OLR1_RABIT
ID OLR1_RABIT Reviewed; 274 AA.
AC Q9XTA8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 107.
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;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Placenta;
RX PubMed=10764681; DOI=10.1161/01.atv.20.4.1107;
RA Chen M., Kakutani M., Minami M., Kataoka H., Kume N., Narumiya S., Kita T.,
RA Masaki T., Sawamura T.;
RT "Increased expression of lectin-like oxidized low density lipoprotein
RT receptor-1 in initial atherosclerotic lesions of Watanabe heritable
RT hyperlipidemic rabbits.";
RL Arterioscler. Thromb. Vasc. Biol. 20:1107-1115(2000).
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 (By similarity). {ECO:0000250}.
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 -!- INDUCTION: Overexpressed in atherosclerotic lesions.
CC {ECO:0000269|PubMed:10764681}.
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 -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA81912.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB016237; BAA81912.1; ALT_INIT; mRNA.
DR RefSeq; NP_001076102.1; NM_001082633.1.
DR AlphaFoldDB; Q9XTA8; -.
DR SMR; Q9XTA8; -.
DR PRIDE; Q9XTA8; -.
DR GeneID; 100009322; -.
DR KEGG; ocu:100009322; -.
DR CTD; 4973; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q9XTA8; -.
DR OrthoDB; 1201127at2759; -.
DR Proteomes; UP000001811; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
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; IPR013600; Ly49_N.
DR InterPro; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF08391; Ly49; 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; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..274
FT /note="Oxidized low-density lipoprotein receptor 1"
FT /id="PRO_0000017449"
FT CHAIN ?..274
FT /note="Oxidized low-density lipoprotein receptor 1, soluble
FT form"
FT /id="PRO_0000017450"
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..274
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..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..150
FT /note="Neck"
FT COILED 84..139
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 36
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 46
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 144..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 172..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 243..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 274 AA; 31159 MW; 9BE37B1122A67F8B CRC64;
MAVDDLKVKP MKDQPDQKSN GKKPKGLRFL SSPWWCPAAV ALGVLCLGSL MTIIMLGMQL
LQVSDLLKQQ QANLTLQENI LEGQVLAQQQ AEAASQESQR ELKEMIETLA KRLDEKSKKQ
MELNHQYLNL QEALKRMDNF SGPCPEDWLW HGKNCYLFSS GSFNWESSQE KCLSLDAQLL
KINSTEDLGF IQQATSHSSF PFWMGLSRRK PDYSWLWEDG SPLMPHLFRF QGAVSQRYPS
GTCAYIQKGN VFAENCILVA YSICQKKANL LRSE
