OLR1_HUMAN
ID OLR1_HUMAN Reviewed; 273 AA.
AC P78380; A8K7V9; B4DI48; G3V1I4; Q2PP00; Q7Z484;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Oxidized low-density lipoprotein receptor 1;
DE Short=Ox-LDL receptor 1;
DE AltName: Full=C-type lectin domain family 8 member A;
DE AltName: Full=Lectin-like oxidized LDL receptor 1;
DE Short=LOX-1;
DE Short=Lectin-like oxLDL receptor 1;
DE Short=hLOX-1;
DE AltName: Full=Lectin-type oxidized LDL receptor 1;
DE Contains:
DE RecName: Full=Oxidized low-density lipoprotein receptor 1, soluble form;
GN Name=OLR1; Synonyms=CLEC8A, LOX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=9052782; DOI=10.1038/386073a0;
RA Sawamura T., Kume N., Aoyama T., Moriwaki H., Hoshikawa H., Aiba Y.,
RA Tanaka T., Miwa S., Katsura Y., Kita T., Masaki T.;
RT "An endothelial receptor for oxidized low-density lipoprotein.";
RL Nature 386:73-77(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9763655; DOI=10.1159/000015059;
RA Li X., Bouzyk M.M., Wang X.;
RT "Assignment of the human oxidized low-density lipoprotein receptor gene
RT (OLR1) to chromosome 12p13.1-->p12.3, and identification of a polymorphic
RT CA-repeat marker in the OLR1 gene.";
RL Cytogenet. Cell Genet. 82:34-36(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAIN, DISULFIDE BONDS,
RP GLYCOSYLATION, AND MUTAGENESIS OF CYS-144; CYS-155; CYS-172; ASN-183;
RP 209-ARG-ASN-210; HIS-226; ARG-229; ARG-231; 235-SER-GLN-236; SER-240;
RP CYS-243; CYS-256; CYS-264 AND 267-LYS--GLN-273.
RX PubMed=11256994; DOI=10.1242/jcs.114.7.1273;
RA Shi X., Niimi S., Ohtani T., Machida S.;
RT "Characterization of residues and sequences of the carbohydrate recognition
RT domain required for cell surface localization and ligand binding of human
RT lectin-like oxidized LDL receptor.";
RL J. Cell Sci. 114:1273-1282(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9828121; DOI=10.1006/geno.1998.5561;
RA Yamanaka S., Zhang X.-Y., Miura K., Kim S., Iwao H.;
RT "The human gene encoding the lectin-type oxidized LDL receptor (OLR1) is a
RT novel member of the natural killer gene complex with a unique expression
RT profile.";
RL Genomics 54:191-199(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN MYOCARDIAL
RP INFARCTION, AND VARIANT ASN-167.
RX PubMed=12646194; DOI=10.1016/s0006-291x(03)00326-7;
RA Tatsuguchi M., Furutani M., Hinagata J., Tanaka T., Furutani Y.,
RA Imamura S., Kawana M., Masaki T., Kasanuki H., Sawamura T., Matsuoka R.;
RT "Oxidized LDL receptor gene (OLR1) is associated with the risk of
RT myocardial infarction.";
RL Biochem. Biophys. Res. Commun. 303:247-250(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Millar D.S.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ASN-167.
RC TISSUE=Corpus callosum, and Synovial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP FUNCTION.
RX PubMed=11821063; DOI=10.1016/s0014-5793(01)03297-5;
RA Hayashida K., Kume N., Minami M., Kita T.;
RT "Lectin-like oxidized LDL receptor-1 (LOX-1) supports adhesion of
RT mononuclear leukocytes and a monocyte-like cell line THP-1 cells under
RT static and flow conditions.";
RL FEBS Lett. 511:133-138(2002).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12354387; DOI=10.1016/s1074-7613(02)00388-6;
RA Delneste Y., Magistrelli G., Gauchat J.-F., Haeuw J.-P., Aubry J.-F.,
RA Nakamura K., Kawakami-Honda N., Goetsch L., Sawamura T., Bonnefoy J.-Y.,
RA Jeannin P.;
RT "Involvement of LOX-1 in dendritic cell-mediated antigen cross-
RT presentation.";
RL Immunity 17:353-362(2002).
RN [15]
RP INVOLVEMENT IN ALZHEIMER DISEASE.
RX PubMed=12384789; DOI=10.1007/s00439-002-0802-7;
RA Luedecking-Zimmer E., DeKosky S.T., Chen Q., Barmada M.M., Kamboh M.I.;
RT "Investigation of oxidized LDL-receptor 1 (OLR1) as the candidate gene for
RT Alzheimer's disease on chromosome 12.";
RL Hum. Genet. 111:443-451(2002).
RN [16]
RP INDUCTION.
RX PubMed=12878212; DOI=10.1016/s0006-291x(03)01295-6;
RA Hu B., Li D., Sawamura T., Mehta J.L.;
RT "Oxidized LDL through LOX-1 modulates LDL-receptor expression in human
RT coronary artery endothelial cells.";
RL Biochem. Biophys. Res. Commun. 307:1008-1012(2003).
RN [17]
RP INVOLVEMENT IN MYOCARDIAL INFARCTION.
RX PubMed=12810610; DOI=10.1161/01.cir.0000074207.85796.36;
RA Chen Q., Reis S.E., Kammerer C., Craig W.Y., LaPierre S.E., Zimmer E.L.,
RA McNamara D.M., Pauly D.F., Sharaf B., Holubkov R., Bairey Merz C.N.,
RA Sopko G., Bontempo F., Kamboh M.I.;
RT "Genetic variation in lectin-like oxidized low-density lipoprotein receptor
RT 1 (LOX1) gene and the risk of coronary artery disease.";
RL Circulation 107:3146-3151(2003).
RN [18]
RP INVOLVEMENT IN ALZHEIMER DISEASE.
RX PubMed=12807963; DOI=10.1136/jmg.40.6.424;
RA Lambert J.-C., Luedecking-Zimmer E., Merrot S., Hayes A., Thaker U.,
RA Desai P., Houzet A., Hermant X., Cottel D., Pritchard A., Iwatsubo T.,
RA Pasquier F., Frigard B., Conneally P.M., Chartier-Harlin M.-C.,
RA DeKosky S.T., Lendon C., Mann D., Kamboh M.I., Amouyel P.;
RT "Association of 3'-UTR polymorphisms of the oxidised LDL receptor 1 (OLR1)
RT gene with Alzheimer's disease.";
RL J. Med. Genet. 40:424-430(2003).
RN [19]
RP HOMODIMERIZATION, INTERCHAIN DISULFIDE BOND, AND MUTAGENESIS OF CYS-140.
RX PubMed=15000751; DOI=10.1089/104454904322759920;
RA Xie Q., Matsunaga S., Niimi S., Ogawa S., Tokuyasu K., Sakakibara Y.,
RA Machida S.;
RT "Human lectin-like oxidized low-density lipoprotein receptor-1 functions as
RT a dimer in living cells.";
RL DNA Cell Biol. 23:111-117(2004).
RN [20]
RP LACK OF INVOLVEMENT IN ALZHEIMER DISEASE.
RX PubMed=15060104; DOI=10.1136/jmg.2003.016980;
RA Bertram L., Parkinson M., Mullin K., Menon R., Blacker D., Tanzi R.E.;
RT "No association between a previously reported OLR1 3' UTR polymorphism and
RT Alzheimer's disease in a large family sample.";
RL J. Med. Genet. 41:286-288(2004).
RN [21]
RP LACK OF INVOLVEMENT IN ALZHEIMER DISEASE.
RX PubMed=15276231; DOI=10.1016/j.neulet.2004.05.023;
RA Pritchard A., St Clair D., Lemmon H., Mann D.M.A., Lendon C.;
RT "No association between polymorphisms in the lectin-like oxidised low
RT density lipoprotein receptor (ORL1) gene on chromosome 12 and Alzheimer's
RT disease in a UK cohort.";
RL Neurosci. Lett. 366:126-129(2004).
RN [22]
RP INVOLVEMENT IN MYOCARDIAL INFARCTION.
RX PubMed=15976314; DOI=10.1161/01.res.0000174563.62625.8e;
RA Mango R., Biocca S., del Vecchio F., Clementi F., Sangiuolo F., Amati F.,
RA Filareto A., Grelli S., Spitalieri P., Filesi I., Favalli C., Lauro R.,
RA Mehta J.L., Romeo F., Novelli G.;
RT "In vivo and in vitro studies support that a new splicing isoform of OLR1
RT gene is protective against acute myocardial infarction.";
RL Circ. Res. 97:152-158(2005).
RN [23]
RP INVOLVEMENT IN ALZHEIMER DISEASE.
RX PubMed=15860461; DOI=10.1093/gerona/60.3.280;
RA D'Introno A., Solfrizzi V., Colacicco A.M., Capurso C., Torres F.,
RA Capurso S.A., Capurso A., Panza F.;
RT "Polymorphisms in the oxidized low-density lipoprotein receptor-1 gene and
RT risk of Alzheimer's disease.";
RL J. Gerontol. 60:280-284(2005).
RN [24]
RP DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 22-LYS--LYS-25 AND GLU-70.
RX PubMed=15935375; DOI=10.1016/j.yjmcc.2005.05.001;
RA Chen M., Sawamura T.;
RT "Essential role of cytoplasmic sequences for cell-surface sorting of the
RT lectin-like oxidized LDL receptor-1 (LOX-1).";
RL J. Mol. Cell. Cardiol. 39:553-561(2005).
RN [25]
RP GLYCOSYLATION AT ASN-139.
RX PubMed=22688517; DOI=10.1007/s10719-012-9408-z;
RA Qian Y., Zhang X., Zhou L., Yun X., Xie J., Xu J., Ruan Y., Ren S.;
RT "Site-specific N-glycosylation identification of recombinant human lectin-
RT like oxidized low density lipoprotein receptor-1 (LOX-1).";
RL Glycoconj. J. 29:399-409(2012).
RN [26]
RP PALMITOYLATION AT CYS-36 AND CYS-46, AND SUBCELLULAR LOCATION.
RX PubMed=23583401; DOI=10.1016/j.bbrc.2013.03.120;
RA Kumano-Kuramochi M., Xie Q., Kajiwara S., Komba S., Minowa T., Machida S.;
RT "Lectin-like oxidized LDL receptor-1 is palmitoylated and internalizes
RT ligands via caveolae/raft-dependent endocytosis.";
RL Biochem. Biophys. Res. Commun. 434:594-599(2013).
RN [27]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH N.MENINGITIDIS ADHESIN
RP A (MICROBIAL INFECTION).
RX PubMed=27302108; DOI=10.1038/srep27996;
RA Scietti L., Sampieri K., Pinzuti I., Bartolini E., Benucci B., Liguori A.,
RA Haag A.F., Lo Surdo P., Pansegrau W., Nardi-Dei V., Santini L., Arora S.,
RA Leber X., Rindi S., Savino S., Costantino P., Maione D., Merola M.,
RA Speziale P., Bottomley M.J., Bagnoli F., Masignani V., Pizza M.,
RA Scharenberg M., Schlaeppi J.M., Nissum M., Liberatori S.;
RT "Exploring host-pathogen interactions through genome wide protein
RT microarray analysis.";
RL Sci. Rep. 6:27996-27996(2016).
RN [28]
RP INTERACTION WITH N.MENINGITIDIS ADHESIN A (MICROBIAL INFECTION).
RX PubMed=30327444; DOI=10.1128/mbio.01914-18;
RA Liguori A., Dello Iacono L., Maruggi G., Benucci B., Merola M.,
RA Lo Surdo P., Lopez-Sagaseta J., Pizza M., Malito E., Bottomley M.J.;
RT "NadA3 Structures Reveal Undecad Coiled Coils and LOX1 Binding Regions
RT Competed by Meningococcus B Vaccine-Elicited Human Antibodies.";
RL MBio 9:0-0(2018).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 136-270, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=15695803; DOI=10.1074/jbc.m500768200;
RA Park H., Adsit F.G., Boyington J.C.;
RT "The 1.4 angstrom crystal structure of the human oxidized low density
RT lipoprotein receptor lox-1.";
RL J. Biol. Chem. 280:13593-13599(2005).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 143-271, SUBUNIT, DISULFIDE BONDS,
RP AND MUTAGENESIS OF TRP-150; ARG-208; ARG-209; HIS-226; ARG-229; ARG-231 AND
RP ARG-248.
RX PubMed=15939022; DOI=10.1016/j.str.2005.03.016;
RA Ohki I., Ishigaki T., Oyama T., Matsunaga S., Xie Q., Ohnishi-Kameyama M.,
RA Murata T., Tsuchiya D., Machida S., Morikawa K., Tate S.;
RT "Crystal structure of human lectin-like, oxidized low-density lipoprotein
RT receptor 1 ligand binding domain and its ligand recognition mode to
RT oxLDL.";
RL Structure 13:905-917(2005).
CC -!- FUNCTION: Receptor that mediates the recognition, internalization and
CC degradation of oxidatively modified low density lipoprotein (oxLDL) by
CC vascular endothelial cells. OxLDL is a marker of atherosclerosis that
CC induces vascular endothelial cell activation and dysfunction, resulting
CC in pro-inflammatory responses, pro-oxidative conditions and apoptosis.
CC Its association with oxLDL induces the activation of NF-kappa-B through
CC an increased production of intracellular reactive oxygen and a variety
CC of pro-atherogenic cellular responses including a reduction of nitric
CC oxide (NO) release, monocyte adhesion and apoptosis. In addition to
CC binding oxLDL, it acts as a receptor for the HSP70 protein involved in
CC antigen cross-presentation to naive T-cells in dendritic cells, thereby
CC participating in cell-mediated antigen cross-presentation. Also
CC involved in inflammatory process, by acting as a leukocyte-adhesion
CC molecule at the vascular interface in endotoxin-induced inflammation.
CC Also acts as a receptor for advanced glycation end (AGE) products,
CC activated platelets, monocytes, apoptotic cells and both Gram-negative
CC and Gram-positive bacteria. {ECO:0000269|PubMed:11821063,
CC ECO:0000269|PubMed:12354387, ECO:0000269|PubMed:9052782}.
CC -!- FUNCTION: (Microbial infection) May serve as a receptor for adhesin A
CC variant 3 (nadA) of N.meningitidis. {ECO:0000305|PubMed:27302108}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. May form a hexamer composed of 3
CC homodimers. Interacts with HSP70. {ECO:0000269|PubMed:11256994,
CC ECO:0000269|PubMed:15695803, ECO:0000269|PubMed:15939022}.
CC -!- SUBUNIT: (Microbial infection) Binds to the head and beginning of the
CC coiled stalk of N.meningitidis adhesin A (nadA) variant 3; binding can
CC be abrogated by monoclonal antibodies against the specific regions of
CC NadA. Binding occurs in protein microarrays, in solution and when LOX-1
CC is expressed on the cell surface. {ECO:0000269|PubMed:27302108,
CC ECO:0000269|PubMed:30327444}.
CC -!- INTERACTION:
CC P78380; P50991: CCT4; NbExp=3; IntAct=EBI-7151999, EBI-356876;
CC P78380; P78380: OLR1; NbExp=4; IntAct=EBI-7151999, EBI-7151999;
CC P78380; P17987: TCP1; NbExp=5; IntAct=EBI-7151999, EBI-356553;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell membrane;
CC Single-pass type II membrane protein. Membrane raft. Secreted. Note=A
CC secreted form also exists. Localization to membrane rafts requires
CC palmitoylation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P78380-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P78380-2; Sequence=VSP_042555;
CC Name=3;
CC IsoId=P78380-3; Sequence=VSP_045277;
CC -!- TISSUE SPECIFICITY: Expressed at high level in endothelial cells and
CC vascular-rich organs such as placenta, lung, liver and brain, aortic
CC intima, bone marrow, spinal cord and substantia nigra. Also expressed
CC at the surface of dendritic cells. Widely expressed at intermediate and
CC low level. {ECO:0000269|PubMed:12354387, ECO:0000269|PubMed:9052782,
CC ECO:0000269|PubMed:9828121}.
CC -!- INDUCTION: By inflammatory cytokines such as TNF, IFNG/IFN-gamma,
CC IL6/interleukin-6 and by pathological conditions such as
CC hyperlipidemia, hypertension and diabetes mellitus. Up-regulated in
CC atherosclerotic lesions, by oxLDL, reactive oxygen species and fluid
CC shear stress, suggesting that it may participate in amplification of
CC oxLDL-induced vascular dysfunction. {ECO:0000269|PubMed:12878212,
CC ECO:0000269|PubMed:9828121}.
CC -!- DOMAIN: The cytoplasmic region is required for subcellular sorting on
CC the cell surface.
CC -!- DOMAIN: The C-type lectin domain mediates the recognition and binding
CC of oxLDL.
CC -!- PTM: The intrachain disulfide-bonds prevent N-glycosylation at some
CC sites.
CC -!- PTM: N-glycosylated.
CC -!- DISEASE: Note=Independent association genetic studies have implicated
CC OLR1 gene variants in myocardial infarction susceptibility.
CC -!- DISEASE: Note=OLR1 may be involved in Alzheimer disease (AD).
CC Involvement in AD is however unclear: according to some authors
CC (PubMed:12354387, PubMed:12810610 and PubMed:15976314), variations in
CC OLR1 modify the risk of AD, while according to others (PubMed:15000751
CC and PubMed:15060104) they do not. {ECO:0000269|PubMed:12384789,
CC ECO:0000269|PubMed:12807963, ECO:0000269|PubMed:15860461}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Oxidized LDL receptor;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_249";
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DR EMBL; AB010710; BAA24580.1; -; mRNA.
DR EMBL; AF035776; AAC82329.1; -; mRNA.
DR EMBL; AF079167; AAC97927.1; -; Genomic_DNA.
DR EMBL; AF079166; AAC97927.1; JOINED; Genomic_DNA.
DR EMBL; AF079164; AAC97927.1; JOINED; Genomic_DNA.
DR EMBL; AF079165; AAC97927.1; JOINED; Genomic_DNA.
DR EMBL; AB102861; BAC81565.1; -; mRNA.
DR EMBL; AJ131757; CAB38175.1; -; Genomic_DNA.
DR EMBL; BX344276; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK292124; BAF84813.1; -; mRNA.
DR EMBL; AK295409; BAG58360.1; -; mRNA.
DR EMBL; DQ314885; ABC40744.1; -; Genomic_DNA.
DR EMBL; AC024224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96157.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96158.1; -; Genomic_DNA.
DR EMBL; BC022295; AAH22295.1; -; mRNA.
DR CCDS; CCDS53745.1; -. [P78380-2]
DR CCDS; CCDS53746.1; -. [P78380-3]
DR CCDS; CCDS8618.1; -. [P78380-1]
DR RefSeq; NP_001166103.1; NM_001172632.1. [P78380-2]
DR RefSeq; NP_001166104.1; NM_001172633.1. [P78380-3]
DR RefSeq; NP_002534.1; NM_002543.3. [P78380-1]
DR PDB; 1YPO; X-ray; 3.00 A; A/B/C/D/E/F/G/H=142-272.
DR PDB; 1YPQ; X-ray; 1.40 A; A/B=136-270.
