SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q924X6

- LRP8_MOUSE

UniProt

Q924X6 - LRP8_MOUSE

(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)

Protein
Low-density lipoprotein receptor-related protein 8
Gene
Lrp8, Apoer2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 ion binding Source: InterPro
  3. calcium-dependent protein binding Source: BHF-UCL
  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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 858830Extracellular Reviewed prediction
Add
BLAST
Transmembranei859 – 88123Helical; Reviewed prediction
Add
BLAST
Topological domaini882 – 996115Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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.
Mutagenesisi102 – 1021E → Q: Same affinity for RAP. Same affinity for Reelin.
Mutagenesisi145 – 1451E → Q: Same affinity for RAP. Lower affinity for Reelin.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.
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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg4Q621083EBI-432319,EBI-300895
Grin1P354384EBI-432319,EBI-400084

Protein-protein interaction databases

DIPiDIP-33284N.
IntActiQ924X6. 5 interactions.
MINTiMINT-111626.

Structurei

3D structure databases

ProteinModelPortaliQ924X6.
SMRiQ924X6. Positions 39-767.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni773 – 83159Clustered O-linked oligosaccharides
Add
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.
Contains 2 EGF-like domains.

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):

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei160 – 285126Missing in isoform 2.
VSP_010309Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321P → L in BAB46965. 1 Publication
Sequence conflicti286 – 2872CS → SA1 Publication
Sequence conflicti610 – 6101T → P in CAC38356. 1 Publication
Sequence conflicti672 – 6732DK → VQ in CAC38356. 1 Publication
Sequence conflicti715 – 7162KQ → NE in CAC38356. 1 Publication
Sequence conflicti750 – 7501Y → F in CAC38356. 1 Publication
Sequence conflicti766 – 7661R → K in CAC38356. 1 Publication
Sequence conflicti802 – 8021T → A in CAC38356. 1 Publication
Sequence conflicti815 – 8173AAA → VAV in CAC38356. 1 Publication

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. 5 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: September 3, 2014
This is version 128 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

Similar proteinsi