OLR1_RAT
ID OLR1_RAT Reviewed; 364 AA.
AC O70156;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 139.
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 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=Lox1, Oldlr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=SHR; TISSUE=Kidney;
RX PubMed=9494115; DOI=10.1042/bj3301417;
RA Nagase M., Hirose S., Fujita T.;
RT "Unique repetitive sequence and unexpected regulation of expression of rat
RT endothelial receptor for oxidized low-density lipoprotein (LOX-1).";
RL Biochem. J. 330:1417-1422(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9837956; DOI=10.1074/jbc.273.50.33702;
RA Nagase M., Abe J., Takahashi K., Ando J., Hirose S., Fujita T.;
RT "Genomic organization and regulation of expression of the lectin-like
RT oxidized low-density lipoprotein receptor (LOX-1) gene.";
RL J. Biol. Chem. 273:33702-33707(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION.
RX PubMed=12538855; DOI=10.1073/pnas.0337528100;
RA Honjo M., Nakamura K., Yamashiro K., Kiryu J., Tanihara H., McEvoy L.M.,
RA Honda Y., Butcher E.C., Masaki T., Sawamura T.;
RT "Lectin-like oxidized LDL receptor-1 is a cell-adhesion molecule involved
RT in endotoxin-induced inflammation.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1274-1279(2003).
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:12538855,
CC ECO:0000269|PubMed:9837956}.
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:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}. Membrane raft {ECO:0000250}. Secreted
CC {ECO:0000250}. Note=A secreted form also exists. Localization to
CC membrane rafts requires palmitoylation (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in lung and at lower level
CC in kidney. Expressed in macrophages but not in vascular smooth muscle
CC cells. {ECO:0000269|PubMed:9494115}.
CC -!- INDUCTION: By hypertension. Up-regulated by shear stress,
CC lipopolysaccharide and TNF-alpha in cultured vascular endothelial
CC cells. {ECO:0000269|PubMed:9494115, ECO:0000269|PubMed:9837956}.
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. {ECO:0000250}.
CC -!- DOMAIN: The Neck region contains 3 internal repeats that are only found
CC in rodents.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; AB005900; BAA25785.1; -; mRNA.
DR EMBL; AB018104; BAA35123.1; -; Genomic_DNA.
DR EMBL; BC097290; AAH97290.1; -; mRNA.
DR RefSeq; NP_579840.2; NM_133306.2.
DR AlphaFoldDB; O70156; -.
DR SMR; O70156; -.
DR STRING; 10116.ENSRNOP00000011196; -.
DR GlyGen; O70156; 3 sites.
DR PhosphoSitePlus; O70156; -.
DR jPOST; O70156; -.
DR PaxDb; O70156; -.
DR PRIDE; O70156; -.
DR GeneID; 140914; -.
DR KEGG; rno:140914; -.
DR UCSC; RGD:620515; rat.
DR CTD; 4973; -.
DR RGD; 620515; Olr1.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; O70156; -.
DR OrthoDB; 1201127at2759; -.
DR PhylomeDB; O70156; -.
DR TreeFam; TF336674; -.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:O70156; -.
DR Proteomes; UP000002494; 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; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; ISO:RGD.
DR GO; GO:0008219; P:cell death; IMP:RGD.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IMP:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
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 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Coiled coil; Disulfide bond; Glycoprotein;
KW Immunity; Inflammatory response; Lectin; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Repeat; Secreted; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..364
FT /note="Oxidized low-density lipoprotein receptor 1"
FT /id="PRO_0000017451"
FT CHAIN ?..364
FT /note="Oxidized low-density lipoprotein receptor 1, soluble
FT form"
FT /id="PRO_0000017452"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..364
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REPEAT 96..141
FT /note="1"
FT REPEAT 142..187
FT /note="2"
FT REPEAT 188..233
FT /note="3"
FT DOMAIN 242..355
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..242
FT /note="Neck"
FT COILED 83..233
FT /evidence="ECO:0000255"
FT LIPID 35
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 45
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 235..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 262..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 333..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ 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
