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P78380

- OLR1_HUMAN

UniProt

P78380 - OLR1_HUMAN

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Protein
Oxidized low-density lipoprotein receptor 1
Gene
OLR1, CLEC8A, LOX1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei183 – 1831Not glycosylated Inferred

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. low-density lipoprotein receptor activity Source: Ensembl

GO - Biological processi

  1. blood circulation Source: ProtInc
  2. blood coagulation Source: Reactome
  3. cell death Source: Ensembl
  4. inflammatory response Source: UniProtKB-KW
  5. leukocyte cell-cell adhesion Source: Ensembl
  6. leukocyte migration Source: Reactome
  7. lipoprotein metabolic process Source: Ensembl
  8. proteolysis Source: ProtInc
  9. response to hydrogen peroxide Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion, Immunity, Inflammatory response

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxidized low-density lipoprotein receptor 1
Short name:
Ox-LDL receptor 1
Alternative name(s):
C-type lectin domain family 8 member A
Lectin-like oxidized LDL receptor 1
Short name:
LOX-1
Short name:
Lectin-like oxLDL receptor 1
Short name:
hLOX-1
Lectin-type oxidized LDL receptor 1
Cleaved into the following chain:
Gene namesi
Name:OLR1
Synonyms:CLEC8A, LOX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:8133. OLR1.

Subcellular locationi

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.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3636Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei37 – 5721Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini58 – 273216Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. integral component of plasma membrane Source: ProtInc
  3. intracellular membrane-bounded organelle Source: HPA
  4. membrane Source: ProtInc
  5. membrane raft Source: UniProtKB-SubCell
  6. nucleus Source: HPA
  7. plasma membrane Source: HPA
  8. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Independent association genetic studies have implicated OLR1 gene variants in myocardial infarction susceptibility.5 Publications
OLR1 may be involved in Alzheimer disease (AD). Involvement in AD is however unclear: according to some authors (1 Publication, 1 Publication and 1 Publication), variations in OLR1 modify the risk of AD, while according to other (1 Publication and 1 Publication) they do not.5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 254KKAK → EEAE: Impairs sorting into the cell surface but retains ability to bind oxLDL. Abolishes sorting into the cell surface; when associated with K-69. 1 Publication
Mutagenesisi70 – 701E → K: Abolishes sorting into the cell surface; when associated with 22-E--E-25. 1 Publication
Mutagenesisi140 – 1401C → S: Abolishes homodimerization. 1 Publication
Mutagenesisi144 – 1441C → 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. 1 Publication
Mutagenesisi150 – 1501W → A: Abolishes binding to acetylated LDL (AcLDL), probably due to inappropriate homodimerization. 1 Publication
Mutagenesisi155 – 1551C → 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. 1 Publication
Mutagenesisi172 – 1721C → 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. 1 Publication
Mutagenesisi183 – 1831N → Q: Does not affect glycosylation state. 1 Publication
Mutagenesisi193 – 1931Q → L: Impairs binding to acetylated LDL (AcLDL); when associated with 198-AA-199.
Mutagenesisi198 – 1992SS → AA: Impairs binding to acetylated LDL (AcLDL); when associated with L-193.
Mutagenesisi208 – 2081R → N: Does not affect subcellular location but displays a strongly reduced affinity for acetylated LDL (AcLDL). 1 Publication
Mutagenesisi209 – 2102RN → LL: Abolishes binding to acetylated LDL (AcLDL). 1 Publication
Mutagenesisi209 – 2091R → N: Does not affect binding to acetylated LDL (AcLDL). 1 Publication
Mutagenesisi226 – 2261H → A: No effect. 2 Publications
Mutagenesisi226 – 2261H → Q: Abolishes binding to acetylated LDL (AcLDL); when associated with N-229 and N-231. 2 Publications
Mutagenesisi229 – 2291R → 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. 2 Publications
Mutagenesisi231 – 2311R → N: Abolishes binding to acetylated LDL (AcLDL). Abolishes binding to AcLDL; when associated with Q-226 and N-229. 2 Publications
Mutagenesisi235 – 2362SQ → AL: Impairs binding to acetylated LDL (AcLDL); when associated with A-240.
Mutagenesisi240 – 2401S → A: Impairs binding to acetylated LDL (AcLDL); when associated with 235-AL-236. 1 Publication
Mutagenesisi243 – 2431C → 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. 1 Publication
Mutagenesisi248 – 2481R → N: Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL). 1 Publication
Mutagenesisi256 – 2561C → 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. 1 Publication
Mutagenesisi264 – 2641C → 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. 1 Publication
Mutagenesisi267 – 2737Missing: Impairs protein folding and transport. 1 Publication

Organism-specific databases

MIMi602601. gene+phenotype.
PharmGKBiPA31920.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 273Oxidized low-density lipoprotein receptor 1, soluble formPRO_0000017444
Chaini1 – 273273Oxidized low-density lipoprotein receptor 1
PRO_0000017443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi36 – 361S-palmitoyl cysteine1 Publication
Lipidationi46 – 461S-palmitoyl cysteine1 Publication
Glycosylationi73 – 731N-linked (GlcNAc...) Reviewed prediction
Glycosylationi139 – 1391N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi140 – 140Interchain4 Publications
Disulfide bondi144 ↔ 1554 Publications
Disulfide bondi172 ↔ 2644 Publications
Disulfide bondi243 ↔ 2564 Publications

Post-translational modificationi

The intrachain disulfide-bonds prevent N-glycosylation at some sites.
N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

MaxQBiP78380.
PaxDbiP78380.
PRIDEiP78380.

Miscellaneous databases

PMAP-CutDBP78380.

Expressioni

Tissue specificityi

Expressed at high level in endothelial cells and vascular-rich organs such as placenta, lung, liver and brain, aortic intima, bone marrow, spinal cord and substantia nigra. Also expressed at the surface of dendritic cells. Widely expressed at intermediate and low level.3 Publications

Inductioni

By inflammatory cytokines such as TNF, IFNG/IFN-gamma, IL6/interleukin-6 and by pathological conditions such as hyperlipidemia, hypertension and diabetes mellitus. Up-regulated in atherosclerotic lesions, by oxLDL, reactive oxygen species and fluid shear stress, suggesting that it may participate in amplification of oxLDL-induced vascular dysfunction.2 Publications

Gene expression databases

ArrayExpressiP78380.
BgeeiP78380.
CleanExiHS_OLR1.
GenevestigatoriP78380.

Organism-specific databases

HPAiHPA050798.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. May form a hexamer composed of 3 homodimers. Interacts with HSP70.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCT4P509913EBI-7151999,EBI-356876
TCP1P179875EBI-7151999,EBI-356553

Protein-protein interaction databases

BioGridi111021. 2 interactions.
DIPiDIP-42040N.
IntActiP78380. 8 interactions.
MINTiMINT-1343572.
STRINGi9606.ENSP00000309124.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi148 – 1514
Beta strandi154 – 1585
Helixi165 – 17410
Helixi185 – 19511
Beta strandi202 – 2109
Beta strandi225 – 2273
Beta strandi230 – 2334
Beta strandi242 – 2476
Beta strandi250 – 2556
Beta strandi260 – 2678

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YPOX-ray3.00A/B/C/D/E/F/G/H142-272[»]
1YPQX-ray1.40A/B136-270[»]
1YPUX-ray2.05A/B136-270[»]
1YXJX-ray1.78A/B143-271[»]
1YXKX-ray2.40A/B136-270[»]
3VLGX-ray2.30A133-273[»]
ProteinModelPortaliP78380.
SMRiP78380. Positions 112-270.

Miscellaneous databases

EvolutionaryTraceiP78380.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini151 – 265115C-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 15093Neck
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili64 – 12360 Reviewed prediction
Add
BLAST

Domaini

The cytoplasmic region is required for subcellular sorting on the cell surface.2 Publications
The C-type lectin domain mediates the recognition and binding of oxLDL.2 Publications

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG242244.
HOGENOMiHOG000069959.
HOVERGENiHBG056863.
InParanoidiP78380.
KOiK08763.
OMAiSICQKKA.
OrthoDBiEOG747PJT.
PhylomeDBiP78380.
TreeFamiTF336674.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[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: P78380-1) [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

MTFDDLKIQT VKDQPDEKSN GKKAKGLQFL YSPWWCLAAA TLGVLCLGLV    50
VTIMVLGMQL SQVSDLLTQE QANLTHQKKK LEGQISARQQ AEEASQESEN 100
ELKEMIETLA RKLNEKSKEQ MELHHQNLNL QETLKRVANC SAPCPQDWIW 150
HGENCYLFSS GSFNWEKSQE KCLSLDAKLL KINSTADLDF IQQAISYSSF 200
PFWMGLSRRN PSYPWLWEDG SPLMPHLFRV RGAVSQTYPS GTCAYIQRGA 250
VYAENCILAA FSICQKKANL RAQ 273
Length:273
Mass (Da):30,959
Last modified:May 1, 1997 - v1
Checksum:i852DE6595DC3D361
GO
Isoform 2 (identifier: P78380-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     142-273: APCPQDWIWH...CQKKANLRAQ → GLHPASNFLF...GRFSFDAPLI

Note: No experimental confirmation available.

Show »
Length:181
Mass (Da):20,227
Checksum:iD9DFBBBEB1948099
GO
Isoform 3 (identifier: P78380-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     189-273: DFIQQAISYS...CQKKANLRAQ → I

Note: No experimental confirmation available.

Show »
Length:189
Mass (Da):21,425
Checksum:iCA0E07E9A69E204F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671K → N Common polymorphism; myocardial infarction susceptibility. 2 Publications
Corresponds to variant rs11053646 [ dbSNP | Ensembl ].
VAR_023200

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei142 – 273132APCPQ…NLRAQ → GLHPASNFLFQFSILDGAVS EEPQLPMALGGRFSFDAPLI in isoform 2.
VSP_042555Add
BLAST
Alternative sequencei189 – 27385DFIQQ…NLRAQ → I in isoform 3.
VSP_045277Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB010710 mRNA. Translation: BAA24580.1.
AF035776 mRNA. Translation: AAC82329.1.
AF079167
, AF079166, AF079164, AF079165 Genomic DNA. Translation: AAC97927.1.
AB102861 mRNA. Translation: BAC81565.1.
AJ131757 Genomic DNA. Translation: CAB38175.1.
BX344276 mRNA. No translation available.
AK292124 mRNA. Translation: BAF84813.1.
AK295409 mRNA. Translation: BAG58360.1.
DQ314885 Genomic DNA. Translation: ABC40744.1.
AC024224 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96157.1.
CH471094 Genomic DNA. Translation: EAW96158.1.
BC022295 mRNA. Translation: AAH22295.1.
CCDSiCCDS53745.1. [P78380-2]
CCDS53746.1. [P78380-3]
CCDS8618.1. [P78380-1]
RefSeqiNP_001166103.1. NM_001172632.1. [P78380-2]
NP_001166104.1. NM_001172633.1. [P78380-3]
NP_002534.1. NM_002543.3. [P78380-1]
UniGeneiHs.412484.

Genome annotation databases

EnsembliENST00000309539; ENSP00000309124; ENSG00000173391. [P78380-1]
ENST00000432556; ENSP00000405116; ENSG00000173391. [P78380-2]
ENST00000545927; ENSP00000439251; ENSG00000173391. [P78380-3]
GeneIDi4973.
KEGGihsa:4973.
UCSCiuc001qxo.1. human. [P78380-1]
uc010sha.1. human. [P78380-2]
uc021qvb.1. human.

Polymorphism databases

DMDMi73621335.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Oxidized LDL receptor

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB010710 mRNA. Translation: BAA24580.1 .
AF035776 mRNA. Translation: AAC82329.1 .
AF079167
, AF079166 , AF079164 , AF079165 Genomic DNA. Translation: AAC97927.1 .
AB102861 mRNA. Translation: BAC81565.1 .
AJ131757 Genomic DNA. Translation: CAB38175.1 .
BX344276 mRNA. No translation available.
AK292124 mRNA. Translation: BAF84813.1 .
AK295409 mRNA. Translation: BAG58360.1 .
DQ314885 Genomic DNA. Translation: ABC40744.1 .
AC024224 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96157.1 .
CH471094 Genomic DNA. Translation: EAW96158.1 .
BC022295 mRNA. Translation: AAH22295.1 .
CCDSi CCDS53745.1. [P78380-2 ]
CCDS53746.1. [P78380-3 ]
CCDS8618.1. [P78380-1 ]
RefSeqi NP_001166103.1. NM_001172632.1. [P78380-2 ]
NP_001166104.1. NM_001172633.1. [P78380-3 ]
NP_002534.1. NM_002543.3. [P78380-1 ]
UniGenei Hs.412484.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YPO X-ray 3.00 A/B/C/D/E/F/G/H 142-272 [» ]
1YPQ X-ray 1.40 A/B 136-270 [» ]
1YPU X-ray 2.05 A/B 136-270 [» ]
1YXJ X-ray 1.78 A/B 143-271 [» ]
1YXK X-ray 2.40 A/B 136-270 [» ]
3VLG X-ray 2.30 A 133-273 [» ]
ProteinModelPortali P78380.
SMRi P78380. Positions 112-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111021. 2 interactions.
DIPi DIP-42040N.
IntActi P78380. 8 interactions.
MINTi MINT-1343572.
STRINGi 9606.ENSP00000309124.

Polymorphism databases

DMDMi 73621335.

Proteomic databases

MaxQBi P78380.
PaxDbi P78380.
PRIDEi P78380.

Protocols and materials databases

DNASUi 4973.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309539 ; ENSP00000309124 ; ENSG00000173391 . [P78380-1 ]
ENST00000432556 ; ENSP00000405116 ; ENSG00000173391 . [P78380-2 ]
ENST00000545927 ; ENSP00000439251 ; ENSG00000173391 . [P78380-3 ]
GeneIDi 4973.
KEGGi hsa:4973.
UCSCi uc001qxo.1. human. [P78380-1 ]
uc010sha.1. human. [P78380-2 ]
uc021qvb.1. human.

Organism-specific databases

CTDi 4973.
GeneCardsi GC12M010310.
HGNCi HGNC:8133. OLR1.
HPAi HPA050798.
MIMi 602601. gene+phenotype.
neXtProti NX_P78380.
PharmGKBi PA31920.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG242244.
HOGENOMi HOG000069959.
HOVERGENi HBG056863.
InParanoidi P78380.
KOi K08763.
OMAi SICQKKA.
OrthoDBi EOG747PJT.
PhylomeDBi P78380.
TreeFami TF336674.

Enzyme and pathway databases

Reactomei REACT_12051. Cell surface interactions at the vascular wall.

Miscellaneous databases

EvolutionaryTracei P78380.
GeneWikii OLR1.
GenomeRNAii 4973.
NextBioi 19142.
PMAP-CutDB P78380.
PROi P78380.
SOURCEi Search...

