SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14114

- LRP8_HUMAN

UniProt

Q14114 - LRP8_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Low-density lipoprotein receptor-related protein 8
Gene
LRP8, APOER2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor.3 Publications

GO - Molecular functioni

  1. apolipoprotein binding Source: BHF-UCL
  2. calcium ion binding Source: InterPro
  3. high-density lipoprotein particle binding Source: Ensembl
  4. protein binding Source: IntAct
  5. reelin receptor activity Source: BHF-UCL
  6. transmembrane signaling receptor activity Source: ProtInc
  7. very-low-density lipoprotein particle receptor activity Source: BHF-UCL

GO - Biological processi

  1. ammon gyrus development Source: BHF-UCL
  2. blood coagulation Source: Reactome
  3. cellular response to cholesterol Source: Ensembl
  4. cellular response to growth factor stimulus Source: Ensembl
  5. cytokine-mediated signaling pathway Source: UniProtKB
  6. endocytosis Source: UniProtKB
  7. layer formation in cerebral cortex Source: Ensembl
  8. lipid metabolic process Source: UniProtKB
  9. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  10. phototransduction, visible light Source: Reactome
  11. positive regulation of CREB transcription factor activity Source: BHF-UCL
  12. positive regulation of dendrite development Source: BHF-UCL
  13. positive regulation of dendritic spine morphogenesis Source: BHF-UCL
  14. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  15. positive regulation of protein tyrosine kinase activity Source: BHF-UCL
  16. proteolysis Source: UniProtKB
  17. receptor-mediated endocytosis Source: GOC
  18. reelin-mediated signaling pathway Source: BHF-UCL
  19. regulation of synaptic transmission Source: BHF-UCL
  20. response to drug Source: Ensembl
  21. retinoid metabolic process Source: Reactome
  22. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_23879. Platelet sensitization by LDL.
REACT_24968. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 8
Short name:
LRP-8
Alternative name(s):
Apolipoprotein E receptor 2
Gene namesi
Name:LRP8
Synonyms:APOER2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6700. LRP8.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein By similarity. Secreted By similarity
Note: Isoforms that contain the exon coding for a furin-type cleavage site are proteolytically processed, leading to a secreted receptor fragment By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 826785Extracellular Reviewed prediction
Add
BLAST
Transmembranei827 – 84721Helical; Reviewed prediction
Add
BLAST
Topological domaini848 – 963116Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. caveola Source: BHF-UCL
  2. dendrite Source: Ensembl
  3. extracellular region Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB
  5. microtubule associated complex Source: Ensembl
  6. neuronal cell body Source: Ensembl
  7. plasma membrane Source: Reactome
  8. postsynaptic density Source: Ensembl
  9. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Myocardial infarction 1 (MCI1) [MIM:608446]: A condition defined by the irreversible necrosis of heart muscle secondary to prolonged ischemia.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi608446. phenotype.
PharmGKBiPA30457.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232 Reviewed prediction
Add
BLAST
Chaini33 – 963931Low-density lipoprotein receptor-related protein 8
PRO_0000017332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 ↔ 59 By similarity
Disulfide bondi54 ↔ 72 By similarity
Disulfide bondi66 ↔ 81 By similarity
Disulfide bondi86 ↔ 98 By similarity
Disulfide bondi93 ↔ 111 By similarity
Disulfide bondi105 ↔ 122 By similarity
Disulfide bondi127 ↔ 141 By similarity
Disulfide bondi134 ↔ 154 By similarity
Disulfide bondi148 ↔ 163 By similarity
Disulfide bondi167 ↔ 179 By similarity
Disulfide bondi174 ↔ 192 By similarity
Glycosylationi176 – 1761N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi186 ↔ 201 By similarity
Disulfide bondi206 ↔ 221 By similarity
Disulfide bondi213 ↔ 234 By similarity
Disulfide bondi228 ↔ 245 By similarity
Disulfide bondi259 ↔ 272 By similarity
Disulfide bondi267 ↔ 285 By similarity
Disulfide bondi279 ↔ 294 By similarity
Disulfide bondi299 ↔ 311 By similarity
Disulfide bondi306 ↔ 324 By similarity
Disulfide bondi318 ↔ 333 By similarity
Disulfide bondi340 ↔ 351 By similarity
Disulfide bondi347 ↔ 360 By similarity
Disulfide bondi362 ↔ 374 By similarity
Disulfide bondi380 ↔ 390 By similarity
Disulfide bondi386 ↔ 399 By similarity
Disulfide bondi401 ↔ 414 By similarity
Glycosylationi441 – 4411N-linked (GlcNAc...) Reviewed prediction
Glycosylationi518 – 5181N-linked (GlcNAc...) Reviewed prediction
Glycosylationi538 – 5381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi772 – 7721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi807 – 8071N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain By similarity.
Undergoes sequential, furin and gamma-secretase dependent, proteolytic processing, resulting in the extracellular release of the entire ligand-binding domain as a soluble polypeptide and in the intracellular domain (ICD) release into the cytoplasm. The gamma-secretase-dependent proteolytical processing occurs after the bulk of the extracellular domain has been shed, in a furin-dependent manner, in alternatively spliced isoforms carrying the furin cleavage site. Hypoglycosylation (mainly hypo-O-glycosylation) leads to increased extracellular cleavage, which in turn results in accelerating release of the intracellular domain (ICD) by the gamma-secretase. The resulting receptor fragment is able to inhibit Reelin signaling and in particular the Reelin-induced DAB1 phosphorylation By similarity.
Tyrosine phosphorylated upon apoE binding.1 Publication
Ubiquitinated by MYLIP leading to degradation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14114.
PaxDbiQ14114.
PRIDEiQ14114.

