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 27-MAR-2024, entry version 207. 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 variations in OLR1 modify the risk of AD(PubMed:12354387, CC PubMed:12810610, PubMed:15976314). While according to others they do CC not (PubMed:15000751, PubMed:15060104). {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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7R8U; X-ray; 1.90 A; AAA/BBB=140-271. DR PDB; 7W5D; X-ray; 1.14 A; A/B=136-273. DR PDB; 7XMP; X-ray; 1.27 A; A=136-273. 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 PDBsum; 7R8U; -. DR PDBsum; 7W5D; -. DR PDBsum; 7XMP; -. DR AlphaFoldDB; P78380; -. DR SMR; P78380; -. DR BioGRID; 111021; 25. DR DIP; DIP-42040N; -. DR IntAct; P78380; 11. DR MINT; P78380; -. DR STRING; 9606.ENSP00000309124; -. DR ChEMBL; CHEMBL3421522; -. DR GlyCosmos; P78380; 2 sites, No reported glycans. 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; 9606-ENSP00000309124; -. DR PeptideAtlas; P78380; -. DR ProteomicsDB; 32344; -. DR ProteomicsDB; 57601; -. [P78380-1] DR ProteomicsDB; 57602; -. [P78380-2] DR ABCD; P78380; 33 sequenced antibodies. DR Antibodypedia; 11685; 764 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 AGR; HGNC:8133; -. 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; NYSWLWE; -. DR OrthoDB; 2883044at2759; -. 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 1158 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 130 other cell types or tissues. DR ExpressionAtlas; P78380; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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:0002376; P:immune system process; IEA:UniProtKB-KW. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. 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; Mannose-Binding Protein A, subunit A; 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 PANTHER; PTHR47298; OXIDIZED LOW-DENSITY LIPOPROTEIN RECEPTOR 1; 1. DR PANTHER; PTHR47298:SF1; OXIDIZED LOW-DENSITY LIPOPROTEIN RECEPTOR 1; 1. DR Pfam; PF00059; Lectin_C; 1. DR Pfam; PF08391; Ly49; 1. DR SMART; SM00034; CLECT; 1. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. DR Genevisible; P78380; HS. 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 FT N-glycosylation; when associated with S-155; S-172; S-243; FT S-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 FT N-glycosylation; when associated with S-144; S-172; S-243; FT S-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 FT N-glycosylation; when associated with S-144; S-155; S-243; FT S-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 FT N-glycosylation; when associated with S-144; S-155; S-172; FT S-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 FT N-glycosylation; when associated with S-144; S-155; S-172; FT S-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 FT N-glycosylation; when associated with S-144; S-155; S-172; FT S-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 //