LRP8
entrez
7804
canonical
uniprot
Q14114
canonical
ensembl
ENSG00000157193
resolver
ensp
ENSP00000303634
resolver
ensp
ENSP00000334522
resolver
ensp
ENSP00000346391
resolver
ensp
ENSP00000360509
resolver
genesymbol
LRP8
resolver
genesymbol_syn
APOER2
resolver
hgnc
HGNC:6700
resolver
uniprot
B1AMT6
resolver
uniprot
B1AMT7
resolver
uniprot
B1AMT8
resolver
uniprot
O14968
resolver
uniprot
Q86V27
resolver
uniprot
Q99876
resolver
uniprot
Q9BR78
resolver
uniprot_entry
LRP8_HUMAN
resolver
uniprot_sec
B1AMT6
resolver
uniprot_sec
B1AMT7
resolver
uniprot_sec
B1AMT8
resolver
uniprot_sec
O14968
resolver
uniprot_sec
Q86V27
resolver
uniprot_sec
Q99876
resolver
uniprot_sec
Q9BR78
resolver
amino_acid_sequence
MGLPEPGPLRLLALLLLLLLLLLLQLQHLAAAAADPLLGGQGPAKDCEKDQFQCRNERCIPSVWRCDEDDDCLDHSDEDDCPKKTCADSDFTCDNGHCIHERWKCDGEEECPDGSDESEATCTKQVCPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCATLCAPHEFQCGNRSCLAAVFVCDGDDDCGDGSDERGCADPACGPREFRCGGDGGGACIPERWVCDRQFDCEDRSDEAAELCGRPGPGATSAPAACATASQFACRSGECVHLGWRCDGDRDCKDKSDEADCPLGTCRGDEFQCGDGTCVLAIKHCNQEQDCPDGSDEAGCLQGLNECLHNNGGCSHICTDLKIGFECTCPAGFQLLDQKTCGDIDECKDPDACSQICVNYKGYFKCECYPGYEMDLLTKNCKAAAGKSPSLIFTNRHEVRRIDLVKRNYSRLIPMLKNVVALDVEVATNRIYWCDLSYRKIYSAYMDKASDPKEQEVLIDEQLHSPEGLAVDWVHKHIYWTDSGNKTISVATVDGGRRRTLFSRNLSEPRAIAVDPLRGFMYWSDWGDQAKIEKSGLNGVDRQTLVSDNIEWPNGITLDLLSQRLYWVDSKLHQLSSIDFSGGNRKTLISSTDFLSHPFGIAVFEDKVFWTDLENEAIFSANRLNGLEISILAENLNNPHDIVIFHELKQPRAPDACELSVQPNGGCEYLCLPAPQISSHSPKYTCACPDTMWLGPDMKRCYRAPQSTSTTTLASTMTRTVPATTRAPGTTVHRSTYQNHSTETPSLTAAVPSSVSVPRAPSISPSTLSPATSNHSQHYANEDSKMGSTVTAAVIGIIVPIVVIALLCMSGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEDEDELHIGRTAQIGHVYPAAISSFDRPLWAEPCLGETREPEDPAPALKELFVLPGEPRSQLHQLPKNPLSELPVVKSKRVALSLEDDGLP
uniprot
proteins
disease_involvement
DISEASE: Myocardial infarction 1 (MCI1) [MIM:608446]: A condition defined by the irreversible necrosis of heart muscle secondary to prolonged ischemia. {ECO:0000269|PubMed:17847002}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands (PubMed:12899622, PubMed:12950167, PubMed:20223215, PubMed:30873003). LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail (By similarity). Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons (By similarity). LRP8 has higher affinity for Reelin than VLDLR (By similarity). LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development (By similarity). Binds the endoplasmic reticulum resident receptor-associated protein (RAP) (By similarity). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature (PubMed:12807892). 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 (By similarity). May also function as an endocytic receptor (By similarity). Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q924X6, ECO:0000269|PubMed:12807892, ECO:0000269|PubMed:12899622, ECO:0000269|PubMed:12950167, ECO:0000269|PubMed:20223215, ECO:0000269|PubMed:30873003}.; FUNCTION: (Microbial infection) Acts as a receptor for Semliki Forest virus. {ECO:0000269|PubMed:34929721}.; FUNCTION: (Microbial infection) Acts as a receptor for tick-borne encephalitis virus by mediating viral cell attachment and internalization. {ECO:0000269|PubMed:34929721}.
uniprot
proteins
mass_dalton
105634
uniprot
proteins
post_translational_modification
PTM: O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain (By similarity). {ECO:0000250|UniProtKB:Q924X6}.; 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 (By similarity). {ECO:0000250|UniProtKB:Q924X6}.; PTM: Tyrosine phosphorylated upon apoE binding. {ECO:0000269|PubMed:12681505}.; PTM: Ubiquitinated by MYLIP leading to degradation. {ECO:0000269|PubMed:20427281}.
uniprot
proteins
protein_family
LDLR family
uniprot
proteins
pubmed
10218790
uniprot
proteins
pubmed
10508213
uniprot
proteins
pubmed
11152697
uniprot
proteins
pubmed
12399018
uniprot
proteins
pubmed
12681505
uniprot
proteins
pubmed
12807892
uniprot
proteins
pubmed
12899622
uniprot
proteins
pubmed
12950167
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17847002
uniprot
proteins
pubmed
18039658
uniprot
proteins
pubmed
20223215
uniprot
proteins
pubmed
20427281
uniprot
proteins
pubmed
24381170
uniprot
proteins
pubmed
30873003
uniprot
proteins
pubmed
34929721
uniprot
proteins
pubmed
39095394
uniprot
proteins
pubmed
40993380
uniprot
proteins
pubmed
8626535
uniprot
proteins
pubmed
9079678
uniprot
proteins
sequence_length
963
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30873003}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:Q924X6}. Note=Isoforms that contain the exon coding for a furin-type cleavage site are proteolytically processed, leading to a secreted receptor fragment. {ECO:0000250|UniProtKB:Q924X6}.
uniprot
proteins
transmembrane_region
TRANSMEM 827..847; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins