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Low-density lipoprotein receptor-related protein 6 (LRP-6)

 LRP6_MOUSE              Reviewed;        1613 AA.
O88572;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
30-AUG-2017, entry version 146.
RecName: Full=Low-density lipoprotein receptor-related protein 6;
Short=LRP-6;
Flags: Precursor;
Name=Lrp6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=9704021; DOI=10.1006/bbrc.1998.9061;
Brown S.D., Twells R.C., Hey P.J., Cox R.D., Levy E.R., Soderman A.R.,
Metzker M.L., Caskey C.T., Todd J.A., Hess J.F.;
"Isolation and characterization of LRP6, a novel member of the low
density lipoprotein receptor gene family.";
Biochem. Biophys. Res. Commun. 248:879-888(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
INTERACTION WITH MESD, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=12581525; DOI=10.1016/S0092-8674(03)00045-X;
Hsieh J.-C., Lee L., Zhang L., Wefer S., Brown K., DeRossi C.,
Wines M.E., Rosenquist T., Holdener B.C.;
"Mesd encodes an LRP5/6 chaperone essential for specification of mouse
embryonic polarity.";
Cell 112:355-367(2003).
[4]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15142971; DOI=10.1242/dev.01137;
Kelly O.G., Pinson K.I., Skarnes W.C.;
"The Wnt co-receptors Lrp5 and Lrp6 are essential for gastrulation in
mice.";
Development 131:2803-2815(2004).
[5]
INTERACTION WITH RSPO1 AND RSPO3.
PubMed=16543246; DOI=10.1074/jbc.M508324200;
Nam J.-S., Turcotte T.J., Smith P.F., Choi S., Yoon J.K.;
"Mouse cristin/R-spondin family proteins are novel ligands for the
Frizzled 8 and LRP6 receptors and activate beta-catenin-dependent gene
expression.";
J. Biol. Chem. 281:13247-13257(2006).
[6]
INTERACTION WITH GRB10.
PubMed=17376403; DOI=10.1016/j.bbrc.2007.03.019;
Tezuka N., Brown A.M., Yanagawa S.;
"GRB10 binds to LRP6, the Wnt co-receptor and inhibits canonical Wnt
signaling pathway.";
Biochem. Biophys. Res. Commun. 356:648-654(2007).
[7]
PHOSPHORYLATION AT SER-1490, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=17698587; DOI=10.1128/MCB.00773-07;
Khan Z., Vijayakumar S., de la Torre T.V., Rotolo S., Bafico A.;
"Analysis of endogenous LRP6 function reveals a novel feedback
mechanism by which Wnt negatively regulates its receptor.";
Mol. Cell. Biol. 27:7291-7301(2007).
[8]
INTERACTION WITH DRAXIN.
PubMed=19857465; DOI=10.1016/j.bbrc.2009.10.113;
Miyake A., Takahashi Y., Miwa H., Shimada A., Konishi M., Itoh N.;
"Neucrin is a novel neural-specific secreted antagonist to canonical
Wnt signaling.";
Biochem. Biophys. Res. Commun. 390:1051-1055(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
VARIANT RS TRP-886.
PubMed=15469977; DOI=10.1242/dev.01405;
Kokubu C., Heinzmann U., Kokubu T., Sakai N., Kubota T., Kawai M.,
Wahl M.B., Galceran J., Grosschedl R., Ozono K., Imai K.;
"Skeletal defects in ringelschwanz mutant mice reveal that Lrp6 is
required for proper somitogenesis and osteogenesis.";
Development 131:5469-5480(2004).
[11]
CHARACTERIZATION OF VARIANT RS TRP-886, SUBCELLULAR LOCATION, AND
INTERACTION WITH DKK1; WNT1 AND MESD.
PubMed=18505367; DOI=10.1359/jbmr.080512;
Kubota T., Michigami T., Sakaguchi N., Kokubu C., Suzuki A., Namba N.,
Sakai N., Nakajima S., Imai K., Ozono K.;
"Lrp6 hypomorphic mutation affects bone mass through bone resorption
in mice and impairs interaction with Mesd.";
J. Bone Miner. Res. 23:1661-1671(2008).
-!- FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers
beta-catenin signaling through inducing aggregation of receptor-
ligand complexes into ribosome-sized signalsomes. Cell-surface
coreceptor of Wnt/beta-catenin signaling, which plays a pivotal
role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor
complex recruits DVL1 polymers to the plasma membrane which, in
turn, recruits the AXIN1/GSK3B-complex to the cell surface
promoting the formation of signalsomes and inhibiting AXIN1/GSK3-
mediated phosphorylation and destruction of beta-catenin. Required
for posterior patterning of the epiblast during gastrulation (By
similarity). {ECO:0000250, ECO:0000269|PubMed:15142971}.
