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Q9EQ09 (OLR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxidized low-density lipoprotein receptor 1

Short name=Ox-LDL receptor 1
Alternative name(s):
Lectin-like oxidized LDL receptor 1
Short name=LOX-1
Short name=Lectin-like oxLDL receptor 1
Lectin-type oxidized LDL receptor 1
Gene names
Name:Olr1
Synonyms:Lox1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Subunit structure

Homodimer; disulfide-linked. May form a hexamer composed of 3 homodimers. Interacts with HSP70 By similarity.

Subcellular location

Cell membrane; Lipid-anchor By similarity. Cell membrane; Single-pass type II membrane protein By similarity. Membrane raft By similarity. Secreted By similarity. Note: A secreted form also exists. Localization to membrane rafts requires palmitoylation By similarity.

Domain

The cytoplasmic region is required for subcellular sorting on the cell surface By similarity.

The C-type lectin domain mediates the recognition and binding of oxLDL By similarity.

The Neck region contains 3 internal repeats that are only found in rodents.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Contains 1 C-type lectin domain.

Ontologies

Keywords
   Biological processCell adhesion
Immunity
Inflammatory response
   Cellular componentCell membrane
Membrane
Secreted
   DomainCoiled coil
Repeat
Signal-anchor
Transmembrane
Transmembrane helix
   LigandLectin
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: Ensembl

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

leukocyte cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

lipoprotein metabolic process

Inferred from electronic annotation. Source: Ensembl

receptor-mediated endocytosis

Inferred from direct assay Ref.1. Source: GOC

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of plasma membrane

Traceable author statement Ref.1. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

low-density lipoprotein receptor activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363Oxidized low-density lipoprotein receptor 1
PRO_0000017445
Chain? – 363Oxidized low-density lipoprotein receptor 1, soluble formPRO_0000017446

Regions

Topological domain1 – 3131Cytoplasmic Potential
Transmembrane32 – 5423Helical; Signal-anchor for type II membrane protein; Potential
Topological domain55 – 363309Extracellular Potential
Repeat96 – 141461
Repeat142 – 187462
Repeat188 – 233463
Domain242 – 355114C-type lectin
Region55 – 241187Neck
Coiled coil57 – 232176 Potential

Amino acid modifications

Lipidation451S-palmitoyl cysteine By similarity
Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation921N-linked (GlcNAc...) Potential
Disulfide bond235 ↔ 246 By similarity
Disulfide bond262 ↔ 354 By similarity
Disulfide bond333 ↔ 346 By similarity

Experimental info

Sequence conflict931T → A in AAG44998. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9EQ09 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 8F370C86B58F11A8

FASTA36341,643
        10         20         30         40         50         60 
MTFDDKMKPA NDEPDQKSCG KKPKGLHLLS SPWWFPAAMT LVILCLVLSV TLIVQWTQLR 

        70         80         90        100        110        120 
QVSDLLKQYQ ANLTQQDRIL EGQMLAQQKA ENTSQESKKE LKGKIDTLTQ KLNEKSKEQE 

       130        140        150        160        170        180 
ELLQKNQNLQ EALQRAANSS EESQRELKGK IDTITRKLDE KSKEQEELLQ MIQNLQEALQ 

       190        200        210        220        230        240 
RAANSSEESQ RELKGKIDTL TLKLNEKSKE QEELLQKNQN LQEALQRAAN FSGPCPQDWL 

       250        260        270        280        290        300 
WHKENCYLFH GPFSWEKNRQ TCQSLGGQLL QINGADDLTF ILQAISHTTS PFWIGLHRKK 

       310        320        330        340        350        360 
PGQPWLWENG TPLNFQFFKT RGVSLQLYSS GNCAYLQDGA VFAENCILIA FSICQKKTNH 


LQI 

« Hide

References

« Hide 'large scale' references
[1]"High affinity binding of oxidized LDL to mouse lectin-like oxidized LDL receptor (LOX-1)."
Hoshikawa H., Sawamura T., Kakutani M., Aoyama T., Nakamura T., Masaki T.
Biochem. Biophys. Res. Commun. 245:841-846(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Mouse LOX-1 is expressed in mast cells after IgE cross-linking."
Park S.-H., Ahn H.-J., Cho J.-J.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF303744 mRNA. Translation: AAG44998.1.
AK154687 mRNA. Translation: BAE32764.1.
PIRJE0111.
RefSeqNP_619589.2. NM_138648.2.
UniGeneMm.293626.

3D structure databases

ProteinModelPortalQ9EQ09.
SMRQ9EQ09. Positions 61-87, 216-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000032265.

Proteomic databases

PaxDbQ9EQ09.
PRIDEQ9EQ09.

Protocols and materials databases

DNASU108078.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032265; ENSMUSP00000032265; ENSMUSG00000030162.
GeneID108078.
KEGGmmu:108078.
UCSCuc009efw.2. mouse.

Organism-specific databases

CTD4973.
MGIMGI:1261434. Olr1.

Phylogenomic databases

eggNOGNOG242244.
GeneTreeENSGT00700000104266.
HOGENOMHOG000220927.
HOVERGENHBG056863.
InParanoidQ3U3M1.
KOK08763.
OMASICQKKA.
OrthoDBEOG747PJT.
TreeFamTF336674.

Gene expression databases

ArrayExpressQ9EQ09.
BgeeQ9EQ09.
GenevestigatorQ9EQ09.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio360012.
PROQ9EQ09.
SOURCESearch...

Entry information

Entry nameOLR1_MOUSE
AccessionPrimary (citable) accession number: Q9EQ09
Secondary accession number(s): Q3U3M1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot