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Oxidized low-density lipoprotein receptor 1 (Ox-LDL receptor 1) (C-type lectin domain family 8 member A) (Lectin-like oxidized LDL receptor 1) (LOX-1) (Lectin-like oxLDL receptor 1) (hLOX-1) (Lectin-type oxidized LDL receptor 1) [Cleaved into: Oxidized low-density lipoprotein receptor 1, soluble form]

 OLR1_HUMAN              Reviewed;         273 AA.
P78380; A8K7V9; B4DI48; G3V1I4; Q2PP00; Q7Z484;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
27-SEP-2017, entry version 167.
RecName: Full=Oxidized low-density lipoprotein receptor 1;
Short=Ox-LDL receptor 1;
AltName: Full=C-type lectin domain family 8 member A;
AltName: Full=Lectin-like oxidized LDL receptor 1;
Short=LOX-1;
Short=Lectin-like oxLDL receptor 1;
Short=hLOX-1;
AltName: Full=Lectin-type oxidized LDL receptor 1;
Contains:
RecName: Full=Oxidized low-density lipoprotein receptor 1, soluble form;
Name=OLR1; Synonyms=CLEC8A, LOX1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Lung;
PubMed=9052782; DOI=10.1038/386073a0;
Sawamura T., Kume N., Aoyama T., Moriwaki H., Hoshikawa H., Aiba Y.,
Tanaka T., Miwa S., Katsura Y., Kita T., Masaki T.;
"An endothelial receptor for oxidized low-density lipoprotein.";
Nature 386:73-77(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9763655;
Li X., Bouzyk M.M., Wang X.;
"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.";
Cytogenet. Cell Genet. 82:34-36(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAIN, DISULFIDE BONDS,
GLYCOSYLATION, AND 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.
PubMed=11256994;
Shi X., Niimi S., Ohtani T., Machida S.;
"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.";
J. Cell Sci. 114:1273-1282(2001).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
PubMed=9828121; DOI=10.1006/geno.1998.5561;
Yamanaka S., Zhang X.-Y., Miura K., Kim S., Iwao H.;
"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.";
Genomics 54:191-199(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN MYOCARDIAL
INFARCTION, AND VARIANT ASN-167.
PubMed=12646194; DOI=10.1016/S0006-291X(03)00326-7;
Tatsuguchi M., Furutani M., Hinagata J., Tanaka T., Furutani Y.,
Imamura S., Kawana M., Masaki T., Kasanuki H., Sawamura T.,
Matsuoka R.;
"Oxidized LDL receptor gene (OLR1) is associated with the risk of
myocardial infarction.";
Biochem. Biophys. Res. Commun. 303:247-250(2003).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Millar D.S.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Placenta;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ASN-167.
TISSUE=Corpus callosum, and Synovial cell;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
FUNCTION.
PubMed=11821063; DOI=10.1016/S0014-5793(01)03297-5;
Hayashida K., Kume N., Minami M., Kita T.;
"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.";
FEBS Lett. 511:133-138(2002).
[14]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12354387; DOI=10.1016/S1074-7613(02)00388-6;
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.;
"Involvement of LOX-1 in dendritic cell-mediated antigen cross-
presentation.";
Immunity 17:353-362(2002).
[15]
INVOLVEMENT IN ALZHEIMER DISEASE.
PubMed=12384789; DOI=10.1007/s00439-002-0802-7;
Luedecking-Zimmer E., DeKosky S.T., Chen Q., Barmada M.M.,
Kamboh M.I.;
"Investigation of oxidized LDL-receptor 1 (OLR1) as the candidate gene
for Alzheimer's disease on chromosome 12.";
Hum. Genet. 111:443-451(2002).
[16]
INDUCTION.
PubMed=12878212; DOI=10.1016/S0006-291X(03)01295-6;
Hu B., Li D., Sawamura T., Mehta J.L.;
"Oxidized LDL through LOX-1 modulates LDL-receptor expression in human
coronary artery endothelial cells.";
Biochem. Biophys. Res. Commun. 307:1008-1012(2003).
[17]
INVOLVEMENT IN MYOCARDIAL INFARCTION.
PubMed=12810610; DOI=10.1161/01.CIR.0000074207.85796.36;
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.;
"Genetic variation in lectin-like oxidized low-density lipoprotein
receptor 1 (LOX1) gene and the risk of coronary artery disease.";
Circulation 107:3146-3151(2003).
[18]
INVOLVEMENT IN ALZHEIMER DISEASE.
PubMed=12807963; DOI=10.1136/jmg.40.6.424;
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.;
"Association of 3'-UTR polymorphisms of the oxidised LDL receptor 1
(OLR1) gene with Alzheimer's disease.";
J. Med. Genet. 40:424-430(2003).
[19]
HOMODIMERIZATION, INTERCHAIN DISULFIDE BOND, AND MUTAGENESIS OF
CYS-140.
PubMed=15000751; DOI=10.1089/104454904322759920;
Xie Q., Matsunaga S., Niimi S., Ogawa S., Tokuyasu K., Sakakibara Y.,
Machida S.;
"Human lectin-like oxidized low-density lipoprotein receptor-1
functions as a dimer in living cells.";
DNA Cell Biol. 23:111-117(2004).
[20]
LACK OF INVOLVEMENT IN ALZHEIMER DISEASE.
PubMed=15060104; DOI=10.1136/jmg.2003.016980;
Bertram L., Parkinson M., Mullin K., Menon R., Blacker D., Tanzi R.E.;
"No association between a previously reported OLR1 3' UTR polymorphism
and Alzheimer's disease in a large family sample.";
J. Med. Genet. 41:286-288(2004).
[21]
LACK OF INVOLVEMENT IN ALZHEIMER DISEASE.
PubMed=15276231; DOI=10.1016/j.neulet.2004.05.023;
Pritchard A., St Clair D., Lemmon H., Mann D.M.A., Lendon C.;
"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.";
Neurosci. Lett. 366:126-129(2004).
[22]
INVOLVEMENT IN MYOCARDIAL INFARCTION.
PubMed=15976314; DOI=10.1161/01.RES.0000174563.62625.8e;
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.;
"In vivo and in vitro studies support that a new splicing isoform of
OLR1 gene is protective against acute myocardial infarction.";
Circ. Res. 97:152-158(2005).
[23]
INVOLVEMENT IN ALZHEIMER DISEASE.
PubMed=15860461; DOI=10.1093/gerona/60.3.280;
D'Introno A., Solfrizzi V., Colacicco A.M., Capurso C., Torres F.,
Capurso S.A., Capurso A., Panza F.;
"Polymorphisms in the oxidized low-density lipoprotein receptor-1 gene
and risk of Alzheimer's disease.";
J. Gerontol. 60:280-284(2005).
[24]
DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 22-LYS--LYS-25 AND
GLU-70.
PubMed=15935375; DOI=10.1016/j.yjmcc.2005.05.001;
Chen M., Sawamura T.;
"Essential role of cytoplasmic sequences for cell-surface sorting of
the lectin-like oxidized LDL receptor-1 (LOX-1).";
J. Mol. Cell. Cardiol. 39:553-561(2005).
[25]
GLYCOSYLATION AT ASN-139.
PubMed=22688517; DOI=10.1007/s10719-012-9408-z;
Qian Y., Zhang X., Zhou L., Yun X., Xie J., Xu J., Ruan Y., Ren S.;
"Site-specific N-glycosylation identification of recombinant human
lectin-like oxidized low density lipoprotein receptor-1 (LOX-1).";
Glycoconj. J. 29:399-409(2012).
[26]
PALMITOYLATION AT CYS-36 AND CYS-46, AND SUBCELLULAR LOCATION.
PubMed=23583401; DOI=10.1016/j.bbrc.2013.03.120;
Kumano-Kuramochi M., Xie Q., Kajiwara S., Komba S., Minowa T.,
Machida S.;
"Lectin-like oxidized LDL receptor-1 is palmitoylated and internalizes
ligands via caveolae/raft-dependent endocytosis.";
Biochem. Biophys. Res. Commun. 434:594-599(2013).
[27]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 136-270, SUBUNIT, AND
DISULFIDE BONDS.
PubMed=15695803; DOI=10.1074/jbc.M500768200;
Park H., Adsit F.G., Boyington J.C.;
"The 1.4 angstrom crystal structure of the human oxidized low density
lipoprotein receptor lox-1.";
J. Biol. Chem. 280:13593-13599(2005).
[28]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 143-271, SUBUNIT, DISULFIDE
BONDS, AND MUTAGENESIS OF TRP-150; ARG-208; ARG-209; HIS-226; ARG-229;
ARG-231 AND ARG-248.
PubMed=15939022; DOI=10.1016/j.str.2005.03.016;
Ohki I., Ishigaki T., Oyama T., Matsunaga S., Xie Q.,
Ohnishi-Kameyama M., Murata T., Tsuchiya D., Machida S., Morikawa K.,
Tate S.;
"Crystal structure of human lectin-like, oxidized low-density
lipoprotein receptor 1 ligand binding domain and its ligand
recognition mode to oxLDL.";
Structure 13:905-917(2005).
-!- 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. {ECO:0000269|PubMed:11821063,
ECO:0000269|PubMed:12354387, ECO:0000269|PubMed:9052782}.
-!- SUBUNIT: Homodimer; disulfide-linked. May form a hexamer composed
of 3 homodimers. Interacts with HSP70.
{ECO:0000269|PubMed:11256994, ECO:0000269|PubMed:15695803,
ECO:0000269|PubMed:15939022}.
-!- INTERACTION:
P50991:CCT4; NbExp=3; IntAct=EBI-7151999, EBI-356876;
P17987:TCP1; NbExp=5; IntAct=EBI-7151999, EBI-356553;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P78380-1; Sequence=Displayed;
Name=2;
IsoId=P78380-2; Sequence=VSP_042555;
Note=No experimental confirmation available.;
Name=3;
IsoId=P78380-3; Sequence=VSP_045277;
Note=No experimental confirmation available.;
-!- 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. {ECO:0000269|PubMed:12354387,
ECO:0000269|PubMed:9052782, ECO:0000269|PubMed:9828121}.
-!- 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.
{ECO:0000269|PubMed:12878212, ECO:0000269|PubMed:9828121}.
-!- DOMAIN: The cytoplasmic region is required for subcellular sorting
on the cell surface.
-!- DOMAIN: The C-type lectin domain mediates the recognition and
binding of oxLDL.
-!- PTM: The intrachain disulfide-bonds prevent N-glycosylation at
some sites.
-!- PTM: N-glycosylated.
-!- DISEASE: Note=Independent association genetic studies have
implicated OLR1 gene variants in myocardial infarction
susceptibility.
-!- DISEASE: Note=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.
{ECO:0000269|PubMed:12384789, ECO:0000269|PubMed:12807963,
ECO:0000269|PubMed:15860461}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Oxidized LDL receptor;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_249";
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EMBL; AB010710; BAA24580.1; -; mRNA.
EMBL; AF035776; AAC82329.1; -; mRNA.
EMBL; AF079167; AAC97927.1; -; Genomic_DNA.
EMBL; AF079166; AAC97927.1; JOINED; Genomic_DNA.
EMBL; AF079164; AAC97927.1; JOINED; Genomic_DNA.
EMBL; AF079165; AAC97927.1; JOINED; Genomic_DNA.
EMBL; AB102861; BAC81565.1; -; mRNA.
EMBL; AJ131757; CAB38175.1; -; Genomic_DNA.
EMBL; BX344276; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK292124; BAF84813.1; -; mRNA.
EMBL; AK295409; BAG58360.1; -; mRNA.
EMBL; DQ314885; ABC40744.1; -; Genomic_DNA.
EMBL; AC024224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471094; EAW96157.1; -; Genomic_DNA.
EMBL; CH471094; EAW96158.1; -; Genomic_DNA.
EMBL; BC022295; AAH22295.1; -; mRNA.
CCDS; CCDS53745.1; -. [P78380-2]
CCDS; CCDS53746.1; -. [P78380-3]
CCDS; CCDS8618.1; -. [P78380-1]
RefSeq; NP_001166103.1; NM_001172632.1. [P78380-2]
RefSeq; NP_001166104.1; NM_001172633.1. [P78380-3]
RefSeq; NP_002534.1; NM_002543.3. [P78380-1]
UniGene; Hs.412484; -.
PDB; 1YPO; X-ray; 3.00 A; A/B/C/D/E/F/G/H=142-272.
PDB; 1YPQ; X-ray; 1.40 A; A/B=136-270.
PDB; 1YPU; X-ray; 2.05 A; A/B=136-270.
PDB; 1YXJ; X-ray; 1.78 A; A/B=143-271.
PDB; 1YXK; X-ray; 2.40 A; A/B=136-270.
PDB; 3VLG; X-ray; 2.30 A; A=133-273.
PDBsum; 1YPO; -.
PDBsum; 1YPQ; -.
PDBsum; 1YPU; -.
PDBsum; 1YXJ; -.
PDBsum; 1YXK; -.
PDBsum; 3VLG; -.
ProteinModelPortal; P78380; -.
SMR; P78380; -.
BioGrid; 111021; 3.
DIP; DIP-42040N; -.
IntAct; P78380; 9.
MINT; MINT-1343572; -.
STRING; 9606.ENSP00000309124; -.
ChEMBL; CHEMBL3421522; -.
iPTMnet; P78380; -.
PhosphoSitePlus; P78380; -.
SwissPalm; P78380; -.
BioMuta; OLR1; -.
DMDM; 73621335; -.
MaxQB; P78380; -.
PaxDb; P78380; -.
PeptideAtlas; P78380; -.
PRIDE; P78380; -.
DNASU; 4973; -.
Ensembl; ENST00000309539; ENSP00000309124; ENSG00000173391. [P78380-1]
Ensembl; ENST00000432556; ENSP00000405116; ENSG00000173391. [P78380-2]
Ensembl; ENST00000545927; ENSP00000439251; ENSG00000173391. [P78380-3]
GeneID; 4973; -.
KEGG; hsa:4973; -.
UCSC; uc001qxo.2; human. [P78380-1]
CTD; 4973; -.
DisGeNET; 4973; -.
EuPathDB; HostDB:ENSG00000173391.8; -.
GeneCards; OLR1; -.
HGNC; HGNC:8133; OLR1.
HPA; HPA050798; -.
MalaCards; OLR1; -.
MIM; 602601; gene+phenotype.
neXtProt; NX_P78380; -.
OpenTargets; ENSG00000173391; -.
PharmGKB; PA31920; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00700000104266; -.
HOGENOM; HOG000220927; -.
HOVERGEN; HBG056863; -.
InParanoid; P78380; -.
KO; K08763; -.
OMA; PSGTCAY; -.
OrthoDB; EOG091G0MM1; -.
PhylomeDB; P78380; -.
TreeFam; TF336674; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; OLR1; human.
EvolutionaryTrace; P78380; -.
GeneWiki; OLR1; -.
GenomeRNAi; 4973; -.
PMAP-CutDB; P78380; -.
PRO; PR:P78380; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000173391; -.
CleanEx; HS_OLR1; -.
ExpressionAtlas; P78380; baseline and differential.
Genevisible; P78380; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0005041; F:low-density lipoprotein receptor activity; IEA:Ensembl.
GO; GO:0008015; P:blood circulation; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
CDD; cd03593; CLECT_NK_receptors_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR013600; Ly49_N.
InterPro; IPR033992; NKR-like_CTLD.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF08391; Ly49; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Coiled coil; Complete proteome; Disulfide bond; Glycoprotein;
Immunity; Inflammatory response; Lectin; Lipoprotein; Membrane;
Palmitate; Polymorphism; Receptor; Reference proteome; Secreted;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 273 Oxidized low-density lipoprotein receptor
1.
/FTId=PRO_0000017443.
CHAIN ? 273 Oxidized low-density lipoprotein receptor
1, soluble form.
/FTId=PRO_0000017444.
TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.
TRANSMEM 37 57 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 58 273 Extracellular. {ECO:0000255}.
DOMAIN 151 265 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
REGION 58 150 Neck.
COILED 64 123 {ECO:0000255}.
SITE 183 183 Not glycosylated. {ECO:0000305}.
LIPID 36 36 S-palmitoyl cysteine.
{ECO:0000269|PubMed:23583401}.
LIPID 46 46 S-palmitoyl cysteine.
{ECO:0000269|PubMed:23583401}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 139 139 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:22688517}.
DISULFID 140 140 Interchain.
DISULFID 144 155
DISULFID 172 264
DISULFID 243 256
VAR_SEQ 142 273 APCPQDWIWHGENCYLFSSGSFNWEKSQEKCLSLDAKLLKI
NSTADLDFIQQAISYSSFPFWMGLSRRNPSYPWLWEDGSPL
MPHLFRVRGAVSQTYPSGTCAYIQRGAVYAENCILAAFSIC
QKKANLRAQ -> GLHPASNFLFQFSILDGAVSEEPQLPMA
LGGRFSFDAPLI (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042555.
VAR_SEQ 189 273 DFIQQAISYSSFPFWMGLSRRNPSYPWLWEDGSPLMPHLFR
VRGAVSQTYPSGTCAYIQRGAVYAENCILAAFSICQKKANL
RAQ -> I (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_045277.
VARIANT 167 167 K -> N (common polymorphism; myocardial
infarction susceptibility;
dbSNP:rs11053646).
{ECO:0000269|PubMed:12646194,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_023200.
MUTAGEN 22 25 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.
{ECO:0000269|PubMed:15935375}.
MUTAGEN 70 70 E->K: Abolishes sorting into the cell
surface; when associated with 22-E--E-25.
{ECO:0000269|PubMed:15935375}.
MUTAGEN 140 140 C->S: Abolishes homodimerization.
{ECO:0000269|PubMed:15000751}.
MUTAGEN 144 144 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.
{ECO:0000269|PubMed:11256994}.
MUTAGEN 150 150 W->A: Abolishes binding to acetylated LDL
(AcLDL), probably due to inappropriate
homodimerization.
{ECO:0000269|PubMed:15939022}.
MUTAGEN 155 155 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.
{ECO:0000269|PubMed:11256994}.
MUTAGEN 172 172 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.
{ECO:0000269|PubMed:11256994}.
MUTAGEN 183 183 N->Q: Does not affect glycosylation
state. {ECO:0000269|PubMed:11256994}.
MUTAGEN 193 193 Q->L: Impairs binding to acetylated LDL
(AcLDL); when associated with 198-AA-199.
MUTAGEN 198 199 SS->AA: Impairs binding to acetylated LDL
(AcLDL); when associated with L-193.
MUTAGEN 208 208 R->N: Does not affect subcellular
location but displays a strongly reduced
affinity for acetylated LDL (AcLDL).
{ECO:0000269|PubMed:15939022}.
MUTAGEN 209 210 RN->LL: Abolishes binding to acetylated
LDL (AcLDL).
{ECO:0000269|PubMed:11256994}.
MUTAGEN 209 209 R->N: Does not affect binding to
acetylated LDL (AcLDL).
{ECO:0000269|PubMed:15939022}.
MUTAGEN 226 226 H->A: No effect.
{ECO:0000269|PubMed:11256994,
ECO:0000269|PubMed:15939022}.
MUTAGEN 226 226 H->Q: Abolishes binding to acetylated LDL
(AcLDL); when associated with N-229 and
N-231. {ECO:0000269|PubMed:11256994,
ECO:0000269|PubMed:15939022}.
MUTAGEN 229 229 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.
{ECO:0000269|PubMed:11256994,
ECO:0000269|PubMed:15939022}.
MUTAGEN 231 231 R->N: Abolishes binding to acetylated LDL
(AcLDL). Abolishes binding to AcLDL; when
associated with Q-226 and N-229.
{ECO:0000269|PubMed:11256994,
ECO:0000269|PubMed:15939022}.
MUTAGEN 235 236 SQ->AL: Impairs binding to acetylated LDL
(AcLDL); when associated with A-240.
{ECO:0000269|PubMed:11256994}.
MUTAGEN 240 240 S->A: Impairs binding to acetylated LDL
(AcLDL); when associated with 235-AL-236.
{ECO:0000269|PubMed:11256994}.
MUTAGEN 243 243 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.
{ECO:0000269|PubMed:11256994}.
MUTAGEN 248 248 R->N: Does not affect subcellular
location but displays a reduced affinity
for acetylated LDL (AcLDL).
{ECO:0000269|PubMed:15939022}.
MUTAGEN 256 256 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.
{ECO:0000269|PubMed:11256994}.
MUTAGEN 264 264 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.
{ECO:0000269|PubMed:11256994}.
MUTAGEN 267 273 Missing: Impairs protein folding and
transport. {ECO:0000269|PubMed:11256994}.
STRAND 148 151 {ECO:0000244|PDB:1YPQ}.
STRAND 154 158 {ECO:0000244|PDB:1YPQ}.
HELIX 165 174 {ECO:0000244|PDB:1YPQ}.
HELIX 185 195 {ECO:0000244|PDB:1YPQ}.
STRAND 202 210 {ECO:0000244|PDB:1YPQ}.
STRAND 225 227 {ECO:0000244|PDB:1YPO}.
STRAND 230 233 {ECO:0000244|PDB:1YPQ}.
STRAND 242 247 {ECO:0000244|PDB:1YPQ}.
STRAND 250 255 {ECO:0000244|PDB:1YPQ}.
STRAND 260 267 {ECO:0000244|PDB:1YPQ}.
SEQUENCE 273 AA; 30959 MW; 852DE6595DC3D361 CRC64;
MTFDDLKIQT VKDQPDEKSN GKKAKGLQFL YSPWWCLAAA TLGVLCLGLV VTIMVLGMQL
SQVSDLLTQE QANLTHQKKK LEGQISARQQ AEEASQESEN ELKEMIETLA RKLNEKSKEQ
MELHHQNLNL QETLKRVANC SAPCPQDWIW HGENCYLFSS GSFNWEKSQE KCLSLDAKLL
KINSTADLDF IQQAISYSSF PFWMGLSRRN PSYPWLWEDG SPLMPHLFRV RGAVSQTYPS
GTCAYIQRGA VYAENCILAA FSICQKKANL RAQ


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