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Protein

Low-density lipoprotein receptor-related protein 2

Gene

Lrp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multiligand endocytic receptor. 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 (PubMed:7544804, PubMed:19202329). 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 (PubMed:17324488). 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 (PubMed:17462596). 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 (PubMed:12724130). Mediates renal uptake and subsequent lysosomal degradation of APOM (PubMed:16099815). 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 (By similarity). Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (PubMed:28659595). Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (PubMed:11964399, PubMed:16801528). Also mediates ShhN transcytosis (PubMed:16801528). 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 (PubMed:18466341). 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 (PubMed:16143106). Mediates endocytosis of angiotensin-2 (PubMed:15467006). Also mediates endocytosis of angiotensin 1-7 (PubMed:16380466). 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 (PubMed:17846082).By similarity15 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1127Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1130CalciumBy similarity1
Metal bindingi1132Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1134CalciumBy similarity1
Metal bindingi1140CalciumBy similarity1
Metal bindingi1141CalciumBy similarity1
Metal bindingi1206Calcium; via carbonyl oxygen1 Publication1
Metal bindingi1209Calcium1 Publication1
Metal bindingi1211Calcium; via carbonyl oxygen1 Publication1
Metal bindingi1213Calcium1 Publication1
Metal bindingi1219Calcium1 Publication1
Metal bindingi1220Calcium1 Publication1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • chaperone binding Source: RGD
  • drug binding Source: UniProtKB
  • hemoglobin binding Source: RGD
  • hormone binding Source: RGD
  • low-density lipoprotein particle receptor binding Source: RGD
  • PDZ domain binding Source: RGD
  • protein complex binding Source: RGD
  • receptor activity Source: RGD
  • SH3 domain binding Source: UniProtKB-KW
  • steroid hormone receptor binding Source: UniProtKB

GO - Biological processi

  • aging Source: RGD
  • animal organ regeneration Source: RGD
  • aorta development Source: RGD
  • cell proliferation Source: RGD
  • coronary artery morphogenesis Source: UniProtKB
  • coronary vasculature development Source: RGD
  • endosomal transport Source: RGD
  • folic acid import across plasma membrane Source: UniProtKB
  • forebrain development Source: RGD
  • heart development Source: RGD
  • hemoglobin import Source: RGD
  • hormone secretion Source: RGD
  • lipoprotein transport Source: RGD
  • male gonad development Source: UniProtKB
  • metal ion transport Source: UniProtKB
  • negative regulation of BMP signaling pathway Source: UniProtKB
  • negative regulation of endopeptidase activity Source: BHF-UCL
  • neural tube closure Source: UniProtKB
  • neuron projection arborization Source: UniProtKB
  • outflow tract septum morphogenesis Source: UniProtKB
  • positive regulation of neurogenesis Source: UniProtKB
  • positive regulation of oligodendrocyte progenitor proliferation Source: UniProtKB
  • pulmonary artery morphogenesis Source: UniProtKB
  • receptor-mediated endocytosis Source: UniProtKB
  • response to drug Source: RGD
  • response to retinoic acid Source: RGD
  • response to vitamin D Source: RGD
  • response to X-ray Source: RGD
  • secondary heart field specification Source: UniProtKB
  • sensory perception of sound Source: UniProtKB
  • transcytosis Source: UniProtKB
  • vagina development Source: UniProtKB
  • ventricular compact myocardium morphogenesis Source: UniProtKB
  • ventricular septum development Source: RGD
  • vitamin metabolic process Source: RGD

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 2
Short name:
LRP-2
Alternative name(s):
Glycoprotein 3301 Publication
Short name:
gp3301 Publication
Megalin
Gene namesi
Name:Lrp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68407. 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 – 4425ExtracellularSequence analysisAdd BLAST4400
Transmembranei4426 – 4446HelicalSequence analysisAdd BLAST21
Topological domaini4447 – 4660CytoplasmicSequence analysisAdd BLAST214

Keywords - Cellular componenti

Cell membrane, Cell projection, Coated pit, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4527Y → C: Reduced interaction with ARH and dynein. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000001732226 – 4660Low-density lipoprotein receptor-related protein 2Add BLAST4635

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 bondi142 ↔ 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
Glycosylationi259N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi265 ↔ 278PROSITE-ProRule annotation
Disulfide bondi272 ↔ 291PROSITE-ProRule annotation
Disulfide bondi285 ↔ 306PROSITE-ProRule annotation
Glycosylationi299N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi340N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi351 ↔ 361PROSITE-ProRule annotation
Disulfide bondi357 ↔ 370PROSITE-ProRule annotation
Glycosylationi462N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi657N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi865N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1025 ↔ 1037PROSITE-ProRule annotation
Disulfide bondi1032 ↔ 1050PROSITE-ProRule annotation
Disulfide bondi1044 ↔ 1059PROSITE-ProRule annotation
Glycosylationi1063N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1066 ↔ 1079PROSITE-ProRule annotation
Disulfide bondi1073 ↔ 1092PROSITE-ProRule annotation
Disulfide bondi1086 ↔ 1101PROSITE-ProRule annotation
Disulfide bondi1110 ↔ 1122PROSITE-ProRule annotation
Disulfide bondi1117 ↔ 1135PROSITE-ProRule annotation
Disulfide bondi1129 ↔ 1144PROSITE-ProRule annotation
Disulfide bondi1150 ↔ 1162PROSITE-ProRule annotation
Disulfide bondi1157 ↔ 1175PROSITE-ProRule annotation
Disulfide bondi1169 ↔ 1184PROSITE-ProRule annotation
Glycosylationi1187N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1188 ↔ 1201PROSITE-ProRule annotation1 Publication
Disulfide bondi1195 ↔ 1214PROSITE-ProRule annotation1 Publication
Disulfide bondi1208 ↔ 1223PROSITE-ProRule annotation1 Publication
Disulfide bondi1231 ↔ 1244PROSITE-ProRule annotation
Disulfide bondi1238 ↔ 1257PROSITE-ProRule annotation
Disulfide bondi1251 ↔ 1267PROSITE-ProRule annotation
Disulfide bondi1272 ↔ 1284PROSITE-ProRule annotation
Disulfide bondi1279 ↔ 1297PROSITE-ProRule annotation
Disulfide bondi1291 ↔ 1306PROSITE-ProRule annotation
Disulfide bondi1313 ↔ 1326PROSITE-ProRule annotation
Disulfide bondi1320 ↔ 1339PROSITE-ProRule annotation
Glycosylationi1328N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1333 ↔ 1349PROSITE-ProRule annotation
Glycosylationi1341N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1354 ↔ 1365PROSITE-ProRule annotation
Disulfide bondi1361 ↔ 1374PROSITE-ProRule annotation
Disulfide bondi1376 ↔ 1389PROSITE-ProRule annotation
Glycosylationi1384N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1395 ↔ 1405PROSITE-ProRule annotation
Disulfide bondi1401 ↔ 1414PROSITE-ProRule annotation
Disulfide bondi1416 ↔ 1429PROSITE-ProRule annotation
Glycosylationi1451N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1497N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1551N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1676N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1733N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1811N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2134N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2178N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2225N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2396N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2488N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2548N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2701 ↔ 2713PROSITE-ProRule annotation
Disulfide bondi2708 ↔ 2726PROSITE-ProRule annotation
Disulfide bondi2720 ↔ 2737PROSITE-ProRule annotation
Disulfide bondi2742 ↔ 2754PROSITE-ProRule annotation
Disulfide bondi2749 ↔ 2767PROSITE-ProRule annotation
Disulfide bondi2761 ↔ 2776PROSITE-ProRule annotation
Disulfide bondi2781 ↔ 2794PROSITE-ProRule annotation
Glycosylationi2782N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2789 ↔ 2807PROSITE-ProRule annotation
Disulfide bondi2801 ↔ 2818PROSITE-ProRule annotation
Glycosylationi2810N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2823 ↔ 2836PROSITE-ProRule annotation
Disulfide bondi2830 ↔ 2849PROSITE-ProRule annotation
Disulfide bondi2843 ↔ 2860PROSITE-ProRule annotation
Disulfide bondi2865 ↔ 2878PROSITE-ProRule annotation
Disulfide bondi2872 ↔ 2891PROSITE-ProRule annotation
Disulfide bondi2885 ↔ 2901PROSITE-ProRule annotation
Disulfide bondi2908 ↔ 2920PROSITE-ProRule annotation
Disulfide bondi2915 ↔ 2933PROSITE-ProRule annotation
Disulfide bondi2927 ↔ 2945PROSITE-ProRule annotation
Glycosylationi2949N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2950 ↔ 2967PROSITE-ProRule annotation
Disulfide bondi2957 ↔ 2980PROSITE-ProRule annotation
Disulfide bondi2974 ↔ 2990PROSITE-ProRule annotation
Glycosylationi2989N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2995 ↔ 3007PROSITE-ProRule annotation
Disulfide bondi3002 ↔ 3020PROSITE-ProRule annotation
Disulfide bondi3014 ↔ 3029PROSITE-ProRule annotation
Disulfide bondi3034 ↔ 3046PROSITE-ProRule annotation
Disulfide bondi3041 ↔ 3059PROSITE-ProRule annotation
Disulfide bondi3053 ↔ 3070PROSITE-ProRule annotation
Disulfide bondi3077 ↔ 3089PROSITE-ProRule annotation
Disulfide bondi3084 ↔ 3102PROSITE-ProRule annotation
Disulfide bondi3096 ↔ 3111PROSITE-ProRule annotation
Disulfide bondi3116 ↔ 3128PROSITE-ProRule annotation
Disulfide bondi3124 ↔ 3137PROSITE-ProRule annotation
Glycosylationi3127N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3139 ↔ 3152PROSITE-ProRule annotation
Disulfide bondi3158 ↔ 3169PROSITE-ProRule annotation
Disulfide bondi3165 ↔ 3178PROSITE-ProRule annotation
Disulfide bondi3180 ↔ 3193PROSITE-ProRule annotation
Glycosylationi3213N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3259N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3317N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3357N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3448N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3514 ↔ 3527PROSITE-ProRule annotation
Disulfide bondi3521 ↔ 3540PROSITE-ProRule annotation
Disulfide bondi3534 ↔ 3550PROSITE-ProRule annotation
Disulfide bondi3555 ↔ 3567PROSITE-ProRule annotation
Disulfide bondi3562 ↔ 3580PROSITE-ProRule annotation
Glycosylationi3566N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3574 ↔ 3591PROSITE-ProRule annotation
Disulfide bondi3596 ↔ 3608PROSITE-ProRule annotation
Disulfide bondi3603 ↔ 3621PROSITE-ProRule annotation
Disulfide bondi3615 ↔ 3632PROSITE-ProRule annotation
Disulfide bondi3637 ↔ 3649PROSITE-ProRule annotation
Disulfide bondi3644 ↔ 3662PROSITE-ProRule annotation
Disulfide bondi3656 ↔ 3673PROSITE-ProRule annotation
Disulfide bondi3680 ↔ 3694PROSITE-ProRule annotation
Glycosylationi3682N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3688 ↔ 3707PROSITE-ProRule annotation
Disulfide bondi3701 ↔ 3716PROSITE-ProRule annotation
Disulfide bondi3721 ↔ 3734PROSITE-ProRule annotation
Disulfide bondi3729 ↔ 3747PROSITE-ProRule annotation
Disulfide bondi3741 ↔ 3756PROSITE-ProRule annotation
Disulfide bondi3761 ↔ 3773PROSITE-ProRule annotation
Disulfide bondi3768 ↔ 3786PROSITE-ProRule annotation
Disulfide bondi3780 ↔ 3795PROSITE-ProRule annotation
Disulfide bondi3800 ↔ 3812PROSITE-ProRule annotation
Disulfide bondi3807 ↔ 3825PROSITE-ProRule annotation
Disulfide bondi3819 ↔ 3834PROSITE-ProRule annotation
Glycosylationi3840N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3844 ↔ 3856PROSITE-ProRule annotation
Disulfide bondi3851 ↔ 3869PROSITE-ProRule annotation
Disulfide bondi3863 ↔ 3880PROSITE-ProRule annotation
Disulfide bondi3885 ↔ 3898PROSITE-ProRule annotation
Disulfide bondi3893 ↔ 3911PROSITE-ProRule annotation
Disulfide bondi3905 ↔ 3922PROSITE-ProRule annotation
Disulfide bondi3930 ↔ 3942PROSITE-ProRule annotation
Disulfide bondi3937 ↔ 3955PROSITE-ProRule annotation
Disulfide bondi3949 ↔ 3964PROSITE-ProRule annotation
Glycosylationi3969N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3972 ↔ 3981PROSITE-ProRule annotation
Disulfide bondi3977 ↔ 3991PROSITE-ProRule annotation
Glycosylationi3980N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4013 ↔ 4023PROSITE-ProRule annotation
Disulfide bondi4019 ↔ 4032PROSITE-ProRule annotation
Disulfide bondi4034 ↔ 4049PROSITE-ProRule annotation
Glycosylationi4070N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi4329N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4383 ↔ 4391PROSITE-ProRule annotation
Disulfide bondi4385 ↔ 4401PROSITE-ProRule annotation
Disulfide bondi4403 ↔ 4412PROSITE-ProRule annotation
Modified residuei4464PhosphoserineCombined sources1
Modified residuei4467PhosphoserineBy similarity1
Modified residuei4577PhosphoserineCombined sources1
Modified residuei4624PhosphoserineCombined sources1
Modified residuei4637PhosphothreonineBy similarity1
Modified residuei4658PhosphoserineCombined sources1

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.1 Publication
N-glycosylation is required for ligand binding.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP98158.
PRIDEiP98158.

PTM databases

iPTMnetiP98158.
PhosphoSitePlusiP98158.
UniCarbKBiP98158.

Expressioni

Tissue specificityi

In the inner ear, expressed in the lumen of the endolymphatic sac where it localizes to macrophage-like cells as well as to mitochondria-rich and ribosome-rich epithelial cells (at protein level) (PubMed:17063000). In the inner ear, expressed in marginal cells of the stria vascularis, epithelial cells at the spiral prominence, epithelial cells of Reissner's membrane facing the cochlear duct, and Kolliker's organ (at protein level) (PubMed:19202329). Expressed in the choroid plexus epithelium in the brain (at protein level) (PubMed:17324488). In the brain, also expressed in astrocytes (at protein level) (PubMed:18466341). Expression also detected in epithelial cells of the kidney glomerulus and proximal tubule, lung, epididymis and yolk sac (PubMed:7510321).5 Publications

Developmental stagei

In the brain, expression is high after birth and gradually decreases from postnatal day 4 until the end of the first postnatal week.1 Publication

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. Forms a multimeric complex together with LRPAP1 (PubMed:1400426). Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (PubMed:22649097). Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif (By similarity). Interacts with MB (PubMed:12724130). 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 (PubMed:17324488). Interacts with ALB (PubMed:18466341). Interacts with the antiapoptotic protein BIRC5/survivin (By similarity). Interacts with matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (PubMed:28659595). 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 (PubMed:23836931). 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 similarity9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • chaperone binding Source: RGD
  • hemoglobin binding Source: RGD
  • low-density lipoprotein particle receptor binding Source: RGD
  • PDZ domain binding Source: RGD
  • protein complex binding Source: RGD
  • SH3 domain binding Source: UniProtKB-KW
  • steroid hormone receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi247894. 2 interactors.
CORUMiP98158.
DIPiDIP-44866N.
IntActiP98158. 6 interactors.
MINTiMINT-1541513.
STRINGi10116.ENSRNOP00000066394.

Structurei

Secondary structure

14660
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1190 – 1194Combined sources5
Beta strandi1196 – 1199Combined sources4
Helixi1204 – 1206Combined sources3
Beta strandi1207 – 1211Combined sources5
Beta strandi1214 – 1217Combined sources4
Helixi1218 – 1221Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I1PNMR-A1185-1229[»]
3V2OX-ray1.89B4448-4466[»]
3V2XX-ray1.85B4455-4465[»]
ProteinModelPortaliP98158.
SMRiP98158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98158.

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
Domaini141 – 180LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST40
Domaini182 – 218LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST37
Domaini221 – 257LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST37
Domaini264 – 307LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST44
Domaini347 – 382EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Repeati435 – 477LDL-receptor class B 1PROSITE-ProRule annotationAdd BLAST43
Repeati478 – 520LDL-receptor class B 2PROSITE-ProRule annotationAdd BLAST43
Repeati521 – 567LDL-receptor class B 3PROSITE-ProRule annotationAdd BLAST47
Repeati568 – 612LDL-receptor class B 4PROSITE-ProRule annotationAdd BLAST45
Repeati752 – 794LDL-receptor class B 5PROSITE-ProRule annotationAdd BLAST43
Repeati795 – 836LDL-receptor class B 6PROSITE-ProRule annotationAdd BLAST42
Repeati837 – 880LDL-receptor class B 7PROSITE-ProRule annotationAdd BLAST44
Repeati881 – 924LDL-receptor class B 8PROSITE-ProRule annotationAdd BLAST44
Domaini1024 – 1060LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST37
Domaini1065 – 1102LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST38
Domaini1109 – 1145LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST37
Domaini1149 – 1185LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST37
Domaini1187 – 1224LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST38
Domaini1230 – 1268LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST39
Domaini1271 – 1307LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST37
Domaini1312 – 1350LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST39
Domaini1350 – 1390EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini1391 – 1430EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Repeati1479 – 1521LDL-receptor class B 9PROSITE-ProRule annotationAdd BLAST43
Repeati1522 – 1564LDL-receptor class B 10PROSITE-ProRule annotationAdd BLAST43
Repeati1567 – 1610LDL-receptor class B 11PROSITE-ProRule annotationAdd BLAST44
Repeati1611 – 1655LDL-receptor class B 12PROSITE-ProRule annotationAdd BLAST45
Repeati1656 – 1696LDL-receptor class B 13PROSITE-ProRule annotationAdd BLAST41
Repeati1791 – 1833LDL-receptor class B 14PROSITE-ProRule annotationAdd BLAST43
Repeati1834 – 1883LDL-receptor class B 15PROSITE-ProRule annotationAdd BLAST50
Repeati1884 – 1931LDL-receptor class B 16PROSITE-ProRule annotationAdd BLAST48
Repeati1932 – 1973LDL-receptor class B 17PROSITE-ProRule annotationAdd BLAST42
Repeati1974 – 2014LDL-receptor class B 18PROSITE-ProRule annotationAdd BLAST41
Repeati2108 – 2157LDL-receptor class B 19PROSITE-ProRule annotationAdd BLAST50
Repeati2158 – 2202LDL-receptor class B 20PROSITE-ProRule annotationAdd BLAST45
Repeati2203 – 2246LDL-receptor class B 21PROSITE-ProRule annotationAdd BLAST44
Repeati2247 – 2290LDL-receptor class B 22PROSITE-ProRule annotationAdd BLAST44
Repeati2432 – 2478LDL-receptor class B 23PROSITE-ProRule annotationAdd BLAST47
Repeati2479 – 2519LDL-receptor class B 24PROSITE-ProRule annotationAdd BLAST41
Repeati2520 – 2563LDL-receptor class B 25PROSITE-ProRule annotationAdd BLAST44
Repeati2564 – 2605LDL-receptor class B 26PROSITE-ProRule annotationAdd BLAST42
Repeati2606 – 2647LDL-receptor class B 27PROSITE-ProRule annotationAdd BLAST42
Domaini2700 – 2738LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST39
Domaini2741 – 2777LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST37
Domaini2780 – 2819LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST40
Domaini2822 – 2861LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST40
Domaini2864 – 2902LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST39
Domaini2907 – 2946LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST40
Domaini2949 – 2991LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST43
Domaini2994 – 3030LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST37
Domaini3033 – 3071LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST39
Domaini3076 – 3112LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST37
Domaini3112 – 3153EGF-like 4PROSITE-ProRule annotationAdd BLAST42
Domaini3154 – 3194EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3241 – 3283LDL-receptor class B 28PROSITE-ProRule annotationAdd BLAST43
Repeati3284 – 3326LDL-receptor class B 29PROSITE-ProRule annotationAdd BLAST43
Repeati3335 – 3378LDL-receptor class B 30PROSITE-ProRule annotationAdd BLAST44
Repeati3379 – 3421LDL-receptor class B 31PROSITE-ProRule annotationAdd BLAST43
Repeati3422 – 3462LDL-receptor class B 32PROSITE-ProRule annotationAdd BLAST41
Domaini3513 – 3551LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST39
Domaini3554 – 3592LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST39
Domaini3595 – 3633LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST39
Domaini3636 – 3674LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST39
Domaini3679 – 3717LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST39
Domaini3720 – 3757LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST38
Domaini3760 – 3796LDL-receptor class A 32PROSITE-ProRule annotationAdd BLAST37
Domaini3799 – 3835LDL-receptor class A 33PROSITE-ProRule annotationAdd BLAST37
Domaini3843 – 3881LDL-receptor class A 34PROSITE-ProRule annotationAdd BLAST39
Domaini3884 – 3923LDL-receptor class A 35PROSITE-ProRule annotationAdd BLAST40
Domaini3929 – 3965LDL-receptor class A 36PROSITE-ProRule annotationAdd BLAST37
Domaini3968 – 4003EGF-like 6PROSITE-ProRule annotationAdd BLAST36
Domaini4009 – 4050EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Repeati4156 – 4198LDL-receptor class B 33PROSITE-ProRule annotationAdd BLAST43
Repeati4199 – 4242LDL-receptor class B 34PROSITE-ProRule annotationAdd BLAST44
Repeati4244 – 4285LDL-receptor class B 35PROSITE-ProRule annotationAdd BLAST42
Domaini4379 – 4413EGF-like 8PROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4597 – 4610Interaction with DAB2By similarityAdd BLAST14

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi4454 – 4463SH3-bindingSequence analysis10
Motifi4457 – 4462PxLPxI/L motif 1; mediates interaction with ANKRA21 Publication6
Motifi4460 – 4465PxLPxI/L motif 2; mediates interaction with ANKRA21 Publication6
Motifi4522 – 4527Endocytosis signalSequence analysis6
Motifi4603 – 4606NPXY motif4
Motifi4606 – 4609SH2-bindingSequence analysis4
Motifi4619 – 4630SH3-bindingSequence analysisAdd BLAST12

Domaini

Two overlapping PxLPxI/L motifs mediate interaction with ankyrin repeats of ANKRA2.1 Publication
The cytoplasmic domain is required for sorting to the apical cell membrane.1 Publication

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.
HOGENOMiHOG000231853.
HOVERGENiHBG097941.
InParanoidiP98158.
KOiK06233.
PhylomeDBiP98158.

Family and domain databases

CDDicd00112. LDLa. 36 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.
PfamiView protein in Pfam
PF12662. cEGF. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 35 hits.
PF00058. Ldl_recept_b. 14 hits.
PRINTSiPR00261. LDLRECEPTOR.
SMARTiView protein in SMART
SM00181. EGF. 22 hits.
SM00179. EGF_CA. 9 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 36 hits.
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57424. SSF57424. 35 hits.
PROSITEiView protein in PROSITE
PS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 8 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.

P98158-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERGAAAAAW MLLLAIAACL EPVSSQECGS GNFRCDNGYC IPASWRCDGT
60 70 80 90 100
RDCLDDTDEI GCPPRSCESG LFLCPAEGTC IPSSWVCDED KDCSDGADEQ
110 120 130 140 150
QNCAGTTCSA QQMTCSNGQC IPSEYRCDHV SDCPDGSDER NCHYPTCDQL
160 170 180 190 200
TCANGACYNT SQRCDQKVDC RDSSDEANCT TLCSQKEFEC GSGECILRAY
210 220 230 240 250
VCDHDNDCED NSDERNCNYD TCGGHQFTCS NGQCINQNWV CDGDDDCQDS
260 270 280 290 300
GDEDGCESNQ SHHRCYPREW ACPGSGRCIS IDKVCDGVPD CPEGDDENNV
310 320 330 340 350
TSGRTCGMGV CSVLNCEYQC HQTPFGGECF CPPGHIINSN DSRTCIDFDD
360 370 380 390 400
CQIWGICDQK CENRQGRHQC LCEEGYILER GQHCKSSDSF SAASVIFSNG
410 420 430 440 450
RDLLVGDLHG RNFRILAESK NRGMVMGVDF HYQKHRVFWT DPMQEKVFST
460 470 480 490 500
DINGLNTQEI LNVSVDTPEN LAVDWINNKL YLVETKVNRI DVVNLEGNQR
510 520 530 540 550
VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA FMDGSNRKDL
560 570 580 590 600
VTTKVGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV
610 620 630 640 650
PHPFGISLFE EHVFFTDWTK MAVMKASKFT ETNPQVYHQS SLRPHGVTVY
660 670 680 690 700
HALRQPNATN PCGSNNGGCA QVCVLSHRTD NGGLGYRCKC EFGFELDDDE
710 720 730 740 750
HRCVAVKNFL LFSSKTAVRG IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ
760 770 780 790 800
HSTVFYSDLS KDIIYKQKID GTGKEVITAN RLESVECLTF DWISRNLYWT
810 820 830 840 850
DGGLKSVTVL RLADKSRRQI ISNLNNPRSI VVHPTAGYMF LSDWFRPAKI
860 870 880 890 900
MRAWSDGSHL MPIVNTSLGW PNGLAIDWSA SRLYWVDAFF DKIEHSTLDG
910 920 930 940 950
LDRKRLGHVD QMTHPFGLTV FKDNVFITDW RLGAIIRVRK SDGGDMTVIR
960 970 980 990 1000
RGISSVMHVK AYDADLQTGS NYCSQTTHAN GDCSHFCFPV PNFQRVCGCP
1010 1020 1030 1040 1050
YGMKLQRDQM TCEGDPAREP PTQQCGSLSF PCNNGKCVPS FFRCDGVDDC
1060 1070 1080 1090 1100
HDNSDEHQCG VFNNTCSPSA FACVRGGQCI PGQWHCDRQN DCLDGSDEQN
1110 1120 1130 1140 1150
CPTHATSSTC PSTSFTCDNH VCIPKDWVCD TDNDCSDGSD EKNCQASGTC
1160 1170 1180 1190 1200
QPTQFRCPDH RCISPLYVCD GDKDCADGSD EAGCVLNCTS AQFKCADGSS
1210 1220 1230 1240 1250
CINSRYRCDG VYDCRDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE
1260 1270 1280 1290 1300
CDGHPDCIHG SDEHTGCVPK TCSPTHFLCD NGNCIYKAWI CDGDNDCRDM
1310 1320 1330 1340 1350
SDEKDCPTQP FHCPSTQWQC PGYSTCINLS ALCDGVFDCP NGTDESPLCN
1360 1370 1380 1390 1400
QDSCSHFNGG CTHQCMQGPF GATCLCPLGY QLANDTKTCE DINECDIPGF
1410 1420 1430 1440 1450
CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTGSENPLLV VASRDKIIVD
1460 1470 1480 1490 1500
NITAHTHNLY SLVQDVSFVV ALDFDSVTGR VFWSDLLQGK TWSVFQNGTD
1510 1520 1530 1540 1550
KRVVHDSGLS VTEMIAVDWI GRNLYWTDYA LETIEVSKID GSHRTVLISK
1560 1570 1580 1590 1600
NVTKPRGLAL DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW
1610 1620 1630 1640 1650
PCGLSIDYPN RLIYFMDAYL DYIEFCDYDG HNRRQVIASD LVLHHPHALT
1660 1670 1680 1690 1700
LFEDFVYWTD RGTRQVMQAN KWHGGNQSVV MYSVHQPLGI TAIHPSRQPP
1710 1720 1730 1740 1750
SRNPCASASC SHLCLLSAQA PRHYSCACPS GWNLSDDSVN CVRGDQPFLM
1760 1770 1780 1790 1800
SVRDNIIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG
1810 1820 1830 1840 1850
EIHRVKTDGS NRTVFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT
1860 1870 1880 1890 1900
LKGDTRYGKT LIANDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK
1910 1920 1930 1940 1950
IASANMDGTS LKILFTGNLQ HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD
1960 1970 1980 1990 2000
GTERMILVHH LAHPWGLVVY GSFLYYSDEQ YEVIERVDKS SGNNKVVLRD
2010 2020 2030 2040 2050
NVPYLRGLRV YHRRNAADSS NGCSNNPNAC QQICLPVPGG MFSCACASGF
2060 2070 2080 2090 2100
KLSPDGRSCS PYNSFMVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH
2110 2120 2130 2140 2150
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP DGSNFTNVVT YGIGANGIRG
2160 2170 2180 2190 2200
VALDWAAGNL YFTNAFVYET LIEVLRINTT YRRVLLKVSV DMPRHIIVDP
2210 2220 2230 2240 2250
KHRYLFWADY GQKPKIERSF LDCTNRTVLV SEGIVTPRGL AMDHDTGYIY
2260 2270 2280 2290 2300
WVDDSLDLIA RIHLDGGESQ VVRYGSRYPT PYGITVFGES IIWVDRNLKK
2310 2320 2330 2340 2350
VFQASKQPGN TDPPVVIRDK INLLRDVTIF DEHAQPLSPA ELNNNPCLQS
2360 2370 2380 2390 2400
NGGCSHFCFA LPELPTPRCG CAFGTLGNDG KSCATSQEDF LIYSLNNSLR
2410 2420 2430 2440 2450
SLHFDPRDHS LPFQVISVAG TAIALDYDRR NNRIFFTQKL NSLRGQISYV
2460 2470 2480 2490 2500
SLYSGSSSPT VLLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN
2510 2520 2530 2540 2550
RAVIARVSKP RAIVLDPCRG YMYWTDWGTN AKIERATLGG NFRVPIVNTS
2560 2570 2580 2590 2600
LVWPNGLALD LETDLLYWAD ASLQKIERST LTGTNREVVV STAFHSFGLT
2610 2620 2630 2640 2650
VYGQYIYWTD LYTRKIYRAN KYDGSDLVAM TTRLPTQPSG ISTVVKTQRQ
2660 2670 2680 2690 2700
QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGNWYLANDN KYCVVDTGTR
2710 2720 2730 2740 2750
CNQLQFTCLN GHCINQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCG
2760 2770 2780 2790 2800
NGRCVPYHYR CDYYNDCGDN SDEAGCLFRN CNSTTEFTCS NGRCIPLSYV
2810 2820 2830 2840 2850
CNGINNCHDN DTSDEKNCPP HTCPPDFTKC QTTNICVPRA FLCDGDNDCG
2860 2870 2880 2890 2900
DGSDENPIYC ASHTCRSNEF QCLSPQRCIP SYWFCDGEAD CADGSDEPDT
2910 2920 2930 2940 2950
CGHSVNTCRA SQFQCDNGRC ISGNWVCDGD NDCGDMSDED QRHHCELQNC
2960 2970 2980 2990 3000
SSTQFTCVNS RPPNRRCIPQ YWVCDGDADC SDALDELQNC TMRTCSAGEF
3010 3020 3030 3040 3050
SCANGRCVRQ SFRCDRRNDC GDYSDERGCS YPPCHANQFT CQNGRCIPRF
3060 3070 3080 3090 3100
FVCDEDNDCG DGSDEQEHLC HTPEPTCPLH QFRCDNGHCI EMGRVCNHVD
3110 3120 3130 3140 3150
DCSDNSDEKG CGINECLDSS ISRCDHNCTD TITSFYCSCL PGYKLMSDKR
3160 3170 3180 3190 3200
SCVDIDECKE SPQLCSQKCE NVVGSYICKC APGYIREPDG KSCRQNSNIE
3210 3220 3230 3240 3250
PYLIFSNRYY IRNLTTDGSS YSLILQGLGN VVALDFDRVE KRLYWIDAEK
3260 3270 3280 3290 3300
QIIERMFLNK TNRETIINHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD
3310 3320 3330 3340 3350
LEGRHRKMIA QHCVDANNTF CFEHPRGIVL HPQRGHVYWA DWGVHAYIGR
3360 3370 3380 3390 3400
IGMDGTNKSV IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH
3410 3420 3430 3440 3450
RHTVYDGSLP HPFALTIFED TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT
3460 3470 3480 3490 3500
HKPFDIHVYH PYRQPIMSNP CGTNNGGCSH LCLIKAGGRG FTCACPDDFQ
3510 3520 3530 3540 3550
TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC SDGSDEPDLC
3560 3570 3580 3590 3600
PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCESNE
3610 3620 3630 3640 3650
WQCANKRCIP QSWQCDSVND CLDNSDEDTS HCASRTCRPG QFKCNNGRCI
3660 3670 3680 3690 3700
PQSWKCDVDN DCGDYSDEPI DECTTAAYNC DNHTEFSCKT NYRCIPQWAV
3710 3720 3730 3740 3750
CNGFDDCRDN SDEQGCESVP CHPSGDFRCA NHHCIPLRWK CDGTDDCGDN
3760 3770 3780 3790 3800
SDEENCVPRE CSESEFRCAD QQCIPSRWVC DQENDCGDNS DERDCEMKTC
3810 3820 3830 3840 3850
HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN GTYCPAAMFE
3860 3870 3880 3890 3900
CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNIPCESPQR FRCDNSRCVY
3910 3920 3930 3940 3950
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCISQHYVCD
3960 3970 3980 3990 4000
NVNDCGDLSD ETGCNLGDNR TCAENICEQN CTQLSSGGFI CSCRPGFKPS
4010 4020 4030 4040 4050
TSDKNSCQDI NECEEFGICP QSCRNSKGSY ECFCVDGFKS MSTHYGERCA
4060 4070 4080 4090 4100
ADGSPPLLLL PENVRIRKYN TSSEKFSEYL EEEEHIQTID YDWDPEHIGL
4110 4120 4130 4140 4150
SVVYYTVLAQ GSQFGAIKRA YIPNFESGSN NPIREVDLGL KYLMQPDGLA
4160 4170 4180 4190 4200
VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL
4210 4220 4230 4240 4250
MFWTDQGKQP KIESAWMNGE HRSVLVSENL GWPNGLSIDY LNDDRVYWSD
4260 4270 4280 4290 4300
SKEDVIEAIK YDGTDRRLII NEAMKPFSLD IFEDKLYWVA KEKGEVWRQN
4310 4320 4330 4340 4350
KFGKENKEKV LVVNPWLTQV RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG
4360 4370 4380 4390 4400
YSCACPQGSD FVTGSTVQCD AASELPVTMP PPCRCMHGGN CYFDENELPK
4410 4420 4430 4440 4450
CKCSSGYSGE YCEVGLSRGI PPGTTMAVLL TFVIVIIVGA LVLVGLFHYR
4460 4470 4480 4490 4500
KTGSLLPTLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI
4510 4520 4530 4540 4550
IDRSMAMNEH FVMEVGKQPV IFENPMYAAK DNTSKVALAV QGPSTGAQVT
4560 4570 4580 4590 4600
VPENVENQNY GRPIDPSEIV PEPKPASPGA DEIQGKKWNI FKRKPKQTTN
4610 4620 4630 4640 4650
FENPIYAEMD SEVKDAVAVA PPPSPSLPAK ASKRNLTPGY TATEDTFKDT
4660
ANLVKEDSDV
Length:4,660
Mass (Da):519,276
Last modified:October 1, 1996 - v1
Checksum:iE2A0CFD23D0923C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34049 mRNA. Translation: AAA51369.1.
PIRiT42737.
RefSeqiNP_110454.1. NM_030827.1.
UniGeneiRn.26430.

Genome annotation databases

GeneIDi29216.
KEGGirno:29216.
UCSCiRGD:68407. rat.

Similar proteinsi

Entry informationi

Entry nameiLRP2_RAT
AccessioniPrimary (citable) accession number: P98158
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 22, 2017
This is version 153 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families