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Entry version 184 (16 Oct 2019)
Sequence version 1 (01 May 1997)
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Protein

Oxidized low-density lipoprotein receptor 1

Gene

OLR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionReceptor
Biological processCell adhesion, Immunity, Inflammatory response
LigandLectin

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-6798695 Neutrophil degranulation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:OLR1
Synonyms:CLEC8A, LOX1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:8133 OLR1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
602601 gene+phenotype

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P78380

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 36CytoplasmicSequence analysisAdd BLAST36
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei37 – 57Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini58 – 273ExtracellularSequence analysisAdd BLAST216

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi22 – 25KKAK → 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 Publication4
Mutagenesisi70E → K: Abolishes sorting into the cell surface; when associated with 22-E--E-25. 1 Publication1
Mutagenesisi140C → S: Abolishes homodimerization. 1 Publication1
Mutagenesisi144C → 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 Publication1
Mutagenesisi150W → A: Abolishes binding to acetylated LDL (AcLDL), probably due to inappropriate homodimerization. 1 Publication1
Mutagenesisi155C → 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 Publication1
Mutagenesisi172C → 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 Publication1
Mutagenesisi183N → Q: Does not affect glycosylation state. 1 Publication1
Mutagenesisi193Q → L: Impairs binding to acetylated LDL (AcLDL); when associated with 198-AA-199. 1
Mutagenesisi198 – 199SS → AA: Impairs binding to acetylated LDL (AcLDL); when associated with L-193. 2
Mutagenesisi208R → N: Does not affect subcellular location but displays a strongly reduced affinity for acetylated LDL (AcLDL). 1 Publication1
Mutagenesisi209 – 210RN → LL: Abolishes binding to acetylated LDL (AcLDL). 1 Publication2
Mutagenesisi209R → N: Does not affect binding to acetylated LDL (AcLDL). 1 Publication1
Mutagenesisi226H → A: No effect. 2 Publications1
Mutagenesisi226H → Q: Abolishes binding to acetylated LDL (AcLDL); when associated with N-229 and N-231. 2 Publications1
Mutagenesisi229R → 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 Publications1
Mutagenesisi231R → N: Abolishes binding to acetylated LDL (AcLDL). Abolishes binding to AcLDL; when associated with Q-226 and N-229. 2 Publications1
Mutagenesisi235 – 236SQ → AL: Impairs binding to acetylated LDL (AcLDL); when associated with A-240. 1 Publication2
Mutagenesisi240S → A: Impairs binding to acetylated LDL (AcLDL); when associated with 235-AL-236. 1 Publication1
Mutagenesisi243C → 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 Publication1
Mutagenesisi248R → N: Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL). 1 Publication1
Mutagenesisi256C → 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 Publication1
Mutagenesisi264C → 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 Publication1
Mutagenesisi267 – 273Missing : Impairs protein folding and transport. 1 Publication7

Organism-specific databases

DisGeNET

More...
DisGeNETi
4973

MalaCards human disease database

More...
MalaCardsi
OLR1
MIMi602601 gene+phenotype

NIAGADS Genomics Database

More...
NIAGADSi
ENSG00000173391

Open Targets

More...
OpenTargetsi
ENSG00000173391

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA31920

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P78380

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3421522

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
OLR1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
73621335

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000174431 – 273Oxidized low-density lipoprotein receptor 1Add BLAST273
ChainiPRO_0000017444? – 273Oxidized low-density lipoprotein receptor 1, soluble form

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi36S-palmitoyl cysteine1 Publication1
Lipidationi46S-palmitoyl cysteine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi73N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi139N-linked (GlcNAc...) (complex) asparagine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi140Interchain
Disulfide bondi144 ↔ 155
Disulfide bondi172 ↔ 264
Disulfide bondi243 ↔ 256

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei183Not glycosylatedCurated1

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P78380

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P78380

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P78380

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P78380

PeptideAtlas

More...
PeptideAtlasi
P78380

PRoteomics IDEntifications database

More...
PRIDEi
P78380

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
32344
57601 [P78380-1]
57602 [P78380-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P78380

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P78380

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P78380

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P78380

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000173391 Expressed in 130 organ(s), highest expression level in substantia nigra

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P78380 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P78380 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA050798

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; disulfide-linked. May form a hexamer composed of 3 homodimers.

Interacts with HSP70.

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111021, 5 interactors

Database of interacting proteins

More...
DIPi
DIP-42040N

Protein interaction database and analysis system

More...
IntActi
P78380, 9 interactors

Molecular INTeraction database

More...
MINTi
P78380

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000309124

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P78380

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P78380

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini151 – 265C-type lectinPROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni58 – 150NeckAdd BLAST93

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili64 – 123Sequence analysisAdd BLAST60

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4297 Eukaryota
ENOG410XPJ1 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000161941

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000220927

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P78380

KEGG Orthology (KO)

More...
KOi
K08763

Identification of Orthologs from Complete Genome Data

More...
OMAi
HSSFPFW

Database of Orthologous Groups

More...
OrthoDBi
1201127at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P78380

TreeFam database of animal gene trees

More...
TreeFami
TF336674

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03593 CLECT_NK_receptors_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.100.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR016187 CTDL_fold
IPR013600 Ly49_N
IPR033992 NKR-like_CTLD

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00059 Lectin_C, 1 hit
PF08391 Ly49, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00034 CLECT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56436 SSF56436, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50041 C_TYPE_LECTIN_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P78380-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MTFDDLKIQT VKDQPDEKSN GKKAKGLQFL YSPWWCLAAA TLGVLCLGLV
60 70 80 90 100
VTIMVLGMQL SQVSDLLTQE QANLTHQKKK LEGQISARQQ AEEASQESEN
110 120 130 140 150
ELKEMIETLA RKLNEKSKEQ MELHHQNLNL QETLKRVANC SAPCPQDWIW
160 170 180 190 200
HGENCYLFSS GSFNWEKSQE KCLSLDAKLL KINSTADLDF IQQAISYSSF
210 220 230 240 250
PFWMGLSRRN PSYPWLWEDG SPLMPHLFRV RGAVSQTYPS GTCAYIQRGA
260 270
VYAENCILAA FSICQKKANL RAQ
Length:273
Mass (Da):30,959
Last modified:May 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5GZH1F5GZH1_HUMAN
Oxidized low-density lipoprotein re...
OLR1
165Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F5H7N8F5H7N8_HUMAN
Oxidized low-density lipoprotein re...
OLR1
214Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F5H001F5H001_HUMAN
Oxidized low-density lipoprotein re...
OLR1
104Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F5H3G7F5H3G7_HUMAN
Oxidized low-density lipoprotein re...
OLR1
122Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QTI8J3QTI8_HUMAN
Oxidized low-density lipoprotein re...
OLR1
104Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F5H0N6F5H0N6_HUMAN
Oxidized low-density lipoprotein re...
OLR1
57Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B7ZAN8B7ZAN8_HUMAN
Oxidized low-density lipoprotein re...
OLR1
77Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_023200167K → N Common polymorphism; myocardial infarction susceptibility. 2 PublicationsCorresponds to variant dbSNP:rs11053646EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_042555142 – 273APCPQ…NLRAQ → GLHPASNFLFQFSILDGAVS EEPQLPMALGGRFSFDAPLI in isoform 2. 1 PublicationAdd BLAST132
Alternative sequenceiVSP_045277189 – 273DFIQQ…NLRAQ → I in isoform 3. 1 PublicationAdd BLAST85

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS53745.1 [P78380-2]
CCDS53746.1 [P78380-3]
CCDS8618.1 [P78380-1]

NCBI Reference Sequences

More...
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]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000309539; ENSP00000309124; ENSG00000173391 [P78380-1]
ENST00000432556; ENSP00000405116; ENSG00000173391 [P78380-2]
ENST00000545927; ENSP00000439251; ENSG00000173391 [P78380-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4973

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4973

UCSC genome browser

More...
UCSCi
uc001qxo.2 human [P78380-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Oxidized LDL receptor

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
SMRiP78380
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi111021, 5 interactors
DIPiDIP-42040N
IntActiP78380, 9 interactors
MINTiP78380
STRINGi9606.ENSP00000309124

Chemistry databases

ChEMBLiCHEMBL3421522

PTM databases

iPTMnetiP78380
PhosphoSitePlusiP78380
SwissPalmiP78380

Polymorphism and mutation databases

BioMutaiOLR1
DMDMi73621335

Proteomic databases

jPOSTiP78380
MassIVEiP78380
MaxQBiP78380
PaxDbiP78380
PeptideAtlasiP78380
PRIDEiP78380
ProteomicsDBi32344
57601 [P78380-1]
57602 [P78380-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4973

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4973
DisGeNETi4973

GeneCards: human genes, protein and diseases

More...
GeneCardsi
OLR1
HGNCiHGNC:8133 OLR1
HPAiHPA050798
MalaCardsiOLR1
MIMi602601 gene+phenotype
neXtProtiNX_P78380
NIAGADSiENSG00000173391
OpenTargetsiENSG00000173391
PharmGKBiPA31920

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4297 Eukaryota
ENOG410XPJ1 LUCA
GeneTreeiENSGT00940000161941
HOGENOMiHOG000220927
InParanoidiP78380
KOiK08763
OMAiHSSFPFW
OrthoDBi1201127at2759
PhylomeDBiP78380
TreeFamiTF336674

Enzyme and pathway databases

ReactomeiR-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
OLR1 human
EvolutionaryTraceiP78380

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
OLR1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
4973
PharosiP78380
PMAP-CutDBiP78380

Protein Ontology

More...
PROi
PR:P78380

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000173391 Expressed in 130 organ(s), highest expression level in substantia nigra
ExpressionAtlasiP78380 baseline and differential
GenevisibleiP78380 HS

Family and domain databases

CDDicd03593 CLECT_NK_receptors_like, 1 hit
Gene3Di3.10.100.10, 1 hit
InterProiView protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR016187 CTDL_fold
IPR013600 Ly49_N
IPR033992 NKR-like_CTLD
PfamiView protein in Pfam
PF00059 Lectin_C, 1 hit
PF08391 Ly49, 1 hit
SMARTiView protein in SMART
SM00034 CLECT, 1 hit
SUPFAMiSSF56436 SSF56436, 1 hit
PROSITEiView protein in PROSITE
PS50041 C_TYPE_LECTIN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOLR1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P78380
Secondary accession number(s): A8K7V9
, B4DI48, G3V1I4, Q2PP00, Q7Z484
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 1, 1997
Last modified: October 16, 2019
This is version 184 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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