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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) (Lectin-type oxidized LDL receptor 1) [Cleaved into: Oxidized low-density lipoprotein receptor 1, soluble form]

 OLR1_RAT                Reviewed;         364 AA.
O70156;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
22-NOV-2017, entry version 125.
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;
AltName: Full=Lectin-type oxidized LDL receptor 1;
Contains:
RecName: Full=Oxidized low-density lipoprotein receptor 1, soluble form;
Name=Olr1; Synonyms=Lox1, Oldlr1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=SHR; TISSUE=Kidney;
PubMed=9494115; DOI=10.1042/bj3301417;
Nagase M., Hirose S., Fujita T.;
"Unique repetitive sequence and unexpected regulation of expression of
rat endothelial receptor for oxidized low-density lipoprotein (LOX-
1).";
Biochem. J. 330:1417-1422(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=9837956; DOI=10.1074/jbc.273.50.33702;
Nagase M., Abe J., Takahashi K., Ando J., Hirose S., Fujita T.;
"Genomic organization and regulation of expression of the lectin-like
oxidized low-density lipoprotein receptor (LOX-1) gene.";
J. Biol. Chem. 273:33702-33707(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
FUNCTION.
PubMed=12538855; DOI=10.1073/pnas.0337528100;
Honjo M., Nakamura K., Yamashiro K., Kiryu J., Tanihara H.,
McEvoy L.M., Honda Y., Butcher E.C., Masaki T., Sawamura T.;
"Lectin-like oxidized LDL receptor-1 is a cell-adhesion molecule
involved in endotoxin-induced inflammation.";
Proc. Natl. Acad. Sci. U.S.A. 100:1274-1279(2003).
-!- 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:12538855,
ECO:0000269|PubMed:9837956}.
-!- 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:0000250}; Single-pass type II
membrane protein {ECO:0000250}. Membrane raft {ECO:0000250}.
Secreted {ECO:0000250}. Note=A secreted form also exists.
Localization to membrane rafts requires palmitoylation (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Predominantly expressed in lung and at lower
level in kidney. Expressed in macrophages but not in vascular
smooth muscle cells. {ECO:0000269|PubMed:9494115}.
-!- INDUCTION: By hypertension. Up-regulated by shear stress,
lipopolysaccharide and TNF-alpha in cultured vascular endothelial
cells. {ECO:0000269|PubMed:9494115, ECO:0000269|PubMed:9837956}.
-!- 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. {ECO:0000250}.
-!- DOMAIN: The Neck region contains 3 internal repeats that are only
found in rodents.
-!- PTM: N-glycosylated. {ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB005900; BAA25785.1; -; mRNA.
EMBL; AB018104; BAA35123.1; -; Genomic_DNA.
EMBL; BC097290; AAH97290.1; -; mRNA.
RefSeq; NP_579840.2; NM_133306.2.
UniGene; Rn.87449; -.
ProteinModelPortal; O70156; -.
SMR; O70156; -.
STRING; 10116.ENSRNOP00000011196; -.
PaxDb; O70156; -.
PRIDE; O70156; -.
GeneID; 140914; -.
KEGG; rno:140914; -.
UCSC; RGD:620515; rat.
CTD; 4973; -.
RGD; 620515; Olr1.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
HOGENOM; HOG000220927; -.
HOVERGEN; HBG056863; -.
InParanoid; O70156; -.
KO; K08763; -.
PhylomeDB; O70156; -.
TreeFam; TF336674; -.
PRO; PR:O70156; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
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:0043235; C:receptor complex; ISO:RGD.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0005041; F:low-density lipoprotein receptor activity; ISO:RGD.
GO; GO:0004872; F:receptor activity; TAS:RGD.
GO; GO:0008219; P:cell death; IMP:RGD.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IMP:RGD.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:RGD.
GO; GO:0042157; P:lipoprotein metabolic process; IMP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
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_sf.
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.
2: Evidence at transcript level;
Cell adhesion; Cell membrane; Coiled coil; Complete proteome;
Disulfide bond; Glycoprotein; Immunity; Inflammatory response; Lectin;
Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome;
Repeat; Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 364 Oxidized low-density lipoprotein receptor
1.
/FTId=PRO_0000017451.
CHAIN ? 364 Oxidized low-density lipoprotein receptor
1, soluble form.
/FTId=PRO_0000017452.
TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}.
TRANSMEM 32 54 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 55 364 Extracellular. {ECO:0000255}.
REPEAT 96 141 1.
REPEAT 142 187 2.
REPEAT 188 233 3.
DOMAIN 242 355 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
REGION 55 242 Neck.
COILED 83 233 {ECO:0000255}.
LIPID 35 35 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 45 45 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 235 246 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 262 354 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 333 346 {ECO:0000255|PROSITE-ProRule:PRU00040}.
SEQUENCE 364 AA; 41890 MW; 0AD2839C07206E09 CRC64;
MAFDDKMKPV NGQPDQKSCG KKPKGLHLLS STWWCPAAVT LAILCLVLSV TLIVQQTQLL
QVSDLLKQYQ ANLTQQDHIL EGQMSAQKKA ENASQESKRE LKEQIDTLTW KLNEKSKEQE
KLLQQNQNLQ EALQRAVNAS EESKWELKEQ IDILNWKLNG ISKEQKELLQ QNQNLQEALQ
KAEKYSEESQ RELKEQIDTL SWKLNEKSKE QEELLQQNQN LQEALQRAAN SSGPCPQDWI
WHKENCYLFH GPFNWEKSRE NCLSLDAQLL QISTTDDLNF VLQATSHSTS PFWMGLHRKN
PNHPWLWENG SPLSFQFFRT RGVSLQMYSS GTCAYIQGGV VFAENCILTA FSICQKKANL
LLTQ


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