Gene expression databases

ArrayExpressi P78380.
Bgeei P78380.
CleanExi HS_OLR1.
Genevestigatori P78380.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view ]
Pfami PF00059. Lectin_C. 1 hit.
[Graphical view ]
SMARTi SM00034. CLECT. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
PROSITEi PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Lung.
  2. "Assignment of the human oxidized low-density lipoprotein receptor gene (OLR1) to chromosome 12p13.1-->p12.3, and identification of a polymorphic CA-repeat marker in the OLR1 gene."
    Li X., Bouzyk M.M., Wang X.
    Cytogenet. Cell Genet. 82:34-36(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Characterization of residues and sequences of the carbohydrate recognition domain required for cell surface localization and ligand binding of human lectin-like oxidized LDL receptor."
    Shi X., Niimi S., Ohtani T., Machida S.
    J. Cell Sci. 114:1273-1282(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAIN, DISULFIDE BONDS, GLYCOSYLATION, MUTAGENESIS OF CYS-144; CYS-155; CYS-172; ASN-183; 209-ARG-ASN-210; HIS-226; ARG-229; ARG-231; 235-SER-GLN-236; SER-240; CYS-243; CYS-256; CYS-264 AND 267-LYS--GLN-273.
  4. "The human gene encoding the lectin-type oxidized LDL receptor (OLR1) is a novel member of the natural killer gene complex with a unique expression profile."
    Yamanaka S., Zhang X.-Y., Miura K., Kim S., Iwao H.
    Genomics 54:191-199(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN MYOCARDIAL INFARCTION, VARIANT ASN-167.
  6. Millar D.S.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Placenta.
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ASN-167.
    Tissue: Corpus callosum and Synovial cell.
  9. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  10. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  13. "Lectin-like oxidized LDL receptor-1 (LOX-1) supports adhesion of mononuclear leukocytes and a monocyte-like cell line THP-1 cells under static and flow conditions."
    Hayashida K., Kume N., Minami M., Kita T.
    FEBS Lett. 511:133-138(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: FUNCTION, TISSUE SPECIFICITY.
  15. "Investigation of oxidized LDL-receptor 1 (OLR1) as the candidate gene for Alzheimer's disease on chromosome 12."
    Luedecking-Zimmer E., DeKosky S.T., Chen Q., Barmada M.M., Kamboh M.I.
    Hum. Genet. 111:443-451(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ALZHEIMER DISEASE.
  16. "Oxidized LDL through LOX-1 modulates LDL-receptor expression in human coronary artery endothelial cells."
    Hu B., Li D., Sawamura T., Mehta J.L.
    Biochem. Biophys. Res. Commun. 307:1008-1012(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  17. "Genetic variation in lectin-like oxidized low-density lipoprotein receptor 1 (LOX1) gene and the risk of coronary artery disease."
    Chen Q., Reis S.E., Kammerer C., Craig W.Y., LaPierre S.E., Zimmer E.L., McNamara D.M., Pauly D.F., Sharaf B., Holubkov R., Bairey Merz C.N., Sopko G., Bontempo F., Kamboh M.I.
    Circulation 107:3146-3151(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MYOCARDIAL INFARCTION.
  18. Cited for: INVOLVEMENT IN ALZHEIMER DISEASE.
  19. "Human lectin-like oxidized low-density lipoprotein receptor-1 functions as a dimer in living cells."
    Xie Q., Matsunaga S., Niimi S., Ogawa S., Tokuyasu K., Sakakibara Y., Machida S.
    DNA Cell Biol. 23:111-117(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, INTERCHAIN DISULFIDE BOND, MUTAGENESIS OF CYS-140.
  20. "No association between a previously reported OLR1 3' UTR polymorphism and Alzheimer's disease in a large family sample."
    Bertram L., Parkinson M., Mullin K., Menon R., Blacker D., Tanzi R.E.
    J. Med. Genet. 41:286-288(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF INVOLVEMENT IN ALZHEIMER DISEASE.
  21. "No association between polymorphisms in the lectin-like oxidised low density lipoprotein receptor (ORL1) gene on chromosome 12 and Alzheimer's disease in a UK cohort."
    Pritchard A., St Clair D., Lemmon H., Mann D.M.A., Lendon C.
    Neurosci. Lett. 366:126-129(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF INVOLVEMENT IN ALZHEIMER DISEASE.
  22. "In vivo and in vitro studies support that a new splicing isoform of OLR1 gene is protective against acute myocardial infarction."
    Mango R., Biocca S., del Vecchio F., Clementi F., Sangiuolo F., Amati F., Filareto A., Grelli S., Spitalieri P., Filesi I., Favalli C., Lauro R., Mehta J.L., Romeo F., Novelli G.
    Circ. Res. 97:152-158(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MYOCARDIAL INFARCTION.
  23. "Polymorphisms in the oxidized low-density lipoprotein receptor-1 gene and risk of Alzheimer's disease."
    D'Introno A., Solfrizzi V., Colacicco A.M., Capurso C., Torres F., Capurso S.A., Capurso A., Panza F.
    J. Gerontol. 60:280-284(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ALZHEIMER DISEASE.
  24. "Essential role of cytoplasmic sequences for cell-surface sorting of the lectin-like oxidized LDL receptor-1 (LOX-1)."
    Chen M., Sawamura T.
    J. Mol. Cell. Cardiol. 39:553-561(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF 22-LYS--LYS-25 AND GLU-70.
  25. "Site-specific N-glycosylation identification of recombinant human lectin-like oxidized low density lipoprotein receptor-1 (LOX-1)."
    Qian Y., Zhang X., Zhou L., Yun X., Xie J., Xu J., Ruan Y., Ren S.
    Glycoconj. J. 29:399-409(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-139.
  26. "Lectin-like oxidized LDL receptor-1 is palmitoylated and internalizes ligands via caveolae/raft-dependent endocytosis."
    Kumano-Kuramochi M., Xie Q., Kajiwara S., Komba S., Minowa T., Machida S.
    Biochem. Biophys. Res. Commun. 434:594-599(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-36 AND CYS-46, SUBCELLULAR LOCATION.
  27. "The 1.4 angstrom crystal structure of the human oxidized low density lipoprotein receptor lox-1."
    Park H., Adsit F.G., Boyington J.C.
    J. Biol. Chem. 280:13593-13599(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 136-270, SUBUNIT, DISULFIDE BONDS.
  28. "Crystal structure of human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to oxLDL."
    Ohki I., Ishigaki T., Oyama T., Matsunaga S., Xie Q., Ohnishi-Kameyama M., Murata T., Tsuchiya D., Machida S., Morikawa K., Tate S.
    Structure 13:905-917(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 143-271, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF TRP-150; ARG-208; ARG-209; HIS-226; ARG-229; ARG-231 AND ARG-248.

Entry informationi

Entry nameiOLR1_HUMAN
AccessioniPrimary (citable) accession number: P78380
Secondary accession number(s): A8K7V9
, B4DI48, G3V1I4, Q2PP00, Q7Z484
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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