P78380 (OLR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Oxidized low-density lipoprotein receptor 1, soluble form

Gene names

Name:	OLR1
Synonyms:	CLEC8A, LOX1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	273 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.25 Ref.26
Subcellular location	Cell membrane; Single-pass type II membrane protein. Secreted. Note: A secreted form also exists. Ref.24
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
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 process	Cell adhesion Immunity Inflammatory response
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Signal-anchor Transmembrane Transmembrane helix
Ligand	Lectin
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood circulation Traceable author statement Ref.1. Source: ProtInc blood coagulation Traceable author statement. Source: Reactome cell death Inferred from electronic annotation. Source: Compara inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW leukocyte cell-cell adhesion Inferred from electronic annotation. Source: Compara leukocyte migration Traceable author statement. Source: Reactome lipoprotein metabolic process Inferred from electronic annotation. Source: Compara proteolysis Traceable author statement Ref.1. Source: ProtInc response to hydrogen peroxide Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro low-density lipoprotein receptor activity Inferred from electronic annotation. Source: Compara
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 273

273

Oxidized low-density lipoprotein receptor 1

PRO_0000017443

Chain

? – 273

Oxidized low-density lipoprotein receptor 1, soluble form

PRO_0000017444

Regions

Topological domain

1 – 36

36

Cytoplasmic Potential

Transmembrane

37 – 57

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

58 – 273

216

Extracellular Potential

Domain

151 – 265

115

C-type lectin

Region

58 – 150

93

Neck

Coiled coil

64 – 123

60

Potential

Sites

Site

183

1

Not glycosylated Probable

Amino acid modifications

Glycosylation

73

1

N-linked (GlcNAc...) Potential

Glycosylation

139

1

N-linked (GlcNAc...) Potential

Disulfide bond

140

Interchain Ref.3 Ref.19 Ref.25 Ref.26

Disulfide bond

144 ↔ 155

Ref.3 Ref.19 Ref.25 Ref.26

Disulfide bond

172 ↔ 264

Ref.3 Ref.19 Ref.25 Ref.26

Disulfide bond

243 ↔ 256

Ref.3 Ref.19 Ref.25 Ref.26

Natural variations

Alternative sequence

142 – 273

132

APCPQ…NLRAQ → GLHPASNFLFQFSILDGAVS EEPQLPMALGGRFSFDAPLI in isoform 2.

VSP_042555

Alternative sequence

189 – 273

85

DFIQQ…NLRAQ → I in isoform 3.

VSP_045277

Natural variant

167

1

K → N Common polymorphism; myocardial infarction susceptibility. Ref.5 Ref.8
Corresponds to variant rs11053646 [ dbSNP | Ensembl ].

VAR_023200

Experimental info

Mutagenesis

22 – 25

4

KKAK → EEAE: Impairs sorting into the cell surface but retains ability to bind oxLDL. Abolishes sorting into the cell surface; when associated with K-69. Ref.24

Mutagenesis

70

1

E → K: Abolishes sorting into the cell surface; when associated with 22-E--E-25. Ref.24

Mutagenesis

140

1

C → S: Abolishes homodimerization. Ref.19

Mutagenesis

144

1

C → S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-155; S-172; S-243; S-256 and S-264. Ref.3

Mutagenesis

150

1

W → A: Abolishes binding to acetylated LDL (AcLDL), probably due to inappropriate homodimerization. Ref.26

Mutagenesis

155

1

C → S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-172; S-243; S-256 and S-264. Ref.3

Mutagenesis

172

1

C → S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-243; S-256 and S-264. Ref.3

Mutagenesis

183

1

N → Q: Does not affect glycosylation state. Ref.3

Mutagenesis

193

1

Q → L: Impairs binding to acetylated LDL (AcLDL); when associated with 198-AA-199.

Mutagenesis

198 – 199

2

SS → AA: Impairs binding to acetylated LDL (AcLDL); when associated with L-193.

Mutagenesis

208

1

R → N: Does not affect subcellular location but displays a strongly reduced affinity for acetylated LDL (AcLDL). Ref.26

Mutagenesis

209 – 210

2

RN → LL: Abolishes binding to acetylated LDL (AcLDL). Ref.26

Mutagenesis

209

1

R → N: Does not affect binding to acetylated LDL (AcLDL). Ref.26

Mutagenesis

226

1

H → A: No effect. Ref.3 Ref.26

Mutagenesis

226

1

H → Q: Abolishes binding to acetylated LDL (AcLDL); when associated with N-229 and N-231. Ref.3 Ref.26

Mutagenesis

229

1

R → N: Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL). Abolishes binding to acetylated LDL (AcLDL); when associated with Q-226 and N-231. Ref.3 Ref.26

Mutagenesis

231

1

R → N: Abolishes binding to acetylated LDL (AcLDL). Abolishes binding to AcLDL; when associated with Q-226 and N-229. Ref.3 Ref.26

Mutagenesis

235 – 236

2

SQ → AL: Impairs binding to acetylated LDL (AcLDL); when associated with A-240.

Mutagenesis

240

1

S → A: Impairs binding to acetylated LDL (AcLDL); when associated with 235-AL-236. Ref.3

Mutagenesis

243

1

C → S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-256 and S-264. Ref.3

Mutagenesis

248

1

R → N: Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL). Ref.26

Mutagenesis

256

1

C → S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-243 and S-264. Ref.3

Mutagenesis

264

1

C → S: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-243 and S-256. Ref.3

Mutagenesis

267 – 273

7

Missing: Impairs protein folding and transport. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

273

Helix Strand Turn

Details...

Beta strand

148 – 151

4

Beta strand

154 – 158

5

Helix

165 – 174

10

Helix

185 – 195

11

Beta strand

202 – 210

9

Beta strand

225 – 227

3

Beta strand

230 – 233

4

Beta strand

242 – 247

6

Beta strand

250 – 255

6

Beta strand

260 – 267

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 852DE6595DC3D361	FASTA	273	30,959
	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
	Isoform 2 [UniParc]. Checksum: D9DFBBBEB1948099	FASTA	181	20,227
	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 SGLHPASNFL FQFSILDGAV SEEPQLPMAL GGRFSFDAPL I
	Isoform 3 [UniParc]. Checksum: CA0E07E9A69E204F	FASTA	189	21,425
	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 KINSTADLI

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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]	"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.
[26]	"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

Functional Glycomics Gateway - Glycan Binding

Oxidized LDL receptor

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00001759.
IPI00910415.

RefSeq

NP_001166103.1. NM_001172632.1.
NP_001166104.1. NM_001172633.1.
NP_002534.1. NM_002543.3.

UniGene

Hs.412484.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P78380.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42040N.

MINT

MINT-1343572.

STRING

9606.ENSP00000309124.

Polymorphism databases

DMDM

73621335.

Proteomic databases

PaxDb

P78380.

PRIDE

P78380.

Protocols and materials databases

DNASU

4973.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309539; ENSP00000309124; ENSG00000173391.
ENST00000432556; ENSP00000405116; ENSG00000173391.
ENST00000545927; ENSP00000439251; ENSG00000173391.

GeneID

4973.

KEGG

hsa:4973.

UCSC

uc001qxo.1. human.

Organism-specific databases

CTD

4973.

GeneCards

GC12M010310.

HGNC

HGNC:8133. OLR1.

HPA

HPA050798.

MIM

602601. gene+phenotype.

neXtProt

NX_P78380.

PharmGKB

PA31920.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG242244.

HOGENOM

HOG000069959.

HOVERGEN

HBG056863.

InParanoid

P78380.

KO

K08763.

OMA

SICQKKA.

OrthoDB

EOG4V9TRM.

PhylomeDB

P78380.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P78380.

Bgee

P78380.

CleanEx

HS_OLR1.

Genevestigator

P78380.

GermOnline

ENSG00000173391. Homo sapiens.

Family and domain databases

Gene3D

3.10.100.10. 1 hit.

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]

Pfam

PF00059. Lectin_C. 1 hit.
[Graphical view]

SMART

SM00034. CLECT. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS00615. C_TYPE_LECTIN_1. False negative.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P78380.

GenomeRNAi

4973.

NextBio

19142.

PMAP-CutDB

P78380.

SOURCE

Search...

Entry information

Entry name

OLR1_HUMAN

Accession

Primary (citable) accession number: P78380
Secondary accession number(s): A8K7V9 , B4DI48, G3V1I4, Q2PP00, Q7Z484

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.