Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

Multiligand endocytic receptor (By similarity). Acts together with CUBN to mediate endocytosis of high-density lipoproteins (By similarity). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and clearance of leptin (By similarity). Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (By similarity). Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells (By similarity). Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP (By similarity). Mediates renal uptake of metallothionein-bound heavy metals (PubMed:15126248). Together with CUBN, mediates renal reabsorption of myoglobin (By similarity). Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (By similarity). Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (PubMed:23825075). Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity). Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (By similarity). Also mediates ShhN transcytosis (By similarity). In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon (By similarity). Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH (By similarity). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (By similarity). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (By similarity). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity). Involved in neurite branching (By similarity). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (By similarity). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (By similarity). Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG (By similarity). Mediates endocytosis of angiotensin-2 (By similarity). Also mediates endocytosis of angiotensis 1-7 (By similarity). Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation (By similarity). Required for embryonic heart development (By similarity). Required for normal hearing, possibly through interaction with estrogen in the inner ear (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1126Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1129CalciumCombined sources1 Publication1
Metal bindingi1131Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1133CalciumCombined sources1 Publication1
Metal bindingi1139CalciumCombined sources1 Publication1
Metal bindingi1140CalciumCombined sources1 Publication1
Metal bindingi1208CalciumBy similarity1
Metal bindingi1210Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1212CalciumBy similarity1
Metal bindingi1218CalciumBy similarity1
Metal bindingi1219CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionReceptor
Biological processEndocytosis, Hearing, Neurogenesis, Transport
LigandCalcium, Metal-binding

Enzyme and pathway databases

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:LRP2Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000081479.12.
HGNCiHGNC:6694. LRP2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

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

Keywords - Cellular componenti

Cell membrane, Cell projection, Coated pit, Endosome, 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 dbSNP:rs80338747Ensembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4036.
GeneReviewsiLRP2.
MalaCardsiLRP2.
MIMi222448. phenotype.
OpenTargetsiENSG00000081479.
Orphaneti2143. Donnai-Barrow syndrome.
PharmGKBiPA30452.

Chemistry databases

DrugBankiDB00798. Gentamicin.
DB00030. Insulin Human.
DB00071. Insulin Pork.
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 ↔ 40PROSITE-ProRule annotation
Disulfide bondi35 ↔ 53PROSITE-ProRule annotation
Disulfide bondi47 ↔ 62PROSITE-ProRule annotation
Disulfide bondi67 ↔ 80PROSITE-ProRule annotation
Disulfide bondi74 ↔ 93PROSITE-ProRule annotation
Disulfide bondi87 ↔ 103PROSITE-ProRule annotation
Disulfide bondi108 ↔ 120PROSITE-ProRule annotation
Disulfide bondi115 ↔ 133PROSITE-ProRule annotation
Disulfide bondi127 ↔ 142PROSITE-ProRule annotation
Disulfide bondi147 ↔ 157PROSITE-ProRule annotation
Disulfide bondi152 ↔ 170PROSITE-ProRule annotation
Glycosylationi159N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi164 ↔ 179PROSITE-ProRule annotation
Glycosylationi178N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi183 ↔ 195PROSITE-ProRule annotation
Disulfide bondi190 ↔ 208PROSITE-ProRule annotation
Disulfide bondi202 ↔ 217PROSITE-ProRule annotation
Disulfide bondi222 ↔ 234PROSITE-ProRule annotation
Disulfide bondi229 ↔ 247PROSITE-ProRule annotation
Disulfide bondi241 ↔ 256PROSITE-ProRule annotation
Disulfide bondi266 ↔ 279PROSITE-ProRule annotation
Disulfide bondi273 ↔ 292PROSITE-ProRule annotation
Disulfide bondi286 ↔ 307PROSITE-ProRule annotation
Glycosylationi299N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi300N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi341N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi388N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi463N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi866N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1026 ↔ 1038PROSITE-ProRule annotation
Disulfide bondi1033 ↔ 1051PROSITE-ProRule annotation
Disulfide bondi1045 ↔ 1060PROSITE-ProRule annotation
Glycosylationi1064N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1067 ↔ 1079PROSITE-ProRule annotation
Disulfide bondi1074 ↔ 1092PROSITE-ProRule annotation
Disulfide bondi1086 ↔ 1101PROSITE-ProRule annotation
Disulfide bondi1109 ↔ 1121PROSITE-ProRule annotation1 Publication
Disulfide bondi1116 ↔ 1134PROSITE-ProRule annotation1 Publication
Disulfide bondi1128 ↔ 1143PROSITE-ProRule annotation1 Publication
Glycosylationi1144N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1149 ↔ 1161PROSITE-ProRule annotation
Disulfide bondi1156 ↔ 1174PROSITE-ProRule annotation
Disulfide bondi1168 ↔ 1183PROSITE-ProRule annotation
Glycosylationi1186N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1187 ↔ 1200PROSITE-ProRule annotation
Disulfide bondi1194 ↔ 1213PROSITE-ProRule annotation
Disulfide bondi1207 ↔ 1222PROSITE-ProRule annotation
Disulfide bondi1230 ↔ 1243PROSITE-ProRule annotation
Disulfide bondi1237 ↔ 1256PROSITE-ProRule annotation
Disulfide bondi1250 ↔ 1266PROSITE-ProRule annotation
Disulfide bondi1271 ↔ 1283PROSITE-ProRule annotation
Disulfide bondi1278 ↔ 1296PROSITE-ProRule annotation
Disulfide bondi1290 ↔ 1305PROSITE-ProRule annotation
Disulfide bondi1305 ↔ 1325PROSITE-ProRule annotation
Disulfide bondi1312 ↔ 1338PROSITE-ProRule annotation
Glycosylationi1327N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1332 ↔ 1348PROSITE-ProRule annotation
Glycosylationi1340N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1383N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1394 ↔ 1404PROSITE-ProRule annotation
Disulfide bondi1400 ↔ 1413PROSITE-ProRule annotation
Disulfide bondi1415 ↔ 1428PROSITE-ProRule annotation
Glycosylationi1464N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1496N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1550N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1675N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1704 ↔ 1713PROSITE-ProRule annotation
Disulfide bondi1709 ↔ 1725PROSITE-ProRule annotation
Disulfide bondi1727 ↔ 1740PROSITE-ProRule annotation
Glycosylationi1810N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2055N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2177N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2224N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2499N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2547N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2700 ↔ 2712PROSITE-ProRule annotation
Disulfide bondi2707 ↔ 2725PROSITE-ProRule annotation
Disulfide bondi2719 ↔ 2736PROSITE-ProRule annotation
Disulfide bondi2741 ↔ 2753PROSITE-ProRule annotation
Disulfide bondi2748 ↔ 2766PROSITE-ProRule annotation
Disulfide bondi2760 ↔ 2775PROSITE-ProRule annotation
Disulfide bondi2780 ↔ 2793PROSITE-ProRule annotation
Glycosylationi2781N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2788 ↔ 2806PROSITE-ProRule annotation
Disulfide bondi2800 ↔ 2817PROSITE-ProRule annotation
Glycosylationi2809N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2810N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2822 ↔ 2835PROSITE-ProRule annotation
Disulfide bondi2829 ↔ 2848PROSITE-ProRule annotation
Disulfide bondi2842 ↔ 2859PROSITE-ProRule annotation
Disulfide bondi2864 ↔ 2876PROSITE-ProRule annotation
Disulfide bondi2871 ↔ 2889PROSITE-ProRule annotation
Disulfide bondi2883 ↔ 2899PROSITE-ProRule annotation
Disulfide bondi2906 ↔ 2918PROSITE-ProRule annotation
Disulfide bondi2913 ↔ 2931PROSITE-ProRule annotation
Disulfide bondi2925 ↔ 2943PROSITE-ProRule annotation
Glycosylationi2947N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2948 ↔ 2965PROSITE-ProRule annotation
Disulfide bondi2955 ↔ 2978PROSITE-ProRule annotation
Disulfide bondi2972 ↔ 2988PROSITE-ProRule annotation
Glycosylationi2987N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2993 ↔ 3005PROSITE-ProRule annotation
Disulfide bondi3000 ↔ 3018PROSITE-ProRule annotation
Disulfide bondi3012 ↔ 3027PROSITE-ProRule annotation
Disulfide bondi3032 ↔ 3044PROSITE-ProRule annotation
Disulfide bondi3039 ↔ 3057PROSITE-ProRule annotation
Disulfide bondi3051 ↔ 3068PROSITE-ProRule annotation
Disulfide bondi3075 ↔ 3087PROSITE-ProRule annotation
Disulfide bondi3082 ↔ 3100PROSITE-ProRule annotation
Disulfide bondi3094 ↔ 3109PROSITE-ProRule annotation
Disulfide bondi3114 ↔ 3126PROSITE-ProRule annotation
Disulfide bondi3122 ↔ 3135PROSITE-ProRule annotation
Glycosylationi3125N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3137 ↔ 3150PROSITE-ProRule annotation
Disulfide bondi3156 ↔ 3167PROSITE-ProRule annotation
Disulfide bondi3163 ↔ 3176PROSITE-ProRule annotation
Disulfide bondi3178 ↔ 3191PROSITE-ProRule annotation
Glycosylationi3211N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3257N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3315N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3355N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3446N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3512 ↔ 3525PROSITE-ProRule annotation
Disulfide bondi3519 ↔ 3538PROSITE-ProRule annotation
Disulfide bondi3532 ↔ 3548PROSITE-ProRule annotation
Disulfide bondi3553 ↔ 3565PROSITE-ProRule annotation
Disulfide bondi3560 ↔ 3578PROSITE-ProRule annotation
Glycosylationi3564N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3572 ↔ 3589PROSITE-ProRule annotation
Disulfide bondi3594 ↔ 3606PROSITE-ProRule annotation
Disulfide bondi3601 ↔ 3619PROSITE-ProRule annotation
Disulfide bondi3613 ↔ 3630PROSITE-ProRule annotation
Disulfide bondi3635 ↔ 3647PROSITE-ProRule annotation
Disulfide bondi3642 ↔ 3660PROSITE-ProRule annotation
Disulfide bondi3654 ↔ 3671PROSITE-ProRule annotation
Disulfide bondi3678 ↔ 3692PROSITE-ProRule annotation
Glycosylationi3680N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3686 ↔ 3705PROSITE-ProRule annotation
Disulfide bondi3699 ↔ 3714PROSITE-ProRule annotation
Disulfide bondi3719 ↔ 3732PROSITE-ProRule annotation
Disulfide bondi3727 ↔ 3745PROSITE-ProRule annotation
Disulfide bondi3739 ↔ 3754PROSITE-ProRule annotation
Disulfide bondi3759 ↔ 3771PROSITE-ProRule annotation
Disulfide bondi3766 ↔ 3784PROSITE-ProRule annotation
Disulfide bondi3778 ↔ 3793PROSITE-ProRule annotation
Disulfide bondi3798 ↔ 3810PROSITE-ProRule annotation
Disulfide bondi3805 ↔ 3823PROSITE-ProRule annotation
Disulfide bondi3817 ↔ 3832PROSITE-ProRule annotation
Disulfide bondi3842 ↔ 3854PROSITE-ProRule annotation
Disulfide bondi3849 ↔ 3867PROSITE-ProRule annotation
Disulfide bondi3861 ↔ 3878PROSITE-ProRule annotation
Disulfide bondi3883 ↔ 3896PROSITE-ProRule annotation
Disulfide bondi3891 ↔ 3909PROSITE-ProRule annotation
Disulfide bondi3903 ↔ 3920PROSITE-ProRule annotation
Disulfide bondi3928 ↔ 3940PROSITE-ProRule annotation
Disulfide bondi3935 ↔ 3953PROSITE-ProRule annotation
Disulfide bondi3947 ↔ 3962PROSITE-ProRule annotation
Glycosylationi3978N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4011 ↔ 4021PROSITE-ProRule annotation
Disulfide bondi4017 ↔ 4030PROSITE-ProRule annotation
Disulfide bondi4032 ↔ 4047PROSITE-ProRule annotation
Glycosylationi4068N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi4327N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4381 ↔ 4389PROSITE-ProRule annotation
Disulfide bondi4383 ↔ 4399PROSITE-ProRule annotation
Disulfide bondi4401 ↔ 4410PROSITE-ProRule annotation
Modified residuei4463PhosphoserineBy similarity1
Modified residuei4466PhosphoserineBy similarity1
Modified residuei4569PhosphoserineBy similarity1
Modified residuei4616PhosphoserineBy similarity1
Modified residuei4632PhosphothreonineBy similarity1
Modified residuei4653PhosphoserineBy similarity1

