bondi1360 ↔ 1373By similarity
Disulfide bondi1375 ↔ 1388By similarity
Glycosylationi1383N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1394 ↔ 1404By similarity
Disulfide bondi1400 ↔ 1413By similarity
Disulfide bondi1415 ↔ 1428By similarity
Glycosylationi1464N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1496N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1550N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1675N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1704 ↔ 1713By similarity
Disulfide bondi1709 ↔ 1725By similarity
Disulfide bondi1727 ↔ 1740By similarity
Glycosylationi1810N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2022 ↔ 2033By similarity
Disulfide bondi2029 ↔ 2043By similarity
Disulfide bondi2045 ↔ 2058By similarity
Glycosylationi2055N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2177N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2224N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2346 ↔ 2357By similarity
Disulfide bondi2353 ↔ 2368By similarity
Disulfide bondi2370 ↔ 2382By similarity
Glycosylationi2499N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2547N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2655 ↔ 2666By similarity
Disulfide bondi2662 ↔ 2675By similarity
Disulfide bondi2677 ↔ 2692By similarity
Disulfide bondi2700 ↔ 2712By similarity
Disulfide bondi2707 ↔ 2725By similarity
Disulfide bondi2719 ↔ 2736By similarity
Disulfide bondi2741 ↔ 2753By similarity
Disulfide bondi2748 ↔ 2766By similarity
Disulfide bondi2760 ↔ 2775By similarity
Disulfide bondi2780 ↔ 2793By similarity
Glycosylationi2781N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2788 ↔ 2806By similarity
Disulfide bondi2800 ↔ 2817By similarity
Glycosylationi2809N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2810N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2822 ↔ 2835By similarity
Disulfide bondi2829 ↔ 2848By similarity
Disulfide bondi2842 ↔ 2859By similarity
Disulfide bondi2864 ↔ 2876By similarity
Disulfide bondi2871 ↔ 2889By similarity
Disulfide bondi2883 ↔ 2899By similarity
Disulfide bondi2906 ↔ 2918By similarity
Disulfide bondi2913 ↔ 2931By similarity
Disulfide bondi2925 ↔ 2943By similarity
Glycosylationi2947N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2948 ↔ 2965By similarity
Disulfide bondi2955 ↔ 2978By similarity
Disulfide bondi2972 ↔ 2988By similarity
Glycosylationi2987N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2993 ↔ 3005By similarity
Disulfide bondi3000 ↔ 3018By similarity
Disulfide bondi3012 ↔ 3027By similarity
Disulfide bondi3032 ↔ 3044By similarity
Disulfide bondi3039 ↔ 3057By similarity
Disulfide bondi3051 ↔ 3068By similarity
Disulfide bondi3075 ↔ 3087By similarity
Disulfide bondi3082 ↔ 3100By similarity
Disulfide bondi3094 ↔ 3109By similarity
Disulfide bondi3114 ↔ 3126By similarity
Disulfide bondi3122 ↔ 3135By similarity
Glycosylationi3125N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3137 ↔ 3150By similarity
Disulfide bondi3156 ↔ 3167By similarity
Disulfide bondi3163 ↔ 3176By similarity
Disulfide bondi3178 ↔ 3191By similarity
Glycosylationi3211N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3257N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3315N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3355N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3446N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3469 ↔ 3480By similarity
Disulfide bondi3476 ↔ 3491By similarity
Disulfide bondi3493 ↔ 3508By similarity
Disulfide bondi3512 ↔ 3525By similarity
Disulfide bondi3519 ↔ 3538By similarity
Disulfide bondi3532 ↔ 3548By similarity
Disulfide bondi3553 ↔ 3565By similarity
Disulfide bondi3560 ↔ 3578By similarity
Glycosylationi3564N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3572 ↔ 3589By similarity
Disulfide bondi3594 ↔ 3606By similarity
Disulfide bondi3601 ↔ 3619By similarity
Disulfide bondi3613 ↔ 3630By similarity
Disulfide bondi3635 ↔ 3647By similarity
Disulfide bondi3642 ↔ 3660By similarity
Disulfide bondi3654 ↔ 3671By similarity
Disulfide bondi3678 ↔ 3692By similarity
Glycosylationi3680N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3686 ↔ 3705By similarity
Disulfide bondi3699 ↔ 3714By similarity
Disulfide bondi3719 ↔ 3732By similarity
Disulfide bondi3727 ↔ 3745By similarity
Disulfide bondi3739 ↔ 3754By similarity
Disulfide bondi3759 ↔ 3771By similarity
Disulfide bondi3766 ↔ 3784By similarity
Disulfide bondi3778 ↔ 3793By similarity
Disulfide bondi3798 ↔ 3810By similarity
Disulfide bondi3805 ↔ 3823By similarity
Disulfide bondi3817 ↔ 3832By similarity
Disulfide bondi3842 ↔ 3854By similarity
Disulfide bondi3849 ↔ 3867By similarity
Disulfide bondi3861 ↔ 3878By similarity
Disulfide bondi3883 ↔ 3896By similarity
Disulfide bondi3891 ↔ 3909By similarity
Disulfide bondi3903 ↔ 3920By similarity
Disulfide bondi3928 ↔ 3940By similarity
Disulfide bondi3935 ↔ 3953By similarity
Disulfide bondi3947 ↔ 3962By similarity
Disulfide bondi3970 ↔ 3979By similarity
Disulfide bondi3975 ↔ 3989By similarity
Glycosylationi3978N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3991 ↔ 4005By similarity
Disulfide bondi4011 ↔ 4021By similarity
Disulfide bondi4017 ↔ 4030By similarity
Disulfide bondi4032 ↔ 4047By similarity
Glycosylationi4068N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4327N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4334 ↔ 4342By similarity
Disulfide bondi4338 ↔ 4351By similarity
Disulfide bondi4353 ↔ 4367By similarity
Disulfide bondi4381 ↔ 4389By similarity
Disulfide bondi4383 ↔ 4399By similarity
Disulfide bondi4401 ↔ 4410By similarity
Modified residuei4463PhosphoserineBy similarity1
Modified residuei4466PhosphoserineBy similarity1
Modified residuei4569PhosphoserineBy similarity1
Modified residuei4616PhosphoserineBy similarity1
Modified residuei4632PhosphothreonineBy similarity1
Modified residuei4653PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP98164.
MaxQBiP98164.
PaxDbiP98164.
PeptideAtlasiP98164.
PRIDEiP98164.

PTM databases

iPTMnetiP98164.
PhosphoSitePlusiP98164.

Expressioni

Tissue specificityi

Absorptive epithelia, including renal proximal tubules.

Gene expression databases

BgeeiENSG00000081479.
CleanExiHS_LRP2.
ExpressionAtlasiP98164. baseline and differential.
GenevisibleiP98164. HS.

Organism-specific databases

HPAiHPA005980.
HPA064792.

Interactioni

Subunit structurei

Binds plasminogen, extracellular matrix components, plasminogen activator-plasminogen activator inhibitor type I complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin, CLU/clusterin and calcium (PubMed:7768901). Forms a multimeric complex together with LRPAP1 (PubMed:1400426). Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (By similarity). Interacts with LRP2BP (PubMed:12508107). Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif (PubMed:10769163, PubMed:15134832).By similarity5 Publications

Protein-protein interaction databases

BioGridi110216. 61 interactors.
IntActiP98164. 10 interactors.
MINTiMINT-2860496.
STRINGi9606.ENSP00000263816.

Structurei

Secondary structure

14655
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1111 – 1115Combined sources5
Beta strandi1121 – 1123Combined sources3
Beta strandi1129 – 1131Combined sources3
Beta strandi1133 – 1136Combined sources4
Helixi1138 – 1141Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M0PNMR-A1103-1148[»]
ProteinModelPortaliP98164.
SMRiP98164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 64LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST39
Domaini65 – 105LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST41
Domaini106 – 144LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST39
Domaini145 – 181LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST37
Domaini182 – 219LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST38
Domaini220 – 258LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST39
Domaini264 – 308LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST45
Domaini309 – 347EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini348 – 386EGF-like 2PROSITE-ProRule annotationAdd BLAST39
Repeati436 – 478LDL-receptor class B 1Add BLAST43
Repeati479 – 521LDL-receptor class B 2Add BLAST43
Repeati522 – 568LDL-receptor class B 3Add BLAST47
Repeati569 – 612LDL-receptor class B 4Add BLAST44
Repeati613 – 653LDL-receptor class B 5Add BLAST41
Domaini659 – 705EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Repeati753 – 795LDL-receptor class B 6Add BLAST43
Repeati796 – 837LDL-receptor class B 7Add BLAST42
Repeati838 – 881LDL-receptor class B 8Add BLAST44
Repeati882 – 925LDL-receptor class B 9Add BLAST44
Domaini970 – 1014EGF-like 4PROSITE-ProRule annotationAdd BLAST45
Domaini1024 – 1062LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST39
Domaini1065 – 1103LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST39
Domaini1107 – 1145LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST39
Domaini1147 – 1185LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST39
Domaini1186 – 1224LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST39
Domaini1228 – 1268LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST41
Domaini1269 – 1307LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST39
Domaini1310 – 1350LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST41
Domaini1349 – 1389EGF-like 5PROSITE-ProRule annotationAdd BLAST41
Domaini1390 – 1429EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Repeati1478 – 1520LDL-receptor class B 10Add BLAST43
Repeati1521 – 1563LDL-receptor class B 11Add BLAST43
Repeati1566 – 1609LDL-receptor class B 12Add BLAST44
Repeati1610 – 1654LDL-receptor class B 13Add BLAST45
Repeati1655 – 1695LDL-receptor class B 14Add BLAST41
Domaini1700 – 1741EGF-like 7PROSITE-ProRule annotationAdd BLAST42
Repeati1790 – 1832LDL-receptor class B 15Add BLAST43
Repeati1833 – 1882LDL-receptor class B 16Add BLAST50
Repeati1883 – 1930LDL-receptor class B 17Add BLAST48
Repeati1931 – 1971LDL-receptor class B 18Add BLAST41
Repeati1972 – 2013LDL-receptor class B 19Add BLAST42
Domaini2018 – 2059EGF-like 8PROSITE-ProRule annotationAdd BLAST42
Repeati2107 – 2156LDL-receptor class B 20Add BLAST50
Repeati2157 – 2201LDL-receptor class B 21Add BLAST45
Repeati2202 – 2245LDL-receptor class B 22Add BLAST44
Repeati2246 – 2289LDL-receptor class B 23Add BLAST44
Repeati2290 – 2331LDL-receptor class B 24Add BLAST42
Domaini2342 – 2383EGF-like 9PROSITE-ProRule annotationAdd BLAST42
Repeati2431 – 2477LDL-receptor class B 25Add BLAST47
Repeati2478 – 2518LDL-receptor class B 26Add BLAST41
Repeati2519 – 2562LDL-receptor class B 27Add BLAST44
Repeati2563 – 2603LDL-receptor class B 28Add BLAST41
Repeati2604 – 2646LDL-receptor class B 29Add BLAST43
Domaini2651 – 2693EGF-like 10PROSITE-ProRule annotationAdd BLAST43
Domaini2698 – 2738LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST41
Domaini2739 – 2777LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST39
Domaini2778 – 2819LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST42
Domaini2820 – 2861LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST42
Domaini2862 – 2901LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST40
Domaini2904 – 2945LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST42
Domaini2946 – 2990LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST45
Domaini2991 – 3029LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST39
Domaini3030 – 3070LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST41
Domaini3073 – 3110LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST38
Domaini3111 – 3151EGF-like 11PROSITE-ProRule annotationAdd BLAST41
Domaini3152 – 3192EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3239 – 3281LDL-receptor class B 30Add BLAST43
Repeati3282 – 3324LDL-receptor class B 31Add BLAST43
Repeati3333 – 3376LDL-receptor class B 32Add BLAST44
Repeati3377 – 3418LDL-receptor class B 33Add BLAST42
Repeati3419 – 3460LDL-receptor class B 34Add BLAST42
Domaini3465 – 3509EGF-like 13PROSITE-ProRule annotationAdd BLAST45
Domaini3510 – 3550LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST41
Domaini3551 – 3591LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST41
Domaini3592 – 3632LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST41
Domaini3633 – 3673LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST41
Domaini3676 – 3716LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST41
Domaini3717 – 3756LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST40
Domaini3757 – 3795LDL-receptor class A 32PROSITE-ProRule annotationAdd BLAST39
Domaini3796 – 3834LDL-receptor class A 33PROSITE-ProRule annotationAdd BLAST39
Domaini3840 – 3880LDL-receptor class A 34PROSITE-ProRule annotationAdd BLAST41
Domaini3881 – 3922LDL-receptor class A 35PROSITE-ProRule annotationAdd BLAST42
Domaini3926 – 3964LDL-receptor class A 36PROSITE-ProRule annotationAdd BLAST39
Domaini3966 – 4006EGF-like 14PROSITE-ProRule annotationAdd BLAST41
Domaini4007 – 4048EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Repeati4154 – 4196LDL-receptor class B 35Add BLAST43
Repeati4197 – 4240LDL-receptor class B 36Add BLAST44
Repeati4242 – 4283LDL-receptor class B 37Add BLAST42
Domaini4330 – 4368EGF-like 16PROSITE-ProRule annotationAdd BLAST39
Domaini4377 – 4411EGF-like 17PROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4589 – 4602Interaction with DAB2Add BLAST14

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi4453 – 4462SH3-bindingSequence analysis10
Motifi4456 – 4461PxLPxI/L motif 1; mediates interaction with ANKRA2By similarity6
Motifi4459 – 4464PxLPxI/L motif 2; mediates interaction with ANKRA2By similarity6
Motifi4521 – 4526Endocytosis signalSequence analysis6
Motifi4593 – 4598NPXY motif6
Motifi4598 – 4601SH2-bindingSequence analysis4
Motifi4611 – 4622SH3-bindingSequence analysisAdd BLAST12

Domaini

Two overlapping PxLPxI/L motifs mediate interaction with ankyrin repeats of ANKRA2.By similarity

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 17 EGF-like domains.PROSITE-ProRule annotation
Contains 36 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 37 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000230574.
HOVERGENiHBG097941.
InParanoidiP98164.
KOiK06233.
OMAiTRPPGMC.
OrthoDBiEOG091G000N.
PhylomeDBiP98164.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 35 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR019825. Lectin_legB_Mn/Ca_BS.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 34 hits.
PF00058. Ldl_recept_b. 14 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 26 hits.
SM00179. EGF_CA. 10 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 38 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57424. SSF57424. 36 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 9 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 31 hits.
PS50068. LDLRA_2. 36 hits.
PS51120. LDLRB. 35 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P98164-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRGPAAVAC TLLLALVACL APASGQECDS AHFRCGSGHC IPADWRCDGT
60 70 80 90 100
KDCSDDADEI GCAVVTCQQG YFKCQSEGQC IPNSWVCDQD QDCDDGSDER
110 120 130 140 150
QDCSQSTCSS HQITCSNGQC IPSEYRCDHV RDCPDGADEN DCQYPTCEQL
160 170 180 190 200
TCDNGACYNT SQKCDWKVDC RDSSDEINCT EICLHNEFSC GNGECIPRAY
210 220 230 240 250
VCDHDNDCQD GSDEHACNYP TCGGYQFTCP SGRCIYQNWV CDGEDDCKDN
260 270 280 290 300
GDEDGCESGP HDVHKCSPRE WSCPESGRCI SIYKVCDGIL DCPGREDENN
310 320 330 340 350
TSTGKYCSMT LCSALNCQYQ CHETPYGGAC FCPPGYIINH NDSRTCVEFD
360 370 380 390 400
DCQIWGICDQ KCESRPGRHL CHCEEGYILE RGQYCKANDS FGEASIIFSN
410 420 430 440 450
GRDLLIGDIH GRSFRILVES QNRGVAVGVA FHYHLQRVFW TDTVQNKVFS
460 470 480 490 500
VDINGLNIQE VLNVSVETPE NLAVDWVNNK IYLVETKVNR IDMVNLDGSY
510 520 530 540 550
RVTLITENLG HPRGIAVDPT VGYLFFSDWE SLSGEPKLER AFMDGSNRKD
560 570 580 590 600
LVKTKLGWPA GVTLDMISKR VYWVDSRFDY IETVTYDGIQ RKTVVHGGSL
610 620 630 640 650
IPHPFGVSLF EGQVFFTDWT KMAVLKANKF TETNPQVYYQ ASLRPYGVTV
660 670 680 690 700
YHSLRQPYAT NPCKDNNGGC EQVCVLSHRT DNDGLGFRCK CTFGFQLDTD
710 720 730 740 750
ERHCIAVQNF LIFSSQVAIR GIPFTLSTQE DVMVPVSGNP SFFVGIDFDA
760 770 780 790 800
QDSTIFFSDM SKHMIFKQKI DGTGREILAA NRVENVESLA FDWISKNLYW
810 820 830 840 850
TDSHYKSISV MRLADKTRRT VVQYLNNPRS VVVHPFAGYL FFTDWFRPAK
860 870 880 890 900
IMRAWSDGSH LLPVINTTLG WPNGLAIDWA ASRLYWVDAY FDKIEHSTFD
910 920 930 940 950
