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Q9EQ09

- OLR1_MOUSE

UniProt

Q9EQ09 - OLR1_MOUSE

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Protein
Oxidized low-density lipoprotein receptor 1
Gene
Olr1, Lox1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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.

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. low-density lipoprotein receptor activity Source: MGI

GO - Biological processi

  1. cell death Source: Ensembl
  2. immune system process Source: UniProtKB-KW
  3. inflammatory response Source: UniProtKB-KW
  4. leukocyte cell-cell adhesion Source: Ensembl
  5. lipoprotein metabolic process Source: Ensembl
  6. receptor-mediated endocytosis Source: GOC
  7. response to hydrogen peroxide Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion, Immunity, Inflammatory response

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiREACT_225233. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following chain:
Gene namesi
Name:Olr1
Synonyms:Lox1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1261434. Olr1.

Subcellular locationi

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3131Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei32 – 5423Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini55 – 363309Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. extrinsic component of plasma membrane Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane raft Source: UniProtKB-SubCell
  5. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 363Oxidized low-density lipoprotein receptor 1, soluble formPRO_0000017446
Chaini1 – 363363Oxidized low-density lipoprotein receptor 1
PRO_0000017445Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi45 – 451S-palmitoyl cysteine By similarity
Glycosylationi72 – 721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi92 – 921N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi235 ↔ 246 By similarity
Disulfide bondi262 ↔ 354 By similarity
Disulfide bondi333 ↔ 346 By similarity

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PaxDbiQ9EQ09.
PRIDEiQ9EQ09.

Expressioni

Gene expression databases

ArrayExpressiQ9EQ09.
BgeeiQ9EQ09.
GenevestigatoriQ9EQ09.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032265.

Structurei

3D structure databases

ProteinModelPortaliQ9EQ09.
SMRiQ9EQ09. Positions 216-359.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati96 – 141461
Add
BLAST
Repeati142 – 187462
Add
BLAST
Repeati188 – 233463
Add
BLAST
Domaini242 – 355114C-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 241187Neck
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili57 – 232176 Reviewed prediction
Add
BLAST

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG242244.
GeneTreeiENSGT00700000104266.
HOGENOMiHOG000220927.
HOVERGENiHBG056863.
InParanoidiQ3U3M1.
KOiK08763.
OMAiSICQKKA.
OrthoDBiEOG747PJT.
TreeFamiTF336674.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9EQ09-1 [UniParc]FASTAAdd to Basket

« Hide

MTFDDKMKPA NDEPDQKSCG KKPKGLHLLS SPWWFPAAMT LVILCLVLSV    50
TLIVQWTQLR QVSDLLKQYQ ANLTQQDRIL EGQMLAQQKA ENTSQESKKE 100
LKGKIDTLTQ KLNEKSKEQE ELLQKNQNLQ EALQRAANSS EESQRELKGK 150
IDTITRKLDE KSKEQEELLQ MIQNLQEALQ RAANSSEESQ RELKGKIDTL 200
TLKLNEKSKE QEELLQKNQN LQEALQRAAN FSGPCPQDWL WHKENCYLFH 250
GPFSWEKNRQ TCQSLGGQLL QINGADDLTF ILQAISHTTS PFWIGLHRKK 300
PGQPWLWENG TPLNFQFFKT RGVSLQLYSS GNCAYLQDGA VFAENCILIA 350
FSICQKKTNH LQI 363
Length:363
Mass (Da):41,643
Last modified:July 27, 2011 - v2
Checksum:i8F370C86B58F11A8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931T → A in AAG44998. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF303744 mRNA. Translation: AAG44998.1.
AK154687 mRNA. Translation: BAE32764.1.
CCDSiCCDS20588.1.
PIRiJE0111.
RefSeqiNP_619589.2. NM_138648.2.
UniGeneiMm.293626.

Genome annotation databases

EnsembliENSMUST00000032265; ENSMUSP00000032265; ENSMUSG00000030162.
GeneIDi108078.
KEGGimmu:108078.
UCSCiuc009efw.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Oxidised LDL receptor

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF303744 mRNA. Translation: AAG44998.1 .
AK154687 mRNA. Translation: BAE32764.1 .
CCDSi CCDS20588.1.
PIRi JE0111.
RefSeqi NP_619589.2. NM_138648.2.
UniGenei Mm.293626.

3D structure databases

ProteinModelPortali Q9EQ09.
SMRi Q9EQ09. Positions 216-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000032265.

Proteomic databases

PaxDbi Q9EQ09.
PRIDEi Q9EQ09.

Protocols and materials databases

DNASUi 108078.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032265 ; ENSMUSP00000032265 ; ENSMUSG00000030162 .
GeneIDi 108078.
KEGGi mmu:108078.
UCSCi uc009efw.2. mouse.

Organism-specific databases

CTDi 4973.
MGIi MGI:1261434. Olr1.

Phylogenomic databases

eggNOGi NOG242244.
GeneTreei ENSGT00700000104266.
HOGENOMi HOG000220927.
HOVERGENi HBG056863.
InParanoidi Q3U3M1.
KOi K08763.
OMAi SICQKKA.
OrthoDBi EOG747PJT.
TreeFami TF336674.

Enzyme and pathway databases

Reactomei REACT_225233. Cell surface interactions at the vascular wall.

Miscellaneous databases

NextBioi 360012.
PROi Q9EQ09.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9EQ09.
Bgeei Q9EQ09.
Genevestigatori Q9EQ09.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view ]
Pfami PF00059. Lectin_C. 1 hit.
[Graphical view ]
SMARTi SM00034. CLECT. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
PROSITEi PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiOLR1_MOUSE
AccessioniPrimary (citable) accession number: Q9EQ09
Secondary accession number(s): Q3U3M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi