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Protein

Low-density lipoprotein receptor-related protein 2

Gene

Lrp2

Organism
Mus musculus (Mouse)
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 (PubMed:10766831). 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 (PubMed:22841573). 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 (PubMed:24825475). 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 (PubMed:10052453). Mediates renal uptake of metallothionein-bound heavy metals (By similarity). 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 (PubMed:18174160). 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 (PubMed:28659595). 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 (PubMed:15623804). 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 (PubMed:22340494). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (PubMed:24639464). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (PubMed:20460439). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity). Involved in neurite branching (PubMed:20637285). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (PubMed:22354480). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (PubMed:26439398). 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 (By similarity). Also mediates endocytosis of angiotensin 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 (PubMed:26822476). Required for normal hearing, possibly through interaction with estrogen in the inner ear (PubMed:17846082).By similarity19 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 oxygenBy similarity1
Metal bindingi1209CalciumBy similarity1
Metal bindingi1211Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1213CalciumBy similarity1
Metal bindingi1219CalciumBy similarity1
Metal bindingi1220CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

  • aorta development Source: MGI
  • cell proliferation Source: MGI
  • coronary artery morphogenesis Source: UniProtKB
  • coronary vasculature development Source: MGI
  • folic acid import across plasma membrane Source: UniProtKB
  • forebrain development Source: MGI
  • heart development Source: MGI
  • male gonad development Source: UniProtKB
  • metal ion transport Source: UniProtKB
  • negative regulation of BMP signaling pathway Source: UniProtKB
  • 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
  • secondary heart field specification Source: UniProtKB
  • sensory perception of sound Source: UniProtKB
  • vagina development Source: UniProtKB
  • ventricular compact myocardium morphogenesis Source: UniProtKB
  • ventricular septum development Source: MGI
  • vitamin metabolic process Source: MGI

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-196791. Vitamin D (calciferol) metabolism.
R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-MMU-8856828. Clathrin-mediated endocytosis.
R-MMU-975634. Retinoid metabolism and transport.

Protein family/group databases

TCDBi9.B.87.1.1. the selenoprotein p receptor (selp-receptor) family.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:95794. 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

Disruption phenotypei

Severe facial dysgenesis and impaired forebrain development around mid-gestation, absence of Shh expression and decreased cell proliferation in the ventral neural tube, and aberrant expression of morphogens Fgf8 and Bmp4 (PubMed:15623804). Reduced expression of homeobox protein Six3 at E8.0 in the prospective forebrain and impaired Shh expression at the ventral midline with resulting midline formation defects and holoprosencephaly (PubMed:22340494). At E9.5, loss of Shh in the ventral anterior diencephalon and increased Bmp4 expression in the dorsal forebrain (PubMed:22340494). Increased Bmp4 expression and impaired proliferation of neural precursor cells in the subependymal zone of the brain which results in decreased numbers of neuroblasts reaching the olfactory bulb (PubMed:20460439). Compound heterozygotes display enlarged and exophthalmic eyes with thinning of the retina (PubMed:26439398). Severe cardiovascular abnormalities including aortic arch anomalies, persistent truncus arteriosus with coronary artery anomalies, ventricular septal defects, overriding of the tricuspid valve, marked thinning of the ventricular myocardium, and abnormal positioning of the neural crest cells and second heart field (PubMed:26822476). Impaired endocytosis of folate bound to the folate receptor FOLR1, reduced folate levels in embryos and impaired closure of the rostral neural tube (PubMed:24639464). High lethality at and after birth with survivors showing profound hearing loss, elevated lipofuscin granule levels and irregular apical surfaces in marginal cells of the stria vascularis, complete loss of potassium ion channel KCQN1 in basal and midbasal cochlear turns, and reduced estrogen uptake in the stria vascularis (PubMed:17846082). Survivors also display severe vitamin D deficiency and bone formation defects (PubMed:10052453). Failure of the vaginal cavity to open after birth in females and impaired testis descent in males with the left testis poorly developed and severely retarded in size (PubMed:16143106). Conditional knockout in the kidney results in reduced expression of CUBN in kidney cells and little or no uptake of myoglobin (PubMed:12724130). It also results in reduced uptake of Cst3 by kidney proximal tubule cells (PubMed:17462596). In addition, it causes pronounced urinary excretion of Apom, Birc5/survivin, and Mmp2 together with Timp1 (PubMed:16099815, PubMed:23825075, PubMed:28659595).14 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000030984526 – 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 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 bondi265 ↔ 278PROSITE-ProRule annotation
Disulfide bondi272 ↔ 291PROSITE-ProRule annotation
Disulfide bondi285 ↔ 306PROSITE-ProRule annotation
Glycosylationi299N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi340N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi387N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi399N-linked (GlcNAc...) asparagine; atypical1 Publication1
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 annotation
Disulfide bondi1195 ↔ 1214PROSITE-ProRule annotation
Disulfide bondi1208 ↔ 1223PROSITE-ProRule annotation
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
Glycosylationi2131N-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
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 residuei4467PhosphoserineCombined sources1
Modified residuei4577PhosphoserineCombined sources1
Modified residuei4624PhosphoserineBy similarity1
Modified residuei4637PhosphothreonineCombined sources1
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.By similarity
N-glycosylation is required for ligand binding. Contains core-fucosylated N-glycans in kidney proximal convoluted tubules (PCTs) and hybrid-type N-glycans in proximal straight tubules (PSTs). Interacts with ligands in a glycoform-dependent manner. Retinol-binding protein and the vitamin D carrier GC/DBP are endocytosed primarily by PCTs, albumin is endocytosed equally by PCTs and PSTs, and the aminoglycoside kanamycin is endocytosed primarily by PSTs.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiA2ARV4.
PaxDbiA2ARV4.
PeptideAtlasiA2ARV4.
PRIDEiA2ARV4.

PTM databases

iPTMnetiA2ARV4.
PhosphoSitePlusiA2ARV4.

Expressioni

Tissue specificityi

In the inner ear, strongly expressed in the marginal cells of the stria vascularis (at protein level) (PubMed:17846082). In the female reproductive tract, expressed on the luminal side of the uterine epithelium (at protein level) (PubMed:16143106). In the adult brain, expressed in ependymal cells of the lateral ventricles where expression is restricted to the ependyma that faces the stem cell niche (at protein level) (PubMed:20460439). Expressed in neurons throughout the brain including in the hippocampus, limbic cortices and cerebellum (at protein level) (PubMed:20637285). In the developing optic nerve, expressed exclusively in astrocytes at E14.5, E16.5 and E18.5 (at protein level) (PubMed:22354480).5 Publications

Developmental stagei

In the developing optic nerve, more strongly expressed at E14.5 and E16.5 than at E18.5 (at protein level) (PubMed:22354480). In the embryo, expression is detected from E7.5 on the apical side of the developing neural plate and persists throughout later stages of development (PubMed:22340494). After neural tube closure at E9.5, becomes progressively restricted to the midline region (PubMed:22340494). During the estrus cycle, expression is highest in metestrus II and diestrus (PubMed:16143106).3 Publications

Inductioni

Down-regulated in the kidney by cannabinoids, such as endocannabinoid anandamide and synthetic cannabinoid HU-210.1 Publication

Gene expression databases

BgeeiENSMUSG00000027070.
ExpressionAtlasiA2ARV4. baseline and differential.
GenevisibleiA2ARV4. MM.

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 (By similarity). Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (By similarity). Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif (PubMed:11247302). Interacts with MB (By similarity). Interacts with BMP4 (PubMed:15623804). Interacts with the Sonic hedgehog protein N-product which is the active product of SHH (PubMed:11964399). Interacts with CST3 in a calcium-dependent manner (By similarity). Interacts with the vitamin-D binding protein GC/DBP (PubMed:10052453). Interacts with sex hormone-binding protein SHBG (By similarity). Interacts with angiotensin-2 (PubMed:15467006). Also interacts with angiotensin 1-7 (PubMed:16380466). Interacts with APOM (PubMed:16099815). Interacts with selenoprotein SEPP1 (PubMed:18174160). Interacts with LEP (By similarity). Interacts with ALB (By similarity). Interacts with the antiapoptotic protein BIRC5/survivin (By similarity). Interacts with matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity). In neurons, forms a trimeric complex with APP and APPB1/FE65 (PubMed:20637285). 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 similarity9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200005. 5 interactors.
IntActiA2ARV4. 11 interactors.
MINTiMINT-4106203.
STRINGi10090.ENSMUSP00000079752.

Structurei

3D structure databases

ProteinModelPortaliA2ARV4.
SMRiA2ARV4.
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
Domaini264 – 307LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST44
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 1PROSITE-ProRule annotationAdd BLAST41
Domaini1391 – 1430EGF-like 2; 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
Repeati2291 – 2333LDL-receptor class B 23PROSITE-ProRule annotationAdd BLAST43
Repeati2432 – 2478LDL-receptor class B 24PROSITE-ProRule annotationAdd BLAST47
Repeati2479 – 2519LDL-receptor class B 25PROSITE-ProRule annotationAdd BLAST41
Repeati2520 – 2563LDL-receptor class B 26PROSITE-ProRule annotationAdd BLAST44
Repeati2564 – 2605LDL-receptor class B 27PROSITE-ProRule annotationAdd BLAST42
Repeati2606 – 2647LDL-receptor class B 28PROSITE-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 3PROSITE-ProRule annotationAdd BLAST42
Domaini3154 – 3194EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3241 – 3283LDL-receptor class B 29PROSITE-ProRule annotationAdd BLAST43
Repeati3284 – 3326LDL-receptor class B 30PROSITE-ProRule annotationAdd BLAST43
Repeati3335 – 3378LDL-receptor class B 31PROSITE-ProRule annotationAdd BLAST44
Repeati3379 – 3421LDL-receptor class B 32PROSITE-ProRule annotationAdd BLAST43
Repeati3422 – 3462LDL-receptor class B 33PROSITE-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
Domaini4009 – 4050EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Repeati4156 – 4198LDL-receptor class B 34PROSITE-ProRule annotationAdd BLAST43
Repeati4199 – 4242LDL-receptor class B 35PROSITE-ProRule annotationAdd BLAST44
Repeati4244 – 4285LDL-receptor class B 36PROSITE-ProRule annotationAdd BLAST42
Domaini4379 – 4413EGF-like 6PROSITE-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 ANKRA2By similarity6
Motifi4460 – 4465PxLPxI/L motif 2; mediates interaction with ANKRA2By similarity6
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.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.
InParanoidiA2ARV4.
KOiK06233.
OMAiPNGDCSH.
OrthoDBiEOG091G000N.
PhylomeDBiA2ARV4.
TreeFamiTF315253.

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_.
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. 34 hits.
PF00058. Ldl_recept_b. 17 hits.
PRINTSiPR00261. LDLRECEPTOR.
SMARTiView protein in SMART
SM00181. EGF. 25 hits.
SM00179. EGF_CA. 9 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 37 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. 6 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 31 hits.
PS50068. LDLRA_2. 36 hits.
PS51120. LDLRB. 36 hits.

Sequencei

Sequence statusi: Complete.

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

A2ARV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERGAAAAAW MLLLAIAACL APVSGQECGS GNFRCDNGYC IPASWRCDGT
60 70 80 90 100
RDCLDDTDEI GCPPRSCGSG FFLCPAEGTC IPSSWVCDQD KDCSDGADEQ
110 120 130 140 150
QNCPGTTCSS QQLTCSNGQC VPIEYRCDHV SDCPDGSDER NCYYPTCDQL
160 170 180 190 200
TCANGACYNT SQKCDHKVDC RDSSDEANCT TLCSQKEFQC GSGECILRAY
210 220 230 240 250
VCDHDNDCED NSDEHNCNYD TCGGHQFTCS NGQCINQNWV CDGDDDCQDS
260 270 280 290 300
GDEDGCESNQ RHHTCYPREW ACPGSGRCIS MDKVCDGVPD CPEGEDENNA
310 320 330 340 350
TSGRYCGTGL CSILNCEYQC HQTPYGGECF CPPGHIINSN DSRTCIDFDD
360 370 380 390 400
CQIWGICDQK CESRQGRHQC LCEEGYILER GQHCKSNDSF SAASIIFSNG
410 420 430 440 450
RDLLVGDLHG RNFRILAESK NRGIVMGVDF HYQKHRVFWT DPMQAKVFST
460 470 480 490 500
DINGLNTQEI LNVSIDAPEN LAVDWINNKL YLVETRVNRI DVVNLEGNQR
510 520 530 540 550
VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA FMDGSNRKDL
560 570 580 590 600
VTTKLGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV
610 620 630 640 650
PHPFGISLFE EHVFFTDWTK MAVMKANKFT DTNPQVYHQS SLTPFGVTVY
660 670 680 690 700
HALRQPNATN PCGNNNGGCA QICVLSHRTD NGGLGYRCKC EFGFELDADE
710 720 730 740 750
HHCVAVKNFL LFSSQTAVRG IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ
760 770 780 790 800
HSTIFYSDLS KNIIYQQKID GTGKEVITAN RLQNVECLSF DWISRNLYWT
810 820 830 840 850
DGGSKSVTVM KLADKSRRQI ISNLNNPRSI VVHPAAGYMF LSDWFRPAKI
860 870 880 890 900
MRAWSDGSHL MPIVNTSLGW PNGLAIDWST SRLYWVDAFF DKIEHSNLDG
910 920 930 940 950
LDRKRLGHVD QMTHPFGLTV FKDNVFLTDW RLGAIIRVRK SDGGDMTVVR
960 970 980 990 1000
RGISSIMHVK AYDADLQTGT NYCSQTTHPN GDCSHFCFPV PNFQRVCGCP
1010 1020 1030 1040 1050
YGMKLQRDQM TCEGDPAREP PTQQCGSSSF PCNNGKCVPS IFRCDGVDDC
1060 1070 1080 1090 1100
HDNSDEHQCG ALNNTCSSSA FTCVHGGQCI PGQWRCDKQN DCLDGSDEQN
1110 1120 1130 1140 1150
CPTRSPSSTC PPTSFTCDNH MCIPKEWVCD TDNDCSDGSD EKNCQASGTC
1160 1170 1180 1190 1200
HPTQFRCPDH RCISPLYVCD GDKDCVDGSD EAGCVLNCTS SQFKCADGSS
1210 1220 1230 1240 1250
CINSRYRCDG VYDCKDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE
1260 1270 1280 1290 1300
CDGHPDCIQG SDEHNGCVPK TCSPSHFLCD NGNCIYNSWV CDGDNDCRDM
1310 1320 1330 1340 1350
SDEKDCPTQP FHCPSSQWQC PGYSICVNLS ALCDGVFDCP NGTDESPLCN
1360 1370 1380 1390 1400
QDSCLHFNGG CTHRCIQGPF GATCVCPIGY QLANDTKTCE DVNECDIPGF
1410 1420 1430 1440 1450
CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTASENLLLV VASRDKIIMD
1460 1470 1480 1490 1500
NITAHTHNIY SLVQDVSFVV ALDFDSVTGR VFWSDLLEGK TWSAFQNGTD
1510 1520 1530 1540 1550
KRVVHDSGLS LTEMIAVDWI GRNIYWTDYT LETIEVSKID GSHRTVLISK
1560 1570 1580 1590 1600
NVTKPRGLAL DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW
1610 1620 1630 1640 1650
PCGLSIDYPN RLIYFMDAYL DYIEFCDYDG QNRRQVIASD LVLHHPHALT
1660 1670 1680 1690 1700
LFEDSVFWTD RGTHQVMQAN KWHGRNQSVV MYSVPQPLGI IAIHPSRQPS
1710 1720 1730 1740 1750
SPNPCASATC SHLCLLSAQE PRHYSCACPS GWNLSDDSVN CVRGDQPFLI
1760 1770 1780 1790 1800
SVRENVIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG
1810 1820 1830 1840 1850
EIHRVKTDGS NRTAFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT
1860 1870 1880 1890 1900
LRGDTRYGKT LITNDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK
1910 1920 1930 1940 1950
IASANMDGTS LKILFTGNME HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD
1960 1970 1980 1990 2000
GTERMILVHH LAHPWGLVVH GSFLYYSDEQ YEVIERVDKS SGSNKVVFRD
2010 2020 2030 2040 2050
NIPYLRGLRV YHHRNAADSS NGCSNNPNAC QQICLPVPGG MFSCACASGF
2060 2070 2080 2090 2100
KLSPDGRSCS PYNSFIVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH
2110 2120 2130 2140 2150
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP NGSNFTNIVT YGIGANGIRG
2160 2170 2180 2190 2200
VAVDWVAGNL YFTNAFVYET LIEVIRINTT YRRVLLKVSV DMPRHIVVDP
2210 2220 2230 2240 2250
KHRYLFWADY GQKPKIERSF LDCTNRTVLV SEGIVTPRGL AVDHDTGYIY
2260 2270 2280 2290 2300
WVDDSLDIIA RIHRDGGESQ VVRYGSRYPT PYGITVFGES IIWVDRNLRK
2310 2320 2330 2340 2350
VFQASKQPGN TDPPTVIRDS INLLRDVTIF DEHVQPLSPA ELNNNPCLQS
2360 2370 2380 2390 2400
NGGCSHFCFA LPELPTPKCG CAFGTLEDDG KNCATSREDF LIYSLNNSLR
2410 2420 2430 2440 2450
SLHFDPQDHN LPFQAISVEG MAIALDYDRR NNRIFFTQKL NPIRGQISYV
2460 2470 2480 2490 2500
NLYSGASSPT ILLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN
2510 2520 2530 2540 2550
RAVIARVSKP RAIVLDPCRG YMYWTDWGTN AKIERATLGG NFRVPIVNTS
2560 2570 2580 2590 2600
LVWPNGLTLD LETDLLYWAD ASLQKIERST LTGSNREVVI STAFHSFGLT
2610 2620 2630 2640 2650
VYGQYIYWTD FYTKKIYRAN KYDGSDLIAM TTRLPTQPSG ISTVVKTQQQ
2660 2670 2680 2690 2700
QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGSWYLANDN KYCVVDTGAR
2710 2720 2730 2740 2750
CNQFQFTCLN GRCISQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCA
2760 2770 2780 2790 2800
NGRCVPYHYR CDFYNDCGDN SDEAGCLFRS CNSTTEFTCS NGRCIPLSYV
2810 2820 2830 2840 2850
CNGINNCHDN DTSDEKNCPP ITCQPDFAKC QTTNICVPRA FLCDGDNDCG
2860 2870 2880 2890 2900
DGSDENPIYC ASHTCRSNEF QCVSPHRCIP SYWFCDGEAD CVDSSDEPDT
2910 2920 2930 2940 2950
CGHSLNSCSA NQFHCDNGRC ISSSWVCDGD NDCGDMSDED QRHHCELQNC
2960 2970 2980 2990 3000
SSTEFTCINS RPPNRRCIPQ HWVCDGDADC ADALDELQNC TMRACSTGEF
3010 3020 3030 3040 3050
SCANGRCIRQ SFRCDRRNDC GDYSDERGCS YPPCRDDQFT CQNGQCITKL
3060 3070 3080 3090 3100
YVCDEDNDCG DGSDEQEHLC HTPEPTCPPH QFRCDNGHCI EMGTVCNHVD
3110 3120 3130 3140 3150
DCSDNSDEKG CGINECQDSS ISHCDHNCTD TITSFYCSCL PGYKLMSDKR
3160 3170 3180 3190 3200
TCVDIDECKE TPQLCSQKCE NVIGSYICKC APGYIREPDG KSCRQNSNIE
3210 3220 3230 3240 3250
PYLVFSNRYY IRNLTIDGTS YSLILQGLGN VVALDFDRVE ERLYWIDAEK
3260 3270 3280 3290 3300
QIIERMFLNK TNQETIISHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD
3310 3320 3330 3340 3350
LEGRQRKMLA QHCVDANNTF CFENPRGIVL HPQRGYVYWA DWGDHAYIAR
3360 3370 3380 3390 3400
IGMDGTNKTV IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH
3410 3420 3430 3440 3450
RHTVYDGTLP HPFALTIFED TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT
3460 3470 3480 3490 3500
HKPFDIHVLH PYRQPIMSNP CATNNGGCSH LCLIKAGGRG FTCECPDDFQ
3510 3520 3530 3540 3550
TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC SDGSDESDLC
3560 3570 3580 3590 3600
PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCEANE
3610 3620 3630 3640 3650
WQCANKRCIP EYWQCDSVDD CLDNSDEDPS HCASRTCRPG QFKCNNGRCI
3660 3670 3680 3690 3700
PQSWKCDVDN DCGDYSDEPI HECMTAAYNC DNHTEFSCKT NYRCIPQWAV
3710 3720 3730 3740 3750
CNGFDDCRDN SDEQGCESVP CHPSGDFRCG NHHCIPLRWK CDGIDDCGDN
3760 3770 3780 3790 3800
SDEESCVPRE CTESEFRCAD QQCIPSRWVC DQENDCGDNS DERDCEMKTC
3810 3820 3830 3840 3850
HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN GTYCPAAMFE
3860 3870 3880 3890 3900
CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNVPCESPQR FRCDNSRCIY
3910 3920 3930 3940 3950
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCVSQHYVCD
3960 3970 3980 3990 4000
NVDDCGDLSD ETGCNLGENR TCAEKICEQN CTQLSNGGFI CSCRPGFKPS
4010 4020 4030 4040 4050
TLDKNSCQDI NECEEFGICP QSCRNSKGSY ECFCVDGFKS MSTHYGERCA
4060 4070 4080 4090 4100
ADGSPPLLLL PENVRIRKYN ISSEKFSEYL EEEEHIQAID YDWDPEGIGL
4110 4120 4130 4140 4150
SVVYYTVLSQ GSQFGAIKRA YLPDFESGSN NPVREVDLGL KYLMQPDGLA
4160 4170 4180 4190 4200
VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL
4210 4220 4230 4240 4250
MFWTDQGKQP KIESAWMNGE HRSVLASANL GWPNGLSIDY LNGDRIYWSD
4260 4270 4280 4290 4300
SKEDVIESIK YDGTDRRLII NDAMKPFSLD IFEDQLYWVA KEKGEVWRQN
4310 4320 4330 4340 4350
KFGKGNKEKL LVVNPWLTQV RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG
4360 4370 4380 4390 4400
YSCACPQGSD FVTGSTVECD AASELPITMP SPCRCMHGGS CYFDENDLPK
4410 4420 4430 4440 4450
CKCSSGYSGE YCEIGLSRGI PPGTTMALLL TFAMVIIVGA LVLVGFFHYR
4460 4470 4480 4490 4500
KTGSLLPSLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI
4510 4520 4530 4540 4550
IDRSMAMNEQ FVMEVGKQPV IFENPMYAAK DSTSKVGLAV QGPSVSSQVT
4560 4570 4580 4590 4600
VPENVENQNY GRSIDPSEIV PEPKPASPGA DETQGTKWNI FKRKPKQTTN
4610 4620 4630 4640 4650
FENPIYAEMD TEQKEAVAVA PPPSPSLPAK ASKRSSTPGY TATEDTFKDT
4660
ANLVKEDSDV
Length:4,660
Mass (Da):519,208
Last modified:February 20, 2007 - v1
Checksum:i4CF399C24DF2FAA4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4198L → F in CAA69877 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL845489 Genomic DNA. Translation: CAM20178.1.
AK166702 mRNA. Translation: BAE38957.1.
Y08566 mRNA. Translation: CAA69877.1.
AF197160 mRNA. Translation: AAF61488.1.
CCDSiCCDS38135.1.
RefSeqiNP_001074557.1. NM_001081088.1.
UniGeneiMm.23847.

Genome annotation databases

EnsembliENSMUST00000080953; ENSMUSP00000079752; ENSMUSG00000027070.
GeneIDi14725.
KEGGimmu:14725.
UCSCiuc008jyc.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiLRP2_MOUSE
AccessioniPrimary (citable) accession number: A2ARV4
Secondary accession number(s): P70215, Q3TL35, Q9JLB3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: February 20, 2007
Last modified: October 25, 2017
This is version 106 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families