DR PDB; 1YPU; X-ray; 2.05 A; A/B=136-270.
DR PDB; 1YXJ; X-ray; 1.78 A; A/B=143-271.
DR PDB; 1YXK; X-ray; 2.40 A; A/B=136-270.
DR PDB; 3VLG; X-ray; 2.30 A; A=133-273.
DR PDB; 6TL7; X-ray; 1.11 A; A/B=143-273.
DR PDB; 6TL9; X-ray; 2.73 A; A/B/C/D/E/F/G/H=143-273.
DR PDB; 6TLA; X-ray; 2.16 A; A/B/C=129-273.
DR PDBsum; 1YPO; -.
DR PDBsum; 1YPQ; -.
DR PDBsum; 1YPU; -.
DR PDBsum; 1YXJ; -.
DR PDBsum; 1YXK; -.
DR PDBsum; 3VLG; -.
DR PDBsum; 6TL7; -.
DR PDBsum; 6TL9; -.
DR PDBsum; 6TLA; -.
DR AlphaFoldDB; P78380; -.
DR SMR; P78380; -.
DR BioGRID; 111021; 23.
DR DIP; DIP-42040N; -.
DR IntAct; P78380; 9.
DR MINT; P78380; -.
DR STRING; 9606.ENSP00000309124; -.
DR ChEMBL; CHEMBL3421522; -.
DR GlyGen; P78380; 2 sites.
DR iPTMnet; P78380; -.
DR PhosphoSitePlus; P78380; -.
DR SwissPalm; P78380; -.
DR BioMuta; OLR1; -.
DR DMDM; 73621335; -.
DR jPOST; P78380; -.
DR MassIVE; P78380; -.
DR MaxQB; P78380; -.
DR PaxDb; P78380; -.
DR PeptideAtlas; P78380; -.
DR PRIDE; P78380; -.
DR ProteomicsDB; 32344; -.
DR ProteomicsDB; 57601; -. [P78380-1]
DR ProteomicsDB; 57602; -. [P78380-2]
DR ABCD; P78380; 33 sequenced antibodies.
DR Antibodypedia; 11685; 672 antibodies from 41 providers.
DR DNASU; 4973; -.
DR Ensembl; ENST00000309539.8; ENSP00000309124.3; ENSG00000173391.9. [P78380-1]
DR Ensembl; ENST00000432556.6; ENSP00000405116.2; ENSG00000173391.9. [P78380-2]
DR Ensembl; ENST00000545927.5; ENSP00000439251.1; ENSG00000173391.9. [P78380-3]
DR GeneID; 4973; -.
DR KEGG; hsa:4973; -.
DR MANE-Select; ENST00000309539.8; ENSP00000309124.3; NM_002543.4; NP_002534.1.
DR UCSC; uc001qxo.2; human. [P78380-1]
DR CTD; 4973; -.
DR DisGeNET; 4973; -.
DR GeneCards; OLR1; -.
DR HGNC; HGNC:8133; OLR1.
DR HPA; ENSG00000173391; Tissue enhanced (lung, placenta).
DR MalaCards; OLR1; -.
DR MIM; 602601; gene+phenotype.
DR neXtProt; NX_P78380; -.
DR NIAGADS; ENSG00000173391; -.
DR OpenTargets; ENSG00000173391; -.
DR PharmGKB; PA31920; -.
DR VEuPathDB; HostDB:ENSG00000173391; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161941; -.
DR InParanoid; P78380; -.
DR OMA; HSSFPFW; -.
DR PhylomeDB; P78380; -.
DR TreeFam; TF336674; -.
DR PathwayCommons; P78380; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P78380; -.
DR BioGRID-ORCS; 4973; 13 hits in 1069 CRISPR screens.
DR ChiTaRS; OLR1; human.
DR EvolutionaryTrace; P78380; -.
DR GeneWiki; OLR1; -.
DR GenomeRNAi; 4973; -.
DR Pharos; P78380; Tbio.
DR PRO; PR:P78380; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P78380; protein.
DR Bgee; ENSG00000173391; Expressed in right lung and 128 other tissues.
DR ExpressionAtlas; P78380; baseline and differential.
DR Genevisible; P78380; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IBA:GO_Central.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0008219; P:cell death; IBA:GO_Central.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR013600; Ly49_N.
DR InterPro; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF08391; Ly49; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Coiled coil; Disulfide bond; Glycoprotein; Immunity; Inflammatory response;
KW Lectin; Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome;
KW Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..273
FT /note="Oxidized low-density lipoprotein receptor 1"
FT /id="PRO_0000017443"
FT CHAIN ?..273
FT /note="Oxidized low-density lipoprotein receptor 1, soluble
FT form"
FT /id="PRO_0000017444"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 151..265
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..150
FT /note="Neck"
FT COILED 64..123
FT /evidence="ECO:0000255"
FT SITE 183
FT /note="Not glycosylated"
FT /evidence="ECO:0000305"
FT LIPID 36
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23583401"
FT LIPID 46
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23583401"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:22688517"
FT DISULFID 140
FT /note="Interchain"
FT DISULFID 144..155
FT DISULFID 172..264
FT DISULFID 243..256
FT VAR_SEQ 142..273
FT /note="APCPQDWIWHGENCYLFSSGSFNWEKSQEKCLSLDAKLLKINSTADLDFIQQ
FT AISYSSFPFWMGLSRRNPSYPWLWEDGSPLMPHLFRVRGAVSQTYPSGTCAYIQRGAVY
FT AENCILAAFSICQKKANLRAQ -> GLHPASNFLFQFSILDGAVSEEPQLPMALGGRFS
FT FDAPLI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042555"
FT VAR_SEQ 189..273
FT /note="DFIQQAISYSSFPFWMGLSRRNPSYPWLWEDGSPLMPHLFRVRGAVSQTYPS
FT GTCAYIQRGAVYAENCILAAFSICQKKANLRAQ -> I (in isoform 3)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_045277"
FT VARIANT 167
FT /note="K -> N (myocardial infarction susceptibility;
FT dbSNP:rs11053646)"
FT /evidence="ECO:0000269|PubMed:12646194,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_023200"
FT MUTAGEN 22..25
FT /note="KKAK->EEAE: Impairs sorting into the cell surface
FT but retains ability to bind oxLDL. Abolishes sorting into
FT the cell surface; when associated with K-69."
FT /evidence="ECO:0000269|PubMed:15935375"
FT MUTAGEN 70
FT /note="E->K: Abolishes sorting into the cell surface; when
FT associated with 22-E--E-25."
FT /evidence="ECO:0000269|PubMed:15935375"
FT MUTAGEN 140
FT /note="C->S: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:15000751"
FT MUTAGEN 144
FT /note="C->S: Abolishes sorting into the cell surface and
FT binding to acetylated LDL (AcLDL) while increasing N-
FT glycosylation; when associated with S-155; S-172; S-243; S-
FT 256 and S-264."
FT /evidence="ECO:0000269|PubMed:11256994"
FT MUTAGEN 150
FT /note="W->A: Abolishes binding to acetylated LDL (AcLDL),
FT probably due to inappropriate homodimerization."
FT /evidence="ECO:0000269|PubMed:15939022"
FT MUTAGEN 155
FT /note="C->S: Abolishes sorting into the cell surface and
FT binding to acetylated LDL (AcLDL) while increasing N-
FT glycosylation; when associated with S-144; S-172; S-243; S-
FT 256 and S-264."
FT /evidence="ECO:0000269|PubMed:11256994"
FT MUTAGEN 172
FT /note="C->S: Abolishes sorting into the cell surface and
FT binding to acetylated LDL (AcLDL) while increasing N-
FT glycosylation; when associated with S-144; S-155; S-243; S-
FT 256 and S-264."
FT /evidence="ECO:0000269|PubMed:11256994"
FT MUTAGEN 183
FT /note="N->Q: Does not affect glycosylation state."
FT /evidence="ECO:0000269|PubMed:11256994"
FT MUTAGEN 193
FT /note="Q->L: Impairs binding to acetylated LDL (AcLDL);
FT when associated with 198-AA-199."
FT MUTAGEN 198..199
FT /note="SS->AA: Impairs binding to acetylated LDL (AcLDL);
FT when associated with L-193."
FT MUTAGEN 208
FT /note="R->N: Does not affect subcellular location but
FT displays a strongly reduced affinity for acetylated LDL
FT (AcLDL)."
FT /evidence="ECO:0000269|PubMed:15939022"
FT MUTAGEN 209..210
FT /note="RN->LL: Abolishes binding to acetylated LDL
FT (AcLDL)."
FT /evidence="ECO:0000269|PubMed:11256994"
FT MUTAGEN 209
FT /note="R->N: Does not affect binding to acetylated LDL
FT (AcLDL)."
FT /evidence="ECO:0000269|PubMed:15939022"
FT MUTAGEN 226
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:11256994,
FT ECO:0000269|PubMed:15939022"
FT MUTAGEN 226
FT /note="H->Q: Abolishes binding to acetylated LDL (AcLDL);
FT when associated with N-229 and N-231."
FT /evidence="ECO:0000269|PubMed:11256994,
FT ECO:0000269|PubMed:15939022"
FT MUTAGEN 229
FT /note="R->N: Does not affect subcellular location but
FT displays a reduced affinity for acetylated LDL (AcLDL).
FT Abolishes binding to acetylated LDL (AcLDL); when
FT associated with Q-226 and N-231."
FT /evidence="ECO:0000269|PubMed:11256994,
FT ECO:0000269|PubMed:15939022"
FT MUTAGEN 231
FT /note="R->N: Abolishes binding to acetylated LDL (AcLDL).
FT Abolishes binding to AcLDL; when associated with Q-226 and
FT N-229."
FT /evidence="ECO:0000269|PubMed:11256994,
FT ECO:0000269|PubMed:15939022"
FT MUTAGEN 235..236
FT /note="SQ->AL: Impairs binding to acetylated LDL (AcLDL);
FT when associated with A-240."
FT /evidence="ECO:0000269|PubMed:11256994"
FT MUTAGEN 240
FT /note="S->A: Impairs binding to acetylated LDL (AcLDL);
FT when associated with 235-AL-236."
FT /evidence="ECO:0000269|PubMed:11256994"
FT MUTAGEN 243
FT /note="C->S: Abolishes sorting into the cell surface and
FT binding to acetylated LDL (AcLDL) while increasing N-
FT glycosylation; when associated with S-144; S-155; S-172; S-
FT 256 and S-264."
FT /evidence="ECO:0000269|PubMed:11256994"
FT MUTAGEN 248
FT /note="R->N: Does not affect subcellular location but
FT displays a reduced affinity for acetylated LDL (AcLDL)."
FT /evidence="ECO:0000269|PubMed:15939022"
FT MUTAGEN 256
FT /note="C->S: Abolishes sorting into the cell surface and
FT binding to acetylated LDL (AcLDL) while increasing N-
FT glycosylation; when associated with S-144; S-155; S-172; S-
FT 243 and S-264."
FT /evidence="ECO:0000269|PubMed:11256994"
FT MUTAGEN 264
FT /note="C->S: Abolishes sorting into the cell surface and
FT binding to acetylated LDL (AcLDL) while increasing N-
FT glycosylation; when associated with S-144; S-155; S-172; S-
FT 243 and S-256."
FT /evidence="ECO:0000269|PubMed:11256994"
FT MUTAGEN 267..273
FT /note="Missing: Impairs protein folding and transport."
FT /evidence="ECO:0000269|PubMed:11256994"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6TL7"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:6TL7"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:6TL7"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:6TL7"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6TL7"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:6TL7"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1YPO"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:6TL7"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:6TL7"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:6TL7"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:6TL7"
SQ 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
