OLR1
entrez
4973
canonical
uniprot
P78380
canonical
ensembl
ENSG00000173391
resolver
ensp
ENSP00000309124
resolver
ensp
ENSP00000405116
resolver
ensp
ENSP00000439251
resolver
ensp
ENSP00000442389
resolver
ensp
ENSP00000704534
resolver
genesymbol
OLR1
resolver
genesymbol_syn
CLEC8A
resolver
genesymbol_syn
LOX1
resolver
hgnc
HGNC:8133
resolver
uniprot
A8K7V9
resolver
uniprot
B4DI48
resolver
uniprot
G3V1I4
resolver
uniprot
Q2PP00
resolver
uniprot
Q7Z484
resolver
uniprot_entry
OLR1_HUMAN
resolver
uniprot_sec
A8K7V9
resolver
uniprot_sec
B4DI48
resolver
uniprot_sec
G3V1I4
resolver
uniprot_sec
Q2PP00
resolver
uniprot_sec
Q7Z484
resolver
amino_acid_sequence
MTFDDLKIQTVKDQPDEKSNGKKAKGLQFLYSPWWCLAAATLGVLCLGLVVTIMVLGMQLSQVSDLLTQEQANLTHQKKKLEGQISARQQAEEASQESENELKEMIETLARKLNEKSKEQMELHHQNLNLQETLKRVANCSAPCPQDWIWHGENCYLFSSGSFNWEKSQEKCLSLDAKLLKINSTADLDFIQQAISYSSFPFWMGLSRRNPSYPWLWEDGSPLMPHLFRVRGAVSQTYPSGTCAYIQRGAVYAENCILAAFSICQKKANLRAQ
uniprot
proteins
disease_involvement
DISEASE: Note=Independent association genetic studies have implicated OLR1 gene variants in myocardial infarction susceptibility.; DISEASE: Note=OLR1 may be involved in Alzheimer disease (AD). Involvement in AD is however unclear: according to some authors, variations in OLR1 modify the risk of AD (PubMed:12354387, PubMed:12810610, PubMed:15976314). While according to others they do not (PubMed:15000751, PubMed:15060104). {ECO:0000269|PubMed:12384789, ECO:0000269|PubMed:12807963, ECO:0000269|PubMed:15860461}.
uniprot
proteins
function
FUNCTION: Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria. {ECO:0000269|PubMed:11821063, ECO:0000269|PubMed:12354387, ECO:0000269|PubMed:9052782}.; FUNCTION: (Microbial infection) May serve as a receptor for adhesin A variant 3 (nadA) of N.meningitidis. {ECO:0000305|PubMed:27302108}.
uniprot
proteins
mass_dalton
30959
uniprot
proteins
mutagenesis
MUTAGEN 22..25; /note="KKAK->EEAE: Impairs sorting into the cell surface but retains ability to bind oxLDL. Abolishes sorting into the cell surface; when associated with K-69."; /evidence="ECO:0000269|PubMed:15935375"; MUTAGEN 70; /note="E->K: Abolishes sorting into the cell surface; when associated with 22-E--E-25."; /evidence="ECO:0000269|PubMed:15935375"; MUTAGEN 140; /note="C->S: Abolishes homodimerization."; /evidence="ECO:0000269|PubMed:15000751"; MUTAGEN 144; /note="C->S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-155; S-172; S-243; S-256 and S-264."; /evidence="ECO:0000269|PubMed:11256994"; MUTAGEN 150; /note="W->A: Abolishes binding to acetylated LDL (AcLDL), probably due to inappropriate homodimerization."; /evidence="ECO:0000269|PubMed:15939022"; MUTAGEN 155; /note="C->S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-172; S-243; S-256 and S-264."; /evidence="ECO:0000269|PubMed:11256994"; MUTAGEN 172; /note="C->S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-243; S-256 and S-264."; /evidence="ECO:0000269|PubMed:11256994"; MUTAGEN 183; /note="N->Q: Does not affect glycosylation state."; /evidence="ECO:0000269|PubMed:11256994"; MUTAGEN 193; /note="Q->L: Impairs binding to acetylated LDL (AcLDL); when associated with 198-AA-199."; MUTAGEN 198..199; /note="SS->AA: Impairs binding to acetylated LDL (AcLDL); when associated with L-193."; MUTAGEN 208; /note="R->N: Does not affect subcellular location but displays a strongly reduced affinity for acetylated LDL (AcLDL)."; /evidence="ECO:0000269|PubMed:15939022"; MUTAGEN 209..210; /note="RN->LL: Abolishes binding to acetylated LDL (AcLDL)."; /evidence="ECO:0000269|PubMed:11256994"; MUTAGEN 209; /note="R->N: Does not affect binding to acetylated LDL (AcLDL)."; /evidence="ECO:0000269|PubMed:15939022"; MUTAGEN 226; /note="H->A: No effect."; /evidence="ECO:0000269|PubMed:11256994, ECO:0000269|PubMed:15939022"; MUTAGEN 226; /note="H->Q: Abolishes binding to acetylated LDL (AcLDL); when associated with N-229 and N-231."; /evidence="ECO:0000269|PubMed:11256994, ECO:0000269|PubMed:15939022"; MUTAGEN 229; /note="R->N: Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL). Abolishes binding to acetylated LDL (AcLDL); when associated with Q-226 and N-231."; /evidence="ECO:0000269|PubMed:11256994, ECO:0000269|PubMed:15939022"; MUTAGEN 231; /note="R->N: Abolishes binding to acetylated LDL (AcLDL). Abolishes binding to AcLDL; when associated with Q-226 and N-229."; /evidence="ECO:0000269|PubMed:11256994, ECO:0000269|PubMed:15939022"; MUTAGEN 235..236; /note="SQ->AL: Impairs binding to acetylated LDL (AcLDL); when associated with A-240."; /evidence="ECO:0000269|PubMed:11256994"; MUTAGEN 240; /note="S->A: Impairs binding to acetylated LDL (AcLDL); when associated with 235-AL-236."; /evidence="ECO:0000269|PubMed:11256994"; MUTAGEN 243; /note="C->S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-256 and S-264."; /evidence="ECO:0000269|PubMed:11256994"; MUTAGEN 248; /note="R->N: Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL)."; /evidence="ECO:0000269|PubMed:15939022"; MUTAGEN 256; /note="C->S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-243 and S-264."; /evidence="ECO:0000269|PubMed:11256994"; MUTAGEN 264; /note="C->S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-243 and S-256."; /evidence="ECO:0000269|PubMed:11256994"; MUTAGEN 267..273; /note="Missing: Impairs protein folding and transport."; /evidence="ECO:0000269|PubMed:11256994
uniprot
proteins
post_translational_modification
PTM: The intrachain disulfide-bonds prevent N-glycosylation at some sites.; PTM: N-glycosylated.
uniprot
proteins
pubmed
11256994
uniprot
proteins
pubmed
11821063
uniprot
proteins
pubmed
12354387
uniprot
proteins
pubmed
12384789
uniprot
proteins
pubmed
12646194
uniprot
proteins
pubmed
12807963
uniprot
proteins
pubmed
12810610
uniprot
proteins
pubmed
12878212
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15000751
uniprot
proteins
pubmed
15060104
uniprot
proteins
pubmed
15276231
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15695803
uniprot
proteins
pubmed
15860461
uniprot
proteins
pubmed
15935375
uniprot
proteins
pubmed
15939022
uniprot
proteins
pubmed
15976314
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
22688517
uniprot
proteins
pubmed
23583401
uniprot
proteins
pubmed
27302108
uniprot
proteins
pubmed
30327444
uniprot
proteins
pubmed
9052782
uniprot
proteins
pubmed
9763655
uniprot
proteins
pubmed
9828121
uniprot
proteins
sequence_length
273
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell membrane; Single-pass type II membrane protein. Membrane raft. Secreted. Note=A secreted form also exists. Localization to membrane rafts requires palmitoylation.
uniprot
proteins
transmembrane_region
TRANSMEM 37..57; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins