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Low-density lipoprotein receptor-related protein 2 (LRP-2) (Glycoprotein 330) (gp330) (Megalin)

 LRP2_RAT                Reviewed;        4660 AA.
P98158;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
23-MAY-2018, entry version 156.
RecName: Full=Low-density lipoprotein receptor-related protein 2;
Short=LRP-2;
AltName: Full=Glycoprotein 330 {ECO:0000303|PubMed:7937880};
Short=gp330 {ECO:0000303|PubMed:7937880};
AltName: Full=Megalin;
Flags: Precursor;
Name=Lrp2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=7937880; DOI=10.1073/pnas.91.21.9725;
Saito A., Pietromonaco S., Loo A.K.C., Farquhar M.G.;
"Complete cloning and sequencing of rat gp330/'megalin,' a distinctive
member of the low density lipoprotein receptor gene family.";
Proc. Natl. Acad. Sci. U.S.A. 91:9725-9729(1994).
[2]
SUBCELLULAR LOCATION.
PubMed=6752952;
Kerjaschki D., Farquhar M.G.;
"The pathogenic antigen of Heymann nephritis is a membrane
glycoprotein of the renal proximal tubule brush border.";
Proc. Natl. Acad. Sci. U.S.A. 79:5557-5561(1982).
[3]
INTERACTION WITH LRPAP1.
PubMed=1400426;
Kounnas M.Z., Argraves W.S., Strickland D.K.;
"The 39-kDa receptor-associated protein interacts with two members of
the low density lipoprotein receptor family, alpha 2-macroglobulin
receptor and glycoprotein 330.";
J. Biol. Chem. 267:21162-21166(1992).
[4]
TISSUE SPECIFICITY.
PubMed=7510321; DOI=10.1177/42.4.7510321;
Zheng G., Bachinsky D.R., Stamenkovic I., Strickland D.K., Brown D.,
Andres G., McCluskey R.T.;
"Organ distribution in rats of two members of the low-density
lipoprotein receptor gene family, gp330 and LRP/alpa 2MR, and the
receptor-associated protein (RAP).";
J. Histochem. Cytochem. 42:531-542(1994).
[5]
FUNCTION IN UPTAKE OF POLYBASIC DRUGS.
PubMed=7544804; DOI=10.1172/JCI118176;
Moestrup S.K., Cui S., Vorum H., Bregengaard C., Bjorn S.E.,
Norris K., Gliemann J., Christensen E.I.;
"Evidence that epithelial glycoprotein 330/megalin mediates uptake of
polybasic drugs.";
J. Clin. Invest. 96:1404-1413(1995).
[6]
FUNCTION.
PubMed=11964399; DOI=10.1074/jbc.M201933200;
McCarthy R.A., Barth J.L., Chintalapudi M.R., Knaak C., Argraves W.S.;
"Megalin functions as an endocytic sonic hedgehog receptor.";
J. Biol. Chem. 277:25660-25667(2002).
[7]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=12519751; DOI=10.1152/ajpcell.00514.2002;
Takeda T., Yamazaki H., Farquhar M.G.;
"Identification of an apical sorting determinant in the cytoplasmic
tail of megalin.";
Am. J. Physiol. 284:C1105-C1113(2003).
[8]
FUNCTION, INTERACTION WITH MB, AND SUBCELLULAR LOCATION.
PubMed=12724130; DOI=10.1152/ajprenal.00062.2003;
Gburek J., Birn H., Verroust P.J., Goj B., Jacobsen C., Moestrup S.K.,
Willnow T.E., Christensen E.I.;
"Renal uptake of myoglobin is mediated by the endocytic receptors
megalin and cubilin.";
Am. J. Physiol. 285:F451-F458(2003).
[9]
FUNCTION.
PubMed=15126248; DOI=10.1152/ajprenal.00233.2003;
Klassen R.B., Crenshaw K., Kozyraki R., Verroust P.J., Tio L.,
Atrian S., Allen P.L., Hammond T.G.;
"Megalin mediates renal uptake of heavy metal metallothionein
complexes.";
Am. J. Physiol. 287:F393-F403(2004).
[10]
FUNCTION.
PubMed=15467006; DOI=10.1152/ajprenal.00243.2004;
Gonzalez-Villalobos R., Klassen R.B., Allen P.L., Navar L.G.,
Hammond T.G.;
"Megalin binds and internalizes angiotensin II.";
Am. J. Physiol. 288:F420-F427(2005).
[11]
FUNCTION, AND INTERACTION WITH SHBG.
PubMed=16143106; DOI=10.1016/j.cell.2005.06.032;
Hammes A., Andreassen T.K., Spoelgen R., Raila J., Hubner N.,
Schulz H., Metzger J., Schweigert F.J., Luppa P.B., Nykjaer A.,
Willnow T.E.;
"Role of endocytosis in cellular uptake of sex steroids.";
Cell 122:751-762(2005).
[12]
FUNCTION.
PubMed=16380466; DOI=10.1152/ajprenal.00164.2005;
Gonzalez-Villalobos R., Klassen R.B., Allen P.L., Johanson K.,
Baker C.B., Kobori H., Navar L.G., Hammond T.G.;
"Megalin binds and internalizes angiotensin-(1-7).";
Am. J. Physiol. 290:F1270-F1275(2006).
