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P78380

- OLR1_HUMAN

UniProt

P78380 - OLR1_HUMAN

Protein

Oxidized low-density lipoprotein receptor 1

Gene

OLR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    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 glycosylatedCurated

    GO - Molecular functioni

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

    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

    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.

    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

    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.
    OLR1 may be involved in Alzheimer disease (AD). Involvement in AD is however unclear: according to some authors (PubMed:12354387, PubMed:12810610 and PubMed:15976314), variations in OLR1 modify the risk of AD, while according to other (PubMed:15000751 and PubMed:15060104) they do not.3 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.
    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.

    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 1PRO_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...)Sequence Analysis
    Glycosylationi139 – 1391N-linked (GlcNAc...) (complex)2 Publications
    Disulfide bondi140 – 140Interchain
    Disulfide bondi144 ↔ 155
    Disulfide bondi172 ↔ 264
    Disulfide bondi243 ↔ 256

    Post-translational modificationi

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

    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 HSP70.3 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

    1
    273
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP78380.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3636CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini58 – 273216ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei37 – 5721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini151 – 265115C-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili64 – 12360Sequence AnalysisAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 C-type lectin domain.PROSITE-ProRule annotation

    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. 1 PublicationVSP_042555Add
    BLAST
    Alternative sequencei189 – 27385DFIQQ…NLRAQ → I in isoform 3. 1 PublicationVSP_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

    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: October 1, 2014
    This is version 138 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