PTM databases

PhosphoSiteiQ14114.

Miscellaneous databases

PMAP-CutDBB1AMT8.

Expressioni

Tissue specificityi

Expressed mainly in brain and placenta. Also expressed in platelets and megakaryocytic cells. Not expressed in the liver.2 Publications

Gene expression databases

ArrayExpressiQ14114.
BgeeiQ14114.
CleanExiHS_LRP8.
GenevestigatoriQ14114.

Interactioni

Subunit structurei

Reelin associates with two or more receptor molecules. Interacts with DAB1 and JNK-interacting proteins. Interacts with SNX17 By similarity. Interacts with PCSK9.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
APOEP026492EBI-2681187,EBI-1222467

Protein-protein interaction databases

BioGridi113579. 18 interactions.
DIPiDIP-48670N.
IntActiQ14114. 2 interactions.
STRINGi9606.ENSP00000303634.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 533
Beta strandi59 – 613
Helixi62 – 643
Beta strandi67 – 693
Beta strandi72 – 754
Turni76 – 783

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A7QX-ray2.60B42-83[»]
ProteinModelPortaliQ14114.
SMRiQ14114. Positions 44-734.

Miscellaneous databases

EvolutionaryTraceiQ14114.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 8237LDL-receptor class A 1
Add
BLAST
Domaini85 – 12339LDL-receptor class A 2
Add
BLAST
Domaini126 – 16439LDL-receptor class A 3
Add
BLAST
Domaini166 – 20237LDL-receptor class A 4
Add
BLAST
Domaini205 – 24642LDL-receptor class A 5
Add
BLAST
Domaini258 – 29538LDL-receptor class A 6
Add
BLAST
Domaini298 – 33437LDL-receptor class A 7
Add
BLAST
Domaini336 – 37540EGF-like 1
Add
BLAST
Domaini376 – 41540EGF-like 2; calcium-binding Reviewed prediction
Add
BLAST
Repeati462 – 50847LDL-receptor class B 1
Add
BLAST
Repeati509 – 55143LDL-receptor class B 2
Add
BLAST
Repeati552 – 59544LDL-receptor class B 3
Add
BLAST
Repeati596 – 63944LDL-receptor class B 4
Add
BLAST
Repeati640 – 68142LDL-receptor class B 5
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni740 – 79859Clustered O-linked oligosaccharides
Add
BLAST

Domaini

The cytoplasmic domain is involved in the binding of DAB1 and in the recruitment of JNK-interacting proteins. Isoforms, which lack part of the cytoplasmic domain, are unable to recruit members of the family of JNK interacting proteins (JIP) to the cytoplasmic tail By similarity.

Sequence similaritiesi

Belongs to the LDLR family.
Contains 2 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG255913.
HOVERGENiHBG006250.
InParanoidiQ14114.
OMAiGCLQEST.
OrthoDBiEOG7NGQ9P.
PhylomeDBiQ14114.
TreeFamiTF351700.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
4.10.400.10. 7 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 7 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00192. LDLa. 7 hits.
SM00135. LY. 5 hits.
[Graphical view]
SUPFAMiSSF57424. SSF57424. 7 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS01209. LDLRA_1. 7 hits.
PS50068. LDLRA_2. 7 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist. No differences were observed in the pattern splicing between control and Alzheimer brains.