[13]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17063000;
Ishida T., Hatae T., Nishi N., Araki N.;
"Soluble megalin is accumulated in the lumen of the rat endolymphatic
sac.";
Cell Struct. Funct. 31:77-85(2006).
[14]
FUNCTION.
PubMed=16801528; DOI=10.1369/jhc.5A6899.2006;
Morales C.R., Zeng J., El Alfy M., Barth J.L., Chintalapudi M.R.,
McCarthy R.A., Incardona J.P., Argraves W.S.;
"Epithelial trafficking of Sonic hedgehog by megalin.";
J. Histochem. Cytochem. 54:1115-1127(2006).
[15]
FUNCTION.
PubMed=16099815; DOI=10.1210/me.2005-0209;
Faber K., Hvidberg V., Moestrup S.K., Dahlbaeck B., Nielsen L.B.;
"Megalin is a receptor for apolipoprotein M, and kidney-specific
megalin-deficiency confers urinary excretion of apolipoprotein M.";
Mol. Endocrinol. 20:212-218(2006).
[16]
FUNCTION, AND INTERACTION WITH CST3.
PubMed=17462596; DOI=10.1016/j.bbrc.2007.04.072;
Kaseda R., Iino N., Hosojima M., Takeda T., Hosaka K., Kobayashi A.,
Yamamoto K., Suzuki A., Kasai A., Suzuki Y., Gejyo F., Saito A.;
"Megalin-mediated endocytosis of cystatin C in proximal tubule
cells.";
Biochem. Biophys. Res. Commun. 357:1130-1134(2007).
[17]
FUNCTION.
PubMed=17846082; DOI=10.1096/fj.07-9171com;
Koenig O., Ruettiger L., Mueller M., Zimmermann U., Erdmann B.,
Kalbacher H., Gross M., Knipper M.;
"Estrogen and the inner ear: megalin knockout mice suffer progressive
hearing loss.";
FASEB J. 22:410-417(2008).
[18]
FUNCTION, INTERACTION WITH ALB, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=18466341; DOI=10.1111/j.1471-4159.2008.05462.x;
Bento-Abreu A., Velasco A., Polo-Hernandez E., Perez-Reyes P.L.,
Tabernero A., Medina J.M.;
"Megalin is a receptor for albumin in astrocytes and is required for
the synthesis of the neurotrophic factor oleic acid.";
J. Neurochem. 106:1149-1159(2008).
[19]
FUNCTION, INTERACTION WITH LEP, AND TISSUE SPECIFICITY.
PubMed=17324488; DOI=10.1016/j.neurobiolaging.2007.01.008;
Dietrich M.O., Spuch C., Antequera D., Rodal I., de Yebenes J.G.,
Molina J.A., Bermejo F., Carro E.;
"Megalin mediates the transport of leptin across the blood-CSF
barrier.";
Neurobiol. Aging 29:902-912(2008).
[20]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19202329; DOI=10.1159/000199446;
Tauris J., Christensen E.I., Nykjaer A., Jacobsen C., Petersen C.M.,
Ovesen T.;
"Cubilin and megalin co-localize in the neonatal inner ear.";
Audiol. Neurootol. 14:267-278(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4464; SER-4577; SER-4624
AND SER-4658, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[22]
INTERACTION WITH LDLRAP1, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
TYR-4527.
PubMed=23836931; DOI=10.1083/jcb.201211110;
Shah M., Baterina O.Y. Jr., Taupin V., Farquhar M.G.;
"ARH directs megalin to the endocytic recycling compartment to
regulate its proteolysis and gene expression.";
J. Cell Biol. 202:113-127(2013).
[23]
FUNCTION, AND INTERACTION WITH MMP2 AND TIMP1.
PubMed=28659595; DOI=10.1038/s41598-017-04648-y;
Johanns M., Lemoine P., Janssens V., Grieco G., Moestrup S.K.,
Nielsen R., Christensen E.I., Courtoy P.J., Emonard H., Marbaix E.,
Henriet P.;
"Cellular uptake of proMMP-2:TIMP-2 complexes by the endocytic
receptor megalin/LRP-2.";
Sci. Rep. 7:4328-4328(2017).
[24]
STRUCTURE BY NMR OF 1185-1229, CALCIUM-BINDING SITE, AND DISULFIDE
BONDS.
PubMed=17245526; DOI=10.1007/s10858-006-9129-3;
Wolf C.A., Dancea F., Shi M., Bade-Noskova V., Ruterjans H.,
Kerjaschki D., Lucke C.;
"Solution structure of the twelfth cysteine-rich ligand-binding repeat
in rat megalin.";
J. Biomol. NMR 37:321-328(2007).
[25]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 4455-4465 IN COMPLEX WITH
ANKRA2, INTERACTION WITH ANKRA2, AND MOTIF.
PubMed=22649097; DOI=10.1126/scisignal.2002979;
Xu C., Jin J., Bian C., Lam R., Tian R., Weist R., You L., Nie J.,
Bochkarev A., Tempel W., Tan C.S., Wasney G.A., Vedadi M., Gish G.D.,
Arrowsmith C.H., Pawson T., Yang X.J., Min J.;
"Sequence-specific recognition of a PxLPxI/L motif by an ankyrin
repeat tumbler lock.";
Sci. Signal. 5:RA39-RA39(2012).
-!- FUNCTION: Multiligand endocytic receptor. Acts together with CUBN
to mediate endocytosis of high-density lipoproteins (By
similarity). Mediates receptor-mediated uptake of polybasic drugs
such as aprotinin, aminoglycosides and polymyxin B
(PubMed:7544804, PubMed:19202329). In the kidney, mediates the
tubular uptake and clearance of leptin (By similarity). Also
mediates transport of leptin across the blood-brain barrier
through endocytosis at the choroid plexus epithelium
(PubMed:17324488). Endocytosis of leptin in neuronal cells is
required for hypothalamic leptin signaling and leptin-mediated
regulation of feeding and body weight (By similarity). Mediates
endocytosis and subsequent lysosomal degradation of CST3 in kidney
proximal tubule cells (PubMed:17462596). Mediates renal uptake of
25-hydroxyvitamin D3 in complex with the vitamin D3 transporter
GC/DBP (By similarity). Mediates renal uptake of metallothionein-
bound heavy metals (PubMed:15126248). Together with CUBN, mediates
renal reabsorption of myoglobin (PubMed:12724130). Mediates renal
uptake and subsequent lysosomal degradation of APOM
(PubMed:16099815). Plays a role in kidney selenium homeostasis by
mediating renal endocytosis of selenoprotein SEPP1 (By
similarity). Mediates renal uptake of the antiapoptotic protein
BIRC5/survivin which may be important for functional integrity of
the kidney (By similarity). Mediates renal uptake of matrix
metalloproteinase MMP2 in complex with metalloproteinase inhibitor
TIMP1 (PubMed:28659595). Mediates endocytosis of Sonic hedgehog
protein N-product (ShhN), the active product of SHH
(PubMed:11964399, PubMed:16801528). Also mediates ShhN
transcytosis (PubMed:16801528). In the embryonic neuroepithelium,
mediates endocytic uptake and degradation of BMP4, is required for
correct SHH localization in the ventral neural tube and plays a
role in patterning of the ventral telencephalon (By similarity).
Required at the onset of neurulation to sequester SHH on the
apical surface of neuroepithelial cells of the rostral
diencephalon ventral midline and to control PTCH1-dependent uptake
and intracellular trafficking of SHH (By similarity). During
neurulation, required in neuroepithelial cells for uptake of
folate bound to the folate receptor FOLR1 which is necessary for
neural tube closure (By similarity). In the adult brain,
negatively regulates BMP signaling in the subependymal zone which
enables neurogenesis to proceed (By similarity). In astrocytes,
mediates endocytosis of ALB which is required for the synthesis of
the neurotrophic factor oleic acid (PubMed:18466341). Involved in
neurite branching (By similarity). During optic nerve development,
required for SHH-mediated migration and proliferation of
oligodendrocyte precursor cells (By similarity). Mediates
endocytic uptake and clearance of SHH in the retinal margin which
protects retinal progenitor cells from mitogenic stimuli and keeps
them quiescent (By similarity). Plays a role in reproductive organ
development by mediating uptake in reproductive tissues of
androgen and estrogen bound to the sex hormone binding protein
SHBG (PubMed:16143106). Mediates endocytosis of angiotensin-2
(PubMed:15467006). Also mediates endocytosis of angiotensin 1-7
(PubMed:16380466). Binds to the complex composed of beta-amyloid
protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal
degradation (By similarity). Required for embryonic heart
development (By similarity). Required for normal hearing, possibly
through interaction with estrogen in the inner ear
(PubMed:17846082). {ECO:0000250|UniProtKB:A2ARV4,
ECO:0000250|UniProtKB:C0HL13, ECO:0000250|UniProtKB:P98164,
ECO:0000269|PubMed:11964399, ECO:0000269|PubMed:12724130,
ECO:0000269|PubMed:15126248, ECO:0000269|PubMed:15467006,
ECO:0000269|PubMed:16099815, ECO:0000269|PubMed:16143106,
ECO:0000269|PubMed:16380466, ECO:0000269|PubMed:16801528,
ECO:0000269|PubMed:17324488, ECO:0000269|PubMed:17462596,
ECO:0000269|PubMed:17846082, ECO:0000269|PubMed:18466341,
ECO:0000269|PubMed:19202329, ECO:0000269|PubMed:28659595,
ECO:0000269|PubMed:7544804}.
-!- SUBUNIT: Binds plasminogen, extracellular matrix components,
plasminogen activator-plasminogen activator inhibitor type I
complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase,
lactoferrin, CLU/clusterin and calcium. Forms a multimeric complex
together with LRPAP1 (PubMed:1400426). Interacts (via PxLPxI/L
motif) with ANKRA2 (via ankyrin repeats) (PubMed:22649097).
Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the
interaction is not affected by tyrosine phosphorylation of the
NPXY motif (By similarity). Interacts with MB (PubMed:12724130).
Interacts with BMP4 (By similarity). Interacts with the Sonic
hedgehog protein N-product which is the active product of SHH (By
similarity). Interacts with CST3 in a calcium-dependent manner
(PubMed:17462596). Interacts with the vitamin-D binding protein
GC/DBP (By similarity). Interacts with sex hormone-binding protein
SHBG (PubMed:16143106). Interacts with angiotensin-2 (By
similarity). Also interacts with angiotensin 1-7 (By similarity).
Interacts with APOM (By similarity). Interacts with selenoprotein
SEPP1 (By similarity). Interacts with LEP (PubMed:17324488).
Interacts with ALB (PubMed:18466341). Interacts with the
antiapoptotic protein BIRC5/survivin (By similarity). Interacts
with matrix metalloproteinase MMP2 in complex with
metalloproteinase inhibitor TIMP1 (PubMed:28659595). In neurons,
forms a trimeric complex with APP and APPB1/FE65 (By similarity).
Interacts with LDLRAP1/ARH; mediates trafficking of LRP2 to the
endocytic recycling compartment (PubMed:23836931). Does not
interact with beta-amyloid protein 40 alone but interacts with the
complex composed of beta-amyloid protein 40 and CLU/APOJ (By
similarity). {ECO:0000250|UniProtKB:A2ARV4,
ECO:0000250|UniProtKB:C0HL13, ECO:0000250|UniProtKB:P98164,
ECO:0000269|PubMed:12724130, ECO:0000269|PubMed:1400426,
ECO:0000269|PubMed:15467006, ECO:0000269|PubMed:16143106,
ECO:0000269|PubMed:17462596, ECO:0000269|PubMed:18466341,
ECO:0000269|PubMed:22649097, ECO:0000269|PubMed:23836931,
ECO:0000269|PubMed:28659595}.
-!- INTERACTION:
O88797:Dab2; NbExp=2; IntAct=EBI-6306650, EBI-6109302;
D3ZAR1:Ldlrap1; NbExp=3; IntAct=EBI-9251342, EBI-9250714;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:12519751, ECO:0000269|PubMed:18466341,
ECO:0000269|PubMed:19202329, ECO:0000269|PubMed:6752952}; Single-
pass type I membrane protein {ECO:0000255}. Endosome lumen
{ECO:0000269|PubMed:17063000}. Membrane, clathrin-coated pit
{ECO:0000250|UniProtKB:A2ARV4}. Cell projection, dendrite
{ECO:0000250|UniProtKB:A2ARV4}. Cell projection, axon
{ECO:0000250|UniProtKB:A2ARV4}. Note=Localizes to brush border
membranes in the kidney (PubMed:6752952, PubMed:12724130). In the
endolymphatic sac of the inner ear, located in the lumen of
endosomes as a soluble form (PubMed:17063000).
{ECO:0000269|PubMed:12724130, ECO:0000269|PubMed:6752952}.
-!- TISSUE SPECIFICITY: In the inner ear, expressed in the lumen of
the endolymphatic sac where it localizes to macrophage-like cells
as well as to mitochondria-rich and ribosome-rich epithelial cells
(at protein level) (PubMed:17063000). In the inner ear, expressed
in marginal cells of the stria vascularis, epithelial cells at the
spiral prominence, epithelial cells of Reissner's membrane facing
the cochlear duct, and Kolliker's organ (at protein level)
(PubMed:19202329). Expressed in the choroid plexus epithelium in
the brain (at protein level) (PubMed:17324488). In the brain, also
expressed in astrocytes (at protein level) (PubMed:18466341).
Expression also detected in epithelial cells of the kidney
glomerulus and proximal tubule, lung, epididymis and yolk sac
(PubMed:7510321). {ECO:0000269|PubMed:17063000,
ECO:0000269|PubMed:17324488, ECO:0000269|PubMed:18466341,
ECO:0000269|PubMed:19202329, ECO:0000269|PubMed:7510321}.
-!- DEVELOPMENTAL STAGE: In the brain, expression is high after birth
and gradually decreases from postnatal day 4 until the end of the
first postnatal week. {ECO:0000269|PubMed:18466341}.
-!- DOMAIN: Two overlapping PxLPxI/L motifs mediate interaction with
ankyrin repeats of ANKRA2. {ECO:0000269|PubMed:22649097}.
-!- DOMAIN: The cytoplasmic domain is required for sorting to the
apical cell membrane. {ECO:0000269|PubMed:12519751}.
-!- PTM: A fraction undergoes proteolytic cleavage of the
extracellular domain at the cell membrane to generate a
cytoplasmic tail fragment. This is internalized into the early
endosome from where it trafficks in an LDLRAP1/ARH-dependent
manner to the endocytic recycling compartment (ERC). In the ERC,
it is further cleaved by gamma-secretase to release a fragment
which translocates to the nucleus and mediates transcriptional
repression. {ECO:0000269|PubMed:23836931}.
-!- PTM: N-glycosylation is required for ligand binding.