GLDRRRLGHI EQMTHPFGLA IFGEHLFFTD WRLGAIIRVR KADGGEMTVI
960 970 980 990 1000
RSGIAYILHL KSYDVNIQTG SNACNQPTHP NGDCSHFCFP VPNFQRVCGC
1010 1020 1030 1040 1050
PYGMRLASNH LTCEGDPTNE PPTEQCGLFS FPCKNGRCVP NYYLCDGVDD
1060 1070 1080 1090 1100
CHDNSDEQLC GTLNNTCSSS AFTCGHGECI PAHWRCDKRN DCVDGSDEHN
1110 1120 1130 1140 1150
CPTHAPASCL DTQYTCDNHQ CISKNWVCDT DNDCGDGSDE KNCNSTETCQ
1160 1170 1180 1190 1200
PSQFNCPNHR CIDLSFVCDG DKDCVDGSDE VGCVLNCTAS QFKCASGDKC
1210 1220 1230 1240 1250
IGVTNRCDGV FDCSDNSDEA GCPTRPPGMC HSDEFQCQED GICIPNFWEC
1260 1270 1280 1290 1300
DGHPDCLYGS DEHNACVPKT CPSSYFHCDN GNCIHRAWLC DRDNDCGDMS
1310 1320 1330 1340 1350
DEKDCPTQPF RCPSWQWQCL GHNICVNLSV VCDGIFDCPN GTDESPLCNG
1360 1370 1380 1390 1400
NSCSDFNGGC THECVQEPFG AKCLCPLGFL LANDSKTCED IDECDILGSC
1410 1420 1430 1440 1450
SQHCYNMRGS FRCSCDTGYM LESDGRTCKV TASESLLLLV ASQNKIIADS
1460 1470 1480 1490 1500
VTSQVHNIYS LVENGSYIVA VDFDSISGRI FWSDATQGKT WSAFQNGTDR
1510 1520 1530 1540 1550
RVVFDSSIIL TETIAIDWVG RNLYWTDYAL ETIEVSKIDG SHRTVLISKN
1560 1570 1580 1590 1600
LTNPRGLALD PRMNEHLLFW SDWGHHPRIE RASMDGSMRT VIVQDKIFWP
1610 1620 1630 1640 1650
CGLTIDYPNR LLYFMDSYLD YMDFCDYNGH HRRQVIASDL IIRHPYALTL
1660 1670 1680 1690 1700
FEDSVYWTDR ATRRVMRANK WHGGNQSVVM YNIQWPLGIV AVHPSKQPNS
1710 1720 1730 1740 1750
VNPCAFSRCS HLCLLSSQGP HFYSCVCPSG WSLSPDLLNC LRDDQPFLIT
1760 1770 1780 1790 1800
VRQHIIFGIS LNPEVKSNDA MVPIAGIQNG LDVEFDDAEQ YIYWVENPGE
1810 1820 1830 1840 1850
IHRVKTDGTN RTVFASISMV GPSMNLALDW ISRNLYSTNP RTQSIEVLTL
1860 1870 1880 1890 1900
HGDIRYRKTL IANDGTALGV GFPIGITVDP ARGKLYWSDQ GTDSGVPAKI
1910 1920 1930 1940 1950
ASANMDGTSV KTLFTGNLEH LECVTLDIEE QKLYWAVTGR GVIERGNVDG
1960 1970 1980 1990 2000
TDRMILVHQL SHPWGIAVHD SFLYYTDEQY EVIERVDKAT GANKIVLRDN
2010 2020 2030 2040 2050
VPNLRGLQVY HRRNAAESSN GCSNNMNACQ QICLPVPGGL FSCACATGFK
2060 2070 2080 2090 2100
LNPDNRSCSP YNSFIVVSML SAIRGFSLEL SDHSETMVPV AGQGRNALHV
2110 2120 2130 2140 2150
DVDVSSGFIY WCDFSSSVAS DNAIRRIKPD GSSLMNIVTH GIGENGVRGI
2160 2170 2180 2190 2200
AVDWVAGNLY FTNAFVSETL IEVLRINTTY RRVLLKVTVD MPRHIVVDPK
2210 2220 2230 2240 2250
NRYLFWADYG QRPKIERSFL DCTNRTVLVS EGIVTPRGLA VDRSDGYVYW
2260 2270 2280 2290 2300
VDDSLDIIAR IRINGENSEV IRYGSRYPTP YGITVFENSI IWVDRNLKKI
2310 2320 2330 2340 2350
FQASKEPENT EPPTVIRDNI NWLRDVTIFD KQVQPRSPAE VNNNPCLENN
2360 2370 2380 2390 2400
GGCSHLCFAL PGLHTPKCDC AFGTLQSDGK NCAISTENFL IFALSNSLRS
2410 2420 2430 2440 2450
LHLDPENHSP PFQTINVERT VMSLDYDSVS DRIYFTQNLA SGVGQISYAT
2460 2470 2480 2490 2500
LSSGIHTPTV IASGIGTADG IAFDWITRRI YYSDYLNQMI NSMAEDGSNR
2510 2520 2530 2540 2550
TVIARVPKPR AIVLDPCQGY LYWADWDTHA KIERATLGGN FRVPIVNSSL
2560 2570 2580 2590 2600
VMPSGLTLDY EEDLLYWVDA SLQRIERSTL TGVDREVIVN AAVHAFGLTL
2610 2620 2630 2640 2650
YGQYIYWTDL YTQRIYRANK YDGSGQIAMT TNLLSQPRGI NTVVKNQKQQ
2660 2670 2680 2690 2700
CNNPCEQFNG GCSHICAPGP NGAECQCPHE GNWYLANNRK HCIVDNGERC
2710 2720 2730 2740 2750
GASSFTCSNG RCISEEWKCD NDNDCGDGSD EMESVCALHT CSPTAFTCAN
2760 2770 2780 2790 2800
GRCVQYSYRC DYYNDCGDGS DEAGCLFRDC NATTEFMCNN RRCIPREFIC
2810 2820 2830 2840 2850
NGVDNCHDNN TSDEKNCPDR TCQSGYTKCH NSNICIPRVY LCDGDNDCGD
2860 2870 2880 2890 2900
NSDENPTYCT THTCSSSEFQ CASGRCIPQH WYCDQETDCF DASDEPASCG
2910 2920 2930 2940 2950
HSERTCLADE FKCDGGRCIP SEWICDGDND CGDMSDEDKR HQCQNQNCSD
2960 2970 2980 2990 3000
SEFLCVNDRP PDRRCIPQSW VCDGDVDCTD GYDENQNCTR RTCSENEFTC
3010 3020 3030 3040 3050
GYGLCIPKIF RCDRHNDCGD YSDERGCLYQ TCQQNQFTCQ NGRCISKTFV
3060 3070 3080 3090 3100
CDEDNDCGDG SDELMHLCHT PEPTCPPHEF KCDNGRCIEM MKLCNHLDDC
3110 3120 3130 3140 3150
LDNSDEKGCG INECHDPSIS GCDHNCTDTL TSFYCSCRPG YKLMSDKRTC
3160 3170 3180 3190 3200
VDIDECTEMP FVCSQKCENV IGSYICKCAP GYLREPDGKT CRQNSNIEPY
3210 3220 3230 3240 3250
LIFSNRYYLR NLTIDGYFYS LILEGLDNVV ALDFDRVEKR LYWIDTQRQV
3260 3270 3280 3290 3300
IERMFLNKTN KETIINHRLP AAESLAVDWV SRKLYWLDAR LDGLFVSDLN
3310 3320 3330 3340 3350
GGHRRMLAQH CVDANNTFCF DNPRGLALHP QYGYLYWADW GHRAYIGRVG
3360 3370 3380 3390 3400
MDGTNKSVII STKLEWPNGI TIDYTNDLLY WADAHLGYIE YSDLEGHHRH
3410 3420 3430 3440 3450
TVYDGALPHP FAITIFEDTI YWTDWNTRTV EKGNKYDGSN RQTLVNTTHR
3460 3470 3480 3490 3500
PFDIHVYHPY RQPIVSNPCG TNNGGCSHLC LIKPGGKGFT CECPDDFRTL
3510 3520 3530 3540 3550
QLSGSTYCMP MCSSTQFLCA NNEKCIPIWW KCDGQKDCSD GSDELALCPQ
3560 3570 3580 3590 3600
RFCRLGQFQC SDGNCTSPQT LCNAHQNCPD GSDEDRLLCE NHHCDSNEWQ
3610 3620 3630 3640 3650
CANKRCIPES WQCDTFNDCE DNSDEDSSHC ASRTCRPGQF RCANGRCIPQ
3660 3670 3680 3690 3700
AWKCDVDNDC GDHSDEPIEE CMSSAHLCDN FTEFSCKTNY RCIPKWAVCN
3710 3720 3730 3740 3750
GVDDCRDNSD EQGCEERTCH PVGDFRCKNH HCIPLRWQCD GQNDCGDNSD
3760 3770 3780 3790 3800
EENCAPRECT ESEFRCVNQQ CIPSRWICDH YNDCGDNSDE RDCEMRTCHP
3810 3820 3830 3840 3850
EYFQCTSGHC VHSELKCDGS ADCLDASDEA DCPTRFPDGA YCQATMFECK
3860 3870 3880 3890 3900
NHVCIPPYWK CDGDDDCGDG SDEELHLCLD VPCNSPNRFR CDNNRCIYSH
3910 3920 3930 3940 3950
EVCNGVDDCG DGTDETEEHC RKPTPKPCTE YEYKCGNGHC IPHDNVCDDA
3960 3970 3980 3990 4000
DDCGDWSDEL GCNKGKERTC AENICEQNCT QLNEGGFICS CTAGFETNVF
4010 4020 4030 4040 4050
DRTSCLDINE CEQFGTCPQH CRNTKGSYEC VCADGFTSMS DRPGKRCAAE
4060 4070 4080 4090 4100
GSSPLLLLPD NVRIRKYNLS SERFSEYLQD EEYIQAVDYD WDPKDIGLSV
4110 4120 4130 4140 4150
VYYTVRGEGS RFGAIKRAYI PNFESGRNNL VQEVDLKLKY VMQPDGIAVD
4160 4170 4180 4190 4200
WVGRHIYWSD VKNKRIEVAK LDGRYRKWLI STDLDQPAAI AVNPKLGLMF
4210 4220 4230 4240 4250
WTDWGKEPKI ESAWMNGEDR NILVFEDLGW PTGLSIDYLN NDRIYWSDFK
4260 4270 4280 4290 4300
EDVIETIKYD GTDRRVIAKE AMNPYSLDIF EDQLYWISKE KGEVWKQNKF
4310 4320 4330 4340 4350
GQGKKEKTLV VNPWLTQVRI FHQLRYNKSV PNLCKQICSH LCLLRPGGYS
4360 4370 4380 4390 4400
CACPQGSSFI EGSTTECDAA IELPINLPPP CRCMHGGNCY FDETDLPKCK
4410 4420 4430 4440 4450
CPSGYTGKYC EMAFSKGISP GTTAVAVLLT ILLIVVIGAL AIAGFFHYRR
4460 4470 4480 4490 4500
TGSLLPALPK LPSLSSLVKP SENGNGVTFR SGADLNMDIG VSGFGPETAI
4510 4520 4530 4540 4550
DRSMAMSEDF VMEMGKQPII FENPMYSARD SAVKVVQPIQ VTVSENVDNK
4560 4570 4580 4590 4600
NYGSPINPSE IVPETNPTSP AADGTQVTKW NLFKRKSKQT TNFENPIYAQ
4610 4620 4630 4640 4650
MENEQKESVA ATPPPSPSLP AKPKPPSRRD PTPTYSATED TFKDTANLVK

EDSEV
Length:4,655
Mass (Da):521,958
Last modified:November 13, 2007 - v3
Checksum:iC73C4206B8B28CE0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2724D → G in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti2773A → T in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti2827T → P in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti2880 – 2882HWY → TFGI in AAB02882 (PubMed:7959795).Curated3
Sequence conflicti2897A → S in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti2908A → S in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti2921S → N in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti2954L → P in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti2971 – 2972VC → PP in AAB02882 (PubMed:7959795).Curated2
Sequence conflicti2982Y → H in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti2985N → I in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti3615T → S in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti3738Q → K in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti3784C → LW in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti3810C → R in AAB02882 (PubMed:7959795).Curated1
Sequence conflicti4220R → P in AAB02882 (PubMed:7959795).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03700983N → S.1 PublicationCorresponds to variant rs2229263dbSNPEnsembl.1
Natural variantiVAR_064727103C → R Found in a renal cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_061294259G → R.Corresponds to variant rs34693334dbSNPEnsembl.1
Natural variantiVAR_037010669G → D.Corresponds to variant rs34291900dbSNPEnsembl.1
Natural variantiVAR_037011909H → R.Corresponds to variant rs36082715dbSNPEnsembl.1
Natural variantiVAR_0370121083H → Q.Corresponds to variant rs2302691dbSNPEnsembl.1
Natural variantiVAR_0291821279D → A.Corresponds to variant rs17848149dbSNPEnsembl.1
Natural variantiVAR_0054211287A → P.1
Natural variantiVAR_0291832012R → K.Corresponds to variant rs4667596dbSNPEnsembl.1
Natural variantiVAR_0202182065I → T.Corresponds to variant rs2228168dbSNPEnsembl.1
Natural variantiVAR_0370132522Y → H in DBS. 1 PublicationCorresponds to variant rs80338747dbSNPEnsembl.1
Natural variantiVAR_0291842632N → D.Corresponds to variant rs17848169dbSNPEnsembl.1
Natural variantiVAR_0054222872A → T.Corresponds to variant rs2228171dbSNPEnsembl.1
Natural variantiVAR_0370143011R → M.Corresponds to variant rs11674973dbSNPEnsembl.1
Natural variantiVAR_0202193305R → H.Corresponds to variant rs3213760dbSNPEnsembl.1
Natural variantiVAR_0755343779D → N Found in patients with mild intellectual disability, unknown pathological significance. 1 PublicationCorresponds to variant rs199583537dbSNPEnsembl.1
Natural variantiVAR_0755353828D → G Found in patients with a phenotype suggestive of Stickler syndrome; unknown pathological significance. 1 Publication1
Natural variantiVAR_0054234094K → E.1 PublicationCorresponds to variant rs2075252dbSNPEnsembl.1
Natural variantiVAR_0054244210I → L.1 PublicationCorresponds to variant rs4667591dbSNPEnsembl.1
Natural variantiVAR_0359964272M → V in a colorectal cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33837 mRNA. Translation: AAB41649.1.
AC007556 Genomic DNA. No translation available.
AC008178 Genomic DNA. No translation available.
U04441 mRNA. Translation: AAB02882.1.
S73145 mRNA. Translation: AAB30825.1.
CCDSiCCDS2232.1.
PIRiI38467.
I53413.
RefSeqiNP_004516.2. NM_004525.2.
UniGeneiHs.657729.

Genome annotation databases

EnsembliENST00000263816; ENSP00000263816; ENSG00000081479.
GeneIDi4036.
KEGGihsa:4036.
UCSCiuc002ues.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33837 mRNA. Translation: AAB41649.1.
AC007556 Genomic DNA. No translation available.
AC008178 Genomic DNA. No translation available.
U04441 mRNA. Translation: AAB02882.1.
S73145 mRNA. Translation: AAB30825.1.
CCDSiCCDS2232.1.
PIRiI38467.
I53413.
RefSeqiNP_004516.2. NM_004525.2.
UniGeneiHs.657729.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M0PNMR-A1103-1148[»]
ProteinModelPortaliP98164.
SMRiP98164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110216. 61 interactors.
IntActiP98164. 10 interactors.
MINTiMINT-2860496.
STRINGi9606.ENSP00000263816.

Chemistry databases

DrugBankiDB00798. Gentamicin.
DB00030. Insulin Regular.
DB00013. Urokinase.

PTM databases

iPTMnetiP98164.
PhosphoSitePlusiP98164.

Polymorphism and mutation databases

BioMutaiLRP2.
DMDMi160332309.

Proteomic databases

EPDiP98164.
MaxQBiP98164.
PaxDbiP98164.
PeptideAtlasiP98164.
PRIDEiP98164.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263816; ENSP00000263816; ENSG00000081479.
GeneIDi4036.
KEGGihsa:4036.
UCSCiuc002ues.4. human.

Organism-specific databases

CTDi4036.
DisGeNETi4036.
GeneCardsiLRP2.
GeneReviewsiLRP2.
H-InvDBHIX0029894.
HGNCiHGNC:6694. LRP2.
HPAiHPA005980.
HPA064792.
MalaCardsiLRP2.
MIMi222448. phenotype.
600073. gene.
neXtProtiNX_P98164.
OpenTargetsiENSG00000081479.
Orphaneti2143. Donnai-Barrow syndrome.
PharmGKBiPA30452.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000230574.
HOVERGENiHBG097941.
InParanoidiP98164.
KOiK06233.
OMAiTRPPGMC.
OrthoDBiEOG091G000N.
PhylomeDBiP98164.
TreeFamiTF315253.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000081479-MONOMER.
ReactomeiR-HSA-196791. Vitamin D (calciferol) metabolism.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-975634. Retinoid metabolism and transport.
SignaLinkiP98164.

Miscellaneous databases

ChiTaRSiLRP2. human.
GeneWikiiLRP2.
GenomeRNAii4036.
PROiP98164.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000081479.
CleanExiHS_LRP2.
ExpressionAtlasiP98164. baseline and differential.
GenevisibleiP98164. HS.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 35 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR019825. Lectin_legB_Mn/Ca_BS.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 34 hits.
PF00058. Ldl_recept_b. 14 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 26 hits.
SM00179. EGF_CA. 10 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 38 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57424. SSF57424. 36 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 9 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 31 hits.
PS50068. LDLRA_2. 36 hits.
PS51120. LDLRB. 35 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLRP2_HUMAN
AccessioniPrimary (citable) accession number: P98164
Secondary accession number(s): O00711, Q16215
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 13, 2007
Last modified: November 30, 2016
This is version 172 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.