UniProtKB - A2ARV4 (LRP2_MOUSE)
Low-density lipoprotein receptor-related protein 2
Lrp2
Functioni
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 1127 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1130 | CalciumBy similarity | 1 | |
Metal bindingi | 1132 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1134 | CalciumBy similarity | 1 | |
Metal bindingi | 1140 | CalciumBy similarity | 1 | |
Metal bindingi | 1141 | CalciumBy similarity | 1 | |
Metal bindingi | 1206 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1209 | CalciumBy similarity | 1 | |
Metal bindingi | 1211 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1213 | CalciumBy similarity | 1 | |
Metal bindingi | 1219 | CalciumBy similarity | 1 | |
Metal bindingi | 1220 | CalciumBy similarity | 1 |
GO - Molecular functioni
- calcium ion binding Source: UniProtKB
- chaperone binding Source: MGI
- hemoglobin binding Source: MGI
- hormone binding Source: MGI
- insulin-like growth factor I binding Source: MGI
- low-density lipoprotein particle receptor binding Source: MGI
- PDZ domain binding Source: MGI
- protein-containing complex binding Source: MGI
- protein transporter activity Source: MGI
- SH3 domain binding Source: UniProtKB-KW
- steroid hormone receptor binding Source: MGI
GO - Biological processi
- amyloid-beta clearance Source: MGI
- aorta development Source: MGI
- cell population proliferation Source: MGI
- cellular response to growth factor stimulus Source: MGI
- chemoattraction of axon Source: MGI
- coronary artery morphogenesis Source: UniProtKB
- coronary vasculature development Source: MGI
- endocytic hemoglobin import into cell Source: MGI
- endocytosis Source: MGI
- endosomal transport Source: MGI
- folate import across plasma membrane Source: UniProtKB
- forebrain development Source: MGI
- heart development Source: MGI
- hormone secretion Source: MGI
- kidney development Source: MGI
- male gonad development Source: UniProtKB
- metal ion transport Source: UniProtKB
- negative regulation of apoptotic process Source: MGI
- 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 endocytosis Source: MGI
- positive regulation of lipoprotein transport Source: MGI
- positive regulation of neurogenesis Source: UniProtKB
- positive regulation of oligodendrocyte progenitor proliferation Source: UniProtKB
- positive regulation of protein kinase B signaling Source: MGI
- protein transport Source: ARUK-UCL
- pulmonary artery morphogenesis Source: UniProtKB
- receptor-mediated endocytosis Source: UniProtKB
- response to leptin Source: ARUK-UCL
- response to X-ray Source: MGI
- secondary heart field specification Source: UniProtKB
- sensory perception of sound Source: UniProtKB
- transcytosis Source: MGI
- vagina development Source: UniProtKB
- ventricular compact myocardium morphogenesis Source: UniProtKB
- ventricular septum development Source: MGI
- vitamin metabolic process Source: MGI
Keywordsi
Molecular function | Receptor |
Biological process | Endocytosis, Hearing, Neurogenesis, Transport |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
Reactomei | 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
TCDBi | 9.B.87.1.1, the selenoprotein p receptor (selp-receptor) family |
Names & Taxonomyi
Protein namesi | Recommended name: Low-density lipoprotein receptor-related protein 2Short name: LRP-2 Alternative name(s): Glycoprotein 330 Short name: gp330 Megalin |
Gene namesi | Name:Lrp2 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:95794, Lrp2 |
Subcellular locationi
Endosome
- Endosome lumen By similarity
Plasma membrane
- Apical cell membrane 4 Publications; Single-pass type I membrane protein Sequence analysis
Other locations
- coated pit 1 Publication
- dendrite 1 Publication
- axon 1 Publication
Note: Localizes to brush border membranes in the kidney. In the endolymphatic sac of the inner ear, located in the lumen of endosomes as a soluble form.By similarity
Endoplasmic reticulum
- endoplasmic reticulum Source: MGI
Endosome
- endosome Source: MGI
- endosome lumen Source: UniProtKB-SubCell
Extracellular region or secreted
- extracellular space Source: MGI
Golgi apparatus
- Golgi apparatus Source: MGI
Plasma Membrane
- apical plasma membrane Source: UniProtKB
- brush border membrane Source: MGI
- clathrin-coated pit Source: MGI
- external side of plasma membrane Source: UniProtKB
- plasma membrane Source: MGI
Other locations
- apical part of cell Source: MGI
- axon Source: UniProtKB
- axonal growth cone Source: MGI
- brush border Source: MGI
- cell surface Source: MGI
- cytoplasm Source: MGI
- dendrite Source: UniProtKB
- endocytic vesicle Source: MGI
- integral component of membrane Source: UniProtKB-KW
- membrane Source: MGI
- membrane raft Source: MGI
- protein-containing complex Source: MGI
- receptor complex Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 26 – 4425 | ExtracellularSequence analysisAdd BLAST | 4400 | |
Transmembranei | 4426 – 4446 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 4447 – 4660 | CytoplasmicSequence analysisAdd BLAST | 214 |
Keywords - Cellular componenti
Cell membrane, Cell projection, Coated pit, Endosome, MembranePathology & Biotechi
Disruption phenotypei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 25 | Sequence analysisAdd BLAST | 25 | |
ChainiPRO_0000309845 | 26 – 4660 | Low-density lipoprotein receptor-related protein 2Add BLAST | 4635 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 28 ↔ 40 | PROSITE-ProRule annotation | ||
Disulfide bondi | 35 ↔ 53 | PROSITE-ProRule annotation | ||
Disulfide bondi | 47 ↔ 62 | PROSITE-ProRule annotation | ||
Disulfide bondi | 67 ↔ 80 | PROSITE-ProRule annotation | ||
Disulfide bondi | 74 ↔ 93 | PROSITE-ProRule annotation | ||
Disulfide bondi | 87 ↔ 103 | PROSITE-ProRule annotation | ||
Disulfide bondi | 108 ↔ 120 | PROSITE-ProRule annotation | ||
Disulfide bondi | 115 ↔ 133 | PROSITE-ProRule annotation | ||
Disulfide bondi | 127 ↔ 142 | PROSITE-ProRule annotation | ||
Disulfide bondi | 147 ↔ 157 | PROSITE-ProRule annotation | ||
Disulfide bondi | 152 ↔ 170 | PROSITE-ProRule annotation | ||
Glycosylationi | 159 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 164 ↔ 179 | PROSITE-ProRule annotation | ||
Glycosylationi | 178 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 183 ↔ 195 | PROSITE-ProRule annotation | ||
Disulfide bondi | 190 ↔ 208 | PROSITE-ProRule annotation | ||
Disulfide bondi | 202 ↔ 217 | PROSITE-ProRule annotation | ||
Disulfide bondi | 222 ↔ 234 | PROSITE-ProRule annotation | ||
Disulfide bondi | 229 ↔ 247 | PROSITE-ProRule annotation | ||
Disulfide bondi | 241 ↔ 256 | PROSITE-ProRule annotation | ||
Disulfide bondi | 265 ↔ 278 | PROSITE-ProRule annotation | ||
Disulfide bondi | 272 ↔ 291 | PROSITE-ProRule annotation | ||
Disulfide bondi | 285 ↔ 306 | PROSITE-ProRule annotation | ||
Glycosylationi | 299 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 340 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 387 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 462 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 657 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 865 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1025 ↔ 1037 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1032 ↔ 1050 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1044 ↔ 1059 | PROSITE-ProRule annotation | ||
Glycosylationi | 1063 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1066 ↔ 1079 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1073 ↔ 1092 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1086 ↔ 1101 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1110 ↔ 1122 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1117 ↔ 1135 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1129 ↔ 1144 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1150 ↔ 1162 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1157 ↔ 1175 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1169 ↔ 1184 | PROSITE-ProRule annotation | ||
Glycosylationi | 1187 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1188 ↔ 1201 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1195 ↔ 1214 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1208 ↔ 1223 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1231 ↔ 1244 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1238 ↔ 1257 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1251 ↔ 1267 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1272 ↔ 1284 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1279 ↔ 1297 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1291 ↔ 1306 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1313 ↔ 1326 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1320 ↔ 1339 | PROSITE-ProRule annotation | ||
Glycosylationi | 1328 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1333 ↔ 1349 | PROSITE-ProRule annotation | ||
Glycosylationi | 1341 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1354 ↔ 1365 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1361 ↔ 1374 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1376 ↔ 1389 | PROSITE-ProRule annotation | ||
Glycosylationi | 1384 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1395 ↔ 1405 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1401 ↔ 1414 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1416 ↔ 1429 | PROSITE-ProRule annotation | ||
Glycosylationi | 1451 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1497 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1551 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1676 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1733 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1811 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2131 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2134 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2178 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2225 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2396 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2488 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2548 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2701 ↔ 2713 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2708 ↔ 2726 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2720 ↔ 2737 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2742 ↔ 2754 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2749 ↔ 2767 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2761 ↔ 2776 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2781 ↔ 2794 | PROSITE-ProRule annotation | ||
Glycosylationi | 2782 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2789 ↔ 2807 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2801 ↔ 2818 | PROSITE-ProRule annotation | ||
Glycosylationi | 2810 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2823 ↔ 2836 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2830 ↔ 2849 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2843 ↔ 2860 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2865 ↔ 2878 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2872 ↔ 2891 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2885 ↔ 2901 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2908 ↔ 2920 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2915 ↔ 2933 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2927 ↔ 2945 | PROSITE-ProRule annotation | ||
Glycosylationi | 2949 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2950 ↔ 2967 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2957 ↔ 2980 | PROSITE-ProRule annotation | ||
Disulfide bondi | 2974 ↔ 2990 | PROSITE-ProRule annotation | ||
Glycosylationi | 2989 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2995 ↔ 3007 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3002 ↔ 3020 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3014 ↔ 3029 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3034 ↔ 3046 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3041 ↔ 3059 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3053 ↔ 3070 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3077 ↔ 3089 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3084 ↔ 3102 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3096 ↔ 3111 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3116 ↔ 3128 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3124 ↔ 3137 | PROSITE-ProRule annotation | ||
Glycosylationi | 3127 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3139 ↔ 3152 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3158 ↔ 3169 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3165 ↔ 3178 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3180 ↔ 3193 | PROSITE-ProRule annotation | ||
Glycosylationi | 3213 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3259 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3317 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3357 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3448 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3514 ↔ 3527 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3521 ↔ 3540 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3534 ↔ 3550 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3555 ↔ 3567 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3562 ↔ 3580 | PROSITE-ProRule annotation | ||
Glycosylationi | 3566 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3574 ↔ 3591 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3596 ↔ 3608 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3603 ↔ 3621 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3615 ↔ 3632 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3637 ↔ 3649 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3644 ↔ 3662 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3656 ↔ 3673 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3680 ↔ 3694 | PROSITE-ProRule annotation | ||
Glycosylationi | 3682 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3688 ↔ 3707 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3701 ↔ 3716 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3721 ↔ 3734 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3729 ↔ 3747 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3741 ↔ 3756 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3761 ↔ 3773 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3768 ↔ 3786 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3780 ↔ 3795 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3800 ↔ 3812 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3807 ↔ 3825 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3819 ↔ 3834 | PROSITE-ProRule annotation | ||
Glycosylationi | 3840 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3844 ↔ 3856 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3851 ↔ 3869 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3863 ↔ 3880 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3885 ↔ 3898 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3893 ↔ 3911 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3905 ↔ 3922 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3930 ↔ 3942 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3937 ↔ 3955 | PROSITE-ProRule annotation | ||
Disulfide bondi | 3949 ↔ 3964 | PROSITE-ProRule annotation | ||
Glycosylationi | 3969 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3980 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 4013 ↔ 4023 | PROSITE-ProRule annotation | ||
Disulfide bondi | 4019 ↔ 4032 | PROSITE-ProRule annotation | ||
Disulfide bondi | 4034 ↔ 4049 | PROSITE-ProRule annotation | ||
Glycosylationi | 4070 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 4329 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 4383 ↔ 4391 | PROSITE-ProRule annotation | ||
Disulfide bondi | 4385 ↔ 4401 | PROSITE-ProRule annotation | ||
Disulfide bondi | 4403 ↔ 4412 | PROSITE-ProRule annotation | ||
Modified residuei | 4464 | PhosphoserineCombined sources | 1 | |
Modified residuei | 4467 | PhosphoserineCombined sources | 1 | |
Modified residuei | 4577 | PhosphoserineCombined sources | 1 | |
Modified residuei | 4624 | PhosphoserineBy similarity | 1 | |
Modified residuei | 4637 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 4658 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
jPOSTi | A2ARV4 |
MaxQBi | A2ARV4 |
PaxDbi | A2ARV4 |
PeptideAtlasi | A2ARV4 |
PRIDEi | A2ARV4 |
PTM databases
GlyGeni | A2ARV4, 43 sites |
iPTMneti | A2ARV4 |
PhosphoSitePlusi | A2ARV4 |
Expressioni
Tissue specificityi
Developmental stagei
Inductioni
Gene expression databases
Bgeei | ENSMUSG00000027070, Expressed in kidney and 179 other tissues |
ExpressionAtlasi | A2ARV4, baseline and differential |
Genevisiblei | A2ARV4, 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).
Interacts with MDK (PubMed:10772929).
By similarity10 PublicationsBinary interactionsi
Hide detailsA2ARV4
GO - Molecular functioni
- chaperone binding Source: MGI
- hemoglobin binding Source: MGI
- insulin-like growth factor I binding Source: MGI
- low-density lipoprotein particle receptor binding Source: MGI
- PDZ domain binding Source: MGI
- SH3 domain binding Source: UniProtKB-KW
- steroid hormone receptor binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 200005, 7 interactors |
CORUMi | A2ARV4 |
IntActi | A2ARV4, 11 interactors |
MINTi | A2ARV4 |
STRINGi | 10090.ENSMUSP00000079752 |
Miscellaneous databases
RNActi | A2ARV4, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 27 – 63 | LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 66 – 104 | LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 107 – 143 | LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 146 – 180 | LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST | 35 | |
Domaini | 182 – 218 | LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 221 – 257 | LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 264 – 307 | LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST | 44 | |
Repeati | 435 – 477 | LDL-receptor class B 1PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 478 – 520 | LDL-receptor class B 2PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 521 – 567 | LDL-receptor class B 3PROSITE-ProRule annotationAdd BLAST | 47 | |
Repeati | 568 – 612 | LDL-receptor class B 4PROSITE-ProRule annotationAdd BLAST | 45 | |
Repeati | 752 – 794 | LDL-receptor class B 5PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 795 – 836 | LDL-receptor class B 6PROSITE-ProRule annotationAdd BLAST | 42 | |
Repeati | 837 – 880 | LDL-receptor class B 7PROSITE-ProRule annotationAdd BLAST | 44 | |
Repeati | 881 – 924 | LDL-receptor class B 8PROSITE-ProRule annotationAdd BLAST | 44 | |
Domaini | 1024 – 1060 | LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1065 – 1102 | LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 1109 – 1145 | LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1149 – 1185 | LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1187 – 1224 | LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 1230 – 1268 | LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1271 – 1307 | LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1312 – 1350 | LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1350 – 1390 | EGF-like 1PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 1391 – 1430 | EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 40 | |
Repeati | 1479 – 1521 | LDL-receptor class B 9PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 1522 – 1564 | LDL-receptor class B 10PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 1567 – 1610 | LDL-receptor class B 11PROSITE-ProRule annotationAdd BLAST | 44 | |
Repeati | 1611 – 1655 | LDL-receptor class B 12PROSITE-ProRule annotationAdd BLAST | 45 | |
Repeati | 1656 – 1696 | LDL-receptor class B 13PROSITE-ProRule annotationAdd BLAST | 41 | |
Repeati | 1791 – 1833 | LDL-receptor class B 14PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 1834 – 1883 | LDL-receptor class B 15PROSITE-ProRule annotationAdd BLAST | 50 | |
Repeati | 1884 – 1931 | LDL-receptor class B 16PROSITE-ProRule annotationAdd BLAST | 48 | |
Repeati | 1932 – 1973 | LDL-receptor class B 17PROSITE-ProRule annotationAdd BLAST | 42 | |
Repeati | 1974 – 2014 | LDL-receptor class B 18PROSITE-ProRule annotationAdd BLAST | 41 | |
Repeati | 2108 – 2157 | LDL-receptor class B 19PROSITE-ProRule annotationAdd BLAST | 50 | |
Repeati | 2158 – 2202 | LDL-receptor class B 20PROSITE-ProRule annotationAdd BLAST | 45 | |
Repeati | 2203 – 2246 | LDL-receptor class B 21PROSITE-ProRule annotationAdd BLAST | 44 | |
Repeati | 2247 – 2290 | LDL-receptor class B 22PROSITE-ProRule annotationAdd BLAST | 44 | |
Repeati | 2291 – 2333 | LDL-receptor class B 23PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 2432 – 2478 | LDL-receptor class B 24PROSITE-ProRule annotationAdd BLAST | 47 | |
Repeati | 2479 – 2519 | LDL-receptor class B 25PROSITE-ProRule annotationAdd BLAST | 41 | |
Repeati | 2520 – 2563 | LDL-receptor class B 26PROSITE-ProRule annotationAdd BLAST | 44 | |
Repeati | 2564 – 2605 | LDL-receptor class B 27PROSITE-ProRule annotationAdd BLAST | 42 | |
Repeati | 2606 – 2647 | LDL-receptor class B 28PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 2700 – 2738 | LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 2741 – 2777 | LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 2780 – 2819 | LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 2822 – 2861 | LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 2864 – 2902 | LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 2907 – 2946 | LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 2949 – 2991 | LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST | 43 | |
Domaini | 2994 – 3030 | LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 3033 – 3071 | LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3076 – 3112 | LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 3112 – 3153 | EGF-like 3PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 3154 – 3194 | EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 41 | |
Repeati | 3241 – 3283 | LDL-receptor class B 29PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 3284 – 3326 | LDL-receptor class B 30PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 3335 – 3378 | LDL-receptor class B 31PROSITE-ProRule annotationAdd BLAST | 44 | |
Repeati | 3379 – 3421 | LDL-receptor class B 32PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 3422 – 3462 | LDL-receptor class B 33PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 3513 – 3551 | LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3554 – 3592 | LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3595 – 3633 | LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3636 – 3674 | LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3679 – 3717 | LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3720 – 3757 | LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 3760 – 3796 | LDL-receptor class A 32PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 3799 – 3835 | LDL-receptor class A 33PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 3843 – 3881 | LDL-receptor class A 34PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3884 – 3923 | LDL-receptor class A 35PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 3929 – 3965 | LDL-receptor class A 36PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 4009 – 4050 | EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 42 | |
Repeati | 4156 – 4198 | LDL-receptor class B 34PROSITE-ProRule annotationAdd BLAST | 43 | |
Repeati | 4199 – 4242 | LDL-receptor class B 35PROSITE-ProRule annotationAdd BLAST | 44 | |
Repeati | 4244 – 4285 | LDL-receptor class B 36PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 4379 – 4413 | EGF-like 6PROSITE-ProRule annotationAdd BLAST | 35 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 4597 – 4610 | Interaction with DAB2By similarityAdd BLAST | 14 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 4454 – 4463 | SH3-bindingSequence analysis | 10 | |
Motifi | 4457 – 4462 | PxLPxI/L motif 1; mediates interaction with ANKRA2By similarity | 6 | |
Motifi | 4460 – 4465 | PxLPxI/L motif 2; mediates interaction with ANKRA2By similarity | 6 | |
Motifi | 4522 – 4527 | Endocytosis signalSequence analysis | 6 | |
Motifi | 4603 – 4606 | NPXY motif | 4 | |
Motifi | 4606 – 4609 | SH2-bindingSequence analysis | 4 | |
Motifi | 4619 – 4630 | SH3-bindingSequence analysisAdd BLAST | 12 |
Domaini
Sequence similaritiesi
Keywords - Domaini
EGF-like domain, Repeat, SH3-binding, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1215, Eukaryota |
GeneTreei | ENSGT00940000157232 |
HOGENOMi | CLU_000085_1_1_1 |
InParanoidi | A2ARV4 |
OrthoDBi | 1606at2759 |
PhylomeDBi | A2ARV4 |
TreeFami | TF315253 |
Family and domain databases
CDDi | cd00112, LDLa, 36 hits |
Gene3Di | 2.120.10.30, 8 hits 4.10.400.10, 36 hits |
InterProi | View protein in InterPro IPR011042, 6-blade_b-propeller_TolB-like IPR026823, cEGF IPR001881, EGF-like_Ca-bd_dom 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 |
Pfami | View protein in Pfam PF12662, cEGF, 2 hits PF07645, EGF_CA, 1 hit PF00057, Ldl_recept_a, 34 hits PF00058, Ldl_recept_b, 17 hits |
PRINTSi | PR00261, LDLRECEPTOR |
SMARTi | View protein in SMART SM00181, EGF, 25 hits SM00179, EGF_CA, 9 hits SM00192, LDLa, 36 hits SM00135, LY, 37 hits |
SUPFAMi | SSF57184, SSF57184, 2 hits SSF57424, SSF57424, 35 hits |
PROSITEi | View 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 |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA2ARV5 | A2ARV5_MOUSE | Low-density lipoprotein receptor-re... | Lrp2 | 1,363 | Annotation score: | ||
Q3V346 | Q3V346_MOUSE | Low-density lipoprotein receptor-re... | Lrp2 | 426 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 4198 | L → F in CAA69877 (Ref. 3) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL845489 Genomic DNA No translation available. AK166702 mRNA Translation: BAE38957.1 Y08566 mRNA Translation: CAA69877.1 AF197160 mRNA Translation: AAF61488.1 |
CCDSi | CCDS38135.1 |
RefSeqi | NP_001074557.1, NM_001081088.1 |
Genome annotation databases
Ensembli | ENSMUST00000080953; ENSMUSP00000079752; ENSMUSG00000027070 |
GeneIDi | 14725 |
KEGGi | mmu:14725 |
UCSCi | uc008jyc.1, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL845489 Genomic DNA No translation available. AK166702 mRNA Translation: BAE38957.1 Y08566 mRNA Translation: CAA69877.1 AF197160 mRNA Translation: AAF61488.1 |
CCDSi | CCDS38135.1 |
RefSeqi | NP_001074557.1, NM_001081088.1 |
3D structure databases
SMRi | A2ARV4 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 200005, 7 interactors |
CORUMi | A2ARV4 |
IntActi | A2ARV4, 11 interactors |
MINTi | A2ARV4 |
STRINGi | 10090.ENSMUSP00000079752 |
Protein family/group databases
TCDBi | 9.B.87.1.1, the selenoprotein p receptor (selp-receptor) family |
PTM databases
GlyGeni | A2ARV4, 43 sites |
iPTMneti | A2ARV4 |
PhosphoSitePlusi | A2ARV4 |
Proteomic databases
jPOSTi | A2ARV4 |
MaxQBi | A2ARV4 |
PaxDbi | A2ARV4 |
PeptideAtlasi | A2ARV4 |
PRIDEi | A2ARV4 |
Protocols and materials databases
Antibodypediai | 962, 337 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000080953; ENSMUSP00000079752; ENSMUSG00000027070 |
GeneIDi | 14725 |
KEGGi | mmu:14725 |
UCSCi | uc008jyc.1, mouse |
Organism-specific databases
CTDi | 4036 |
MGIi | MGI:95794, Lrp2 |
Phylogenomic databases
eggNOGi | KOG1215, Eukaryota |
GeneTreei | ENSGT00940000157232 |
HOGENOMi | CLU_000085_1_1_1 |
InParanoidi | A2ARV4 |
OrthoDBi | 1606at2759 |
PhylomeDBi | A2ARV4 |
TreeFami | TF315253 |
Enzyme and pathway databases
Reactomei | R-MMU-8856825, Cargo recognition for clathrin-mediated endocytosis R-MMU-8856828, Clathrin-mediated endocytosis R-MMU-975634, Retinoid metabolism and transport |
Miscellaneous databases
BioGRID-ORCSi | 14725, 1 hit in 17 CRISPR screens |
ChiTaRSi | Lrp2, mouse |
PROi | PR:A2ARV4 |
RNActi | A2ARV4, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000027070, Expressed in kidney and 179 other tissues |
ExpressionAtlasi | A2ARV4, baseline and differential |
Genevisiblei | A2ARV4, MM |
Family and domain databases
CDDi | cd00112, LDLa, 36 hits |
Gene3Di | 2.120.10.30, 8 hits 4.10.400.10, 36 hits |
InterProi | View protein in InterPro IPR011042, 6-blade_b-propeller_TolB-like IPR026823, cEGF IPR001881, EGF-like_Ca-bd_dom 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 |
Pfami | View protein in Pfam PF12662, cEGF, 2 hits PF07645, EGF_CA, 1 hit PF00057, Ldl_recept_a, 34 hits PF00058, Ldl_recept_b, 17 hits |
PRINTSi | PR00261, LDLRECEPTOR |
SMARTi | View protein in SMART SM00181, EGF, 25 hits SM00179, EGF_CA, 9 hits SM00192, LDLa, 36 hits SM00135, LY, 37 hits |
SUPFAMi | SSF57184, SSF57184, 2 hits SSF57424, SSF57424, 35 hits |
PROSITEi | View 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LRP2_MOUSE | |
Accessioni | A2ARV4Primary (citable) accession number: A2ARV4 Secondary accession number(s): P70215, Q3TL35, Q9JLB3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 13, 2007 |
Last sequence update: | February 20, 2007 | |
Last modified: | February 10, 2021 | |
This is version 132 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families