Isoform 1 (identifier: Q14114-1) [UniParc]FASTAAdd to Basket

Also known as: ApoER2 922

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGLPEPGPLR LLALLLLLLL LLLLQLQHLA AAAADPLLGG QGPAKDCEKD    50
QFQCRNERCI PSVWRCDEDD DCLDHSDEDD CPKKTCADSD FTCDNGHCIH 100
ERWKCDGEEE CPDGSDESEA TCTKQVCPAE KLSCGPTSHK CVPASWRCDG 150
EKDCEGGADE AGCATLCAPH EFQCGNRSCL AAVFVCDGDD DCGDGSDERG 200
CADPACGPRE FRCGGDGGGA CIPERWVCDR QFDCEDRSDE AAELCGRPGP 250
GATSAPAACA TASQFACRSG ECVHLGWRCD GDRDCKDKSD EADCPLGTCR 300
GDEFQCGDGT CVLAIKHCNQ EQDCPDGSDE AGCLQGLNEC LHNNGGCSHI 350
CTDLKIGFEC TCPAGFQLLD QKTCGDIDEC KDPDACSQIC VNYKGYFKCE 400
CYPGYEMDLL TKNCKAAAGK SPSLIFTNRH EVRRIDLVKR NYSRLIPMLK 450
NVVALDVEVA TNRIYWCDLS YRKIYSAYMD KASDPKEQEV LIDEQLHSPE 500
GLAVDWVHKH IYWTDSGNKT ISVATVDGGR RRTLFSRNLS EPRAIAVDPL 550
RGFMYWSDWG DQAKIEKSGL NGVDRQTLVS DNIEWPNGIT LDLLSQRLYW 600
VDSKLHQLSS IDFSGGNRKT LISSTDFLSH PFGIAVFEDK VFWTDLENEA 650
IFSANRLNGL EISILAENLN NPHDIVIFHE LKQPRAPDAC ELSVQPNGGC 700
EYLCLPAPQI SSHSPKYTCA CPDTMWLGPD MKRCYRAPQS TSTTTLASTM 750
TRTVPATTRA PGTTVHRSTY QNHSTETPSL TAAVPSSVSV PRAPSISPST 800
LSPATSNHSQ HYANEDSKMG STVTAAVIGI IVPIVVIALL CMSGYLIWRN 850
WKRKNTKSMN FDNPVYRKTT EEEDEDELHI GRTAQIGHVY PAAISSFDRP 900
LWAEPCLGET REPEDPAPAL KELFVLPGEP RSQLHQLPKN PLSELPVVKS 950
KRVALSLEDD GLP 963
Length:963
Mass (Da):105,634
Last modified:September 22, 2009 - v4
Checksum:iB10DCF72F62DE71C
GO
Isoform 2 (identifier: Q14114-2) [UniParc]FASTAAdd to Basket

Also known as: ApoER2 906

The sequence of this isoform differs from the canonical sequence as follows:
     166-295: LCAPHEFQCG...KDKSDEADCP → S
     737-812: APQSTSTTTL...PATSNHSQHY → D
     893-951: Missing.

Show »
Length:700
Mass (Da):77,845
Checksum:iB996C9CAEC69C1E9
GO
Isoform 3 (identifier: Q14114-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     893-951: Missing.

Show »
Length:904
Mass (Da):99,092
Checksum:i043E708314261E3C
GO
Isoform 4 (identifier: Q14114-4) [UniParc]FASTAAdd to Basket

Also known as: ApoER2delta4-7

The sequence of this isoform differs from the canonical sequence as follows:
     166-166: L → W
     167-336: Missing.

Show »
Length:793
Mass (Da):87,959
Checksum:i1A414B09D40BA1BC
GO
Isoform 5 (identifier: Q14114-5)

Sequence is not available

Note: Contains an insert in the extracellular part which carries a furin cleavage site.

Length:
Mass (Da):

Sequence cautioni

The sequence CAA99509.1 differs from that shown. Reason: Frameshift at positions 430, 432 and 438.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251Q → R.4 Publications
Corresponds to variant rs4926972 [ dbSNP | Ensembl ].
VAR_046974
Natural varianti46 – 461D → E.5 Publications
Corresponds to variant rs3820198 [ dbSNP | Ensembl ].
VAR_018468
Natural varianti453 – 4531V → M.
Corresponds to variant rs5180 [ dbSNP | Ensembl ].
VAR_037624
Natural varianti466 – 4661W → C.
Corresponds to variant rs5181 [ dbSNP | Ensembl ].
VAR_037625
Natural varianti607 – 6071Q → R.
Corresponds to variant rs5172 [ dbSNP | Ensembl ].
VAR_037626
Natural varianti611 – 6111I → L.
Corresponds to variant rs5170 [ dbSNP | Ensembl ].
VAR_037627
Natural varianti653 – 6531S → T.
Corresponds to variant rs5171 [ dbSNP | Ensembl ].
VAR_037628
Natural varianti736 – 7361R → Q.
Corresponds to variant rs5172 [ dbSNP | Ensembl ].
VAR_059079
Natural varianti952 – 9521R → Q Associated with susceptibility to myocardial infarction type 1; increases activation of MAPK14 by oxidized low density lipoprotein. 2 Publications
Corresponds to variant rs5174 [ dbSNP | Ensembl ].
VAR_018469

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei166 – 295130LCAPH…EADCP → S in isoform 2.
VSP_010305Add
BLAST
Alternative sequencei166 – 1661L → W in isoform 4.
VSP_038181
Alternative sequencei167 – 336170Missing in isoform 4.
VSP_010306Add
BLAST
Alternative sequencei737 – 81276APQST…HSQHY → D in isoform 2.
VSP_010307Add
BLAST
Alternative sequencei893 – 95159Missing in isoform 2 and isoform 3.
VSP_010308Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621A → V in BAA09328. 1 Publication
Sequence conflicti262 – 2621A → V in BAA21824. 1 Publication
Sequence conflicti405 – 4051Y → C in CAA99509. 1 Publication
Sequence conflicti418 – 4181A → G in BAA09328. 1 Publication
Sequence conflicti418 – 4181A → G in BAA21824. 1 Publication
Sequence conflicti418 – 4181A → G in BAA21825. 1 Publication
Sequence conflicti430 – 4301H → Y in BAA09328. 1 Publication
Sequence conflicti430 – 4301H → Y in BAA21824. 1 Publication
Sequence conflicti430 – 4301H → Y in BAA21825. 1 Publication
Sequence conflicti430 – 4301H → Y in CAA99509. 1 Publication
Sequence conflicti488 – 4881Q → R in CAA99509. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50678 mRNA. Translation: BAA09328.1.
D86407 Genomic DNA. Translation: BAA21824.1.
D86407 Genomic DNA. Translation: BAA21825.1.
Z75190 mRNA. Translation: CAA99509.1. Frameshift.
AL606760, AL355483 Genomic DNA. Translation: CAI18908.1.
AL606760, AL355483 Genomic DNA. Translation: CAI18909.1.
AL355483, AL606760 Genomic DNA. Translation: CAI22782.1.
AL606760, AL355483 Genomic DNA. Translation: CAI18910.1.
AL355483, AL606760 Genomic DNA. Translation: CAI22780.1.
AL355483, AL606760 Genomic DNA. Translation: CAI22781.1.
BC006443 mRNA. Translation: AAH06443.1.
BC051836 mRNA. Translation: AAH51836.2.
CCDSiCCDS30720.1. [Q14114-3]
CCDS578.1. [Q14114-1]
CCDS579.1. [Q14114-2]
CCDS580.1. [Q14114-4]
RefSeqiNP_001018064.1. NM_001018054.2. [Q14114-3]
NP_004622.2. NM_004631.4. [Q14114-1]
NP_059992.3. NM_017522.4. [Q14114-2]
NP_150643.2. NM_033300.3. [Q14114-4]
UniGeneiHs.280387.

Genome annotation databases

EnsembliENST00000306052; ENSP00000303634; ENSG00000157193. [Q14114-1]
ENST00000347547; ENSP00000334522; ENSG00000157193. [Q14114-4]
ENST00000354412; ENSP00000346391; ENSG00000157193. [Q14114-2]
ENST00000371454; ENSP00000360509; ENSG00000157193. [Q14114-3]
GeneIDi7804.
KEGGihsa:7804.
UCSCiuc001cvi.2. human. [Q14114-1]
uc001cvj.2. human. [Q14114-3]
uc001cvk.2. human. [Q14114-4]
uc001cvl.2. human. [Q14114-2]

Polymorphism databases

DMDMi259016389.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50678 mRNA. Translation: BAA09328.1 .
D86407 Genomic DNA. Translation: BAA21824.1 .
D86407 Genomic DNA. Translation: BAA21825.1 .
Z75190 mRNA. Translation: CAA99509.1 . Frameshift.
AL606760 , AL355483 Genomic DNA. Translation: CAI18908.1 .
AL606760 , AL355483 Genomic DNA. Translation: CAI18909.1 .
AL355483 , AL606760 Genomic DNA. Translation: CAI22782.1 .
AL606760 , AL355483 Genomic DNA. Translation: CAI18910.1 .
AL355483 , AL606760 Genomic DNA. Translation: CAI22780.1 .
AL355483 , AL606760 Genomic DNA. Translation: CAI22781.1 .
BC006443 mRNA. Translation: AAH06443.1 .
BC051836 mRNA. Translation: AAH51836.2 .
CCDSi CCDS30720.1. [Q14114-3 ]
CCDS578.1. [Q14114-1 ]
CCDS579.1. [Q14114-2 ]
CCDS580.1. [Q14114-4 ]
RefSeqi NP_001018064.1. NM_001018054.2. [Q14114-3 ]
NP_004622.2. NM_004631.4. [Q14114-1 ]
NP_059992.3. NM_017522.4. [Q14114-2 ]
NP_150643.2. NM_033300.3. [Q14114-4 ]
UniGenei Hs.280387.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3A7Q X-ray 2.60 B 42-83 [» ]
ProteinModelPortali Q14114.
SMRi Q14114. Positions 44-734.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113579. 18 interactions.
DIPi DIP-48670N.
IntActi Q14114. 2 interactions.
STRINGi 9606.ENSP00000303634.

PTM databases

PhosphoSitei Q14114.

Polymorphism databases

DMDMi 259016389.

Proteomic databases

MaxQBi Q14114.
PaxDbi Q14114.
PRIDEi Q14114.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306052 ; ENSP00000303634 ; ENSG00000157193 . [Q14114-1 ]
ENST00000347547 ; ENSP00000334522 ; ENSG00000157193 . [Q14114-4 ]
ENST00000354412 ; ENSP00000346391 ; ENSG00000157193 . [Q14114-2 ]
ENST00000371454 ; ENSP00000360509 ; ENSG00000157193 . [Q14114-3 ]
GeneIDi 7804.
KEGGi hsa:7804.
UCSCi uc001cvi.2. human. [Q14114-1 ]
uc001cvj.2. human. [Q14114-3 ]
uc001cvk.2. human. [Q14114-4 ]
uc001cvl.2. human. [Q14114-2 ]

Organism-specific databases

CTDi 7804.
GeneCardsi GC01M053711.
HGNCi HGNC:6700. LRP8.
MIMi 602600. gene.
608446. phenotype.
neXtProti NX_Q14114.
PharmGKBi PA30457.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG255913.
HOVERGENi HBG006250.
InParanoidi Q14114.
OMAi GCLQEST.
OrthoDBi EOG7NGQ9P.
PhylomeDBi Q14114.
TreeFami TF351700.

Enzyme and pathway databases

Reactomei REACT_23879. Platelet sensitization by LDL.
REACT_24968. Retinoid metabolism and transport.

Miscellaneous databases

EvolutionaryTracei Q14114.
GeneWikii Low_density_lipoprotein_receptor-related_protein_8.
GenomeRNAii 7804.
NextBioi 30188.
PMAP-CutDB B1AMT8.
PROi Q14114.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14114.
Bgeei Q14114.
CleanExi HS_LRP8.
Genevestigatori Q14114.

Family and domain databases

Gene3Di 2.120.10.30. 1 hit.
4.10.400.10. 7 hits.
InterProi IPR011042. 6-blade_b-propeller_TolB-like.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view ]
Pfami PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 7 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view ]
PRINTSi PR00261. LDLRECEPTOR.
SMARTi SM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00192. LDLa. 7 hits.
SM00135. LY. 5 hits.
[Graphical view ]
SUPFAMi SSF57424. SSF57424. 7 hits.
PROSITEi PS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS01209. LDLRA_1. 7 hits.
PS50068. LDLRA_2. 7 hits.
PS51120. LDLRB. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human apolipoprotein E receptor 2. A novel lipoprotein receptor of the low density lipoprotein receptor family predominantly expressed in brain."
    Kim D.-H., Iijima H., Goto K., Sakai J., Ishii H., Kim H.-J., Suzuki H., Kondo H., Saeki S., Yamamoto T.
    J. Biol. Chem. 271:8373-8380(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-25 AND GLU-46.
    Tissue: Placenta.
  2. "Exon/intron organization, chromosome localization, alternative splicing, and transcription units of the human apolipoprotein E receptor 2 gene."
    Kim D.-H., Magoori K., Inoue T.R., Mao C.C., Kim H.-J., Suzuki H., Fujita T., Endo Y., Saeki S., Yamamoto T.T.
    J. Biol. Chem. 272:8498-8504(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 4), VARIANTS ARG-25 AND GLU-46.
    Tissue: Peripheral blood.
  3. "Identification of a novel exon in apolipoprotein E receptor 2 leading to alternatively spliced mRNAs found in cells of the vascular wall but not in neuronal tissue."
    Korschineck I., Ziegler S., Breuss J., Lang I., Lorenz M., Kaun C., Ambros P.F., Binder B.R.
    J. Biol. Chem. 276:13192-13197(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS ARG-25 AND GLU-46.
    Tissue: Umbilical vein.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 720-963 (ISOFORM 1), VARIANTS ARG-25 AND GLU-46.
    Tissue: Eye and Lung.
  6. "Expression and alternate splicing of apolipoprotein E receptor 2 in brain."
    Clatworthy A.E., Stockinger W., Christie R.H., Schneider W.J., Nimpf J., Hyman B.T., Rebeck G.W.
    Neuroscience 90:903-911(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  7. "Apolipoprotein E (apoE) isoforms differentially induce nitric oxide production in endothelial cells."
    Sacre S.M., Stannard A.K., Owen J.S.
    FEBS Lett. 540:181-187(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES.
  8. "Identification and characterization of LRP8 (apoER2) in human blood platelets."
    Riddell D.R., Vinogradov D.V., Stannard A.K., Chadwick N., Owen J.S.
    J. Lipid Res. 40:1925-1930(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
  9. "Differential binding of ligands to the apolipoprotein E receptor 2."
    Andersen O.M., Benhayon D., Curran T., Willnow T.E.
    Biochemistry 42:9355-9364(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A RECEPTOR FOR REELIN.
  10. "Domains of apoE required for binding to apoE receptor 2 and to phospholipids: implications for the functions of apoE in the brain."
    Li X., Kypreos K., Zanni E.E., Zannis V.
    Biochemistry 42:10406-10417(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A RECEPTOR FOR APOE.
  11. "Dimers of beta 2-glycoprotein I increase platelet deposition to collagen via interaction with phospholipids and the apolipoprotein E receptor 2'."
    Lutters B.C., Derksen R.H., Tekelenburg W.L., Lenting P.J., Arnout J., de Groot P.G.
    J. Biol. Chem. 278:33831-33838(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A RECEPTOR FOR BETA 2-GLYCOPROTEIN I.
  12. "The proprotein convertase PCSK9 induces the degradation of low density lipoprotein receptor (LDLR) and its closest family members VLDLR and ApoER2."
    Poirier S., Mayer G., Benjannet S., Bergeron E., Marcinkiewicz J., Nassoury N., Mayer H., Nimpf J., Prat A., Seidah N.G.
    J. Biol. Chem. 283:2363-2372(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCSK9.
  13. "The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2."
    Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V., Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D., Nimpf J., van Berkel T.J., Tontonoz P., Zelcer N.
    J. Biol. Chem. 285:19720-19726(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  14. "Low-density lipoprotein receptor-related protein 8 (apolipoprotein E receptor 2) gene polymorphisms in Alzheimer's disease."
    Ma S.L., Ng H.K., Baum L., Pang J.C., Chiu H.F., Woo J., Tang N.L., Lam L.C.
    Neurosci. Lett. 332:216-218(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLU-46 AND GLN-952.
  15. Cited for: VARIANT GLN-952, CHARACTERIZATION OF VARIANT GLN-952, ASSOCIATION WITH SUSCEPTIBILITY TO MYOCARDIAL INFARCTION TYPE 1.

Entry informationi

Entry nameiLRP8_HUMAN
AccessioniPrimary (citable) accession number: Q14114
Secondary accession number(s): B1AMT6
, B1AMT7, B1AMT8, O14968, Q86V27, Q99876, Q9BR78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: September 22, 2009
Last modified: September 3, 2014
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Natural isoforms of apoE (E2, E3, E4) have similar affinities for LRP8.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi