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Low-density lipoprotein receptor-related protein 8 (LRP-8) (Apolipoprotein E receptor 2)

 LRP8_HUMAN              Reviewed;         963 AA.
Q14114; B1AMT6; B1AMT7; B1AMT8; O14968; Q86V27; Q99876; Q9BR78;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 4.
22-NOV-2017, entry version 173.
RecName: Full=Low-density lipoprotein receptor-related protein 8;
Short=LRP-8;
AltName: Full=Apolipoprotein E receptor 2;
Flags: Precursor;
Name=LRP8; Synonyms=APOER2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-25 AND
GLU-46.
TISSUE=Placenta;
PubMed=8626535; DOI=10.1074/jbc.271.14.8373;
Kim D.-H., Iijima H., Goto K., Sakai J., Ishii H., Kim H.-J.,
Suzuki H., Kondo H., Saeki S., Yamamoto T.;
"Human apolipoprotein E receptor 2. A novel lipoprotein receptor of
the low density lipoprotein receptor family predominantly expressed in
brain.";
J. Biol. Chem. 271:8373-8380(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 4), AND VARIANTS
ARG-25 AND GLU-46.
TISSUE=Peripheral blood;
PubMed=9079678; DOI=10.1074/jbc.272.13.8498;
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.;
"Exon/intron organization, chromosome localization, alternative
splicing, and transcription units of the human apolipoprotein E
receptor 2 gene.";
J. Biol. Chem. 272:8498-8504(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS ARG-25 AND
GLU-46.
TISSUE=Umbilical vein;
PubMed=11152697; DOI=10.1074/jbc.M011795200;
Korschineck I., Ziegler S., Breuss J., Lang I., Lorenz M., Kaun C.,
Ambros P.F., Binder B.R.;
"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.";
J. Biol. Chem. 276:13192-13197(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 720-963 (ISOFORM 1), AND VARIANTS
ARG-25 AND GLU-46.
TISSUE=Eye, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=10218790; DOI=10.1016/S0306-4522(98)00489-8;
Clatworthy A.E., Stockinger W., Christie R.H., Schneider W.J.,
Nimpf J., Hyman B.T., Rebeck G.W.;
"Expression and alternate splicing of apolipoprotein E receptor 2 in
brain.";
Neuroscience 90:903-911(1999).
[7]
PHOSPHORYLATION AT TYROSINE RESIDUES.
PubMed=12681505; DOI=10.1016/S0014-5793(03)00261-8;
Sacre S.M., Stannard A.K., Owen J.S.;
"Apolipoprotein E (apoE) isoforms differentially induce nitric oxide
production in endothelial cells.";
FEBS Lett. 540:181-187(2003).
[8]
CHARACTERIZATION, AND TISSUE SPECIFICITY.
PubMed=10508213;
Riddell D.R., Vinogradov D.V., Stannard A.K., Chadwick N., Owen J.S.;
"Identification and characterization of LRP8 (apoER2) in human blood
platelets.";
J. Lipid Res. 40:1925-1930(1999).
[9]
FUNCTION AS A RECEPTOR FOR REELIN.
PubMed=12899622; DOI=10.1021/bi034475p;
Andersen O.M., Benhayon D., Curran T., Willnow T.E.;
"Differential binding of ligands to the apolipoprotein E receptor 2.";
Biochemistry 42:9355-9364(2003).
[10]
FUNCTION AS A RECEPTOR FOR APOE.
PubMed=12950167; DOI=10.1021/bi027093c;
Li X., Kypreos K., Zanni E.E., Zannis V.;
"Domains of apoE required for binding to apoE receptor 2 and to
phospholipids: implications for the functions of apoE in the brain.";
Biochemistry 42:10406-10417(2003).
[11]
FUNCTION AS A RECEPTOR FOR BETA 2-GLYCOPROTEIN I.
PubMed=12807892; DOI=10.1074/jbc.M212655200;
Lutters B.C., Derksen R.H., Tekelenburg W.L., Lenting P.J., Arnout J.,
de Groot P.G.;
"Dimers of beta 2-glycoprotein I increase platelet deposition to
collagen via interaction with phospholipids and the apolipoprotein E
receptor 2'.";
J. Biol. Chem. 278:33831-33838(2003).
[12]
INTERACTION WITH PCSK9.
PubMed=18039658; DOI=10.1074/jbc.M708098200;
Poirier S., Mayer G., Benjannet S., Bergeron E., Marcinkiewicz J.,
Nassoury N., Mayer H., Nimpf J., Prat A., Seidah N.G.;
"The proprotein convertase PCSK9 induces the degradation of low
density lipoprotein receptor (LDLR) and its closest family members
VLDLR and ApoER2.";
J. Biol. Chem. 283:2363-2372(2008).
[13]
UBIQUITINATION.
PubMed=20427281; DOI=10.1074/jbc.M110.123729;
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.;
"The E3 ubiquitin ligase IDOL induces the degradation of the low
density lipoprotein receptor family members VLDLR and ApoER2.";
J. Biol. Chem. 285:19720-19726(2010).
[14]
VARIANTS GLU-46 AND GLN-952.
PubMed=12399018; DOI=10.1016/S0304-3940(02)00942-4;
Ma S.L., Ng H.K., Baum L., Pang J.C., Chiu H.F., Woo J., Tang N.L.,
Lam L.C.;
"Low-density lipoprotein receptor-related protein 8 (apolipoprotein E
receptor 2) gene polymorphisms in Alzheimer's disease.";
Neurosci. Lett. 332:216-218(2002).
[15]
VARIANT GLN-952, CHARACTERIZATION OF VARIANT GLN-952, AND ASSOCIATION
WITH SUSCEPTIBILITY TO MYOCARDIAL INFARCTION TYPE 1.
PubMed=17847002; DOI=10.1086/521581;
Shen G.-Q., Li L., Girelli D., Seidelmann S.B., Rao S., Fan C.,
Park J.E., Xi Q., Li J., Hu Y., Olivieri O., Marchant K., Barnard J.,
Corrocher R., Elston R., Cassano J., Henderson S., Hazen S.L.,
Plow E.F., Topol E.J., Wang Q.K.;
"An LRP8 variant is associated with familial and premature coronary
artery disease and myocardial infarction.";
Am. J. Hum. Genet. 81:780-791(2007).
-!- FUNCTION: 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. Not required for endocytic
uptake of SEPP1 in the kidney which is mediated by LRP2 (By
similarity). {ECO:0000250|UniProtKB:Q924X6,
ECO:0000269|PubMed:12807892, ECO:0000269|PubMed:12899622,
ECO:0000269|PubMed:12950167}.
-!- SUBUNIT: Reelin associates with two or more receptor molecules.
Interacts with DAB1 and JNK-interacting proteins. Interacts with
SNX17 (By similarity). Interacts with PCSK9. {ECO:0000250,
ECO:0000269|PubMed:18039658}.
-!- INTERACTION:
P25054:APC; NbExp=2; IntAct=EBI-2681187, EBI-727707;
P02649:APOE; NbExp=2; IntAct=EBI-2681187, EBI-1222467;
Q60841:Reln (xeno); NbExp=10; IntAct=EBI-2681187, EBI-9248666;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Secreted {ECO:0000250}.
Note=Isoforms that contain the exon coding for a furin-type
cleavage site are proteolytically processed, leading to a secreted
receptor fragment. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist. No differences were
observed in the pattern splicing between control and Alzheimer
brains.;
Name=1; Synonyms=ApoER2 922;
IsoId=Q14114-1; Sequence=Displayed;
Name=2; Synonyms=ApoER2 906;
IsoId=Q14114-2; Sequence=VSP_010305, VSP_010307, VSP_010308;
Name=3;
IsoId=Q14114-3; Sequence=VSP_010308;
Name=4; Synonyms=ApoER2delta4-7;
IsoId=Q14114-4; Sequence=VSP_038181, VSP_010306;
Name=5;
IsoId=Q14114-5; Sequence=Not described;
Note=Contains an insert in the extracellular part which carries
a furin cleavage site.;
-!- TISSUE SPECIFICITY: Expressed mainly in brain and placenta. Also
expressed in platelets and megakaryocytic cells. Not expressed in
the liver. {ECO:0000269|PubMed:10218790,
ECO:0000269|PubMed:10508213}.
