Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q924X6

- LRP8_MOUSE

UniProt

Q924X6 - LRP8_MOUSE

Protein

Low-density lipoprotein receptor-related protein 8

Gene

Lrp8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor.1 Publication

    GO - Molecular functioni

    1. apolipoprotein binding Source: BHF-UCL
    2. calcium-dependent protein binding Source: BHF-UCL
    3. calcium ion binding Source: InterPro
    4. glycoprotein binding Source: BHF-UCL
    5. low-density lipoprotein receptor activity Source: MGI
    6. protein binding Source: IntAct
    7. reelin receptor activity Source: BHF-UCL

    GO - Biological processi

    1. ammon gyrus development Source: BHF-UCL
    2. endocytosis Source: UniProtKB
    3. hippocampus development Source: MGI
    4. layer formation in cerebral cortex Source: MGI
    5. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    6. positive regulation of CREB transcription factor activity Source: BHF-UCL
    7. positive regulation of dendrite development Source: BHF-UCL
    8. positive regulation of dendritic spine morphogenesis Source: BHF-UCL
    9. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    10. positive regulation of protein kinase activity Source: MGI
    11. positive regulation of protein tyrosine kinase activity Source: BHF-UCL
    12. receptor-mediated endocytosis Source: GOC
    13. reelin-mediated signaling pathway Source: BHF-UCL
    14. regulation of synaptic transmission Source: BHF-UCL
    15. ventral spinal cord development Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_198569. Retinoid metabolism and transport.

    Protein family/group databases

    TCDBi9.B.87.2.1. the selenoprotein p receptor (selp-receptor) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Low-density lipoprotein receptor-related protein 8
    Short name:
    LRP-8
    Alternative name(s):
    Apolipoprotein E receptor 2
    Gene namesi
    Name:Lrp8
    Synonyms:Apoer2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1340044. Lrp8.

    Subcellular locationi

    Cell membrane Curated; Single-pass type I membrane protein Curated. Secreted
    Note: Isoforms that contain the exon coding for a furin-type cleavage site are proteolytically processed, leading to a secreted receptor fragment.

    GO - Cellular componenti

    1. extracellular space Source: BHF-UCL
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: MGI
    4. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi61 – 611D → N: Lower affinity for RAP. Abolishes binding to Reelin. 1 Publication
    Mutagenesisi102 – 1021E → Q: Same affinity for RAP. Same affinity for Reelin. 1 Publication
    Mutagenesisi145 – 1451E → Q: Same affinity for RAP. Lower affinity for Reelin. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 996968Low-density lipoprotein receptor-related protein 8PRO_0000017333Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi41 ↔ 53By similarity
    Disulfide bondi48 ↔ 66By similarity
    Disulfide bondi60 ↔ 75By similarity
    Disulfide bondi80 ↔ 92By similarity
    Disulfide bondi87 ↔ 105By similarity
    Disulfide bondi99 ↔ 116By similarity
    Disulfide bondi121 ↔ 135By similarity
    Disulfide bondi128 ↔ 148By similarity
    Disulfide bondi142 ↔ 157By similarity
    Disulfide bondi161 ↔ 173By similarity
    Disulfide bondi168 ↔ 186By similarity
    Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi180 ↔ 195By similarity
    Disulfide bondi200 ↔ 213By similarity
    Disulfide bondi207 ↔ 226By similarity
    Disulfide bondi220 ↔ 237By similarity
    Disulfide bondi251 ↔ 264By similarity
    Disulfide bondi259 ↔ 277By similarity
    Disulfide bondi271 ↔ 286By similarity
    Disulfide bondi291 ↔ 303By similarity
    Disulfide bondi298 ↔ 316By similarity
    Disulfide bondi310 ↔ 325By similarity
    Disulfide bondi331 ↔ 344By similarity
    Disulfide bondi339 ↔ 357By similarity
    Disulfide bondi351 ↔ 368By similarity
    Disulfide bondi373 ↔ 384By similarity
    Disulfide bondi380 ↔ 393By similarity
    Disulfide bondi395 ↔ 407By similarity
    Disulfide bondi413 ↔ 423By similarity
    Disulfide bondi419 ↔ 432By similarity
    Disulfide bondi434 ↔ 447By similarity
    Glycosylationi551 – 5511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi805 – 8051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi840 – 8401N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain.1 Publication
    Undergoes sequential, furin and gamma-secretase dependent, proteolytic processing, resulting in the extracellular release of the entire ligand-binding domain as a soluble polypeptide and in the intracellular domain (ICD) release into the cytoplasm. The gamma-secretase-dependent proteolytical processing occurs after the bulk of the extracellular domain has been shed, in a furin-dependent manner, in alternatively spliced isoforms carrying the furin cleavage site. Hypoglycosylation (mainly hypo-O-glycosylation) leads to increased extracellular cleavage, which in turn results in accelerating release of the intracellular domain (ICD) by the gamma-secretase. The resulting receptor fragment is able to inhibit Reelin signaling and in particular the Reelin-induced DAB1 phosphorylation.2 Publications
    Tyrosine phosphorylated upon apoE binding.By similarity
    Ubiquitinated by MYLIP leading to degradation.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ924X6.
    PRIDEiQ924X6.

    PTM databases

    PhosphoSiteiQ924X6.

    Expressioni

    Tissue specificityi

    Expressed in neurons throughout the brain, with strong expression in pyramidal neurons of the hippocampus, granule cells of the dentate gyrus, cortical neurons and Purkinje cells of the cerebellum. Also expressed in the epithelium of the choroid plexus and of the blood vessels (apical expression), as well as in the epididymis.1 Publication

    Developmental stagei

    Expressed from embryonic day E12 to E16. Mice which are deficient in LRP8 have neuronal migration defect.

    Gene expression databases

    ArrayExpressiQ924X6.
    BgeeiQ924X6.
    GenevestigatoriQ924X6.

    Interactioni

    Subunit structurei

    Reelin associates with two or more receptor molecules. Interacts with DAB1 and JNK-interacting proteins. Interacts with SNX17. Interacts with PCSK9 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dlg4Q621083EBI-432319,EBI-300895
    Grin1P354384EBI-432319,EBI-400084
    Lrpap1Q990682EBI-432319,EBI-919734From a different organism.
    RelnQ608414EBI-432319,EBI-9248666

    Protein-protein interaction databases

    DIPiDIP-33284N.
    IntActiQ924X6. 7 interactions.
    MINTiMINT-111626.

    Structurei

    3D structure databases

    ProteinModelPortaliQ924X6.
    SMRiQ924X6. Positions 39-767.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 858830ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini882 – 996115CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei859 – 88123HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 7637LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini79 – 11739LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini120 – 15839LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini160 – 19637LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini199 – 23840LDL-receptor class A 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini250 – 28738LDL-receptor class A 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini290 – 32637LDL-receptor class A 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini330 – 36940LDL-receptor class A 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini364 – 40845EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini409 – 44840EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati495 – 54147LDL-receptor class B 1Add
    BLAST
    Repeati542 – 58443LDL-receptor class B 2Add
    BLAST
    Repeati585 – 62844LDL-receptor class B 3Add
    BLAST
    Repeati629 – 67143LDL-receptor class B 4Add
    BLAST
    Repeati672 – 71443LDL-receptor class B 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni773 – 83159Clustered O-linked oligosaccharidesAdd
    BLAST

    Domaini

    The cytoplasmic domain is involved in the binding of DAB1 and in the recruitment of JNK-interacting proteins. Isoforms, which lack part of the cytoplasmic domain, are unable to recruit members of the family of JNK interacting proteins (JIP) to the cytoplasmic tail.

    Sequence similaritiesi

    Belongs to the LDLR family.Curated
    Contains 2 EGF-like domains.PROSITE-ProRule annotation
    Contains 8 LDL-receptor class A domains.PROSITE-ProRule annotation
    Contains 5 LDL-receptor class B repeats.PROSITE-ProRule annotation

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiNOG255913.
    GeneTreeiENSGT00740000114992.
    HOGENOMiHOG000115656.
    HOVERGENiHBG006250.
    InParanoidiQ924X6.
    OMAiGCLQEST.
    OrthoDBiEOG7NGQ9P.
    PhylomeDBiQ924X6.

    Family and domain databases

    Gene3Di2.120.10.30. 1 hit.
    4.10.400.10. 8 hits.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    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.
    IPR023415. LDLR_class-A_CS.
    IPR000033. LDLR_classB_rpt.
    IPR002172. LDrepeatLR_classA_rpt.
    [Graphical view]
    PfamiPF07645. EGF_CA. 1 hit.
    PF00057. Ldl_recept_a. 8 hits.
    PF00058. Ldl_recept_b. 5 hits.
    [Graphical view]
    PRINTSiPR00261. LDLRECEPTOR.
    SMARTiSM00181. EGF. 2 hits.
    SM00179. EGF_CA. 1 hit.
    SM00192. LDLa. 8 hits.
    SM00135. LY. 5 hits.
    [Graphical view]
    SUPFAMiSSF57424. SSF57424. 8 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 2 hits.
    PS01187. EGF_CA. 1 hit.
    PS01209. LDLRA_1. 8 hits.
    PS50068. LDLRA_2. 8 hits.
    PS51120. LDLRB. 5 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q924X6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGRPELGALR PLALLLLLLL QLQHLSAADP LPGGQGPVKE CEEDQFRCRN    50
    ERCIPLVWRC DEDNDCSDNS DEDDCPKRTC ADSDFTCDNG HCIPERWKCD 100
    GEEECPDGSD ESKATCSSEE CPAEKLSCGP TSHKCVPASW RCDGEKDCEG 150
    GADEAGCPTL CAPHEFQCSN RSCLASVFVC DGDDDCGDGS DERGCSDPAC 200
    PPREFRCGGG GTCIPERWVC DRQFDCEDRS DEAAELCGRA GQGTTATPAA 250
    CAPTAQFTCR SGECIHLGWR CDGDRDCKDK SDEADCSPGP CRENEFQCGD 300
    GTCVLAIKRC NQERDCPDGS DEAGCLQEST CEGPRRFQCK SGECVDGGKV 350
    CDDQRDCRDW SDEPQKVCGL NECLHNNGGC SHICTDLKIG FECTCPAGFQ 400
    LLDQKTCGDI DECQDPDACS QICVNYKGYF KCECHPGYEM DTLTKNCKAV 450
    AGKSPSLIFT NRHEVRRIDL VKRDYSRLIP MLKNVVALDV EVATNRIYWC 500
    DLSYRKIYSA HMDKASIPDE QVVLIDEQLH SPEGLAVDWV HKHIYWTDSG 550
    NKTISVATTD GRRRCTLFSR ELSEPRAIAV DPLRGFMYWS DWGFQAKIEK 600
    AGLNGADRQT LVSDNIEWPN GITLDLLSQR LYWVDSKLHQ LSSIDFNGGN 650
    RKMLIFSTDF LSHPFGVAVF EDKVFWTDLE NEAIFSANRL NGLEIAILAE 700
    NLNNPHDIVI FHELKQPKAA DACDLSAQPN GGCEYLCLPA PQISSHSPKY 750
    TCACPDTMWL GPDMKRCYRA PQSTSTTTLA SAMTRTVPAT TRAPGTTIHD 800
    PTYQNHSTET PSQTAAAPHS VNVPRAPSTS PSTPSPATSN HSQHYGNEGS 850
    QMGSTVTAAV IGVIVPIVVI ALLCMSGYLI WRNWKRKNTK SMNFDNPVYR 900
    KTTEEEEEDE LHIGRTAQIG HVYPAAISNY DRPLWAEPCL GETRDLEDPA 950
    PALKELFVLP GEPRSQLHQL PKNPLSELPV VKCKRVALSL EDDGLP 996
    Length:996
    Mass (Da):109,818
    Last modified:May 10, 2004 - v2
    Checksum:iBA1AF0132A964EBA
    GO
    Isoform 2 (identifier: Q924X6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         160-285: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:870
    Mass (Da):96,351
    Checksum:i3531262B7C9D6446
    GO
    Isoform 3 (identifier: Q924X6-5)

    Also known as: ApoER2delta4-6,8-F

    Sequence is not available

    Note: Contains a 18 aa insert in the extracellular part which carries a furin cleavage site.

    Length:
    Mass (Da):

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321P → L in BAB46965. (PubMed:9685741)Curated
    Sequence conflicti286 – 2872CS → SA(PubMed:11294845)Curated
    Sequence conflicti610 – 6101T → P in CAC38356. (PubMed:11294845)Curated
    Sequence conflicti672 – 6732DK → VQ in CAC38356. (PubMed:11294845)Curated
    Sequence conflicti715 – 7162KQ → NE in CAC38356. (PubMed:11294845)Curated
    Sequence conflicti750 – 7501Y → F in CAC38356. (PubMed:11294845)Curated
    Sequence conflicti766 – 7661R → K in CAC38356. (PubMed:11294845)Curated
    Sequence conflicti802 – 8021T → A in CAC38356. (PubMed:11294845)Curated
    Sequence conflicti815 – 8173AAA → VAV in CAC38356. (PubMed:11294845)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei160 – 285126Missing in isoform 2. 1 PublicationVSP_010309Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85463 mRNA. Translation: BAB46965.1.
    AJ312058 mRNA. Translation: CAC38356.1.
    CCDSiCCDS51255.1. [Q924X6-2]
    PIRiJE0237.
    UniGeneiMm.442134.

    Genome annotation databases

    EnsembliENSMUST00000143601; ENSMUSP00000115854; ENSMUSG00000028613. [Q924X6-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85463 mRNA. Translation: BAB46965.1 .
    AJ312058 mRNA. Translation: CAC38356.1 .
    CCDSi CCDS51255.1. [Q924X6-2 ]
    PIRi JE0237.
    UniGenei Mm.442134.

    3D structure databases

    ProteinModelPortali Q924X6.
    SMRi Q924X6. Positions 39-767.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-33284N.
    IntActi Q924X6. 7 interactions.
    MINTi MINT-111626.

    Protein family/group databases

    TCDBi 9.B.87.2.1. the selenoprotein p receptor (selp-receptor) family.

    PTM databases

    PhosphoSitei Q924X6.

    Proteomic databases

    PaxDbi Q924X6.
    PRIDEi Q924X6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000143601 ; ENSMUSP00000115854 ; ENSMUSG00000028613 . [Q924X6-1 ]

    Organism-specific databases

    MGIi MGI:1340044. Lrp8.

    Phylogenomic databases

    eggNOGi NOG255913.
    GeneTreei ENSGT00740000114992.
    HOGENOMi HOG000115656.
    HOVERGENi HBG006250.
    InParanoidi Q924X6.
    OMAi GCLQEST.
    OrthoDBi EOG7NGQ9P.
    PhylomeDBi Q924X6.

    Enzyme and pathway databases

    Reactomei REACT_198569. Retinoid metabolism and transport.

    Miscellaneous databases

    NextBioi 13887235.
    PROi Q924X6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q924X6.
    Bgeei Q924X6.
    Genevestigatori Q924X6.

    Family and domain databases

    Gene3Di 2.120.10.30. 1 hit.
    4.10.400.10. 8 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    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.
    IPR023415. LDLR_class-A_CS.
    IPR000033. LDLR_classB_rpt.
    IPR002172. LDrepeatLR_classA_rpt.
    [Graphical view ]
    Pfami PF07645. EGF_CA. 1 hit.
    PF00057. Ldl_recept_a. 8 hits.
    PF00058. Ldl_recept_b. 5 hits.
    [Graphical view ]
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00181. EGF. 2 hits.
    SM00179. EGF_CA. 1 hit.
    SM00192. LDLa. 8 hits.
    SM00135. LY. 5 hits.
    [Graphical view ]
    SUPFAMi SSF57424. SSF57424. 8 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 2 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 2 hits.
    PS01187. EGF_CA. 1 hit.
    PS01209. LDLRA_1. 8 hits.
    PS50068. LDLRA_2. 8 hits.
    PS51120. LDLRB. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evolution of the apolipoprotein E receptor 2 gene by exon loss."
      Kim H.-J., Kim D.-H., Magoori K., Saeki S., Yamamoto T.
      J. Biochem. 124:451-456(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Alternative splicing in the ligand binding domain of mouse ApoE receptor-2 produces receptor variants binding reelin but not alpha2-macroglobulin."
      Brandes C., Kahr L., Stockinger W., Hiesberger T., Schneider W.J., Nimpf J.
      J. Biol. Chem. 276:22160-22169(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, INTERACTION WITH REELIN AND ALPHA2-MACROGLOBULIN.
    3. "The PX-domain protein SNX17 interacts with members of the LDL receptor family and modulates endocytosis of the LDL receptor."
      Stockinger W., Sailler B., Strasser V., Recheis B., Fasching D., Kahr L., Schneider W.J., Nimpf J.
      EMBO J. 21:4259-4267(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNX17.
    4. "Differential glycosylation regulates processing of lipoprotein receptors by gamma-secretase."
      May P., Bock H.H., Nimpf J., Herz J.
      J. Biol. Chem. 278:37386-37392(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, GLYCOSYLATION, PROTEOLYTIC PROCESSING.
    5. "A secreted soluble form of ApoE receptor 2 acts as a dominant-negative receptor and inhibits Reelin signaling."
      Koch S., Strasser V., Hauser C., Fasching D., Brandes C., Bajari T.M., Schneider W.J., Nimpf J.
      EMBO J. 21:5996-6004(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, PROTEOLYTIC PROCESSING.
    6. Cited for: FUNCTION IN SPERM DEVELOPMENT.
    7. "Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2."
      Trommsdorff M., Gotthardt M., Hiesberger T., Shelton J., Stockinger W., Nimpf J., Hammer R.E., Richardson J.A., Herz J.
      Cell 97:689-701(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB1.
    8. Cited for: INTERACTION WITH JNK-INTERACTING PROTEINS, TISSUE SPECIFICITY.
    9. "Differential binding of ligands to the apolipoprotein E receptor 2."
      Andersen O.M., Benhayon D., Curran T., Willnow T.E.
      Biochemistry 42:9355-9364(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAP AND REELIN, STOICHIOMETRY, MUTAGENESIS.

    Entry informationi

    Entry nameiLRP8_MOUSE
    AccessioniPrimary (citable) accession number: Q924X6
    Secondary accession number(s): Q8CAK9, Q8CDF5, Q921B6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    LRP8 and VLVLR together are required for correct embryonic development in the brain. Targeted disruption of both genes results in a phenotype virtually indistinguishable from that seen in "reeler" and "scrambler" mice. Subtle effects of VLDLR deletion are found mainly in the cerebellum, whereas lack of LRP8 predominantly affects the positioning of the neurons in the neocortex. Besides brain formation defects, LRP8-deficient mice also exhibit male infertility.

    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

    External Data

    Dasty 3