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P98164

- LRP2_HUMAN

UniProt

P98164 - LRP2_HUMAN

Protein

Low-density lipoprotein receptor-related protein 2

Gene

LRP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (13 Nov 2007)
      Previous versions | rss
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    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1208 – 12081CalciumBy similarity
    Metal bindingi1210 – 12101Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1212 – 12121CalciumBy similarity
    Metal bindingi1218 – 12181CalciumBy similarity
    Metal bindingi1219 – 12191CalciumBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: Ensembl
    2. endocytosis Source: ProtInc
    3. forebrain development Source: Ensembl
    4. lipid metabolic process Source: ProtInc
    5. phototransduction, visible light Source: Reactome
    6. protein glycosylation Source: ProtInc
    7. receptor-mediated endocytosis Source: ProtInc
    8. retinoid metabolic process Source: Reactome
    9. small molecule metabolic process Source: Reactome
    10. steroid metabolic process Source: Reactome
    11. vitamin D metabolic process Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_13523. Vitamin D (calciferol) metabolism.
    REACT_24968. Retinoid metabolism and transport.
    SignaLinkiP98164.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Low-density lipoprotein receptor-related protein 2
    Short name:
    LRP-2
    Alternative name(s):
    Glycoprotein 330
    Short name:
    gp330
    Megalin
    Gene namesi
    Name:LRP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6694. LRP2.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. brush border membrane Source: Ensembl
    3. coated pit Source: UniProtKB-SubCell
    4. endocytic vesicle Source: Ensembl
    5. endoplasmic reticulum Source: Ensembl
    6. endosome Source: Ensembl
    7. extracellular vesicular exosome Source: UniProt
    8. Golgi apparatus Source: Ensembl
    9. integral component of membrane Source: UniProtKB-KW
    10. lysosomal membrane Source: UniProtKB
    11. lysosome Source: ProtInc
    12. plasma membrane Source: Reactome
    13. receptor complex Source: MGI

    Keywords - Cellular componenti

    Coated pit, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Donnai-Barrow syndrome (DBS) [MIM:222448]: Rare autosomal recessive disorder characterized by major malformations including agenesis of the corpus callosum, congenital diaphragmatic hernia, facial dysmorphology, ocular anomalies, sensorineural hearing loss and developmental delay. The FOAR syndrome was first described as comprising facial anomalies, ocular anomalies, sensorineural hearing loss, and proteinuria. DBS and FOAR were first described as distinct disorders but the classic distinguishing features between the 2 disorders were presence of proteinuria and absence of diaphragmatic hernia and corpus callosum anomalies in FOAR. Early reports noted that the 2 disorders shared many phenotypic features and may be identical. Although there is variability in the expression of some features (e.g., agenesis of the corpus callosum and proteinuria), DBS and FOAR are now considered to represent the same entity.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2522 – 25221Y → H in DBS. 1 Publication
    VAR_037013

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi222448. phenotype.
    Orphaneti2143. Donnai-Barrow syndrome.
    PharmGKBiPA30452.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 46554630Low-density lipoprotein receptor-related protein 2PRO_0000017321Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 40By similarity
    Disulfide bondi35 ↔ 53By similarity
    Disulfide bondi47 ↔ 62By similarity
    Disulfide bondi67 ↔ 80By similarity
    Disulfide bondi74 ↔ 93By similarity
    Disulfide bondi87 ↔ 103By similarity
    Disulfide bondi108 ↔ 120By similarity
    Disulfide bondi115 ↔ 133By similarity
    Disulfide bondi127 ↔ 142By similarity
    Disulfide bondi147 ↔ 157By similarity
    Disulfide bondi152 ↔ 170By similarity
    Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi164 ↔ 179By similarity
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi183 ↔ 195By similarity
    Disulfide bondi190 ↔ 208By similarity
    Disulfide bondi202 ↔ 217By similarity
    Disulfide bondi222 ↔ 234By similarity
    Disulfide bondi229 ↔ 247By similarity
    Disulfide bondi241 ↔ 256By similarity
    Disulfide bondi266 ↔ 279By similarity
    Disulfide bondi273 ↔ 292By similarity
    Disulfide bondi286 ↔ 307By similarity
    Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi312 ↔ 321By similarity
    Disulfide bondi317 ↔ 330By similarity
    Disulfide bondi332 ↔ 346By similarity
    Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi352 ↔ 362By similarity
    Disulfide bondi358 ↔ 371By similarity
    Disulfide bondi373 ↔ 385By similarity
    Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi663 ↔ 674By similarity
    Disulfide bondi670 ↔ 689By similarity
    Disulfide bondi691 ↔ 704By similarity
    Glycosylationi866 – 8661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi974 ↔ 988By similarity
    Disulfide bondi984 ↔ 998By similarity
    Disulfide bondi1000 ↔ 1013By similarity
    Disulfide bondi1026 ↔ 1038By similarity
    Disulfide bondi1033 ↔ 1051By similarity
    Disulfide bondi1045 ↔ 1060By similarity
    Glycosylationi1064 – 10641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1067 ↔ 1079By similarity
    Disulfide bondi1074 ↔ 1092By similarity
    Disulfide bondi1086 ↔ 1101By similarity
    Disulfide bondi1109 ↔ 1121By similarity
    Disulfide bondi1116 ↔ 1134By similarity
    Disulfide bondi1128 ↔ 1143By similarity
    Glycosylationi1144 – 11441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1149 ↔ 1161By similarity
    Disulfide bondi1156 ↔ 1174By similarity
    Disulfide bondi1168 ↔ 1183By similarity
    Glycosylationi1186 – 11861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1187 ↔ 1200By similarity
    Disulfide bondi1194 ↔ 1213By similarity
    Disulfide bondi1207 ↔ 1222By similarity
    Disulfide bondi1230 ↔ 1243By similarity
    Disulfide bondi1237 ↔ 1256By similarity
    Disulfide bondi1250 ↔ 1266By similarity
    Disulfide bondi1271 ↔ 1283By similarity
    Disulfide bondi1278 ↔ 1296By similarity
    Disulfide bondi1290 ↔ 1305By similarity
    Disulfide bondi1312 ↔ 1325By similarity
    Disulfide bondi1319 ↔ 1338By similarity
    Glycosylationi1327 – 13271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1332 ↔ 1348By similarity
    Glycosylationi1340 – 13401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1353 ↔ 1364By similarity
    Disulfide bondi1360 ↔ 1373By similarity
    Disulfide bondi1375 ↔ 1388By similarity
    Glycosylationi1383 – 13831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1394 ↔ 1404By similarity
    Disulfide bondi1400 ↔ 1413By similarity
    Disulfide bondi1415 ↔ 1428By similarity
    Glycosylationi1464 – 14641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1496 – 14961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1550 – 15501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1675 – 16751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1704 ↔ 1713By similarity
    Disulfide bondi1709 ↔ 1725By similarity
    Disulfide bondi1727 ↔ 1740By similarity
    Glycosylationi1810 – 18101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2022 ↔ 2033By similarity
    Disulfide bondi2029 ↔ 2043By similarity
    Disulfide bondi2045 ↔ 2058By similarity
    Glycosylationi2055 – 20551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2177 – 21771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2224 – 22241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2346 ↔ 2357By similarity
    Disulfide bondi2353 ↔ 2368By similarity
    Disulfide bondi2370 ↔ 2382By similarity
    Glycosylationi2499 – 24991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2547 – 25471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2655 ↔ 2666By similarity
    Disulfide bondi2662 ↔ 2675By similarity
    Disulfide bondi2677 ↔ 2692By similarity
    Disulfide bondi2700 ↔ 2712By similarity
    Disulfide bondi2707 ↔ 2725By similarity
    Disulfide bondi2719 ↔ 2736By similarity
    Disulfide bondi2741 ↔ 2753By similarity
    Disulfide bondi2748 ↔ 2766By similarity
    Disulfide bondi2760 ↔ 2775By similarity
    Disulfide bondi2780 ↔ 2793By similarity
    Glycosylationi2781 – 27811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2788 ↔ 2806By similarity
    Disulfide bondi2800 ↔ 2817By similarity
    Glycosylationi2809 – 28091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2810 – 28101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2822 ↔ 2835By similarity
    Disulfide bondi2829 ↔ 2848By similarity
    Disulfide bondi2842 ↔ 2859By similarity
    Disulfide bondi2864 ↔ 2876By similarity
    Disulfide bondi2871 ↔ 2889By similarity
    Disulfide bondi2883 ↔ 2899By similarity
    Disulfide bondi2906 ↔ 2918By similarity
    Disulfide bondi2913 ↔ 2931By similarity
    Disulfide bondi2925 ↔ 2943By similarity
    Glycosylationi2947 – 29471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2948 ↔ 2965By similarity
    Disulfide bondi2955 ↔ 2978By similarity
    Disulfide bondi2972 ↔ 2988By similarity
    Glycosylationi2987 – 29871N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2993 ↔ 3005By similarity
    Disulfide bondi3000 ↔ 3018By similarity
    Disulfide bondi3012 ↔ 3027By similarity
    Disulfide bondi3032 ↔ 3044By similarity
    Disulfide bondi3039 ↔ 3057By similarity
    Disulfide bondi3051 ↔ 3068By similarity
    Disulfide bondi3075 ↔ 3087By similarity
    Disulfide bondi3082 ↔ 3100By similarity
    Disulfide bondi3094 ↔ 3109By similarity
    Disulfide bondi3114 ↔ 3126By similarity
    Disulfide bondi3122 ↔ 3135By similarity
    Glycosylationi3125 – 31251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3137 ↔ 3150By similarity
    Disulfide bondi3156 ↔ 3167By similarity
    Disulfide bondi3163 ↔ 3176By similarity
    Disulfide bondi3178 ↔ 3191By similarity
    Glycosylationi3211 – 32111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3257 – 32571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3315 – 33151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3355 – 33551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3446 – 34461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3469 ↔ 3480By similarity
    Disulfide bondi3476 ↔ 3491By similarity
    Disulfide bondi3493 ↔ 3508By similarity
    Disulfide bondi3512 ↔ 3525By similarity
    Disulfide bondi3519 ↔ 3538By similarity
    Disulfide bondi3532 ↔ 3548By similarity
    Disulfide bondi3553 ↔ 3565By similarity
    Disulfide bondi3560 ↔ 3578By similarity
    Glycosylationi3564 – 35641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3572 ↔ 3589By similarity
    Disulfide bondi3594 ↔ 3606By similarity
    Disulfide bondi3601 ↔ 3619By similarity
    Disulfide bondi3613 ↔ 3630By similarity
    Disulfide bondi3635 ↔ 3647By similarity
    Disulfide bondi3642 ↔ 3660By similarity
    Disulfide bondi3654 ↔ 3671By similarity
    Disulfide bondi3678 ↔ 3692By similarity
    Glycosylationi3680 – 36801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3686 ↔ 3705By similarity
    Disulfide bondi3699 ↔ 3714By similarity
    Disulfide bondi3719 ↔ 3732By similarity
    Disulfide bondi3727 ↔ 3745By similarity
    Disulfide bondi3739 ↔ 3754By similarity
    Disulfide bondi3759 ↔ 3771By similarity
    Disulfide bondi3766 ↔ 3784By similarity
    Disulfide bondi3778 ↔ 3793By similarity
    Disulfide bondi3798 ↔ 3810By similarity
    Disulfide bondi3805 ↔ 3823By similarity
    Disulfide bondi3817 ↔ 3832By similarity
    Disulfide bondi3842 ↔ 3854By similarity
    Disulfide bondi3849 ↔ 3867By similarity
    Disulfide bondi3861 ↔ 3878By similarity
    Disulfide bondi3883 ↔ 3896By similarity
    Disulfide bondi3891 ↔ 3909By similarity
    Disulfide bondi3903 ↔ 3920By similarity
    Disulfide bondi3928 ↔ 3940By similarity
    Disulfide bondi3935 ↔ 3953By similarity
    Disulfide bondi3947 ↔ 3962By similarity
    Disulfide bondi3970 ↔ 3979By similarity
    Disulfide bondi3975 ↔ 3989By similarity
    Glycosylationi3978 – 39781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3991 ↔ 4005By similarity
    Disulfide bondi4011 ↔ 4021By similarity
    Disulfide bondi4017 ↔ 4030By similarity
    Disulfide bondi4032 ↔ 4047By similarity
    Glycosylationi4068 – 40681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4327 – 43271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4334 ↔ 4342By similarity
    Disulfide bondi4338 ↔ 4351By similarity
    Disulfide bondi4353 ↔ 4367By similarity
    Disulfide bondi4381 ↔ 4389By similarity
    Disulfide bondi4383 ↔ 4399By similarity
    Disulfide bondi4401 ↔ 4410By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP98164.
    PaxDbiP98164.
    PRIDEiP98164.

    PTM databases

    PhosphoSiteiP98164.

    Expressioni

    Tissue specificityi

    Absorptive epithelia, including renal proximal tubules.

    Gene expression databases

    ArrayExpressiP98164.
    BgeeiP98164.
    CleanExiHS_LRP2.
    GenevestigatoriP98164.

    Organism-specific databases

    HPAiHPA005980.

    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 a receptor-associated protein (RAP). Binds to ankyrin-repeat family A protein 2 (ANKRA2). Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif.4 Publications

    Protein-protein interaction databases

    BioGridi110216. 34 interactions.
    IntActiP98164. 9 interactions.
    MINTiMINT-2860496.
    STRINGi9606.ENSP00000263816.

    Structurei

    Secondary structure

    1
    4655
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1111 – 11155
    Beta strandi1121 – 11233
    Beta strandi1129 – 11313
    Beta strandi1133 – 11364
    Helixi1138 – 11414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2M0PNMR-A1103-1148[»]
    ProteinModelPortaliP98164.
    SMRiP98164. Positions 26-1346, 1351-4373.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 44234398ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini4447 – 4655209CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4424 – 444623HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 6439LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini65 – 10541LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini106 – 14439LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini145 – 18137LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini182 – 21938LDL-receptor class A 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini220 – 25839LDL-receptor class A 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini264 – 30845LDL-receptor class A 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini309 – 34739EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini348 – 38639EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati436 – 47843LDL-receptor class B 1Add
    BLAST
    Repeati479 – 52143LDL-receptor class B 2Add
    BLAST
    Repeati522 – 56847LDL-receptor class B 3Add
    BLAST
    Repeati569 – 61244LDL-receptor class B 4Add
    BLAST
    Repeati613 – 65341LDL-receptor class B 5Add
    BLAST
    Domaini659 – 70547EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati753 – 79543LDL-receptor class B 6Add
    BLAST
    Repeati796 – 83742LDL-receptor class B 7Add
    BLAST
    Repeati838 – 88144LDL-receptor class B 8Add
    BLAST
    Repeati882 – 92544LDL-receptor class B 9Add
    BLAST
    Domaini970 – 101445EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1024 – 106239LDL-receptor class A 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1065 – 110339LDL-receptor class A 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1107 – 114539LDL-receptor class A 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1147 – 118539LDL-receptor class A 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1186 – 122439LDL-receptor class A 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1228 – 126841LDL-receptor class A 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1269 – 130739LDL-receptor class A 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1310 – 135041LDL-receptor class A 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1349 – 138941EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1390 – 142940EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati1478 – 152043LDL-receptor class B 10Add
    BLAST
    Repeati1521 – 156343LDL-receptor class B 11Add
    BLAST
    Repeati1566 – 160944LDL-receptor class B 12Add
    BLAST
    Repeati1610 – 165445LDL-receptor class B 13Add
    BLAST
    Repeati1655 – 169541LDL-receptor class B 14Add
    BLAST
    Domaini1700 – 174142EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Repeati1790 – 183243LDL-receptor class B 15Add
    BLAST
    Repeati1833 – 188250LDL-receptor class B 16Add
    BLAST
    Repeati1883 – 193048LDL-receptor class B 17Add
    BLAST
    Repeati1931 – 197141LDL-receptor class B 18Add
    BLAST
    Repeati1972 – 201342LDL-receptor class B 19Add
    BLAST
    Domaini2018 – 205942EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Repeati2107 – 215650LDL-receptor class B 20Add
    BLAST
    Repeati2157 – 220145LDL-receptor class B 21Add
    BLAST
    Repeati2202 – 224544LDL-receptor class B 22Add
    BLAST
    Repeati2246 – 228944LDL-receptor class B 23Add
    BLAST
    Repeati2290 – 233142LDL-receptor class B 24Add
    BLAST
    Domaini2342 – 238342EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Repeati2431 – 247747LDL-receptor class B 25Add
    BLAST
    Repeati2478 – 251841LDL-receptor class B 26Add
    BLAST
    Repeati2519 – 256244LDL-receptor class B 27Add
    BLAST
    Repeati2563 – 260341LDL-receptor class B 28Add
    BLAST
    Repeati2604 – 264643LDL-receptor class B 29Add
    BLAST
    Domaini2651 – 269343EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini2698 – 273841LDL-receptor class A 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2739 – 277739LDL-receptor class A 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2778 – 281942LDL-receptor class A 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini2820 – 286142LDL-receptor class A 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini2862 – 290140LDL-receptor class A 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini2904 – 294542LDL-receptor class A 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini2946 – 299045LDL-receptor class A 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini2991 – 302939LDL-receptor class A 23PROSITE-ProRule annotationAdd
    BLAST
    Domaini3030 – 307041LDL-receptor class A 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini3073 – 311038LDL-receptor class A 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini3111 – 315141EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini3152 – 319241EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati3239 – 328143LDL-receptor class B 30Add
    BLAST
    Repeati3282 – 332443LDL-receptor class B 31Add
    BLAST
    Repeati3333 – 337644LDL-receptor class B 32Add
    BLAST
    Repeati3377 – 341842LDL-receptor class B 33Add
    BLAST
    Repeati3419 – 346042LDL-receptor class B 34Add
    BLAST
    Domaini3465 – 350945EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini3510 – 355041LDL-receptor class A 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini3551 – 359141LDL-receptor class A 27PROSITE-ProRule annotationAdd
    BLAST
    Domaini3592 – 363241LDL-receptor class A 28PROSITE-ProRule annotationAdd
    BLAST
    Domaini3633 – 367341LDL-receptor class A 29PROSITE-ProRule annotationAdd
    BLAST
    Domaini3676 – 371641LDL-receptor class A 30PROSITE-ProRule annotationAdd
    BLAST
    Domaini3717 – 375640LDL-receptor class A 31PROSITE-ProRule annotationAdd
    BLAST
    Domaini3757 – 379539LDL-receptor class A 32PROSITE-ProRule annotationAdd
    BLAST
    Domaini3796 – 383439LDL-receptor class A 33PROSITE-ProRule annotationAdd
    BLAST
    Domaini3840 – 388041LDL-receptor class A 34PROSITE-ProRule annotationAdd
    BLAST
    Domaini3881 – 392242LDL-receptor class A 35PROSITE-ProRule annotationAdd
    BLAST
    Domaini3926 – 396439LDL-receptor class A 36PROSITE-ProRule annotationAdd
    BLAST
    Domaini3966 – 400641EGF-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini4007 – 404842EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati4154 – 419643LDL-receptor class B 35Add
    BLAST
    Repeati4197 – 424044LDL-receptor class B 36Add
    BLAST
    Repeati4242 – 428342LDL-receptor class B 37Add
    BLAST
    Domaini4330 – 436839EGF-like 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini4377 – 441135EGF-like 17PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4589 – 460214Interaction with DAB2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi4453 – 446210SH3-bindingSequence Analysis
    Motifi4521 – 45266Endocytosis signalSequence Analysis
    Motifi4593 – 45986NPXY motif
    Motifi4598 – 46014SH2-bindingSequence Analysis
    Motifi4611 – 462212SH3-bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiNOG235850.
    HOGENOMiHOG000230574.
    HOVERGENiHBG097941.
    InParanoidiP98164.
    KOiK06233.
    OMAiFWADYGQ.
    OrthoDBiEOG790FZT.
    PhylomeDBiP98164.
    TreeFamiTF315253.

    Family and domain databases

    Gene3Di2.120.10.30. 8 hits.
    4.10.400.10. 35 hits.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR023415. LDLR_class-A_CS.
    IPR000033. LDLR_classB_rpt.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR019825. Lectin_legB_Mn/Ca_BS.
    [Graphical view]
    PfamiPF12662. cEGF. 1 hit.
    PF07645. EGF_CA. 2 hits.
    PF00057. Ldl_recept_a. 34 hits.
    PF00058. Ldl_recept_b. 14 hits.
    [Graphical view]
    PRINTSiPR00261. LDLRECEPTOR.
    SMARTiSM00181. EGF. 15 hits.
    SM00179. EGF_CA. 3 hits.
    SM00192. LDLa. 36 hits.
    SM00135. LY. 38 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 5 hits.
    SSF57424. SSF57424. 36 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 9 hits.
    PS50026. EGF_3. 6 hits.
    PS01187. EGF_CA. 3 hits.
    PS01209. LDLRA_1. 31 hits.
    PS50068. LDLRA_2. 36 hits.
    PS51120. LDLRB. 35 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P98164-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDRGPAAVAC TLLLALVACL APASGQECDS AHFRCGSGHC IPADWRCDGT     50
    KDCSDDADEI GCAVVTCQQG YFKCQSEGQC IPNSWVCDQD QDCDDGSDER 100
    QDCSQSTCSS HQITCSNGQC IPSEYRCDHV RDCPDGADEN DCQYPTCEQL 150
    TCDNGACYNT SQKCDWKVDC RDSSDEINCT EICLHNEFSC GNGECIPRAY 200
    VCDHDNDCQD GSDEHACNYP TCGGYQFTCP SGRCIYQNWV CDGEDDCKDN 250
    GDEDGCESGP HDVHKCSPRE WSCPESGRCI SIYKVCDGIL DCPGREDENN 300
    TSTGKYCSMT LCSALNCQYQ CHETPYGGAC FCPPGYIINH NDSRTCVEFD 350
    DCQIWGICDQ KCESRPGRHL CHCEEGYILE RGQYCKANDS FGEASIIFSN 400
    GRDLLIGDIH GRSFRILVES QNRGVAVGVA FHYHLQRVFW TDTVQNKVFS 450
    VDINGLNIQE VLNVSVETPE NLAVDWVNNK IYLVETKVNR IDMVNLDGSY 500
    RVTLITENLG HPRGIAVDPT VGYLFFSDWE SLSGEPKLER AFMDGSNRKD 550
    LVKTKLGWPA GVTLDMISKR VYWVDSRFDY IETVTYDGIQ RKTVVHGGSL 600
    IPHPFGVSLF EGQVFFTDWT KMAVLKANKF TETNPQVYYQ ASLRPYGVTV 650
    YHSLRQPYAT NPCKDNNGGC EQVCVLSHRT DNDGLGFRCK CTFGFQLDTD 700
    ERHCIAVQNF LIFSSQVAIR GIPFTLSTQE DVMVPVSGNP SFFVGIDFDA 750
    QDSTIFFSDM SKHMIFKQKI DGTGREILAA NRVENVESLA FDWISKNLYW 800
    TDSHYKSISV MRLADKTRRT VVQYLNNPRS VVVHPFAGYL FFTDWFRPAK 850
    IMRAWSDGSH LLPVINTTLG WPNGLAIDWA ASRLYWVDAY FDKIEHSTFD 900
    GLDRRRLGHI EQMTHPFGLA IFGEHLFFTD WRLGAIIRVR KADGGEMTVI 950
    RSGIAYILHL KSYDVNIQTG SNACNQPTHP NGDCSHFCFP VPNFQRVCGC 1000
    PYGMRLASNH LTCEGDPTNE PPTEQCGLFS FPCKNGRCVP NYYLCDGVDD 1050
    CHDNSDEQLC GTLNNTCSSS AFTCGHGECI PAHWRCDKRN DCVDGSDEHN 1100
    CPTHAPASCL DTQYTCDNHQ CISKNWVCDT DNDCGDGSDE KNCNSTETCQ 1150
    PSQFNCPNHR CIDLSFVCDG DKDCVDGSDE VGCVLNCTAS QFKCASGDKC 1200
    IGVTNRCDGV FDCSDNSDEA GCPTRPPGMC HSDEFQCQED GICIPNFWEC 1250
    DGHPDCLYGS DEHNACVPKT CPSSYFHCDN GNCIHRAWLC DRDNDCGDMS 1300
    DEKDCPTQPF RCPSWQWQCL GHNICVNLSV VCDGIFDCPN GTDESPLCNG 1350
    NSCSDFNGGC THECVQEPFG AKCLCPLGFL LANDSKTCED IDECDILGSC 1400
    SQHCYNMRGS FRCSCDTGYM LESDGRTCKV TASESLLLLV ASQNKIIADS 1450
    VTSQVHNIYS LVENGSYIVA VDFDSISGRI FWSDATQGKT WSAFQNGTDR 1500
    RVVFDSSIIL TETIAIDWVG RNLYWTDYAL ETIEVSKIDG SHRTVLISKN 1550
    LTNPRGLALD PRMNEHLLFW SDWGHHPRIE RASMDGSMRT VIVQDKIFWP 1600
    CGLTIDYPNR LLYFMDSYLD YMDFCDYNGH HRRQVIASDL IIRHPYALTL 1650
    FEDSVYWTDR ATRRVMRANK WHGGNQSVVM YNIQWPLGIV AVHPSKQPNS 1700
    VNPCAFSRCS HLCLLSSQGP HFYSCVCPSG WSLSPDLLNC LRDDQPFLIT 1750
    VRQHIIFGIS LNPEVKSNDA MVPIAGIQNG LDVEFDDAEQ YIYWVENPGE 1800
    IHRVKTDGTN RTVFASISMV GPSMNLALDW ISRNLYSTNP RTQSIEVLTL 1850
    HGDIRYRKTL IANDGTALGV GFPIGITVDP ARGKLYWSDQ GTDSGVPAKI 1900
    ASANMDGTSV KTLFTGNLEH LECVTLDIEE QKLYWAVTGR GVIERGNVDG 1950
    TDRMILVHQL SHPWGIAVHD SFLYYTDEQY EVIERVDKAT GANKIVLRDN 2000
    VPNLRGLQVY HRRNAAESSN GCSNNMNACQ QICLPVPGGL FSCACATGFK 2050
    LNPDNRSCSP YNSFIVVSML SAIRGFSLEL SDHSETMVPV AGQGRNALHV 2100
    DVDVSSGFIY WCDFSSSVAS DNAIRRIKPD GSSLMNIVTH GIGENGVRGI 2150
    AVDWVAGNLY FTNAFVSETL IEVLRINTTY RRVLLKVTVD MPRHIVVDPK 2200
    NRYLFWADYG QRPKIERSFL DCTNRTVLVS EGIVTPRGLA VDRSDGYVYW 2250
    VDDSLDIIAR IRINGENSEV IRYGSRYPTP YGITVFENSI IWVDRNLKKI 2300
    FQASKEPENT EPPTVIRDNI NWLRDVTIFD KQVQPRSPAE VNNNPCLENN 2350
    GGCSHLCFAL PGLHTPKCDC AFGTLQSDGK NCAISTENFL IFALSNSLRS 2400
    LHLDPENHSP PFQTINVERT VMSLDYDSVS DRIYFTQNLA SGVGQISYAT 2450
    LSSGIHTPTV IASGIGTADG IAFDWITRRI YYSDYLNQMI NSMAEDGSNR 2500
    TVIARVPKPR AIVLDPCQGY LYWADWDTHA KIERATLGGN FRVPIVNSSL 2550
    VMPSGLTLDY EEDLLYWVDA SLQRIERSTL TGVDREVIVN AAVHAFGLTL 2600
    YGQYIYWTDL YTQRIYRANK YDGSGQIAMT TNLLSQPRGI NTVVKNQKQQ 2650
    CNNPCEQFNG GCSHICAPGP NGAECQCPHE GNWYLANNRK HCIVDNGERC 2700
    GASSFTCSNG RCISEEWKCD NDNDCGDGSD EMESVCALHT CSPTAFTCAN 2750
    GRCVQYSYRC DYYNDCGDGS DEAGCLFRDC NATTEFMCNN RRCIPREFIC 2800
    NGVDNCHDNN TSDEKNCPDR TCQSGYTKCH NSNICIPRVY LCDGDNDCGD 2850
    NSDENPTYCT THTCSSSEFQ CASGRCIPQH WYCDQETDCF DASDEPASCG 2900
    HSERTCLADE FKCDGGRCIP SEWICDGDND CGDMSDEDKR HQCQNQNCSD 2950
    SEFLCVNDRP PDRRCIPQSW VCDGDVDCTD GYDENQNCTR RTCSENEFTC 3000
    GYGLCIPKIF RCDRHNDCGD YSDERGCLYQ TCQQNQFTCQ NGRCISKTFV 3050
    CDEDNDCGDG SDELMHLCHT PEPTCPPHEF KCDNGRCIEM MKLCNHLDDC 3100
    LDNSDEKGCG INECHDPSIS GCDHNCTDTL TSFYCSCRPG YKLMSDKRTC 3150
    VDIDECTEMP FVCSQKCENV IGSYICKCAP GYLREPDGKT CRQNSNIEPY 3200
    LIFSNRYYLR NLTIDGYFYS LILEGLDNVV ALDFDRVEKR LYWIDTQRQV 3250
    IERMFLNKTN KETIINHRLP AAESLAVDWV SRKLYWLDAR LDGLFVSDLN 3300
    GGHRRMLAQH CVDANNTFCF DNPRGLALHP QYGYLYWADW GHRAYIGRVG 3350
    MDGTNKSVII STKLEWPNGI TIDYTNDLLY WADAHLGYIE YSDLEGHHRH 3400
    TVYDGALPHP FAITIFEDTI YWTDWNTRTV EKGNKYDGSN RQTLVNTTHR 3450
    PFDIHVYHPY RQPIVSNPCG TNNGGCSHLC LIKPGGKGFT CECPDDFRTL 3500
    QLSGSTYCMP MCSSTQFLCA NNEKCIPIWW KCDGQKDCSD GSDELALCPQ 3550
    RFCRLGQFQC SDGNCTSPQT LCNAHQNCPD GSDEDRLLCE NHHCDSNEWQ 3600
    CANKRCIPES WQCDTFNDCE DNSDEDSSHC ASRTCRPGQF RCANGRCIPQ 3650
    AWKCDVDNDC GDHSDEPIEE CMSSAHLCDN FTEFSCKTNY RCIPKWAVCN 3700
    GVDDCRDNSD EQGCEERTCH PVGDFRCKNH HCIPLRWQCD GQNDCGDNSD 3750
    EENCAPRECT ESEFRCVNQQ CIPSRWICDH YNDCGDNSDE RDCEMRTCHP 3800
    EYFQCTSGHC VHSELKCDGS ADCLDASDEA DCPTRFPDGA YCQATMFECK 3850
    NHVCIPPYWK CDGDDDCGDG SDEELHLCLD VPCNSPNRFR CDNNRCIYSH 3900
    EVCNGVDDCG DGTDETEEHC RKPTPKPCTE YEYKCGNGHC IPHDNVCDDA 3950
    DDCGDWSDEL GCNKGKERTC AENICEQNCT QLNEGGFICS CTAGFETNVF 4000
    DRTSCLDINE CEQFGTCPQH CRNTKGSYEC VCADGFTSMS DRPGKRCAAE 4050
    GSSPLLLLPD NVRIRKYNLS SERFSEYLQD EEYIQAVDYD WDPKDIGLSV 4100
    VYYTVRGEGS RFGAIKRAYI PNFESGRNNL VQEVDLKLKY VMQPDGIAVD 4150
    WVGRHIYWSD VKNKRIEVAK LDGRYRKWLI STDLDQPAAI AVNPKLGLMF 4200
    WTDWGKEPKI ESAWMNGEDR NILVFEDLGW PTGLSIDYLN NDRIYWSDFK 4250
    EDVIETIKYD GTDRRVIAKE AMNPYSLDIF EDQLYWISKE KGEVWKQNKF 4300
    GQGKKEKTLV VNPWLTQVRI FHQLRYNKSV PNLCKQICSH LCLLRPGGYS 4350
    CACPQGSSFI EGSTTECDAA IELPINLPPP CRCMHGGNCY FDETDLPKCK 4400
    CPSGYTGKYC EMAFSKGISP GTTAVAVLLT ILLIVVIGAL AIAGFFHYRR 4450
    TGSLLPALPK LPSLSSLVKP SENGNGVTFR SGADLNMDIG VSGFGPETAI 4500
    DRSMAMSEDF VMEMGKQPII FENPMYSARD SAVKVVQPIQ VTVSENVDNK 4550
    NYGSPINPSE IVPETNPTSP AADGTQVTKW NLFKRKSKQT TNFENPIYAQ 4600
    MENEQKESVA ATPPPSPSLP AKPKPPSRRD PTPTYSATED TFKDTANLVK 4650
    EDSEV 4655
    Length:4,655
    Mass (Da):521,958
    Last modified:November 13, 2007 - v3
    Checksum:iC73C4206B8B28CE0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2724 – 27241D → G in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti2773 – 27731A → T in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti2827 – 28271T → P in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti2880 – 28823HWY → TFGI in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti2897 – 28971A → S in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti2908 – 29081A → S in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti2921 – 29211S → N in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti2954 – 29541L → P in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti2971 – 29722VC → PP in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti2982 – 29821Y → H in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti2985 – 29851N → I in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti3615 – 36151T → S in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti3738 – 37381Q → K in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti3784 – 37841C → LW in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti3810 – 38101C → R in AAB02882. (PubMed:7959795)Curated
    Sequence conflicti4220 – 42201R → P in AAB02882. (PubMed:7959795)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti83 – 831N → S.1 Publication
    Corresponds to variant rs2229263 [ dbSNP | Ensembl ].
    VAR_037009
    Natural varianti103 – 1031C → R Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
    VAR_064727
    Natural varianti259 – 2591G → R.
    Corresponds to variant rs34693334 [ dbSNP | Ensembl ].
    VAR_061294
    Natural varianti669 – 6691G → D.
    Corresponds to variant rs34291900 [ dbSNP | Ensembl ].
    VAR_037010
    Natural varianti909 – 9091H → R.
    Corresponds to variant rs36082715 [ dbSNP | Ensembl ].
    VAR_037011
    Natural varianti1083 – 10831H → Q.
    Corresponds to variant rs2302691 [ dbSNP | Ensembl ].
    VAR_037012
    Natural varianti1279 – 12791D → A.
    Corresponds to variant rs17848149 [ dbSNP | Ensembl ].
    VAR_029182
    Natural varianti1287 – 12871A → P.
    VAR_005421
    Natural varianti2012 – 20121R → K.
    Corresponds to variant rs4667596 [ dbSNP | Ensembl ].
    VAR_029183
    Natural varianti2065 – 20651I → T.
    Corresponds to variant rs2228168 [ dbSNP | Ensembl ].
    VAR_020218
    Natural varianti2522 – 25221Y → H in DBS. 1 Publication
    VAR_037013
    Natural varianti2632 – 26321N → D.
    Corresponds to variant rs17848169 [ dbSNP | Ensembl ].
    VAR_029184
    Natural varianti2872 – 28721A → T.
    Corresponds to variant rs2228171 [ dbSNP | Ensembl ].
    VAR_005422
    Natural varianti3011 – 30111R → M.
    Corresponds to variant rs11674973 [ dbSNP | Ensembl ].
    VAR_037014
    Natural varianti3305 – 33051R → H.
    Corresponds to variant rs3213760 [ dbSNP | Ensembl ].
    VAR_020219
    Natural varianti4094 – 40941K → E.1 Publication
    Corresponds to variant rs2075252 [ dbSNP | Ensembl ].
    VAR_005423
    Natural varianti4210 – 42101I → L.1 Publication
    Corresponds to variant rs4667591 [ dbSNP | Ensembl ].
    VAR_005424
    Natural varianti4272 – 42721M → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035996

    Sequence databases

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

    Genome annotation databases

    EnsembliENST00000263816; ENSP00000263816; ENSG00000081479.
    GeneIDi4036.
    KEGGihsa:4036.
    UCSCiuc002ues.3. human.

    Polymorphism databases

    DMDMi160332309.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33837 mRNA. Translation: AAB41649.1 .
    AC007556 Genomic DNA. No translation available.
    AC008178 Genomic DNA. No translation available.
    U04441 mRNA. Translation: AAB02882.1 .
    S73145 mRNA. Translation: AAB30825.1 .
    CCDSi CCDS2232.1.
    PIRi I38467.
    I53413.
    RefSeqi NP_004516.2. NM_004525.2.
    UniGenei Hs.657729.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2M0P NMR - A 1103-1148 [» ]
    ProteinModelPortali P98164.
    SMRi P98164. Positions 26-1346, 1351-4373.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110216. 34 interactions.
    IntActi P98164. 9 interactions.
    MINTi MINT-2860496.
    STRINGi 9606.ENSP00000263816.

    Chemistry

    DrugBanki DB00798. Gentamicin.
    DB00047. Insulin Glargine recombinant.
    DB00046. Insulin Lyspro recombinant.
    DB00030. Insulin recombinant.
    DB00071. Insulin, porcine.
    DB00013. Urokinase.

    PTM databases

    PhosphoSitei P98164.

    Polymorphism databases

    DMDMi 160332309.