-!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms
phosphorylated oligomer aggregates on Wnt-signaling (By
similarity). Component of the Wnt-Fzd-LRP5-LRP6 complex. Interacts
(via the extracellular domain) with WNT1; the interaction is
enhanced by prior formation of the Wnt/Fzd complex. Interacts (via
the beta-propeller regions 3 and 4) with WNT3A. Interacts (via the
beta-propeller regions 1 and 2) with WNT9B. Interacts with FZD5;
the interaction forms a coreceptor complex for Wnt signaling and
is inhibited by DKK1 and DRAXIN. Interacts (via beta propeller
region) with DKK1; the interaction inhibits FZD5/LRP6 complex
formation. Interacts with DKK2. Interacts (via the phosphorylated
PPPSP motifs) with AXIN1; the interaction recruits the AXIN1/GSK3B
complex to cell surface LRP6 signalsomes. Interacts (via the
extracellular domain) with RSPO1; the interaction activates
Wnt/beta-catenin signaling. Interacts (via the extracellular
domain) with RSPO3 (via the cysteine rich domain); the interaction
activates Wnt/beta-catenin signaling. Interacts (via the beta-
propeller regions 1 and 2) with SOST; the interaction competes
with DKK1 for binding for inhibiting beta-catenin signaling.
Interacts (via the cytoplasmic domain) with CSNKIE; the
interaction phosphorylates LRP6, binds AXIN1 and inhibits
AXIN1/GSK3B-mediated phosphorylation of beta-catenin (By
similarity). Interacts with DRAXIN; the interaction inhibits Wnt
signaling. Interacts with GRB10; the interaction prevents AXIN1
binding, thus negatively regulating the Wnt signaling pathway.
Interacts with MESD; the interaction prevents the formation of
LRP6 aggregates and targets LRP6 to the plasma membrane. Interacts
with MACF1. Interacts with DAB2; the interaction involves LRP6
phosphorylation by CK2 and sequesters LRP6 towards clathrin-
mediated endocytosis. Interacts with TMEM198 (By similarity).
Interacts with CAPRIN2; the interaction promotes LRP6
phosphorylation at Ser-1490 (By similarity). Found in a complex
with CAPRIN2, CCNY and CDK14 during G2/M stage; CAPRIN2 functions
as a scaffold for the complex by binding to CCNY via its N
terminus and to CDK14 via its C terminus. Interacts with LYPD6.
Forms a ternary complex with DKK1 and KREM1 (By similarity).
Interacts with KREM1 in a DKK1-dependent manner (By similarity).
{ECO:0000250|UniProtKB:O75581, ECO:0000269|PubMed:12581525,
ECO:0000269|PubMed:16543246, ECO:0000269|PubMed:17376403,
ECO:0000269|PubMed:18505367, ECO:0000269|PubMed:19857465}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Endoplasmic reticulum. Membrane raft
{ECO:0000250|UniProtKB:O75581}. Note=On Wnt signaling, undergoes a
cycle of caveolin- or clathrin-mediated endocytosis and plasma
membrane location. Released from the endoplasmic reticulum on
palmitoylation. Mono-ubiquitination retains it in the endoplasmic
reticulum in the absence of palmitoylation. On Wnt signaling,
phosphorylated, aggregates and colocalizes with AXIN1 and GSK3B at
the plasma membrane in LRP6-signalsomes (By similarity).
Chaperoned to the plasma membrane by MESD. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in early embryo. Broadly expressed
throughout the embryonic ectoderm and in nascent mesoderm, and in
endoderm emerging from the primitive streak.
{ECO:0000269|PubMed:15142971}.
-!- DOMAIN: The YWTD-EGF-like domains 1 and 2 are required for the
interaction with Wnt-frizzled complex. The YWTD-EGF-like domains 3
and 4 are required for the interaction with DKK1 (By similarity).
{ECO:0000250}.
-!- DOMAIN: The PPPSP motifs play a central role in signal
transduction by being phosphorylated, leading to activate the Wnt
signaling pathway.
-!- PTM: Dual phosphorylation of cytoplasmic PPPSP motifs sequentially
by GSK3 and CK1 is required for AXIN1-binding, and subsequent
stabilization and activation of beta-catenin via preventing GSK3-
mediated phosphorylation of beta-catenin. Phosphorylated, in
vitro, by GRK5/6 within and outside the PPPSP motifs.
Phosphorylation at Ser-1490 by CDK14 during G2/M phase leads to
regulation of the Wnt signaling pathway during the cell cycle.
Phosphorylation by GSK3B is induced by RPSO1 binding and inhibited
by DKK1. Phosphorylated, in vitro, by casein kinase I on Thr-1479
(By similarity). {ECO:0000250}.
-!- PTM: Undergoes gamma-secretase-dependent regulated intramembrane
proteolysis (RIP). The extracellular domain is first released by
shedding, and then, through the action of gamma-secretase, the
intracellular domain (ICD) is released into the cytoplasm where it
is free to bind to GSK3B and to activate canonical Wnt signaling
(By similarity). {ECO:0000250}.
-!- PTM: Palmitoylation on the two sites near the transmembrane domain
leads to release of LRP6 from the endoplasmic reticulum.
{ECO:0000250}.
-!- PTM: Mono-ubiquitinated which retains LRP6 in the endoplasmic
reticulum. Ubiquitinated by ZNRF3, leading to its degradation by
the proteasome (By similarity). {ECO:0000250}.
-!- PTM: N-glycosylation is required for cell surface location.
{ECO:0000250}.
-!- DISEASE: Note=Defects in Lrp6 are the cause of Ringelschwanz (rs)
phenotype. Rs phenotype is a spontaneous mutation that is
characterized by a combination of multiple Wnt-deficient
phenotypes including dysmorphologies of the axial skeleton, digits
and the neural tube. The establishment of the anteroposterior
somite compartments, the epithelialization of nascent somites, and
the formation of segment borders are disturbed in (rs) mutants.
There is delayed ossification at birth and a low bone mass
phenotype in adults. Functional analyzes reveal impaired targeting
to the plasma surface due to reduced interaction with MESD leading
to inhibited Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:15469977, ECO:0000269|PubMed:18505367}.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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EMBL; AF074265; AAC33007.1; -; mRNA.
EMBL; BC060704; AAH60704.1; -; mRNA.
CCDS; CCDS39678.1; -.
PIR; JE0273; JE0273.
RefSeq; NP_032540.2; NM_008514.4.
UniGene; Mm.321990; -.
ProteinModelPortal; O88572; -.
SMR; O88572; -.
BioGrid; 201203; 8.
DIP; DIP-46460N; -.
IntAct; O88572; 4.
STRING; 10090.ENSMUSP00000032322; -.
iPTMnet; O88572; -.
PhosphoSitePlus; O88572; -.
MaxQB; O88572; -.
PaxDb; O88572; -.
PeptideAtlas; O88572; -.
PRIDE; O88572; -.
GeneID; 16974; -.
KEGG; mmu:16974; -.
UCSC; uc009ekl.2; mouse.
CTD; 4040; -.
MGI; MGI:1298218; Lrp6.
eggNOG; ENOG410IPT4; Eukaryota.
eggNOG; ENOG410XSY5; LUCA.
HOGENOM; HOG000230697; -.
HOVERGEN; HBG049167; -.
InParanoid; O88572; -.
KO; K03068; -.
PhylomeDB; O88572; -.
TreeFam; TF315253; -.
ChiTaRS; Lrp6; mouse.
PRO; PR:O88572; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005901; C:caveola; IBA:GO_Central.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005769; C:early endosome; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0045202; C:synapse; IBA:GO_Central.
GO; GO:1990909; C:Wnt signalosome; ISO:MGI.
GO; GO:1990851; C:Wnt-Frizzled-LRP5/6 complex; ISO:MGI.
GO; GO:0071936; F:coreceptor activity involved in Wnt signaling pathway; ISO:MGI.
GO; GO:0005109; F:frizzled binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0019210; F:kinase inhibitor activity; ISO:MGI.
GO; GO:0005041; F:low-density lipoprotein receptor activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0019534; F:toxin transporter activity; IMP:BHF-UCL.
GO; GO:0042813; F:Wnt-activated receptor activity; IBA:GO_Central.
GO; GO:0017147; F:Wnt-protein binding; IPI:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0003401; P:axis elongation; IMP:MGI.
GO; GO:0090245; P:axis elongation involved in somitogenesis; IGI:MGI.
GO; GO:0046849; P:bone remodeling; IGI:MGI.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0061310; P:canonical Wnt signaling pathway involved in cardiac neural crest cell differentiation involved in heart development; IMP:MGI.
GO; GO:0061324; P:canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation; IMP:MGI.
GO; GO:0042074; P:cell migration involved in gastrulation; IGI:MGI.
GO; GO:0071397; P:cellular response to cholesterol; ISO:MGI.
GO; GO:0021587; P:cerebellum morphogenesis; IMP:MGI.
GO; GO:0021795; P:cerebral cortex cell migration; IMP:MGI.
GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0060026; P:convergent extension; IGI:MGI.
GO; GO:0071542; P:dopaminergic neuron differentiation; IMP:MGI.
GO; GO:0009950; P:dorsal/ventral axis specification; IMP:MGI.
GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:MGI.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IMP:MGI.
GO; GO:0035261; P:external genitalia morphogenesis; IMP:MGI.
GO; GO:0060325; P:face morphogenesis; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0021872; P:forebrain generation of neurons; IMP:MGI.
GO; GO:0021861; P:forebrain radial glial cell differentiation; IGI:MGI.
GO; GO:0021943; P:formation of radial glial scaffolds; IGI:MGI.
GO; GO:0001702; P:gastrulation with mouth forming second; IGI:MGI.
GO; GO:0048699; P:generation of neurons; IMP:MGI.
GO; GO:0001947; P:heart looping; IGI:MGI.
GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
GO; GO:0060603; P:mammary gland duct morphogenesis; IGI:MGI.
GO; GO:0060596; P:mammary placode formation; IMP:MGI.
GO; GO:0030901; P:midbrain development; IMP:MGI.
GO; GO:0030917; P:midbrain-hindbrain boundary development; IMP:MGI.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
GO; GO:2000051; P:negative regulation of non-canonical Wnt signaling pathway; IGI:MGI.
GO; GO:2000151; P:negative regulation of planar cell polarity pathway involved in cardiac muscle tissue morphogenesis; IGI:MGI.
GO; GO:2000162; P:negative regulation of planar cell polarity pathway involved in cardiac right atrium morphogenesis; IGI:MGI.
GO; GO:2000168; P:negative regulation of planar cell polarity pathway involved in neural tube closure; IGI:MGI.
GO; GO:2000164; P:negative regulation of planar cell polarity pathway involved in outflow tract morphogenesis; IGI:MGI.
GO; GO:2000166; P:negative regulation of planar cell polarity pathway involved in pericardium morphogenesis; IGI:MGI.
GO; GO:2000149; P:negative regulation of planar cell polarity pathway involved in ventricular septum morphogenesis; IGI:MGI.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISO:MGI.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI:MGI.
GO; GO:0014033; P:neural crest cell differentiation; ISO:MGI.
GO; GO:0014029; P:neural crest formation; ISO:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:0021915; P:neural tube development; IGI:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0060021; P:palate development; IMP:MGI.
GO; GO:0003344; P:pericardium morphogenesis; IGI:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0045780; P:positive regulation of bone resorption; IMP:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0045787; P:positive regulation of cell cycle; ISO:MGI.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; IGI:ARUK-UCL.
GO; GO:0045778; P:positive regulation of ossification; IMP:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:2000055; P:positive regulation of Wnt signaling pathway involved in dorsal/ventral axis specification; ISO:MGI.
GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
GO; GO:0090009; P:primitive streak formation; IGI:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IMP:MGI.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0060284; P:regulation of cell development; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0051593; P:response to folic acid; IMP:MGI.
GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
GO; GO:0001756; P:somitogenesis; IGI:MGI.
GO; GO:0021794; P:thalamus development; IMP:MGI.
GO; GO:0060535; P:trachea cartilage morphogenesis; IGI:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IGI:MGI.
GO; GO:0044332; P:Wnt signaling pathway involved in dorsal/ventral axis specification; ISO:MGI.
GO; GO:0021874; P:Wnt signaling pathway involved in forebrain neuroblast division; IMP:MGI.
GO; GO:0090244; P:Wnt signaling pathway involved in somitogenesis; IMP:MGI.
Gene3D; 2.120.10.30; -; 4.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR017049; LRP5/6.
Pfam; PF00057; Ldl_recept_a; 3.
Pfam; PF00058; Ldl_recept_b; 11.
PIRSF; PIRSF036314; LDL_recpt-rel_p5/6; 1.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 4.