Post-translational modificationi

A fraction undergoes proteolytic cleavage of the extracellular domain at the cell membrane to generate a cytoplasmic tail fragment. This is internalized into the early endosome from where it trafficks in an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment (ERC). In the ERC, it is further cleaved by gamma-secretase to release a fragment which translocates to the nucleus and mediates transcriptional repression.By similarity
N-glycosylation is required for ligand binding.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP98164.
MaxQBiP98164.
PaxDbiP98164.
PeptideAtlasiP98164.
PRIDEiP98164.

PTM databases

iPTMnetiP98164.
PhosphoSitePlusiP98164.

Expressioni

Tissue specificityi

Expressed in first and third trimester cytotrophoblasts in the placenta (at protein level) (PubMed:27798286). Absorptive epithelia, including renal proximal tubules.1 Publication

Developmental stagei

Expression in the choroid plexus of the brain is markedly reduced in aging subjects when compared with younger adults.1 Publication

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). Interacts with MB (By similarity). Interacts with BMP4 (By similarity). Interacts with the Sonic hedgehog protein N-product which is the active product of SHH (By similarity). Interacts with CST3 in a calcium-dependent manner (PubMed:17462596). Interacts with the vitamin-D binding protein GC/DBP (By similarity). Interacts with sex hormone-binding protein SHBG (PubMed:16143106). Interacts with angiotensin-2 (By similarity). Also interacts with angiotensin 1-7 (By similarity). Interacts with APOM (By similarity). Interacts with selenoprotein SEPP1 (By similarity). Interacts with LEP (By similarity). Interacts with ALB (By similarity). Interacts with the antiapoptotic protein BIRC5/survivin (PubMed:23825075). Interacts with matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity). In neurons, forms a trimeric complex with APP and APPB1/FE65 (By similarity). Interacts with LDLRAP1/ARH; mediates trafficking of LRP2 to the endocytic recycling compartment (By similarity). Does not interact with beta-amyloid protein 40 alone but interacts with the complex composed of beta-amyloid protein 40 and CLU/APOJ (By similarity).By similarity8 Publications

GO - Molecular functioni

  • chaperone binding Source: ARUK-UCL
  • SH3 domain binding Source: UniProtKB-KW
  • steroid hormone receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110216. 82 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
Domaini27 – 63LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST37
Domaini66 – 104LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST39
Domaini107 – 143LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST37
Domaini146 – 180LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST35
Domaini182 – 218LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST37
Domaini221 – 257LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST37
Domaini265 – 308LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST44
Repeati436 – 478LDL-receptor class B 1PROSITE-ProRule annotationAdd BLAST43
Repeati479 – 521LDL-receptor class B 2PROSITE-ProRule annotationAdd BLAST43
Repeati522 – 568LDL-receptor class B 3PROSITE-ProRule annotationAdd BLAST47
Repeati569 – 613LDL-receptor class B 4PROSITE-ProRule annotationAdd BLAST45
Repeati753 – 795LDL-receptor class B 5PROSITE-ProRule annotationAdd BLAST43
Repeati796 – 837LDL-receptor class B 6PROSITE-ProRule annotationAdd BLAST42
Repeati838 – 881LDL-receptor class B 7PROSITE-ProRule annotationAdd BLAST44
Repeati882 – 925LDL-receptor class B 8PROSITE-ProRule annotationAdd BLAST44
Domaini1025 – 1061LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST37
Domaini1066 – 1102LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST37
Domaini1108 – 1144LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST37
Domaini1148 – 1184LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST37
Domaini1186 – 1223LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST38
Domaini1229 – 1267LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST39
Domaini1270 – 1306LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST37
Domaini1304 – 1349LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST46
Domaini1390 – 1429EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Repeati1478 – 1520LDL-receptor class B 9PROSITE-ProRule annotationAdd BLAST43
Repeati1521 – 1563LDL-receptor class B 10PROSITE-ProRule annotationAdd BLAST43
Repeati1566 – 1609LDL-receptor class B 11PROSITE-ProRule annotationAdd BLAST44
Repeati1610 – 1654LDL-receptor class B 12PROSITE-ProRule annotationAdd BLAST45
Repeati1655 – 1695LDL-receptor class B 13PROSITE-ProRule annotationAdd BLAST41
Domaini1700 – 1741EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Repeati1790 – 1832LDL-receptor class B 14PROSITE-ProRule annotationAdd BLAST43
Repeati1833 – 1882LDL-receptor class B 15PROSITE-ProRule annotationAdd BLAST50
Repeati1883 – 1930LDL-receptor class B 16PROSITE-ProRule annotationAdd BLAST48
Repeati1931 – 1972LDL-receptor class B 17PROSITE-ProRule annotationAdd BLAST42
Repeati1973 – 2013LDL-receptor class B 18PROSITE-ProRule annotationAdd BLAST41
Repeati2107 – 2156LDL-receptor class B 19PROSITE-ProRule annotationAdd BLAST50
Repeati2157 – 2201LDL-receptor class B 20PROSITE-ProRule annotationAdd BLAST45
Repeati2202 – 2245LDL-receptor class B 21PROSITE-ProRule annotationAdd BLAST44
Repeati2246 – 2289LDL-receptor class B 22PROSITE-ProRule annotationAdd BLAST44
Repeati2431 – 2477LDL-receptor class B 23PROSITE-ProRule annotationAdd BLAST47
Repeati2478 – 2518LDL-receptor class B 24PROSITE-ProRule annotationAdd BLAST41
Repeati2519 – 2562LDL-receptor class B 25PROSITE-ProRule annotationAdd BLAST44
Repeati2563 – 2604LDL-receptor class B 26PROSITE-ProRule annotationAdd BLAST42
Repeati2605 – 2646LDL-receptor class B 27PROSITE-ProRule annotationAdd BLAST42
Domaini2699 – 2737LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST39
Domaini2740 – 2776LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST37
Domaini2779 – 2818LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST40
Domaini2821 – 2860LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST40
Domaini2863 – 2900LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST38
Domaini2905 – 2944LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST40
Domaini2947 – 2989LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST43
Domaini2992 – 3028LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST37
Domaini3031 – 3069LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST39
Domaini3074 – 3110LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST37
Domaini3110 – 3151EGF-like 3PROSITE-ProRule annotationAdd BLAST42
Domaini3152 – 3192EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3239 – 3281LDL-receptor class B 28PROSITE-ProRule annotationAdd BLAST43
Repeati3282 – 3324LDL-receptor class B 29PROSITE-ProRule annotationAdd BLAST43
Repeati3333 – 3376LDL-receptor class B 30PROSITE-ProRule annotationAdd BLAST44
Repeati3377 – 3419LDL-receptor class B 31PROSITE-ProRule annotationAdd BLAST43
Repeati3420 – 3460LDL-receptor class B 32PROSITE-ProRule annotationAdd BLAST41
Domaini3511 – 3549LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST39
Domaini3552 – 3590LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST39
Domaini3593 – 3631LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST39
Domaini3634 – 3672LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST39
Domaini3677 – 3715LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST39
Domaini3718 – 3755LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST38
Domaini3758 – 3794LDL-receptor class A 32PROSITE-ProRule annotationAdd BLAST37
Domaini3797 – 3833LDL-receptor class A 33PROSITE-ProRule annotationAdd BLAST37
Domaini3841 – 3879LDL-receptor class A 34PROSITE-ProRule annotationAdd BLAST39
Domaini3882 – 3921LDL-receptor class A 35PROSITE-ProRule annotationAdd BLAST40
Domaini3927 – 3963LDL-receptor class A 36PROSITE-ProRule annotationAdd BLAST37
Domaini4007 – 4048EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Repeati4154 – 4196LDL-receptor class B 33PROSITE-ProRule annotationAdd BLAST43
Repeati4197 – 4240LDL-receptor class B 34PROSITE-ProRule annotationAdd BLAST44
Repeati4242 – 4283LDL-receptor class B 35PROSITE-ProRule annotationAdd BLAST42
Domaini4377 – 4411EGF-like 6PROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4589 – 4602Interaction with DAB21 PublicationAdd 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
Motifi4595 – 4598NPXY motif4
Motifi4598 – 4601SH2-bindingSequence analysis4
Motifi4611 – 4622SH3-bindingSequence analysisAdd BLAST12

Domaini

Two overlapping PxLPxI/L motifs mediate interaction with ankyrin repeats of ANKRA2.By similarity
The cytoplasmic domain is required for sorting to the apical cell membrane.By similarity

Sequence similaritiesi

Belongs to the LDLR family.Curated

Keywords - Domaini

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

Phylogenomic databases

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

Family and domain databases

CDDicd00112. LDLa. 34 hits.
Gene3Di2.120.10.30. 8 hits.
InterProiView protein in InterPro
IPR011042. 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_cys_sf.
IPR036055. LDL_receptor-like_sf.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR019825. Lectin_legB_Mn/Ca_BS.
PfamiView protein in Pfam
PF12662. cEGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 34 hits.
PF00058. Ldl_recept_b. 14 hits.
PRINTSiPR00261. LDLRECEPTOR.
SMARTiView protein in SMART
SM00181. EGF. 26 hits.
SM00179. EGF_CA. 10 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 38 hits.
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57424. SSF57424. 36 hits.
PROSITEiView protein in PROSITE
PS00010. 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.

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 → S1 PublicationCorresponds to variant dbSNP:rs2229263Ensembl.1
Natural variantiVAR_064727103C → R Found in a renal cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_061294259G → R. Corresponds to variant dbSNP:rs34693334Ensembl.1
Natural variantiVAR_037010669G → D. Corresponds to variant dbSNP:rs34291900Ensembl.1
Natural variantiVAR_037011909H → R. Corresponds to variant dbSNP:rs36082715Ensembl.1
Natural variantiVAR_0370121083H → Q. Corresponds to variant dbSNP:rs2302691Ensembl.1
Natural variantiVAR_0291821279D → A. Corresponds to variant dbSNP:rs17848149Ensembl.1
Natural variantiVAR_0054211287A → P. 1
Natural variantiVAR_0291832012R → K. Corresponds to variant dbSNP:rs4667596Ensembl.1
Natural variantiVAR_0202182065I → T. Corresponds to variant dbSNP:rs2228168Ensembl.1
Natural variantiVAR_0370132522Y → H in DBS. 1 PublicationCorresponds to variant dbSNP:rs80338747Ensembl.1
Natural variantiVAR_0291842632N → D. Corresponds to variant dbSNP:rs17848169Ensembl.1
Natural variantiVAR_0054222872A → T. Corresponds to variant dbSNP:rs2228171Ensembl.1
Natural variantiVAR_0370143011R → M. Corresponds to variant dbSNP:rs11674973Ensembl.1
Natural variantiVAR_0202193305R → H. Corresponds to variant dbSNP:rs3213760Ensembl.1
Natural variantiVAR_0755343779D → N Found in patients with mild intellectual disability, unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs199583537Ensembl.1
Natural variantiVAR_0755353828D → G Found in patients with a phenotype suggestive of Stickler syndrome; unknown pathological significance. 1 Publication1
Natural variantiVAR_0054234094K → E1 PublicationCorresponds to variant dbSNP:rs2075252Ensembl.1
Natural variantiVAR_0054244210I → L1 PublicationCorresponds to variant dbSNP:rs4667591Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiLRP2_HUMAN
AccessioniPrimary (citable) accession number: P98164
Secondary accession number(s): O00711, Q16215
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 13, 2007
Last modified: November 22, 2017
This is version 182 of the entry and version 3 of the sequence. See 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