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P78380 (OLR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:OLR1
Synonyms:CLEC8A, LOX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria. Ref.1 Ref.13 Ref.14

Subunit structure

Homodimer; disulfide-linked. May form a hexamer composed of 3 homodimers. Interacts with HSP70. Ref.3 Ref.19 Ref.27 Ref.28

Subcellular location

Cell membrane; Lipid-anchor. Cell membrane; Single-pass type II membrane protein. Membrane raft. Secreted. Note: A secreted form also exists. Localization to membrane rafts requires palmitoylation. Ref.24 Ref.26

Tissue specificity

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. Ref.1 Ref.4 Ref.14

Induction

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. Ref.4 Ref.16

Domain

The cytoplasmic region is required for subcellular sorting on the cell surface. Ref.3 Ref.24

The C-type lectin domain mediates the recognition and binding of oxLDL. Ref.3 Ref.24

Post-translational modification

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

N-glycosylated. Ref.3 Ref.25

Involvement in disease

Independent association genetic studies have implicated OLR1 gene variants in myocardial infarction susceptibility. Ref.15 Ref.18 Ref.20 Ref.21 Ref.23

OLR1 may be involved in Alzheimer disease (AD). Involvement in AD is however unclear: according to some authors (Ref.14, Ref.17 and Ref.22), variations in OLR1 modify the risk of AD, while according to other (Ref.19 and Ref.20) they do not. Ref.15 Ref.18 Ref.20 Ref.21 Ref.23

Sequence similarities

Contains 1 C-type lectin domain.

Ontologies

Keywords
   Biological processCell adhesion
Immunity
Inflammatory response
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Signal-anchor
Transmembrane
Transmembrane helix
   LigandLectin
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood circulation

Traceable author statement Ref.1. Source: ProtInc

blood coagulation

Traceable author statement. Source: Reactome

cell death

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

leukocyte cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Traceable author statement. Source: Reactome

lipoprotein metabolic process

Inferred from electronic annotation. Source: Ensembl

proteolysis

Traceable author statement Ref.1. Source: ProtInc

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

membrane

Traceable author statement Ref.1. Source: ProtInc

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

low-density lipoprotein receptor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78380-1)

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.
Isoform 2 (identifier: P78380-2)

The sequence of this isoform differs from the canonical sequence as follows:
     142-273: APCPQDWIWH...CQKKANLRAQ → GLHPASNFLF...GRFSFDAPLI
Note: No experimental confirmation available.
Isoform 3 (identifier: P78380-3)

The sequence of this isoform differs from the canonical sequence as follows:
     189-273: DFIQQAISYS...CQKKANLRAQ → I
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 273273Oxidized low-density lipoprotein receptor 1
PRO_0000017443
Chain? – 273Oxidized low-density lipoprotein receptor 1, soluble formPRO_0000017444

Regions

Topological domain1 – 3636Cytoplasmic Potential
Transmembrane37 – 5721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain58 – 273216Extracellular Potential
Domain151 – 265115C-type lectin
Region58 – 15093Neck
Coiled coil64 – 12360 Potential

Sites

Site1831Not glycosylated Probable

Amino acid modifications

Lipidation361S-palmitoyl cysteine Ref.26
Lipidation461S-palmitoyl cysteine Ref.26
Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation1391N-linked (GlcNAc...) (complex) Ref.25
Disulfide bond140Interchain Ref.3 Ref.19 Ref.27 Ref.28
Disulfide bond144 ↔ 155 Ref.3 Ref.19 Ref.27 Ref.28
Disulfide bond172 ↔ 264 Ref.3 Ref.19 Ref.27 Ref.28
Disulfide bond243 ↔ 256 Ref.3 Ref.19 Ref.27 Ref.28

Natural variations

Alternative sequence142 – 273132APCPQ…NLRAQ → GLHPASNFLFQFSILDGAVS EEPQLPMALGGRFSFDAPLI in isoform 2.
VSP_042555
Alternative sequence189 – 27385DFIQQ…NLRAQ → I in isoform 3.
VSP_045277
Natural variant1671K → N Common polymorphism; myocardial infarction susceptibility. Ref.5 Ref.8
Corresponds to variant rs11053646 [ dbSNP | Ensembl ].
VAR_023200

Experimental info

Mutagenesis22 – 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. Ref.24
Mutagenesis701E → K: Abolishes sorting into the cell surface; when associated with 22-E--E-25. Ref.24
Mutagenesis1401C → S: Abolishes homodimerization. Ref.19
Mutagenesis1441C → 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. Ref.3
Mutagenesis1501W → A: Abolishes binding to acetylated LDL (AcLDL), probably due to inappropriate homodimerization. Ref.28
Mutagenesis1551C → 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. Ref.3
Mutagenesis1721C → 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. Ref.3
Mutagenesis1831N → Q: Does not affect glycosylation state. Ref.3
Mutagenesis1931Q → L: Impairs binding to acetylated LDL (AcLDL); when associated with 198-AA-199.
Mutagenesis198 – 1992SS → AA: Impairs binding to acetylated LDL (AcLDL); when associated with L-193.
Mutagenesis2081R → N: Does not affect subcellular location but displays a strongly reduced affinity for acetylated LDL (AcLDL). Ref.28
Mutagenesis209 – 2102RN → LL: Abolishes binding to acetylated LDL (AcLDL). Ref.28
Mutagenesis2091R → N: Does not affect binding to acetylated LDL (AcLDL). Ref.28
Mutagenesis2261H → A: No effect. Ref.3 Ref.28
Mutagenesis2261H → Q: Abolishes binding to acetylated LDL (AcLDL); when associated with N-229 and N-231. Ref.3 Ref.28
Mutagenesis2291R → 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. Ref.3 Ref.28
Mutagenesis2311R → N: Abolishes binding to acetylated LDL (AcLDL). Abolishes binding to AcLDL; when associated with Q-226 and N-229. Ref.3 Ref.28
Mutagenesis235 – 2362SQ → AL: Impairs binding to acetylated LDL (AcLDL); when associated with A-240.
Mutagenesis2401S → A: Impairs binding to acetylated LDL (AcLDL); when associated with 235-AL-236. Ref.3
Mutagenesis2431C → 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. Ref.3
Mutagenesis2481R → N: Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL). Ref.28
Mutagenesis2561C → 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. Ref.3
Mutagenesis2641C → 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. Ref.3
Mutagenesis267 – 2737Missing: Impairs protein folding and transport. Ref.3

Secondary structure

..................... 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 852DE6595DC3D361

FASTA27330,959
        10         20         30         40         50         60 
MTFDDLKIQT VKDQPDEKSN GKKAKGLQFL YSPWWCLAAA TLGVLCLGLV VTIMVLGMQL 

        70         80         90        100        110        120 
SQVSDLLTQE QANLTHQKKK LEGQISARQQ AEEASQESEN ELKEMIETLA RKLNEKSKEQ 

       130        140        150        160        170        180 
MELHHQNLNL QETLKRVANC SAPCPQDWIW HGENCYLFSS GSFNWEKSQE KCLSLDAKLL 

       190        200        210        220        230        240 
KINSTADLDF IQQAISYSSF PFWMGLSRRN PSYPWLWEDG SPLMPHLFRV RGAVSQTYPS 

       250        260        270 
GTCAYIQRGA VYAENCILAA FSICQKKANL RAQ 

« Hide

Isoform 2 [UniParc].

Checksum: D9DFBBBEB1948099
Show »

FASTA18120,227
Isoform 3 [UniParc].

Checksum: CA0E07E9A69E204F
Show »

FASTA18921,425

References

« Hide 'large scale' references
[1]"An endothelial receptor for oxidized low-density lipoprotein."
Sawamura T., Kume N., Aoyama T., Moriwaki H., Hoshikawa H., Aiba Y., Tanaka T., Miwa S., Katsura Y., Kita T., Masaki T.
Nature 386:73-77(1997) [PubMed] [Europe PMC] [Abstract]
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]"Oxidized LDL receptor gene (OLR1) is associated with the risk of myocardial infarction."
Tatsuguchi M., Furutani M., Hinagata J., Tanaka T., Furutani Y., Imamura S., Kawana M., Masaki T., Kasanuki H., Sawamura T., Matsuoka R.
Biochem. Biophys. Res. Commun. 303:247-250(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation."
Delneste Y., Magistrelli G., Gauchat J.-F., Haeuw J.-P., Aubry J.-F., Nakamura K., Kawakami-Honda N., Goetsch L., Sawamura T., Bonnefoy J.-Y., Jeannin P.
Immunity 17:353-362(2002) [PubMed] [Europe PMC] [Abstract]
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]"Association of 3'-UTR polymorphisms of the oxidised LDL receptor 1 (OLR1) gene with Alzheimer's disease."
Lambert J.-C., Luedecking-Zimmer E., Merrot S., Hayes A., Thaker U., Desai P., Houzet A., Hermant X., Cottel D., Pritchard A., Iwatsubo T., Pasquier F., Frigard B., Conneally P.M., Chartier-Harlin M.-C., DeKosky S.T., Lendon C., Mann D., Kamboh M.I., Amouyel P.
J. Med. Genet. 40:424-430(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB010710 mRNA. Translation: BAA24580.1.
AF035776 mRNA. Translation: AAC82329.1.
AF079167 expand/collapse EMBL AC list , 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.
CCDSCCDS53745.1. [P78380-2]
CCDS53746.1. [P78380-3]
CCDS8618.1. [P78380-1]
RefSeqNP_001166103.1. NM_001172632.1. [P78380-2]
NP_001166104.1. NM_001172633.1. [P78380-3]
NP_002534.1. NM_002543.3. [P78380-1]
UniGeneHs.412484.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP78380.
SMRP78380. Positions 112-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111021. 2 interactions.
DIPDIP-42040N.
MINTMINT-1343572.
STRING9606.ENSP00000309124.

Polymorphism databases

DMDM73621335.

Proteomic databases

MaxQBP78380.
PaxDbP78380.
PRIDEP78380.

Protocols and materials databases

DNASU4973.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309539; ENSP00000309124; ENSG00000173391. [P78380-1]
ENST00000432556; ENSP00000405116; ENSG00000173391. [P78380-2]
ENST00000545927; ENSP00000439251; ENSG00000173391. [P78380-3]
GeneID4973.
KEGGhsa:4973.
UCSCuc001qxo.1. human. [P78380-1]
uc010sha.1. human. [P78380-2]
uc021qvb.1. human.

Organism-specific databases

CTD4973.
GeneCardsGC12M010310.
HGNCHGNC:8133. OLR1.
HPAHPA050798.
MIM602601. gene+phenotype.
neXtProtNX_P78380.
PharmGKBPA31920.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242244.
HOGENOMHOG000069959.
HOVERGENHBG056863.
InParanoidP78380.
KOK08763.
OMASICQKKA.
OrthoDBEOG747PJT.
PhylomeDBP78380.
TreeFamTF336674.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP78380.
BgeeP78380.
CleanExHS_OLR1.
GenevestigatorP78380.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP78380.
GeneWikiOLR1.
GenomeRNAi4973.
NextBio19142.
PMAP-CutDBP78380.
PROP78380.
SOURCESearch...

Entry information

Entry nameOLR1_HUMAN
AccessionPrimary (citable) accession number: P78380
Secondary accession number(s): A8K7V9 expand/collapse secondary AC list , B4DI48, G3V1I4, Q2PP00, Q7Z484
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM