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Protein

Low-density lipoprotein receptor-related protein 8

Gene

LRP8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • apolipoprotein binding Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • high-density lipoprotein particle binding Source: Ensembl
  • low-density lipoprotein receptor activity Source: Reactome
  • reelin receptor activity Source: BHF-UCL
  • transmembrane signaling receptor activity Source: ProtInc
  • very-low-density lipoprotein particle receptor activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-HSA-432142. Platelet sensitization by LDL.
R-HSA-975634. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6700. LRP8.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini42 – 826ExtracellularSequence analysisAdd BLAST785
Transmembranei827 – 847HelicalSequence analysisAdd BLAST21
Topological domaini848 – 963CytoplasmicSequence analysisAdd BLAST116

GO - Cellular componenti

  • axon Source: Ensembl
  • caveola Source: BHF-UCL
  • dendrite Source: Ensembl
  • extracellular region Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • microtubule associated complex Source: Ensembl
  • neuronal cell body Source: Ensembl
  • plasma membrane Source: Reactome
  • postsynaptic density Source: Ensembl
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Myocardial infarction 1 (MCI1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition defined by the irreversible necrosis of heart muscle secondary to prolonged ischemia.
See also OMIM:608446

Organism-specific databases

DisGeNETi7804.
MalaCardsiLRP8.
MIMi608446. phenotype.
OpenTargetsiENSG00000157193.
PharmGKBiPA30457.

Polymorphism and mutation databases

BioMutaiLRP8.
DMDMi259016389.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Sequence analysisAdd BLAST32
ChainiPRO_000001733233 – 963Low-density lipoprotein receptor-related protein 8Add BLAST931

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi47 ↔ 59By similarity
Disulfide bondi54 ↔ 72By similarity
Disulfide bondi66 ↔ 81By similarity
Disulfide bondi86 ↔ 98By similarity
Disulfide bondi93 ↔ 111By similarity
Disulfide bondi105 ↔ 122By similarity
Disulfide bondi127 ↔ 141By similarity
Disulfide bondi134 ↔ 154By similarity
Disulfide bondi148 ↔ 163By similarity
Disulfide bondi167 ↔ 179By similarity
Disulfide bondi174 ↔ 192By similarity
Glycosylationi176N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi186 ↔ 201By similarity
Disulfide bondi206 ↔ 221By similarity
Disulfide bondi213 ↔ 234By similarity
Disulfide bondi228 ↔ 245By similarity
Disulfide bondi259 ↔ 272By similarity
Disulfide bondi267 ↔ 285By similarity
Disulfide bondi279 ↔ 294By similarity
Disulfide bondi299 ↔ 311By similarity
Disulfide bondi306 ↔ 324By similarity
Disulfide bondi318 ↔ 333By similarity
Disulfide bondi340 ↔ 351By similarity
Disulfide bondi347 ↔ 360By similarity
Disulfide bondi362 ↔ 374By similarity
Disulfide bondi380 ↔ 390By similarity
Disulfide bondi386 ↔ 399By similarity
Disulfide bondi401 ↔ 414By similarity
Glycosylationi441N-linked (GlcNAc...)Sequence analysis1
Glycosylationi518N-linked (GlcNAc...)Sequence analysis1
Glycosylationi538N-linked (GlcNAc...)Sequence analysis1
Glycosylationi772N-linked (GlcNAc...)Sequence analysis1
Glycosylationi807N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain (By similarity).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).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

EPDiQ14114.
PaxDbiQ14114.
PeptideAtlasiQ14114.
PRIDEiQ14114.

PTM databases

iPTMnetiQ14114.
PhosphoSitePlusiQ14114.
SwissPalmiQ14114.

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

BgeeiENSG00000157193.
CleanExiHS_LRP8.
ExpressionAtlasiQ14114. baseline and differential.
GenevisibleiQ14114. HS.

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.By similarity1 Publication

Binary interactionsi

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

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi113579. 35 interactors.
DIPiDIP-48670N.
IntActiQ14114. 18 interactors.
STRINGi9606.ENSP00000303634.

Structurei

Secondary structure

1963
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi51 – 53Combined sources3
Beta strandi59 – 61Combined sources3
Helixi62 – 64Combined sources3
Beta strandi67 – 69Combined sources3
Beta strandi72 – 75Combined sources4
Turni76 – 78Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A7QX-ray2.60B42-83[»]
ProteinModelPortaliQ14114.
SMRiQ14114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14114.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 82LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST37
Domaini85 – 123LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST39
Domaini126 – 164LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST39
Domaini166 – 202LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST37
Domaini205 – 246LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST42
Domaini258 – 295LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST38
Domaini298 – 334LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST37
Domaini336 – 375EGF-like 1PROSITE-ProRule annotationAdd BLAST40
Domaini376 – 415EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Repeati462 – 508LDL-receptor class B 1Add BLAST47
Repeati509 – 551LDL-receptor class B 2Add BLAST43
Repeati552 – 595LDL-receptor class B 3Add BLAST44
Repeati596 – 639LDL-receptor class B 4Add BLAST44
Repeati640 – 681LDL-receptor class B 5Add BLAST42

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni740 – 798Clustered O-linked oligosaccharidesAdd BLAST59

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).By similarity

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 7 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 5 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IPT5. Eukaryota.
ENOG410YQ6J. LUCA.
GeneTreeiENSGT00760000118968.
HOVERGENiHBG006250.
InParanoidiQ14114.
KOiK20052.
OMAiVCDSHRD.
OrthoDBiEOG091G01MX.
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.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
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]
PfamiPF00057. Ldl_recept_a. 7 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 2 hits.
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. AlignAdd to basket

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

        10         20         30         40         50
MGLPEPGPLR LLALLLLLLL LLLLQLQHLA AAAADPLLGG QGPAKDCEKD
60 70 80 90 100
QFQCRNERCI PSVWRCDEDD DCLDHSDEDD CPKKTCADSD FTCDNGHCIH
110 120 130 140 150
ERWKCDGEEE CPDGSDESEA TCTKQVCPAE KLSCGPTSHK CVPASWRCDG
160 170 180 190 200
EKDCEGGADE AGCATLCAPH EFQCGNRSCL AAVFVCDGDD DCGDGSDERG
210 220 230 240 250
CADPACGPRE FRCGGDGGGA CIPERWVCDR QFDCEDRSDE AAELCGRPGP
260 270 280 290 300
GATSAPAACA TASQFACRSG ECVHLGWRCD GDRDCKDKSD EADCPLGTCR
310 320 330 340 350
GDEFQCGDGT CVLAIKHCNQ EQDCPDGSDE AGCLQGLNEC LHNNGGCSHI
360 370 380 390 400
CTDLKIGFEC TCPAGFQLLD QKTCGDIDEC KDPDACSQIC VNYKGYFKCE
410 420 430 440 450
CYPGYEMDLL TKNCKAAAGK SPSLIFTNRH EVRRIDLVKR NYSRLIPMLK
460 470 480 490 500
NVVALDVEVA TNRIYWCDLS YRKIYSAYMD KASDPKEQEV LIDEQLHSPE
510 520 530 540 550
GLAVDWVHKH IYWTDSGNKT ISVATVDGGR RRTLFSRNLS EPRAIAVDPL
560 570 580 590 600
RGFMYWSDWG DQAKIEKSGL NGVDRQTLVS DNIEWPNGIT LDLLSQRLYW
610 620 630 640 650
VDSKLHQLSS IDFSGGNRKT LISSTDFLSH PFGIAVFEDK VFWTDLENEA
660 670 680 690 700
IFSANRLNGL EISILAENLN NPHDIVIFHE LKQPRAPDAC ELSVQPNGGC
710 720 730 740 750
EYLCLPAPQI SSHSPKYTCA CPDTMWLGPD MKRCYRAPQS TSTTTLASTM
760 770 780 790 800
TRTVPATTRA PGTTVHRSTY QNHSTETPSL TAAVPSSVSV PRAPSISPST
810 820 830 840 850
LSPATSNHSQ HYANEDSKMG STVTAAVIGI IVPIVVIALL CMSGYLIWRN
860 870 880 890 900
WKRKNTKSMN FDNPVYRKTT EEEDEDELHI GRTAQIGHVY PAAISSFDRP
910 920 930 940 950
LWAEPCLGET REPEDPAPAL KELFVLPGEP RSQLHQLPKN PLSELPVVKS
960
KRVALSLEDD GLP
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 differs from that shown. Reason: Frameshift at positions 430, 432 and 438.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti262A → V in BAA09328 (PubMed:8626535).Curated1
Sequence conflicti262A → V in BAA21824 (PubMed:9079678).Curated1
Sequence conflicti405Y → C in CAA99509 (PubMed:11152697).Curated1
Sequence conflicti418A → G in BAA09328 (PubMed:8626535).Curated1
Sequence conflicti418A → G in BAA21824 (PubMed:9079678).Curated1
Sequence conflicti418A → G in BAA21825 (PubMed:9079678).Curated1
Sequence conflicti430H → Y in BAA09328 (PubMed:8626535).Curated1
Sequence conflicti430H → Y in BAA21824 (PubMed:9079678).Curated1
Sequence conflicti430H → Y in BAA21825 (PubMed:9079678).Curated1
Sequence conflicti430H → Y in CAA99509 (PubMed:11152697).Curated1
Sequence conflicti488Q → R in CAA99509 (PubMed:11152697).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04697425Q → R.4 PublicationsCorresponds to variant rs4926972dbSNPEnsembl.1
Natural variantiVAR_01846846D → E.5 PublicationsCorresponds to variant rs3820198dbSNPEnsembl.1
Natural variantiVAR_037624453V → M.Corresponds to variant rs5180dbSNPEnsembl.1
Natural variantiVAR_037625466W → C.Corresponds to variant rs5181dbSNPEnsembl.1
Natural variantiVAR_037626607Q → R.Corresponds to variant rs5172dbSNPEnsembl.1
Natural variantiVAR_037627611I → L.Corresponds to variant rs5170dbSNPEnsembl.1
Natural variantiVAR_037628653S → T.Corresponds to variant rs5171dbSNPEnsembl.1
Natural variantiVAR_059079736R → Q.Corresponds to variant rs5172dbSNPEnsembl.1
Natural variantiVAR_018469952R → Q Associated with susceptibility to myocardial infarction type 1; increases activation of MAPK14 by oxidized low density lipoprotein. 2 PublicationsCorresponds to variant rs5174dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_010305166 – 295LCAPH…EADCP → S in isoform 2. 1 PublicationAdd BLAST130
Alternative sequenceiVSP_038181166L → W in isoform 4. Curated1
Alternative sequenceiVSP_010306167 – 336Missing in isoform 4. CuratedAdd BLAST170
Alternative sequenceiVSP_010307737 – 812APQST…HSQHY → D in isoform 2. 1 PublicationAdd BLAST76
Alternative sequenceiVSP_010308893 – 951Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST59

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [Q14114-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A7QX-ray2.60B42-83[»]
ProteinModelPortaliQ14114.
SMRiQ14114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113579. 35 interactors.
DIPiDIP-48670N.
IntActiQ14114. 18 interactors.
STRINGi9606.ENSP00000303634.

PTM databases

iPTMnetiQ14114.
PhosphoSitePlusiQ14114.
SwissPalmiQ14114.

Polymorphism and mutation databases

BioMutaiLRP8.
DMDMi259016389.

Proteomic databases

EPDiQ14114.
PaxDbiQ14114.
PeptideAtlasiQ14114.
PRIDEiQ14114.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.4. human. [Q14114-1]

Organism-specific databases

CTDi7804.
DisGeNETi7804.
GeneCardsiLRP8.
HGNCiHGNC:6700. LRP8.
MalaCardsiLRP8.
MIMi602600. gene.
608446. phenotype.
neXtProtiNX_Q14114.
OpenTargetsiENSG00000157193.
PharmGKBiPA30457.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPT5. Eukaryota.
ENOG410YQ6J. LUCA.
GeneTreeiENSGT00760000118968.
HOVERGENiHBG006250.
InParanoidiQ14114.
KOiK20052.
OMAiVCDSHRD.
OrthoDBiEOG091G01MX.
PhylomeDBiQ14114.
TreeFamiTF351700.

Enzyme and pathway databases

ReactomeiR-HSA-432142. Platelet sensitization by LDL.
R-HSA-975634. Retinoid metabolism and transport.

Miscellaneous databases

ChiTaRSiLRP8. human.
EvolutionaryTraceiQ14114.
GeneWikiiLow_density_lipoprotein_receptor-related_protein_8.
GenomeRNAii7804.
PMAP-CutDBB1AMT8.
PROiQ14114.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000157193.
CleanExiHS_LRP8.
ExpressionAtlasiQ14114. baseline and differential.
GenevisibleiQ14114. HS.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
4.10.400.10. 7 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
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]
PfamiPF00057. Ldl_recept_a. 7 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 2 hits.
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]
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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: November 2, 2016
This is version 164 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.