-!- DOMAIN: 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). {ECO:0000250}.
-!- PTM: O-glycosylated. Some alternatively spliced isoforms lack the
O-linked sugar domain (By similarity). {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: Tyrosine phosphorylated upon apoE binding.
{ECO:0000269|PubMed:12681505}.
-!- PTM: Ubiquitinated by MYLIP leading to degradation.
{ECO:0000269|PubMed:20427281}.
-!- DISEASE: Myocardial infarction 1 (MCI1) [MIM:608446]: A condition
defined by the irreversible necrosis of heart muscle secondary to
prolonged ischemia. {ECO:0000269|PubMed:17847002}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: Natural isoforms of apoE (E2, E3, E4) have similar
affinities for LRP8.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA99509.1; Type=Frameshift; Positions=430, 432, 438; Evidence={ECO:0000305};
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EMBL; D50678; BAA09328.1; -; mRNA.
EMBL; D86407; BAA21824.1; -; Genomic_DNA.
EMBL; D86407; BAA21825.1; -; Genomic_DNA.
EMBL; Z75190; CAA99509.1; ALT_FRAME; mRNA.
EMBL; AL606760; CAI18908.1; -; Genomic_DNA.
EMBL; AL355483; CAI18908.1; JOINED; Genomic_DNA.
EMBL; AL606760; CAI18909.1; -; Genomic_DNA.
EMBL; AL355483; CAI18909.1; JOINED; Genomic_DNA.
EMBL; AL355483; CAI22782.1; -; Genomic_DNA.
EMBL; AL606760; CAI22782.1; JOINED; Genomic_DNA.
EMBL; AL606760; CAI18910.1; -; Genomic_DNA.
EMBL; AL355483; CAI18910.1; JOINED; Genomic_DNA.
EMBL; AL355483; CAI22780.1; -; Genomic_DNA.
EMBL; AL606760; CAI22780.1; JOINED; Genomic_DNA.
EMBL; AL355483; CAI22781.1; -; Genomic_DNA.
EMBL; AL606760; CAI22781.1; JOINED; Genomic_DNA.
EMBL; BC006443; AAH06443.1; -; mRNA.
EMBL; BC051836; AAH51836.2; -; mRNA.
CCDS; CCDS30720.1; -. [Q14114-3]
CCDS; CCDS578.1; -. [Q14114-1]
CCDS; CCDS579.1; -. [Q14114-2]
CCDS; CCDS580.1; -. [Q14114-4]
RefSeq; NP_001018064.1; NM_001018054.2. [Q14114-3]
RefSeq; NP_004622.2; NM_004631.4. [Q14114-1]
RefSeq; NP_059992.3; NM_017522.4. [Q14114-2]
RefSeq; NP_150643.2; NM_033300.3. [Q14114-4]
UniGene; Hs.280387; -.
PDB; 3A7Q; X-ray; 2.60 A; B=42-83.
PDB; 5B4X; X-ray; 3.20 A; B/D=42-736.
PDB; 5B4Y; X-ray; 1.90 A; B=42-124.
PDBsum; 3A7Q; -.
PDBsum; 5B4X; -.
PDBsum; 5B4Y; -.
ProteinModelPortal; Q14114; -.
SMR; Q14114; -.
BioGrid; 113579; 36.
DIP; DIP-48670N; -.
ELM; Q14114; -.
IntAct; Q14114; 21.
STRING; 9606.ENSP00000303634; -.
iPTMnet; Q14114; -.
PhosphoSitePlus; Q14114; -.
SwissPalm; Q14114; -.
BioMuta; LRP8; -.
DMDM; 259016389; -.
EPD; Q14114; -.
PaxDb; Q14114; -.
PeptideAtlas; Q14114; -.
