OLR1_PIG
ID OLR1_PIG Reviewed; 274 AA.
AC Q9TTK7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 106.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
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 -!- 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}.
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DR EMBL; AB018668; BAA88894.1; -; mRNA.
DR RefSeq; NP_998970.1; NM_213805.1.
DR AlphaFoldDB; Q9TTK7; -.
DR SMR; Q9TTK7; -.
DR STRING; 9823.ENSSSCP00000000683; -.
DR PaxDb; Q9TTK7; -.
DR PRIDE; Q9TTK7; -.
DR Ensembl; ENSSSCT00005066676; ENSSSCP00005041351; ENSSSCG00005041517.
DR Ensembl; ENSSSCT00030092381; ENSSSCP00030042506; ENSSSCG00030066071.
DR Ensembl; ENSSSCT00045051623; ENSSSCP00045035909; ENSSSCG00045030240.
DR Ensembl; ENSSSCT00060005911; ENSSSCP00060002006; ENSSSCG00060004754.
DR Ensembl; ENSSSCT00065093185; ENSSSCP00065040781; ENSSSCG00065067860.
DR GeneID; 396724; -.
DR KEGG; ssc:396724; -.
DR CTD; 4973; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q9TTK7; -.
DR OrthoDB; 1201127at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:AgBase.
DR GO; GO:0042310; P:vasoconstriction; IMP: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 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_0000017447"
FT CHAIN ?..274
FT /note="Oxidized low-density lipoprotein receptor 1, soluble
FT form"
FT /id="PRO_0000017448"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..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..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..150
FT /note="Neck"
FT COILED 89..142
FT /evidence="ECO:0000255"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 46
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
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; 31143 MW; D141776C79FB42E0 CRC64;
MTLDDLKSNS MKDQPDEKSN GDKAEGPRSL STLRWRPAAL ILGLLCLGLL VTVILLIIQL
SQVSDLLKQQ KVKLTHQEDI LEGQALAQRQ AEKSSQESQR ELTEMIETLA HKLDEKSKKL
MELQQQNLNL QKALEKAANF SGPCPQDWLW HEENCYKFSS GPFSWEKSRE NCLSLDAQLL
KINSTDDLEF IQQTIAHSSF PFWMGLSLRK PNNSWLWEDG TPLMPHLFRL QGAASQMYPS
GTCAYIHRGI VFAENCILNA FSICQKRANL LRAQ