    Proteomic databases

    MaxQBi P98164.
    PaxDbi P98164.
    PRIDEi P98164.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263816 ; ENSP00000263816 ; ENSG00000081479 .
    GeneIDi 4036.
    KEGGi hsa:4036.
    UCSCi uc002ues.3. human.

    Organism-specific databases

    CTDi 4036.
    GeneCardsi GC02M169947.
    GeneReviewsi LRP2.
    H-InvDB HIX0029894.
    HGNCi HGNC:6694. LRP2.
    HPAi HPA005980.
    MIMi 222448. phenotype.
    600073. gene.
    neXtProti NX_P98164.
    Orphaneti 2143. Donnai-Barrow syndrome.
    PharmGKBi PA30452.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235850.
    HOGENOMi HOG000230574.
    HOVERGENi HBG097941.
    InParanoidi P98164.
    KOi K06233.
    OMAi FWADYGQ.
    OrthoDBi EOG790FZT.
    PhylomeDBi P98164.
    TreeFami TF315253.

    Enzyme and pathway databases

    Reactomei REACT_13523. Vitamin D (calciferol) metabolism.
    REACT_24968. Retinoid metabolism and transport.
    SignaLinki P98164.

    Miscellaneous databases

    ChiTaRSi LRP2. human.
    GeneWikii LRP2.
    GenomeRNAii 4036.
    NextBioi 15810.
    PROi P98164.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P98164.
    Bgeei P98164.
    CleanExi HS_LRP2.
    Genevestigatori P98164.

    Family and domain databases

    Gene3Di 2.120.10.30. 8 hits.
    4.10.400.10. 35 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR023415. LDLR_class-A_CS.
    IPR000033. LDLR_classB_rpt.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR019825. Lectin_legB_Mn/Ca_BS.
    [Graphical view ]
    Pfami PF12662. cEGF. 1 hit.
    PF07645. EGF_CA. 2 hits.
    PF00057. Ldl_recept_a. 34 hits.
    PF00058. Ldl_recept_b. 14 hits.
    [Graphical view ]
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00181. EGF. 15 hits.
    SM00179. EGF_CA. 3 hits.
    SM00192. LDLa. 36 hits.
    SM00135. LY. 38 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 5 hits.
    SSF57424. SSF57424. 36 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 4 hits.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 9 hits.
    PS50026. EGF_3. 6 hits.
    PS01187. EGF_CA. 3 hits.
    PS01209. LDLRA_1. 31 hits.
    PS50068. LDLRA_2. 36 hits.
    PS51120. LDLRB. 35 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of human gp330, a Ca(2+)-binding receptor with potential intracellular signaling properties."
      Hjaelm G., Murray E., Crumley G., Harazim W., Lundgren S., Onyango I., Ek B., Larsson M., Juhlin C., Hellman P., Davis H., Aekerstroem G., Rask L., Morse B.
      Eur. J. Biochem. 239:132-137(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-83.
      Tissue: Kidney.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Chromosomal localization of human genes for the LDL receptor family member glycoprotein 330 (LRP2) and its associated protein RAP (LRPAP1)."
      Korenberg J.R., Argraves K.M., Chen X.N., Tran H., Strickland D.K., Argraves W.S.
      Genomics 22:88-93(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2705-4453, VARIANTS GLU-4094 AND LEU-4210.
      Tissue: Kidney.
    4. "A protein involved in calcium sensing of the human parathyroid and placental cytotrophoblast cells belongs to the LDL-receptor protein superfamily."
      Lundgren S., Hjaelm G., Hellman P., Ek B., Juhlin C., Rastad J., Klareskog L., Aakerstroem G., Rask L.
      Exp. Cell Res. 212:344-350(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4139-4406.
    5. "Identification of glycoprotein 330 as an endocytic receptor for apolipoprotein J/clusterin."
      Kounnas M.Z., Loukinova E.B., Stefansson S., Harmony J.A.K., Brewer B.H., Strickland D.K., Argraves W.S.
      J. Biol. Chem. 270:13070-13075(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLU.
    6. "Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin."
      Oleinikov A.V., Zhao J., Makker S.P.
      Biochem. J. 347:613-621(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2.
    7. "Functional interaction of megalin with the megalin-binding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule."
      Petersen H.H., Hilpert J., Militz D., Zandler V., Jacobsen C., Roebroek A.J.M., Willnow T.E.
      J. Cell Sci. 116:453-461(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRP2BP.
    8. "The adaptor disabled-2 binds to the third psi xNPxY sequence on the cytoplasmic tail of megalin."
      Gallagher H., Oleinikov A.V., Fenske C., Newman D.J.
      Biochimie 86:179-182(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2.
    9. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-4272.
    10. "Mutations in LRP2, which encodes the multiligand receptor megalin, cause Donnai-Barrow and facio-oculo-acoustico-renal syndromes."
      Kantarci S., Al-Gazali L., Hill R.S., Donnai D., Black G.C.M., Bieth E., Chassaing N., Lacombe D., Devriendt K., Teebi A., Loscertales M., Robson C., Liu T., MacLaughlin D.T., Noonan K.M., Russell M.K., Walsh C.A., Donahoe P.K., Pober B.R.
      Nat. Genet. 39:957-959(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DBS HIS-2522.
    11. Cited for: VARIANT ARG-103.

    Entry informationi

    Entry nameiLRP2_HUMAN
    AccessioniPrimary (citable) accession number: P98164
    Secondary accession number(s): O00711, Q16215
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3