PRIDE; Q14114; -.
Ensembl; ENST00000306052; ENSP00000303634; ENSG00000157193. [Q14114-1]
Ensembl; ENST00000347547; ENSP00000334522; ENSG00000157193. [Q14114-4]
Ensembl; ENST00000354412; ENSP00000346391; ENSG00000157193. [Q14114-2]
Ensembl; ENST00000371454; ENSP00000360509; ENSG00000157193. [Q14114-3]
GeneID; 7804; -.
KEGG; hsa:7804; -.
UCSC; uc001cvi.4; human. [Q14114-1]
CTD; 7804; -.
DisGeNET; 7804; -.
EuPathDB; HostDB:ENSG00000157193.14; -.
GeneCards; LRP8; -.
HGNC; HGNC:6700; LRP8.
MalaCards; LRP8; -.
MIM; 602600; gene.
MIM; 608446; phenotype.
neXtProt; NX_Q14114; -.
OpenTargets; ENSG00000157193; -.
PharmGKB; PA30457; -.
eggNOG; ENOG410IPT5; Eukaryota.
eggNOG; ENOG410YQ6J; LUCA.
GeneTree; ENSGT00760000118968; -.
HOVERGEN; HBG006250; -.
InParanoid; Q14114; -.
KO; K20052; -.
OMA; GEKDCES; -.
OrthoDB; EOG091G01MX; -.
PhylomeDB; Q14114; -.
TreeFam; TF351700; -.
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SIGNOR; Q14114; -.
ChiTaRS; LRP8; human.
EvolutionaryTrace; Q14114; -.
GeneWiki; Low_density_lipoprotein_receptor-related_protein_8; -.
GenomeRNAi; 7804; -.
PMAP-CutDB; B1AMT8; -.
PRO; PR:Q14114; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000157193; -.
CleanEx; HS_LRP8; -.
ExpressionAtlas; Q14114; baseline and differential.
Genevisible; Q14114; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005901; C:caveola; IDA:BHF-UCL.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0034185; F:apolipoprotein binding; IC:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
GO; GO:0005041; F:low-density lipoprotein receptor activity; TAS:ARUK-UCL.
GO; GO:0038025; F:reelin receptor activity; ISS:BHF-UCL.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IDA:BHF-UCL.
GO; GO:0021541; P:ammon gyrus development; ISS:BHF-UCL.
GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:BHF-UCL.
GO; GO:1900006; P:positive regulation of dendrite development; ISS:BHF-UCL.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:BHF-UCL.
GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
GO; GO:0038026; P:reelin-mediated signaling pathway; ISS:BHF-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00112; LDLa; 6.
Gene3D; 2.120.10.30; -; 2.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
Pfam; PF00057; Ldl_recept_a; 7.
Pfam; PF00058; Ldl_recept_b; 5.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 4.
SMART; SM00179; EGF_CA; 2.
SMART; SM00192; LDLa; 7.
SMART; SM00135; LY; 5.
SUPFAM; SSF57424; SSF57424; 7.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS01209; LDLRA_1; 7.
PROSITE; PS50068; LDLRA_2; 7.
PROSITE; PS51120; LDLRB; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell membrane;
Complete proteome; Disulfide bond; EGF-like domain; Endocytosis;
Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 963 Low-density lipoprotein receptor-related
protein 8.
/FTId=PRO_0000017332.
TOPO_DOM 42 826 Extracellular. {ECO:0000255}.
TRANSMEM 827 847 Helical. {ECO:0000255}.
TOPO_DOM 848 963 Cytoplasmic. {ECO:0000255}.
DOMAIN 46 82 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 85 123 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 126 164 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 166 202 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 205 246 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 258 295 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 298 334 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 336 375 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 376 415 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 462 508 LDL-receptor class B 1.
REPEAT 509 551 LDL-receptor class B 2.
REPEAT 552 595 LDL-receptor class B 3.
REPEAT 596 639 LDL-receptor class B 4.
REPEAT 640 681 LDL-receptor class B 5.
REGION 740 798 Clustered O-linked oligosaccharides.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 441 441 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 518 518 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 538 538 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 772 772 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 807 807 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 47 59 {ECO:0000250}.
DISULFID 54 72 {ECO:0000250}.
DISULFID 66 81 {ECO:0000250}.
DISULFID 86 98 {ECO:0000250}.
DISULFID 93 111 {ECO:0000250}.
DISULFID 105 122 {ECO:0000250}.
DISULFID 127 141 {ECO:0000250}.
DISULFID 134 154 {ECO:0000250}.
DISULFID 148 163 {ECO:0000250}.
DISULFID 167 179 {ECO:0000250}.
DISULFID 174 192 {ECO:0000250}.
DISULFID 186 201 {ECO:0000250}.
DISULFID 206 221 {ECO:0000250}.
DISULFID 213 234 {ECO:0000250}.
DISULFID 228 245 {ECO:0000250}.
DISULFID 259 272 {ECO:0000250}.
DISULFID 267 285 {ECO:0000250}.
DISULFID 279 294 {ECO:0000250}.
DISULFID 299 311 {ECO:0000250}.
DISULFID 306 324 {ECO:0000250}.
DISULFID 318 333 {ECO:0000250}.
DISULFID 340 351 {ECO:0000250}.
DISULFID 347 360 {ECO:0000250}.
DISULFID 362 374 {ECO:0000250}.
DISULFID 380 390 {ECO:0000250}.
DISULFID 386 399 {ECO:0000250}.
DISULFID 401 414 {ECO:0000250}.
VAR_SEQ 166 295 LCAPHEFQCGNRSCLAAVFVCDGDDDCGDGSDERGCADPAC
GPREFRCGGDGGGACIPERWVCDRQFDCEDRSDEAAELCGR
PGPGATSAPAACATASQFACRSGECVHLGWRCDGDRDCKDK
SDEADCP -> S (in isoform 2).
{ECO:0000303|PubMed:11152697}.
/FTId=VSP_010305.
VAR_SEQ 166 166 L -> W (in isoform 4). {ECO:0000305}.
/FTId=VSP_038181.
VAR_SEQ 167 336 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_010306.
VAR_SEQ 737 812 APQSTSTTTLASTMTRTVPATTRAPGTTVHRSTYQNHSTET
PSLTAAVPSSVSVPRAPSISPSTLSPATSNHSQHY -> D
(in isoform 2).
{ECO:0000303|PubMed:11152697}.
/FTId=VSP_010307.
VAR_SEQ 893 951 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11152697,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010308.
VARIANT 25 25 Q -> R (in dbSNP:rs4926972).
{ECO:0000269|PubMed:11152697,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8626535,
ECO:0000269|PubMed:9079678}.
/FTId=VAR_046974.
VARIANT 46 46 D -> E (in dbSNP:rs3820198).
{ECO:0000269|PubMed:11152697,
ECO:0000269|PubMed:12399018,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8626535,
ECO:0000269|PubMed:9079678}.
/FTId=VAR_018468.
VARIANT 453 453 V -> M (in dbSNP:rs5180).
/FTId=VAR_037624.
VARIANT 466 466 W -> C (in dbSNP:rs5181).
/FTId=VAR_037625.
VARIANT 607 607 Q -> R (in dbSNP:rs5172).
/FTId=VAR_037626.
VARIANT 611 611 I -> L (in dbSNP:rs5170).
/FTId=VAR_037627.
VARIANT 653 653 S -> T (in dbSNP:rs5171).
/FTId=VAR_037628.
VARIANT 736 736 R -> Q (in dbSNP:rs5172).
/FTId=VAR_059079.
VARIANT 952 952 R -> Q (associated with susceptibility to
myocardial infarction type 1; increases
activation of MAPK14 by oxidized low
density lipoprotein; dbSNP:rs5174).
{ECO:0000269|PubMed:12399018,
ECO:0000269|PubMed:17847002}.
/FTId=VAR_018469.
CONFLICT 262 262 A -> V (in Ref. 1; BAA09328 and 2;
BAA21824). {ECO:0000305}.
CONFLICT 405 405 Y -> C (in Ref. 3; CAA99509).
{ECO:0000305}.
CONFLICT 418 418 A -> G (in Ref. 1; BAA09328 and 2;
BAA21824/BAA21825). {ECO:0000305}.
CONFLICT 430 430 H -> Y (in Ref. 1; BAA09328, 2; BAA21824/
BAA21825 and 3; CAA99509). {ECO:0000305}.
CONFLICT 488 488 Q -> R (in Ref. 3; CAA99509).
{ECO:0000305}.
STRAND 51 53 {ECO:0000244|PDB:5B4Y}.
STRAND 59 61 {ECO:0000244|PDB:5B4Y}.
HELIX 62 64 {ECO:0000244|PDB:5B4Y}.
STRAND 67 69 {ECO:0000244|PDB:5B4Y}.
STRAND 72 75 {ECO:0000244|PDB:5B4Y}.
HELIX 76 78 {ECO:0000244|PDB:5B4Y}.
STRAND 88 92 {ECO:0000244|PDB:5B4Y}.
STRAND 98 100 {ECO:0000244|PDB:5B4Y}.
HELIX 101 103 {ECO:0000244|PDB:5B4Y}.
STRAND 106 108 {ECO:0000244|PDB:5B4Y}.
HELIX 115 117 {ECO:0000244|PDB:5B4X}.
TURN 119 121 {ECO:0000244|PDB:5B4Y}.
TURN 339 341 {ECO:0000244|PDB:5B4X}.
HELIX 342 344 {ECO:0000244|PDB:5B4X}.
STRAND 348 352 {ECO:0000244|PDB:5B4X}.
STRAND 355 357 {ECO:0000244|PDB:5B4X}.
STRAND 359 361 {ECO:0000244|PDB:5B4X}.
STRAND 368 372 {ECO:0000244|PDB:5B4X}.
HELIX 379 381 {ECO:0000244|PDB:5B4X}.
STRAND 385 393 {ECO:0000244|PDB:5B4X}.
STRAND 396 400 {ECO:0000244|PDB:5B4X}.
STRAND 405 407 {ECO:0000244|PDB:5B4X}.
STRAND 409 412 {ECO:0000244|PDB:5B4X}.
STRAND 414 416 {ECO:0000244|PDB:5B4X}.
STRAND 418 420 {ECO:0000244|PDB:5B4X}.
STRAND 423 427 {ECO:0000244|PDB:5B4X}.
STRAND 429 439 {ECO:0000244|PDB:5B4X}.
STRAND 442 458 {ECO:0000244|PDB:5B4X}.
TURN 459 462 {ECO:0000244|PDB:5B4X}.
STRAND 463 468 {ECO:0000244|PDB:5B4X}.
TURN 469 472 {ECO:0000244|PDB:5B4X}.
STRAND 473 478 {ECO:0000244|PDB:5B4X}.
HELIX 479 481 {ECO:0000244|PDB:5B4X}.
HELIX 485 487 {ECO:0000244|PDB:5B4X}.
STRAND 489 492 {ECO:0000244|PDB:5B4X}.
STRAND 501 505 {ECO:0000244|PDB:5B4X}.
TURN 506 509 {ECO:0000244|PDB:5B4X}.
STRAND 510 515 {ECO:0000244|PDB:5B4X}.
TURN 516 519 {ECO:0000244|PDB:5B4X}.
STRAND 520 525 {ECO:0000244|PDB:5B4X}.
STRAND 530 535 {ECO:0000244|PDB:5B4X}.
STRAND 540 548 {ECO:0000244|PDB:5B4X}.
TURN 549 552 {ECO:0000244|PDB:5B4X}.
STRAND 553 558 {ECO:0000244|PDB:5B4X}.
STRAND 560 562 {ECO:0000244|PDB:5B4X}.
STRAND 564 569 {ECO:0000244|PDB:5B4X}.
STRAND 576 579 {ECO:0000244|PDB:5B4X}.
