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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_MOUSE              Reviewed;         363 AA.
Q9EQ09; Q3U3M1;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 129.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9588202; DOI=10.1006/bbrc.1998.8526;
Hoshikawa H., Sawamura T., Kakutani M., Aoyama T., Nakamura T.,
Masaki T.;
"High affinity binding of oxidized LDL to mouse lectin-like oxidized
LDL receptor (LOX-1).";
Biochem. Biophys. Res. Commun. 245:841-846(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Park S.-H., Ahn H.-J., Cho J.-J.;
"Mouse LOX-1 is expressed in mast cells after IgE cross-linking.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
-!- 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 (By similarity). {ECO:0000250}.
-!- 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}.
-!- 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}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Oxidised LDL receptor;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_179";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF303744; AAG44998.1; -; mRNA.
EMBL; AK154687; BAE32764.1; -; mRNA.
CCDS; CCDS20588.1; -.
PIR; JE0111; JE0111.
RefSeq; NP_619589.2; NM_138648.2.
UniGene; Mm.293626; -.
ProteinModelPortal; Q9EQ09; -.
SMR; Q9EQ09; -.
STRING; 10090.ENSMUSP00000032265; -.
MaxQB; Q9EQ09; -.
PaxDb; Q9EQ09; -.
PRIDE; Q9EQ09; -.
DNASU; 108078; -.
Ensembl; ENSMUST00000032265; ENSMUSP00000032265; ENSMUSG00000030162.
GeneID; 108078; -.
KEGG; mmu:108078; -.
UCSC; uc009efw.2; mouse.
CTD; 4973; -.
MGI; MGI:1261434; Olr1.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00700000104266; -.
HOGENOM; HOG000220927; -.
HOVERGEN; HBG056863; -.
InParanoid; Q9EQ09; -.
KO; K08763; -.
OMA; PSGTCAY; -.
OrthoDB; EOG091G0MM1; -.
TreeFam; TF336674; -.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:Q9EQ09; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030162; Expressed in 47 organ(s), highest expression level in placenta.
ExpressionAtlas; Q9EQ09; baseline and differential.
Genevisible; Q9EQ09; MM.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0019897; C:extrinsic component of plasma membrane; TAS:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IDA:MGI.
GO; GO:0008219; P:cell death; ISO:MGI.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; ISO:MGI.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
GO; GO:0042157; P:lipoprotein metabolic process; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
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 1 363 Oxidized low-density lipoprotein receptor
1.
/FTId=PRO_0000017445.
CHAIN ? 363 Oxidized low-density lipoprotein receptor
1, soluble form.
/FTId=PRO_0000017446.
TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}.
TRANSMEM 32 54 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 55 363 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 55 241 Neck.
COILED 57 232 {ECO:0000255}.
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}.
DISULFID 235 246 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 262 354 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 333 346 {ECO:0000255|PROSITE-ProRule:PRU00040}.
CONFLICT 93 93 T -> A (in Ref. 1; AAG44998).
{ECO:0000305}.
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


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