OLR1_MOUSE
ID OLR1_MOUSE Reviewed; 363 AA.
AC Q9EQ09; Q3U3M1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9588202; DOI=10.1006/bbrc.1998.8526;
RA Hoshikawa H., Sawamura T., Kakutani M., Aoyama T., Nakamura T., Masaki T.;
RT "High affinity binding of oxidized LDL to mouse lectin-like oxidized LDL
RT receptor (LOX-1).";
RL Biochem. Biophys. Res. Commun. 245:841-846(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Park S.-H., Ahn H.-J., Cho J.-J.;
RT "Mouse LOX-1 is expressed in mast cells after IgE cross-linking.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 -!- DOMAIN: The Neck region contains 3 internal repeats that are only found
CC in rodents.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Oxidised LDL receptor;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_179";
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DR EMBL; AF303744; AAG44998.1; -; mRNA.
DR EMBL; AK154687; BAE32764.1; -; mRNA.
DR CCDS; CCDS20588.1; -.
DR PIR; JE0111; JE0111.
DR RefSeq; NP_619589.2; NM_138648.2.
DR AlphaFoldDB; Q9EQ09; -.
DR SMR; Q9EQ09; -.
DR STRING; 10090.ENSMUSP00000032265; -.
DR GlyGen; Q9EQ09; 2 sites.
DR PhosphoSitePlus; Q9EQ09; -.
DR MaxQB; Q9EQ09; -.
DR PaxDb; Q9EQ09; -.
DR PRIDE; Q9EQ09; -.
DR ProteomicsDB; 289988; -.
DR Antibodypedia; 11685; 672 antibodies from 41 providers.
DR DNASU; 108078; -.
DR Ensembl; ENSMUST00000032265; ENSMUSP00000032265; ENSMUSG00000030162.
DR GeneID; 108078; -.
DR KEGG; mmu:108078; -.
DR UCSC; uc009efw.2; mouse.
DR CTD; 4973; -.
DR MGI; MGI:1261434; Olr1.
DR VEuPathDB; HostDB:ENSMUSG00000030162; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161941; -.
DR HOGENOM; CLU_049894_4_0_1; -.
DR InParanoid; Q9EQ09; -.
DR OMA; HSSFPFW; -.
DR OrthoDB; 1201127at2759; -.
DR PhylomeDB; Q9EQ09; -.
DR TreeFam; TF336674; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 108078; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Olr1; mouse.
DR PRO; PR:Q9EQ09; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9EQ09; protein.
DR Bgee; ENSMUSG00000030162; Expressed in gastrula and 34 other tissues.
DR ExpressionAtlas; Q9EQ09; baseline and differential.
DR Genevisible; Q9EQ09; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; TAS:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IDA:MGI.
DR GO; GO:0008219; P:cell death; ISO:MGI.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
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..363
FT /note="Oxidized low-density lipoprotein receptor 1"
FT /id="PRO_0000017445"
FT CHAIN ?..363
FT /note="Oxidized low-density lipoprotein receptor 1, soluble
FT form"
FT /id="PRO_0000017446"
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..363
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..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..241
FT /note="Neck"
FT COILED 57..232
FT /evidence="ECO:0000255"
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 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"
FT CONFLICT 93
FT /note="T -> A (in Ref. 1; AAG44998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 41643 MW; 8F370C86B58F11A8 CRC64;
MTFDDKMKPA NDEPDQKSCG KKPKGLHLLS SPWWFPAAMT LVILCLVLSV TLIVQWTQLR
QVSDLLKQYQ ANLTQQDRIL EGQMLAQQKA ENTSQESKKE LKGKIDTLTQ KLNEKSKEQE
ELLQKNQNLQ EALQRAANSS EESQRELKGK IDTITRKLDE KSKEQEELLQ MIQNLQEALQ
RAANSSEESQ RELKGKIDTL TLKLNEKSKE QEELLQKNQN LQEALQRAAN FSGPCPQDWL
WHKENCYLFH GPFSWEKNRQ TCQSLGGQLL QINGADDLTF ILQAISHTTS PFWIGLHRKK
PGQPWLWENG TPLNFQFFKT RGVSLQLYSS GNCAYLQDGA VFAENCILIA FSICQKKTNH
LQI