SMART; SM00192; LDLa; 3.
SMART; SM00135; LY; 20.
SUPFAM; SSF57424; SSF57424; 3.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS01209; LDLRA_1; 3.
PROSITE; PS50068; LDLRA_2; 3.
PROSITE; PS51120; LDLRB; 20.
1: Evidence at protein level;
Cell membrane; Complete proteome; Developmental protein;
Disease mutation; Disulfide bond; EGF-like domain; Endocytosis;
Endoplasmic reticulum; Glycoprotein; Isopeptide bond; Lipoprotein;
Membrane; Palmitate; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation; Wnt signaling pathway.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1613 Low-density lipoprotein receptor-related
protein 6.
/FTId=PRO_0000017331.
TOPO_DOM 20 1370 Extracellular. {ECO:0000255}.
TRANSMEM 1371 1393 Helical. {ECO:0000255}.
TOPO_DOM 1394 1613 Cytoplasmic. {ECO:0000255}.
REPEAT 63 106 LDL-receptor class B 1.
REPEAT 107 149 LDL-receptor class B 2.
REPEAT 150 193 LDL-receptor class B 3.
REPEAT 194 235 LDL-receptor class B 4.
REPEAT 236 277 LDL-receptor class B 5.
DOMAIN 282 324 EGF-like 1.
REPEAT 372 414 LDL-receptor class B 6.
REPEAT 415 457 LDL-receptor class B 7.
REPEAT 458 501 LDL-receptor class B 8.
REPEAT 502 542 LDL-receptor class B 9.
REPEAT 543 587 LDL-receptor class B 10.
DOMAIN 588 628 EGF-like 2.
REPEAT 674 716 LDL-receptor class B 11.
REPEAT 717 759 LDL-receptor class B 12.
REPEAT 760 802 LDL-receptor class B 13.
REPEAT 803 842 LDL-receptor class B 14.
REPEAT 843 885 LDL-receptor class B 15.
DOMAIN 889 930 EGF-like 3.
REPEAT 977 1025 LDL-receptor class B 16.
REPEAT 1026 1068 LDL-receptor class B 17.
REPEAT 1069 1113 LDL-receptor class B 18.
REPEAT 1114 1156 LDL-receptor class B 19.
REPEAT 1157 1198 LDL-receptor class B 20.
DOMAIN 1203 1244 EGF-like 4.
DOMAIN 1248 1286 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1287 1323 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1325 1361 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
REGION 20 275 Beta-propeller 1.
REGION 328 589 Beta-propeller 2.
REGION 631 890 Beta-propeller 3.
REGION 933 1202 Beta-propeller 4.
MOTIF 1487 1493 PPPSP motif A.
MOTIF 1527 1534 PPPSP motif B.
MOTIF 1568 1575 PPPSP motif C.
MOTIF 1588 1593 PPPSP motif D.
MOTIF 1603 1610 PPPSP motif E.
COMPBIAS 1469 1475 Poly-Ser.
COMPBIAS 1566 1573 Poly-Pro.
COMPBIAS 1603 1608 Poly-Pro.
MOD_RES 1420 1420 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:O75581}.
MOD_RES 1430 1430 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:O75581}.
MOD_RES 1479 1479 Phosphothreonine.
{ECO:0000250|UniProtKB:O75581}.
MOD_RES 1490 1490 Phosphoserine; by CDK14, GRK5 and GRK6.
{ECO:0000250|UniProtKB:O75581}.
MOD_RES 1493 1493 Phosphothreonine; by CK1.
{ECO:0000250|UniProtKB:O75581}.
LIPID 1394 1394 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 1399 1399 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 486 486 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 692 692 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 859 859 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 865 865 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 286 297 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 293 308 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 310 323 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 592 603 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 599 612 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 614 627 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 893 904 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 900 914 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 916 929 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1207 1218 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1214 1228 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1230 1243 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1249 1263 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1256 1276 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1270 1285 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1288 1300 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1295 1313 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1307 1322 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1326 1338 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1333 1351 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1345 1360 {ECO:0000255|PROSITE-ProRule:PRU00124}.
CROSSLNK 1403 1403 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O75581}.
VARIANT 886 886 R -> W (in rs).
{ECO:0000269|PubMed:15469977,
ECO:0000269|PubMed:18505367}.
CONFLICT 83 83 S -> T (in Ref. 2; AAH60704).
{ECO:0000305}.
CONFLICT 317 317 M -> L (in Ref. 2; AAH60704).
{ECO:0000305}.
CONFLICT 586 586 V -> I (in Ref. 2; AAH60704).
{ECO:0000305}.
CONFLICT 622 622 G -> S (in Ref. 2; AAH60704).
{ECO:0000305}.
CONFLICT 933 933 S -> T (in Ref. 2; AAH60704).
{ECO:0000305}.
SEQUENCE 1613 AA; 180255 MW; 3C2ABC8EEEB17622 CRC64;
MGAVLRSLLA CSFCVLLRAA PLLLYANRRD LRLVDATNGK ENATIVVGGL EDAAAVDFVF
GHGLIYWSDV SEEAIKRTEF NKSESVQNVV VSGLLSPDGL ACDWLGEKLY WTDSETNRIE
VSNLDGSLRK VLFWQELDQP RAIALDPSSG FMYWTDWGEV PKIERAGMDG SSRFVIINTE
IYWPNGLTLD YQERKLYWAD AKLNFIHKSN LDGTNRQAVV KGSLPHPFAL TLFEDTLYWT
DWNTHSILAC NKYTGEGLRE IHSNIFSPMD IHAFSQQRQP NATNPCGIDN GGCSHLCLMS
PVKPFYQCAC PTGVKLMENG KTCKDGATEL LLLARRTDLR RISLDTPDFT DIVLQLEDIR
HAIAIDYDPV EGYIYWTDDE VRAIRRSFID GSGSQFVVTA QIAHPDGIAV DWVARNLYWT
DTGTDRIEVT RLNGTMRKIL ISEDLEEPRA IVLDPMVGYM YWTDWGEIPK IERAALDGSD
RVVLVNTSLG WPNGLALDYD EGTIYWGDAK TDKIEVMNTD GTGRRVLVED KIPHIFGFTL
LGDYVYWTDW QRRSIERVHK RSAEREVIID QLPDLMGLKA TSVHRVIGSN PCAEDNGGCS
HLCLYRPQGL RCACPIGFEL IGDMKTCIVP EAFLLFSRRA DIRRISLETN NNNVAIPLTG
VKEASALDFD VTDNRIYWTD ISLKTISRAF MNGSALEHVV EFGLDYPEGM AVDWLGKNLY
WADTGTNRIE VSKLDGQHRQ VLVWKDLDSP RALALDPAEG FMYWTEWGGK PKIDRAAMDG
SERTTLVPNV GRANGLTIDY AKRRLYWTDL DTNLIESSDM LGLNREVIAD DLPHPFGLTQ
YQDYIYWTDW SRRSIERANK TSGQNRTIIQ GHLDYVMDIL VFHSSRQAGW NECASSNGHC
SHLCLAVPVG GFVCGCPAHY SLNADNRTCS APSTFLLFSQ KSAINRMVID EQQSPDIILP
IHSLRNVRAI DYDPLDKQLY WIDSRQNSIR KAHEDGGQGF NVVANSVANQ NLEIQPYDLS
IDIYSRYIYW TCEATNVIDV TRLDGRSVGV VLKGEQDRPR AIVVNPEKGY MYFTNLQERS
PKIERAALDG TEREVLFFSG LSKPIALALD SKLGKLFWAD SDLRRIESSD LSGANRIVLE
DSNILQPVGL TVFENWLYWI DKQQQMIEKI DMTGREGRTK VQARIAQLSD IHAVKELNLQ
EYRQHPCAQD NGGCSHICLV KGDGTTRCSC PMHLVLLQDE LSCGEPPTCS PQQFTCFTGD
IDCIPVAWRC DGFTECEDHS DELNCPVCSE SQFQCASGQC IDGALRCNGD ANCQDKSDEK
NCEVLCLIDQ FRCANGQCVG KHKKCDHSVD CSDRSDELDC YPTEEPAPQA TNTVGSVIGV
IVTIFVSGTI YFICQRMLCP RMKGDGETMT NDYVVHSPAS VPLGYVPHPS SLSGSLPGMS
RGKSMISSLS IMGGSSGPPY DRAHVTGASS SSSSSTKGTY FPAILNPPPS PATERSHYTM
EFGYSSNSPS THRSYSYRPY SYRHFAPPTT PCSTDVCDSD YAPSRRMTSV ATAKGYTSDV
NYDSEPVPPP PTPRSQYLSA EENYESCPPS PYTERSYSHH LYPPPPSPCT DSS


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