Lrp8
entrez
16975
canonical
uniprot
Q924X6
canonical
ensembl
ENSMUSG00000028613
resolver
ensp
ENSMUSP00000030356
resolver
ensp
ENSMUSP00000102342
resolver
ensp
ENSMUSP00000102343
resolver
ensp
ENSMUSP00000102344
resolver
ensp
ENSMUSP00000158610
resolver
ensp
ENSMUSP00000158644
resolver
ensp
ENSMUSP00000207876
resolver
ensp
ENSMUSP00000207877
resolver
ensp
ENSMUSP00000207878
resolver
ensp
ENSMUSP00000207879
resolver
ensp
ENSMUSP00000207880
resolver
ensp
ENSMUSP00000207882
resolver
ensp
ENSMUSP00000207883
resolver
ensp
ENSMUSP00000207884
resolver
ensp
ENSMUSP00000207885
resolver
ensp
ENSMUSP00000207886
resolver
ensp
ENSMUSP00000207887
resolver
ensp
ENSMUSP00000207888
resolver
ensp
ENSMUSP00000207889
resolver
ensp
ENSMUSP00000207890
resolver
ensp
ENSMUSP00000207891
resolver
ensp
ENSMUSP00000207892
resolver
ensp
ENSMUSP00000207893
resolver
ensp
ENSMUSP00000207894
resolver
ensp
ENSMUSP00000207895
resolver
ensp
ENSMUSP00000207897
resolver
enst
ENSMUST00000030356
resolver
enst
ENSMUST00000106731
resolver
enst
ENSMUST00000106733
resolver
enst
ENSMUST00000238584
resolver
genesymbol
Lrp8
resolver
genesymbol_syn
Apoer2
resolver
uniprot
A0A571BE60
resolver
uniprot
B1AXJ4
resolver
uniprot
B1AXJ5
resolver
uniprot
F6YZZ8
resolver
uniprot
Q8CAK9
resolver
uniprot
Q8CDF5
resolver
uniprot
Q921B6
resolver
uniprot_entry
A0A571BE60_MOUSE
resolver
uniprot_entry
B1AXJ4_MOUSE
resolver
uniprot_entry
B1AXJ5_MOUSE
resolver
uniprot_entry
F6YZZ8_MOUSE
resolver
uniprot_entry
LRP8_MOUSE
resolver
uniprot_sec
Q8CAK9
resolver
uniprot_sec
Q8CDF5
resolver
uniprot_sec
Q921B6
resolver
amino_acid_sequence
MGRPELGALRPLALLLLLLLQLQHLSAADPLPGGQGPVKECEEDQFRCRNERCIPLVWRCDEDNDCSDNSDEDDCPKRTCADSDFTCDNGHCIPERWKCDGEEECPDGSDESKATCSSEECPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCPTLCAPHEFQCSNRSCLASVFVCDGDDDCGDGSDERGCSDPACPPREFRCGGGGTCIPERWVCDRQFDCEDRSDEAAELCGRAGQGTTATPAACAPTAQFTCRSGECIHLGWRCDGDRDCKDKSDEADCSPGPCRENEFQCGDGTCVLAIKRCNQERDCPDGSDEAGCLQESTCEGPRRFQCKSGECVDGGKVCDDQRDCRDWSDEPQKVCGLNECLHNNGGCSHICTDLKIGFECTCPAGFQLLDQKTCGDIDECQDPDACSQICVNYKGYFKCECHPGYEMDTLTKNCKAVAGKSPSLIFTNRHEVRRIDLVKRDYSRLIPMLKNVVALDVEVATNRIYWCDLSYRKIYSAHMDKASIPDEQVVLIDEQLHSPEGLAVDWVHKHIYWTDSGNKTISVATTDGRRRCTLFSRELSEPRAIAVDPLRGFMYWSDWGFQAKIEKAGLNGADRQTLVSDNIEWPNGITLDLLSQRLYWVDSKLHQLSSIDFNGGNRKMLIFSTDFLSHPFGVAVFEDKVFWTDLENEAIFSANRLNGLEIAILAENLNNPHDIVIFHELKQPKAADACDLSAQPNGGCEYLCLPAPQISSHSPKYTCACPDTMWLGPDMKRCYRAPQSTSTTTLASAMTRTVPATTRAPGTTIHDPTYQNHSTETPSQTAAAPHSVNVPRAPSTSPSTPSPATSNHSQHYGNEGSQMGSTVTAAVIGVIVPIVVIALLCMSGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEEEDELHIGRTAQIGHVYPAAISNYDRPLWAEPCLGETRDLEDPAPALKELFVLPGEPRSQLHQLPKNPLSELPVVKCKRVALSLEDDGLP
uniprot
proteins
function
FUNCTION: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands (PubMed:10380922, PubMed:11294845, PubMed:12899622, PubMed:18778775). LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail (PubMed:10380922). Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons (PubMed:10380922). LRP8 has higher affinity for Reelin than VLDLR (PubMed:10380922, PubMed:11294845). LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development (PubMed:10380922, PubMed:11294845, PubMed:18778775). Binds the endoplasmic reticulum resident receptor-associated protein (RAP) (PubMed:12899622). 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 (PubMed:12695510). May also function as an endocytic receptor (PubMed:12169628). Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (PubMed:18174160). Together with its ligand, apolipoprotein E (apoE), may indirectly play a role in the suppression of the innate immune response by controlling the survival of myeloid-derived suppressor cells (PubMed:29336888). {ECO:0000269|PubMed:10380922, ECO:0000269|PubMed:11294845, ECO:0000269|PubMed:12169628, ECO:0000269|PubMed:12695510, ECO:0000269|PubMed:12899622, ECO:0000269|PubMed:18174160, ECO:0000269|PubMed:18778775, ECO:0000269|PubMed:29336888}.
uniprot
proteins
mass_dalton
109818
uniprot
proteins
mutagenesis
MUTAGEN 61; /note="D->N: Lower affinity for RAP. Abolishes binding to Reelin."; /evidence="ECO:0000269|PubMed:12899622"; MUTAGEN 102; /note="E->Q: Same affinity for RAP. Same affinity for Reelin."; /evidence="ECO:0000269|PubMed:12899622"; MUTAGEN 145; /note="E->Q: Same affinity for RAP. Lower affinity for Reelin."; /evidence="ECO:0000269|PubMed:12899622
uniprot
proteins
post_translational_modification
PTM: O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain. {ECO:0000269|PubMed:12871934}.; PTM: 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. {ECO:0000269|PubMed:12426372, ECO:0000269|PubMed:12871934}.; PTM: Tyrosine phosphorylated upon apoE binding. {ECO:0000250|UniProtKB:Q14114}.; PTM: Ubiquitinated by MYLIP leading to degradation. {ECO:0000250|UniProtKB:Q14114}.
uniprot
proteins
protein_family
LDLR family
uniprot
proteins
pubmed
10380922
uniprot
proteins
pubmed
10827199
uniprot
proteins
pubmed
11294845
uniprot
proteins
pubmed
12169628
uniprot
proteins
pubmed
12426372
uniprot
proteins
pubmed
12573468
uniprot
proteins
pubmed
12695510
uniprot
proteins
pubmed
12871934
uniprot
proteins
pubmed
12899622
uniprot
proteins
pubmed
18174160
uniprot
proteins
pubmed
18778775
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
29336888
uniprot
proteins
pubmed
9685741
uniprot
proteins
sequence_length
996
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14114}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:12426372, ECO:0000269|PubMed:12871934}. Note=Isoforms that contain the exon coding for a furin-type cleavage site are proteolytically processed, leading to a secreted receptor fragment. {ECO:0000269|PubMed:12426372, ECO:0000269|PubMed:12871934}.
uniprot
proteins
transmembrane_region
TRANSMEM 859..881; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins