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Oxidized low-density lipoprotein receptor 1 (Ox-LDL receptor 1) (Lectin-like oxidized LDL receptor 1) (LOX-1) (Lectin-like oxLDL receptor 1) (bLOX-1) (Lectin-type oxidized LDL receptor 1) [Cleaved into: Oxidized low-density lipoprotein receptor 1, soluble form A; Oxidized low-density lipoprotein receptor 1, soluble form B]

 OLR1_BOVIN              Reviewed;         270 AA.
P79391;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
10-MAY-2017, entry version 110.
RecName: Full=Oxidized low-density lipoprotein receptor 1;
Short=Ox-LDL receptor 1;
AltName: Full=Lectin-like oxidized LDL receptor 1;
Short=LOX-1;
Short=Lectin-like oxLDL receptor 1;
Short=bLOX-1;
AltName: Full=Lectin-type oxidized LDL receptor 1;
Contains:
RecName: Full=Oxidized low-density lipoprotein receptor 1, soluble form A;
Contains:
RecName: Full=Oxidized low-density lipoprotein receptor 1, soluble form B;
Name=OLR1; Synonyms=LOX1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, 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]
PROTEIN SEQUENCE OF 87-91 AND 90-94, AND IDENTIFICATION OF SOLUBLE
FORMS.
PubMed=10712396; DOI=10.1161/01.ATV.20.3.715;
Murase T., Kume N., Kataoka H., Minami M., Sawamura T., Masaki T.,
Kita T.;
"Identification of soluble forms of lectin-like oxidized LDL receptor-
1.";
Arterioscler. Thromb. Vasc. Biol. 20:715-720(2000).
[3]
FUNCTION.
PubMed=9689115; DOI=10.1073/pnas.95.16.9535;
Oka K., Sawamura T., Kikuta K., Itokawa S., Kume N., Kita T.,
Masaki T.;
"Lectin-like oxidized low-density lipoprotein receptor 1 mediates
phagocytosis of aged/apoptotic cells in endothelial cells.";
Proc. Natl. Acad. Sci. U.S.A. 95:9535-9540(1998).
[4]
FUNCTION.
PubMed=10618423; DOI=10.1073/pnas.97.1.360;
Kakutani M., Masaki T., Sawamura T.;
"A platelet-endothelium interaction mediated by lectin-like oxidized
low-density lipoprotein receptor-1.";
Proc. Natl. Acad. Sci. U.S.A. 97:360-364(2000).
[5]
MUTAGENESIS OF LYS-262; LYS-263 AND ASN-265.
PubMed=11284714; DOI=10.1042/0264-6021:3550289;
Chen M., Narumiya S., Masaki T., Sawamura T.;
"Conserved C-terminal residues within the lectin-like domain of LOX-1
are essential for oxidized low-density-lipoprotein binding.";
Biochem. J. 355:289-296(2001).
[6]
GLYCOSYLATION.
PubMed=10692464; DOI=10.1074/jbc.275.9.6573;
Kataoka H., Kume N., Miyamoto S., Minami M., Murase T., Sawamura T.,
Masaki T., Hashimoto N., Kita T.;
"Biosynthesis and post-translational processing of lectin-like
oxidized low density lipoprotein receptor-1 (LOX-1). N-linked
glycosylation affects cell-surface expression and ligand binding.";
J. Biol. Chem. 275:6573-6579(2000).
[7]
FUNCTION.
PubMed=10777555; DOI=10.1074/jbc.275.17.12633;
Cominacini L., Pasini A.F., Garbin U., Davoli A., Tosetti M.L.,
Campagnola M., Rigoni A., Pastorino A.M., Lo Cascio V., Sawamura T.;
"Oxidized low density lipoprotein (ox-LDL) binding to ox-LDL receptor-
1 in endothelial cells induces the activation of NF-kappaB through an
increased production of intracellular reactive oxygen species.";
J. Biol. Chem. 275:12633-12638(2000).
[8]
FUNCTION.
PubMed=11290792; DOI=10.4049/jimmunol.166.8.5108;
Shimaoka T., Kume N., Minami M., Hayashida K., Sawamura T., Kita T.,
Yonehara S.;
"LOX-1 supports adhesion of Gram-positive and Gram-negative
bacteria.";
J. Immunol. 166:5108-5114(2001).
[9]
MUTAGENESIS OF 205-ARG-LYS-206; ARG-225; ARG-232 AND ARG-244.
PubMed=11423119; DOI=10.1016/S0014-5793(01)02557-1;
Chen M., Inoue K., Narumiya S., Masaki T., Sawamura T.;
"Requirements of basic amino acid residues within the lectin-like
domain of LOX-1 for the binding of oxidized low-density lipoprotein.";
FEBS Lett. 499:215-219(2001).
[10]
FUNCTION.
PubMed=11821070; DOI=10.1016/S0014-5793(01)03325-7;
Jono T., Miyazaki A., Nagai R., Sawamura T., Kitamura T., Horiuchi S.;
"Lectin-like oxidized low density lipoprotein receptor-1 (LOX-1)
serves as an endothelial receptor for advanced glycation end products
(AGE).";
FEBS Lett. 511:170-174(2002).
-!- 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:10618423,
ECO:0000269|PubMed:10777555, ECO:0000269|PubMed:11290792,
ECO:0000269|PubMed:11821070, ECO:0000269|PubMed:9052782,
ECO:0000269|PubMed:9689115}.
-!- SUBUNIT: Homodimer; disulfide-linked. May form a hexamer composed
of 3 homodimers. Interacts with HSP70 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}. Cell membrane {ECO:0000269|PubMed:9052782}; Single-
pass type II membrane protein {ECO:0000269|PubMed:9052782}.
Membrane raft {ECO:0000250}. Secreted
{ECO:0000269|PubMed:9052782}. Note=Localization to membrane rafts
requires palmitoylation (By similarity). A secreted form also
exists. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in endothelial cells, aortic
intima and lung. Expressed at low level in other tissues.
{ECO:0000269|PubMed:9052782}.
-!- DOMAIN: The cytoplasmic region is required for subcellular sorting
on the cell surface. {ECO:0000250}.
-!- DOMAIN: The C-type lectin domain mediates the recognition and
binding of oxLDL.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:10692464}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; D89049; BAA19005.1; -; mRNA.
RefSeq; NP_776557.1; NM_174132.2.
UniGene; Bt.367; -.
ProteinModelPortal; P79391; -.
SMR; P79391; -.
STRING; 9913.ENSBTAP00000005975; -.
PaxDb; P79391; -.
PRIDE; P79391; -.
GeneID; 281368; -.
KEGG; bta:281368; -.
CTD; 4973; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
HOVERGEN; HBG056863; -.
InParanoid; P79391; -.
KO; K08763; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
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; IPR033992; NKR-like_CTLD.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
Coiled coil; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Immunity; Inflammatory response; Lectin;
Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome;
Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 270 Oxidized low-density lipoprotein receptor
1.
/FTId=PRO_0000017440.
CHAIN 87 270 Oxidized low-density lipoprotein receptor
1, soluble form A.
/FTId=PRO_0000017441.
CHAIN 90 270 Oxidized low-density lipoprotein receptor
1, soluble form B.
/FTId=PRO_0000017442.
TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.
TRANSMEM 34 56 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 57 270 Extracellular. {ECO:0000255}.
DOMAIN 147 261 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
REGION 57 146 Neck.
COILED 85 135 {ECO:0000255}.
LIPID 42 42 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 140 151 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 168 260 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 239 252 {ECO:0000255|PROSITE-ProRule:PRU00040}.
MUTAGEN 205 206 RK->AA: Does not affect oxLDL binding.
Impairs oxLDL binding; when associated
with A-225; A-232 and A-234.
{ECO:0000269|PubMed:11423119}.
MUTAGEN 225 225 R->A: Reduces oxLDL binding. Impairs
oxLDL binding; when associated with A-
205; A-206; A-225; A-232 and A-234.
{ECO:0000269|PubMed:11423119}.
MUTAGEN 232 232 R->A: Does not affect oxLDL binding.
Impairs oxLDL binding; when associated
with A-205; A-206; A-225 and A-234.
{ECO:0000269|PubMed:11423119}.
MUTAGEN 244 244 R->A: Does not affect oxLDL binding.
Impairs oxLDL binding; when associated
with A-205; A-206; A-225 and A-232.
{ECO:0000269|PubMed:11423119}.
MUTAGEN 262 262 K->A: Impairs the binding to oxLDL.
{ECO:0000269|PubMed:11284714}.
MUTAGEN 263 263 K->A: Impairs the binding to oxLDL.
{ECO:0000269|PubMed:11284714}.
MUTAGEN 265 265 N->D: Impairs the binding to oxLDL.
{ECO:0000269|PubMed:11284714}.
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


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