STRAND 586 592 {ECO:0000244|PDB:5B4X}.
TURN 593 596 {ECO:0000244|PDB:5B4X}.
STRAND 597 602 {ECO:0000244|PDB:5B4X}.
TURN 603 606 {ECO:0000244|PDB:5B4X}.
STRAND 607 612 {ECO:0000244|PDB:5B4X}.
STRAND 619 622 {ECO:0000244|PDB:5B4X}.
TURN 625 627 {ECO:0000244|PDB:5B4X}.
STRAND 629 637 {ECO:0000244|PDB:5B4X}.
STRAND 640 645 {ECO:0000244|PDB:5B4X}.
TURN 646 649 {ECO:0000244|PDB:5B4X}.
STRAND 650 655 {ECO:0000244|PDB:5B4X}.
TURN 656 658 {ECO:0000244|PDB:5B4X}.
STRAND 663 666 {ECO:0000244|PDB:5B4X}.
STRAND 675 678 {ECO:0000244|PDB:5B4X}.
HELIX 680 682 {ECO:0000244|PDB:5B4X}.
TURN 689 691 {ECO:0000244|PDB:5B4X}.
STRAND 692 695 {ECO:0000244|PDB:5B4X}.
HELIX 696 699 {ECO:0000244|PDB:5B4X}.
STRAND 701 706 {ECO:0000244|PDB:5B4X}.
STRAND 710 714 {ECO:0000244|PDB:5B4X}.
STRAND 716 720 {ECO:0000244|PDB:5B4X}.
STRAND 731 735 {ECO:0000244|PDB:5B4X}.
SEQUENCE 963 AA; 105634 MW; B10DCF72F62DE71C CRC64;
MGLPEPGPLR LLALLLLLLL LLLLQLQHLA AAAADPLLGG QGPAKDCEKD QFQCRNERCI
PSVWRCDEDD DCLDHSDEDD CPKKTCADSD FTCDNGHCIH ERWKCDGEEE CPDGSDESEA
TCTKQVCPAE KLSCGPTSHK CVPASWRCDG EKDCEGGADE AGCATLCAPH EFQCGNRSCL
AAVFVCDGDD DCGDGSDERG CADPACGPRE FRCGGDGGGA CIPERWVCDR QFDCEDRSDE
AAELCGRPGP GATSAPAACA TASQFACRSG ECVHLGWRCD GDRDCKDKSD EADCPLGTCR
GDEFQCGDGT CVLAIKHCNQ EQDCPDGSDE AGCLQGLNEC LHNNGGCSHI CTDLKIGFEC
TCPAGFQLLD QKTCGDIDEC KDPDACSQIC VNYKGYFKCE CYPGYEMDLL TKNCKAAAGK
SPSLIFTNRH EVRRIDLVKR NYSRLIPMLK NVVALDVEVA TNRIYWCDLS YRKIYSAYMD
KASDPKEQEV LIDEQLHSPE GLAVDWVHKH IYWTDSGNKT ISVATVDGGR RRTLFSRNLS
EPRAIAVDPL RGFMYWSDWG DQAKIEKSGL NGVDRQTLVS DNIEWPNGIT LDLLSQRLYW
VDSKLHQLSS IDFSGGNRKT LISSTDFLSH PFGIAVFEDK VFWTDLENEA IFSANRLNGL
EISILAENLN NPHDIVIFHE LKQPRAPDAC ELSVQPNGGC EYLCLPAPQI SSHSPKYTCA
CPDTMWLGPD MKRCYRAPQS TSTTTLASTM TRTVPATTRA PGTTVHRSTY QNHSTETPSL
TAAVPSSVSV PRAPSISPST LSPATSNHSQ HYANEDSKMG STVTAAVIGI IVPIVVIALL
CMSGYLIWRN WKRKNTKSMN FDNPVYRKTT EEEDEDELHI GRTAQIGHVY PAAISSFDRP
LWAEPCLGET REPEDPAPAL KELFVLPGEP RSQLHQLPKN PLSELPVVKS KRVALSLEDD
GLP


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