OLR1_BOVIN
ID OLR1_BOVIN Reviewed; 270 AA.
AC P79391;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Oxidized low-density lipoprotein receptor 1;
DE Short=Ox-LDL receptor 1;
DE AltName: Full=Lectin-like oxidized LDL receptor 1;
DE Short=LOX-1;
DE Short=Lectin-like oxLDL receptor 1;
DE Short=bLOX-1;
DE AltName: Full=Lectin-type oxidized LDL receptor 1;
DE Contains:
DE RecName: Full=Oxidized low-density lipoprotein receptor 1, soluble form A;
DE Contains:
DE RecName: Full=Oxidized low-density lipoprotein receptor 1, soluble form B;
GN Name=OLR1; Synonyms=LOX1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP 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 PROTEIN SEQUENCE OF 87-91 AND 90-94, AND IDENTIFICATION OF SOLUBLE FORMS.
RX PubMed=10712396; DOI=10.1161/01.atv.20.3.715;
RA Murase T., Kume N., Kataoka H., Minami M., Sawamura T., Masaki T., Kita T.;
RT "Identification of soluble forms of lectin-like oxidized LDL receptor-1.";
RL Arterioscler. Thromb. Vasc. Biol. 20:715-720(2000).
RN [3]
RP FUNCTION.
RX PubMed=9689115; DOI=10.1073/pnas.95.16.9535;
RA Oka K., Sawamura T., Kikuta K., Itokawa S., Kume N., Kita T., Masaki T.;
RT "Lectin-like oxidized low-density lipoprotein receptor 1 mediates
RT phagocytosis of aged/apoptotic cells in endothelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9535-9540(1998).
RN [4]
RP FUNCTION.
RX PubMed=10618423; DOI=10.1073/pnas.97.1.360;
RA Kakutani M., Masaki T., Sawamura T.;
RT "A platelet-endothelium interaction mediated by lectin-like oxidized low-
RT density lipoprotein receptor-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:360-364(2000).
RN [5]
RP MUTAGENESIS OF LYS-262; LYS-263 AND ASN-265.
RX PubMed=11284714; DOI=10.1042/0264-6021:3550289;
RA Chen M., Narumiya S., Masaki T., Sawamura T.;
RT "Conserved C-terminal residues within the lectin-like domain of LOX-1 are
RT essential for oxidized low-density-lipoprotein binding.";
RL Biochem. J. 355:289-296(2001).
RN [6]
RP GLYCOSYLATION.
RX PubMed=10692464; DOI=10.1074/jbc.275.9.6573;
RA Kataoka H., Kume N., Miyamoto S., Minami M., Murase T., Sawamura T.,
RA Masaki T., Hashimoto N., Kita T.;
RT "Biosynthesis and post-translational processing of lectin-like oxidized low
RT density lipoprotein receptor-1 (LOX-1). N-linked glycosylation affects
RT cell-surface expression and ligand binding.";
RL J. Biol. Chem. 275:6573-6579(2000).
RN [7]
RP FUNCTION.
RX PubMed=10777555; DOI=10.1074/jbc.275.17.12633;
RA Cominacini L., Pasini A.F., Garbin U., Davoli A., Tosetti M.L.,
RA Campagnola M., Rigoni A., Pastorino A.M., Lo Cascio V., Sawamura T.;
RT "Oxidized low density lipoprotein (ox-LDL) binding to ox-LDL receptor-1 in
RT endothelial cells induces the activation of NF-kappaB through an increased
RT production of intracellular reactive oxygen species.";
RL J. Biol. Chem. 275:12633-12638(2000).
RN [8]
RP FUNCTION.
RX PubMed=11290792; DOI=10.4049/jimmunol.166.8.5108;
RA Shimaoka T., Kume N., Minami M., Hayashida K., Sawamura T., Kita T.,
RA Yonehara S.;
RT "LOX-1 supports adhesion of Gram-positive and Gram-negative bacteria.";
RL J. Immunol. 166:5108-5114(2001).
RN [9]
RP MUTAGENESIS OF 205-ARG-LYS-206; ARG-225; ARG-232 AND ARG-244.
RX PubMed=11423119; DOI=10.1016/s0014-5793(01)02557-1;
RA Chen M., Inoue K., Narumiya S., Masaki T., Sawamura T.;
RT "Requirements of basic amino acid residues within the lectin-like domain of
RT LOX-1 for the binding of oxidized low-density lipoprotein.";
RL FEBS Lett. 499:215-219(2001).
RN [10]
RP FUNCTION.
RX PubMed=11821070; DOI=10.1016/s0014-5793(01)03325-7;
RA Jono T., Miyazaki A., Nagai R., Sawamura T., Kitamura T., Horiuchi S.;
RT "Lectin-like oxidized low density lipoprotein receptor-1 (LOX-1) serves as
RT an endothelial receptor for advanced glycation end products (AGE).";
RL FEBS Lett. 511:170-174(2002).
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:10618423,
CC ECO:0000269|PubMed:10777555, ECO:0000269|PubMed:11290792,
CC ECO:0000269|PubMed:11821070, ECO:0000269|PubMed:9052782,
CC ECO:0000269|PubMed:9689115}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. May form a hexamer composed of 3
CC homodimers. Interacts with HSP70 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:9052782}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:9052782}. Membrane raft
CC {ECO:0000250}. Secreted {ECO:0000269|PubMed:9052782}. Note=Localization
CC to membrane rafts requires palmitoylation (By similarity). A secreted
CC form also exists. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in endothelial cells, aortic
CC intima and lung. Expressed at low level in other tissues.
CC {ECO:0000269|PubMed:9052782}.
CC -!- DOMAIN: The cytoplasmic region is required for subcellular sorting on
CC the cell surface. {ECO:0000250}.
CC -!- DOMAIN: The C-type lectin domain mediates the recognition and binding
CC of oxLDL.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10692464}.
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DR EMBL; D89049; BAA19005.1; -; mRNA.
DR RefSeq; NP_776557.1; NM_174132.2.
DR AlphaFoldDB; P79391; -.
DR SMR; P79391; -.
DR STRING; 9913.ENSBTAP00000005975; -.
DR BindingDB; P79391; -.
DR PaxDb; P79391; -.
DR GeneID; 281368; -.
DR KEGG; bta:281368; -.
DR CTD; 4973; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P79391; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IBA:GO_Central.
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 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; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 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 Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Coiled coil; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunity; Inflammatory response; Lectin; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..270
FT /note="Oxidized low-density lipoprotein receptor 1"
FT /id="PRO_0000017440"
FT CHAIN 87..270
FT /note="Oxidized low-density lipoprotein receptor 1, soluble
FT form A"
FT /id="PRO_0000017441"
FT CHAIN 90..270
FT /note="Oxidized low-density lipoprotein receptor 1, soluble
FT form B"
FT /id="PRO_0000017442"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 147..261
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 57..146
FT /note="Neck"
FT COILED 85..135
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 42
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 168..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 239..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MUTAGEN 205..206
FT /note="RK->AA: Does not affect oxLDL binding. Impairs oxLDL
FT binding; when associated with A-225; A-232 and A-234."
FT /evidence="ECO:0000269|PubMed:11423119"
FT MUTAGEN 225
FT /note="R->A: Reduces oxLDL binding. Impairs oxLDL binding;
FT when associated with A-205; A-206; A-225; A-232 and A-234."
FT /evidence="ECO:0000269|PubMed:11423119"
FT MUTAGEN 232
FT /note="R->A: Does not affect oxLDL binding. Impairs oxLDL
FT binding; when associated with A-205; A-206; A-225 and A-
FT 234."
FT /evidence="ECO:0000269|PubMed:11423119"
FT MUTAGEN 244
FT /note="R->A: Does not affect oxLDL binding. Impairs oxLDL
FT binding; when associated with A-205; A-206; A-225 and A-
FT 232."
FT /evidence="ECO:0000269|PubMed:11423119"
FT MUTAGEN 262
FT /note="K->A: Impairs the binding to oxLDL."
FT /evidence="ECO:0000269|PubMed:11284714"
FT MUTAGEN 263
FT /note="K->A: Impairs the binding to oxLDL."
FT /evidence="ECO:0000269|PubMed:11284714"
FT MUTAGEN 265
FT /note="N->D: Impairs the binding to oxLDL."
FT /evidence="ECO:0000269|PubMed:11284714"
SQ SEQUENCE 270 AA; 30892 MW; 6055B6881AD7053D CRC64;
MTVDDPKGMK DQLDQKPNGK TAKGFVSSWR WYPAAVTLGV LCLGLLVTVI LLILQLSQVS
DLIKKQQANI THQEDILEGQ ILAQRRSEKS AQESQKELKE MIETLAHKLD EKSKKLMELH
RQNLNLQEVL KEAANYSGPC PQDWLWHEEN CYQFSSGSFN WEKSQENCLS LDAHLLKINS
TDELEFIQQM IAHSSFPFWM GLSMRKPNYS WLWEDGTPLT PHLFRIQGAV SRMYPSGTCA
YIQRGTVFAE NCILTAFSIC QKKANLLRAQ