{ECO:0000250|UniProtKB:A2ARV4}.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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EMBL; L34049; AAA51369.1; -; mRNA.
PIR; T42737; T42737.
RefSeq; NP_110454.1; NM_030827.1.
UniGene; Rn.26430; -.
PDB; 2I1P; NMR; -; A=1185-1229.
PDB; 3V2O; X-ray; 1.89 A; B=4448-4466.
PDB; 3V2X; X-ray; 1.85 A; B=4455-4465.
PDBsum; 2I1P; -.
PDBsum; 3V2O; -.
PDBsum; 3V2X; -.
ProteinModelPortal; P98158; -.
SMR; P98158; -.
BioGrid; 247894; 2.
CORUM; P98158; -.
DIP; DIP-44866N; -.
IntAct; P98158; 6.
STRING; 10116.ENSRNOP00000066394; -.
GlyConnect; 344; -.
iPTMnet; P98158; -.
PhosphoSitePlus; P98158; -.
UniCarbKB; P98158; -.
PaxDb; P98158; -.
PRIDE; P98158; -.
GeneID; 29216; -.
KEGG; rno:29216; -.
UCSC; RGD:68407; rat.
CTD; 4036; -.
RGD; 68407; Lrp2.
eggNOG; KOG1215; Eukaryota.
eggNOG; ENOG410XP34; LUCA.
HOGENOM; HOG000231853; -.
HOVERGEN; HBG097941; -.
InParanoid; P98158; -.
KO; K06233; -.
PhylomeDB; P98158; -.
EvolutionaryTrace; P98158; -.
PRO; PR:P98158; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005903; C:brush border; IDA:RGD.
GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0038024; F:cargo receptor activity; IMP:RGD.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0030492; F:hemoglobin binding; IDA:RGD.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0038023; F:signaling receptor activity; TAS:RGD.
GO; GO:0035258; F:steroid hormone receptor binding; IPI:UniProtKB.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
GO; GO:0060982; P:coronary artery morphogenesis; ISS:UniProtKB.
GO; GO:0020028; P:endocytic hemoglobin import; IMP:RGD.
GO; GO:0016197; P:endosomal transport; IMP:RGD.
GO; GO:1904447; P:folate import across plasma membrane; ISS:UniProtKB.
GO; GO:0046879; P:hormone secretion; IMP:RGD.
GO; GO:0042953; P:lipoprotein transport; IMP:RGD.
GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
GO; GO:0030001; P:metal ion transport; IDA:UniProtKB.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
GO; GO:0010951; P:negative regulation of endopeptidase activity; IC:BHF-UCL.
GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
GO; GO:0140058; P:neuron projection arborization; ISS:UniProtKB.
GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; ISS:UniProtKB.
GO; GO:0061156; P:pulmonary artery morphogenesis; ISS:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0033280; P:response to vitamin D; IEP:RGD.
GO; GO:0010165; P:response to X-ray; IDA:RGD.
GO; GO:0003139; P:secondary heart field specification; ISS:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
GO; GO:0045056; P:transcytosis; IMP:UniProtKB.
GO; GO:0060068; P:vagina development; ISS:UniProtKB.
GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:UniProtKB.
GO; GO:0006766; P:vitamin metabolic process; TAS:RGD.
CDD; cd00112; LDLa; 36.
Gene3D; 2.120.10.30; -; 8.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR026823; cEGF.
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; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
Pfam; PF12662; cEGF; 2.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00057; Ldl_recept_a; 35.
Pfam; PF00058; Ldl_recept_b; 14.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 22.
SMART; SM00179; EGF_CA; 9.
SMART; SM00192; LDLa; 36.
SMART; SM00135; LY; 36.
SUPFAM; SSF57184; SSF57184; 5.
SUPFAM; SSF57424; SSF57424; 35.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 8.
PROSITE; PS01187; EGF_CA; 3.
PROSITE; PS01209; LDLRA_1; 31.
PROSITE; PS50068; LDLRA_2; 36.
PROSITE; PS51120; LDLRB; 35.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Cell projection; Coated pit;
Complete proteome; Disulfide bond; EGF-like domain; Endocytosis;
Endosome; Glycoprotein; Hearing; Membrane; Metal-binding;
Neurogenesis; Phosphoprotein; Receptor; Reference proteome; Repeat;
SH3-binding; Signal; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 4660 Low-density lipoprotein receptor-related
protein 2.
/FTId=PRO_0000017322.
TOPO_DOM 26 4425 Extracellular. {ECO:0000255}.
TRANSMEM 4426 4446 Helical. {ECO:0000255}.
TOPO_DOM 4447 4660 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 63 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 66 104 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 107 143 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 141 180 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 182 218 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 221 257 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 264 307 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 347 382 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 435 477 LDL-receptor class B 1.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 478 520 LDL-receptor class B 2.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 521 567 LDL-receptor class B 3.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 568 612 LDL-receptor class B 4.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 752 794 LDL-receptor class B 5.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 795 836 LDL-receptor class B 6.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 837 880 LDL-receptor class B 7.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 881 924 LDL-receptor class B 8.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 1024 1060 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1065 1102 LDL-receptor class A 9.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1109 1145 LDL-receptor class A 10.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1149 1185 LDL-receptor class A 11.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1187 1224 LDL-receptor class A 12.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1230 1268 LDL-receptor class A 13.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1271 1307 LDL-receptor class A 14.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1312 1350 LDL-receptor class A 15.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1350 1390 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1391 1430 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 1479 1521 LDL-receptor class B 9.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1522 1564 LDL-receptor class B 10.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1567 1610 LDL-receptor class B 11.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1611 1655 LDL-receptor class B 12.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1656 1696 LDL-receptor class B 13.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1791 1833 LDL-receptor class B 14.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1834 1883 LDL-receptor class B 15.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1884 1931 LDL-receptor class B 16.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1932 1973 LDL-receptor class B 17.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1974 2014 LDL-receptor class B 18.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2108 2157 LDL-receptor class B 19.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2158 2202 LDL-receptor class B 20.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2203 2246 LDL-receptor class B 21.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2247 2290 LDL-receptor class B 22.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2432 2478 LDL-receptor class B 23.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2479 2519 LDL-receptor class B 24.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2520 2563 LDL-receptor class B 25.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2564 2605 LDL-receptor class B 26.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2606 2647 LDL-receptor class B 27.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 2700 2738 LDL-receptor class A 16.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2741 2777 LDL-receptor class A 17.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2780 2819 LDL-receptor class A 18.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2822 2861 LDL-receptor class A 19.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2864 2902 LDL-receptor class A 20.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2907 2946 LDL-receptor class A 21.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2949 2991 LDL-receptor class A 22.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2994 3030 LDL-receptor class A 23.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3033 3071 LDL-receptor class A 24.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3076 3112 LDL-receptor class A 25.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3112 3153 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3154 3194 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 3241 3283 LDL-receptor class B 28.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3284 3326 LDL-receptor class B 29.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3335 3378 LDL-receptor class B 30.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3379 3421 LDL-receptor class B 31.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3422 3462 LDL-receptor class B 32.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 3513 3551 LDL-receptor class A 26.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3554 3592 LDL-receptor class A 27.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3595 3633 LDL-receptor class A 28.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3636 3674 LDL-receptor class A 29.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3679 3717 LDL-receptor class A 30.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3720 3757 LDL-receptor class A 31.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3760 3796 LDL-receptor class A 32.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3799 3835 LDL-receptor class A 33.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3843 3881 LDL-receptor class A 34.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3884 3923 LDL-receptor class A 35.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3929 3965 LDL-receptor class A 36.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3968 4003 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4009 4050 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 4156 4198 LDL-receptor class B 33.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 4199 4242 LDL-receptor class B 34.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 4244 4285 LDL-receptor class B 35.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 4379 4413 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 4597 4610 Interaction with DAB2.
{ECO:0000250|UniProtKB:P98164}.
MOTIF 4454 4463 SH3-binding. {ECO:0000255}.
MOTIF 4457 4462 PxLPxI/L motif 1; mediates interaction
with ANKRA2.
{ECO:0000269|PubMed:22649097}.
MOTIF 4460 4465 PxLPxI/L motif 2; mediates interaction
with ANKRA2.
{ECO:0000269|PubMed:22649097}.
MOTIF 4522 4527 Endocytosis signal. {ECO:0000255}.
MOTIF 4603 4606 NPXY motif.
MOTIF 4606 4609 SH2-binding. {ECO:0000255}.
MOTIF 4619 4630 SH3-binding. {ECO:0000255}.
METAL 1127 1127 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98164}.
METAL 1130 1130 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1132 1132 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98164}.
METAL 1134 1134 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1140 1140 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1141 1141 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1206 1206 Calcium; via carbonyl oxygen.
{ECO:0000269|PubMed:17245526}.
METAL 1209 1209 Calcium. {ECO:0000269|PubMed:17245526}.
METAL 1211 1211 Calcium; via carbonyl oxygen.
{ECO:0000269|PubMed:17245526}.
METAL 1213 1213 Calcium. {ECO:0000269|PubMed:17245526}.
METAL 1219 1219 Calcium. {ECO:0000269|PubMed:17245526}.
METAL 1220 1220 Calcium. {ECO:0000269|PubMed:17245526}.
MOD_RES 4464 4464 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 4467 4467 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4577 4577 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 4624 4624 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 4637 4637 Phosphothreonine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4658 4658 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 259 259 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 462 462 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 865 865 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1063 1063 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1187 1187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1328 1328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1341 1341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1384 1384 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1451 1451 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1497 1497 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1551 1551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1676 1676 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1733 1733 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1811 1811 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2134 2134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2178 2178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2225 2225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2396 2396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2488 2488 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2548 2548 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2782 2782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2810 2810 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2949 2949 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2989 2989 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3127 3127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3213 3213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3259 3259 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3317 3317 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3357 3357 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3448 3448 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3566 3566 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3682 3682 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3840 3840 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3969 3969 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3980 3980 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4070 4070 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4329 4329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 40 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 35 53 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 47 62 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 67 80 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 74 93 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 87 103 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 108 120 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 115 133 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 127 142 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 142 157 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 152 170 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 164 179 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 183 195 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 190 208 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 202 217 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 222 234 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 229 247 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 241 256 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 265 278 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 272 291 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 285 306 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 351 361 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 357 370 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1025 1037 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1032 1050 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1044 1059 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1066 1079 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1073 1092 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1086 1101 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1110 1122 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1117 1135 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1129 1144 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1150 1162 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1157 1175 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1169 1184 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1188 1201 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:17245526}.
DISULFID 1195 1214 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:17245526}.
DISULFID 1208 1223 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:17245526}.
DISULFID 1231 1244 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1238 1257 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1251 1267 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1272 1284 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1279 1297 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1291 1306 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1313 1326 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1320 1339 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1333 1349 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1354 1365 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1361 1374 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1376 1389 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1395 1405 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1401 1414 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1416 1429 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2701 2713 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2708 2726 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2720 2737 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2742 2754 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2749 2767 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2761 2776 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2781 2794 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2789 2807 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2801 2818 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2823 2836 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2830 2849 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2843 2860 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2865 2878 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2872 2891 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2885 2901 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2908 2920 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2915 2933 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2927 2945 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2950 2967 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2957 2980 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2974 2990 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2995 3007 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3002 3020 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3014 3029 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3034 3046 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3041 3059 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3053 3070 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3077 3089 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3084 3102 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3096 3111 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3116 3128 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3124 3137 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3139 3152 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3158 3169 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3165 3178 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3180 3193 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3514 3527 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3521 3540 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3534 3550 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3555 3567 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3562 3580 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3574 3591 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3596 3608 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3603 3621 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3615 3632 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3637 3649 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3644 3662 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3656 3673 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3680 3694 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3688 3707 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3701 3716 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3721 3734 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3729 3747 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3741 3756 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3761 3773 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3768 3786 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3780 3795 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3800 3812 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3807 3825 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3819 3834 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3844 3856 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3851 3869 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3863 3880 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3885 3898 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3893 3911 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3905 3922 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3930 3942 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3937 3955 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3949 3964 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3972 3981 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3977 3991 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4013 4023 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4019 4032 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4034 4049 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4383 4391 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4385 4401 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4403 4412 {ECO:0000255|PROSITE-ProRule:PRU00076}.
MUTAGEN 4527 4527 Y->C: Reduced interaction with ARH and
dynein. {ECO:0000269|PubMed:23836931}.
STRAND 1190 1194 {ECO:0000244|PDB:2I1P}.
STRAND 1196 1199 {ECO:0000244|PDB:2I1P}.
HELIX 1204 1206 {ECO:0000244|PDB:2I1P}.
STRAND 1207 1211 {ECO:0000244|PDB:2I1P}.
STRAND 1214 1217 {ECO:0000244|PDB:2I1P}.
HELIX 1218 1221 {ECO:0000244|PDB:2I1P}.
SEQUENCE 4660 AA; 519276 MW; E2A0CFD23D0923C3 CRC64;
MERGAAAAAW MLLLAIAACL EPVSSQECGS GNFRCDNGYC IPASWRCDGT RDCLDDTDEI
GCPPRSCESG LFLCPAEGTC IPSSWVCDED KDCSDGADEQ QNCAGTTCSA QQMTCSNGQC
IPSEYRCDHV SDCPDGSDER NCHYPTCDQL TCANGACYNT SQRCDQKVDC RDSSDEANCT
TLCSQKEFEC GSGECILRAY VCDHDNDCED NSDERNCNYD TCGGHQFTCS NGQCINQNWV
CDGDDDCQDS GDEDGCESNQ SHHRCYPREW ACPGSGRCIS IDKVCDGVPD CPEGDDENNV
TSGRTCGMGV CSVLNCEYQC HQTPFGGECF CPPGHIINSN DSRTCIDFDD CQIWGICDQK
CENRQGRHQC LCEEGYILER GQHCKSSDSF SAASVIFSNG RDLLVGDLHG RNFRILAESK
NRGMVMGVDF HYQKHRVFWT DPMQEKVFST DINGLNTQEI LNVSVDTPEN LAVDWINNKL
YLVETKVNRI DVVNLEGNQR VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA
FMDGSNRKDL VTTKVGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV
PHPFGISLFE EHVFFTDWTK MAVMKASKFT ETNPQVYHQS SLRPHGVTVY HALRQPNATN
PCGSNNGGCA QVCVLSHRTD NGGLGYRCKC EFGFELDDDE HRCVAVKNFL LFSSKTAVRG
IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ HSTVFYSDLS KDIIYKQKID GTGKEVITAN
RLESVECLTF DWISRNLYWT DGGLKSVTVL RLADKSRRQI ISNLNNPRSI VVHPTAGYMF
LSDWFRPAKI MRAWSDGSHL MPIVNTSLGW PNGLAIDWSA SRLYWVDAFF DKIEHSTLDG
LDRKRLGHVD QMTHPFGLTV FKDNVFITDW RLGAIIRVRK SDGGDMTVIR RGISSVMHVK
AYDADLQTGS NYCSQTTHAN GDCSHFCFPV PNFQRVCGCP YGMKLQRDQM TCEGDPAREP
PTQQCGSLSF PCNNGKCVPS FFRCDGVDDC HDNSDEHQCG VFNNTCSPSA FACVRGGQCI
PGQWHCDRQN DCLDGSDEQN CPTHATSSTC PSTSFTCDNH VCIPKDWVCD TDNDCSDGSD
EKNCQASGTC QPTQFRCPDH RCISPLYVCD GDKDCADGSD EAGCVLNCTS AQFKCADGSS
CINSRYRCDG VYDCRDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE CDGHPDCIHG
SDEHTGCVPK TCSPTHFLCD NGNCIYKAWI CDGDNDCRDM SDEKDCPTQP FHCPSTQWQC
PGYSTCINLS ALCDGVFDCP NGTDESPLCN QDSCSHFNGG CTHQCMQGPF GATCLCPLGY
QLANDTKTCE DINECDIPGF CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTGSENPLLV
VASRDKIIVD NITAHTHNLY SLVQDVSFVV ALDFDSVTGR VFWSDLLQGK TWSVFQNGTD
KRVVHDSGLS VTEMIAVDWI GRNLYWTDYA LETIEVSKID GSHRTVLISK NVTKPRGLAL
DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW PCGLSIDYPN RLIYFMDAYL
DYIEFCDYDG HNRRQVIASD LVLHHPHALT LFEDFVYWTD RGTRQVMQAN KWHGGNQSVV
MYSVHQPLGI TAIHPSRQPP SRNPCASASC SHLCLLSAQA PRHYSCACPS GWNLSDDSVN
CVRGDQPFLM SVRDNIIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG
EIHRVKTDGS NRTVFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT LKGDTRYGKT
LIANDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK IASANMDGTS LKILFTGNLQ
HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD GTERMILVHH LAHPWGLVVY GSFLYYSDEQ
YEVIERVDKS SGNNKVVLRD NVPYLRGLRV YHRRNAADSS NGCSNNPNAC QQICLPVPGG
MFSCACASGF KLSPDGRSCS PYNSFMVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP DGSNFTNVVT YGIGANGIRG VALDWAAGNL
YFTNAFVYET LIEVLRINTT YRRVLLKVSV DMPRHIIVDP KHRYLFWADY GQKPKIERSF
LDCTNRTVLV SEGIVTPRGL AMDHDTGYIY WVDDSLDLIA RIHLDGGESQ VVRYGSRYPT
PYGITVFGES IIWVDRNLKK VFQASKQPGN TDPPVVIRDK INLLRDVTIF DEHAQPLSPA
ELNNNPCLQS NGGCSHFCFA LPELPTPRCG CAFGTLGNDG KSCATSQEDF LIYSLNNSLR
SLHFDPRDHS LPFQVISVAG TAIALDYDRR NNRIFFTQKL NSLRGQISYV SLYSGSSSPT
VLLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN RAVIARVSKP RAIVLDPCRG
YMYWTDWGTN AKIERATLGG NFRVPIVNTS LVWPNGLALD LETDLLYWAD ASLQKIERST
LTGTNREVVV STAFHSFGLT VYGQYIYWTD LYTRKIYRAN KYDGSDLVAM TTRLPTQPSG
ISTVVKTQRQ QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGNWYLANDN KYCVVDTGTR
CNQLQFTCLN GHCINQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCG NGRCVPYHYR
CDYYNDCGDN SDEAGCLFRN CNSTTEFTCS NGRCIPLSYV CNGINNCHDN DTSDEKNCPP
HTCPPDFTKC QTTNICVPRA FLCDGDNDCG DGSDENPIYC ASHTCRSNEF QCLSPQRCIP
SYWFCDGEAD CADGSDEPDT CGHSVNTCRA SQFQCDNGRC ISGNWVCDGD NDCGDMSDED
QRHHCELQNC SSTQFTCVNS RPPNRRCIPQ YWVCDGDADC SDALDELQNC TMRTCSAGEF
SCANGRCVRQ SFRCDRRNDC GDYSDERGCS YPPCHANQFT CQNGRCIPRF FVCDEDNDCG
DGSDEQEHLC HTPEPTCPLH QFRCDNGHCI EMGRVCNHVD DCSDNSDEKG CGINECLDSS
ISRCDHNCTD TITSFYCSCL PGYKLMSDKR SCVDIDECKE SPQLCSQKCE NVVGSYICKC
APGYIREPDG KSCRQNSNIE PYLIFSNRYY IRNLTTDGSS YSLILQGLGN VVALDFDRVE
KRLYWIDAEK QIIERMFLNK TNRETIINHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD
LEGRHRKMIA QHCVDANNTF CFEHPRGIVL HPQRGHVYWA DWGVHAYIGR IGMDGTNKSV
IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH RHTVYDGSLP HPFALTIFED
TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT HKPFDIHVYH PYRQPIMSNP CGTNNGGCSH
LCLIKAGGRG FTCACPDDFQ TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC
SDGSDEPDLC PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCESNE
WQCANKRCIP QSWQCDSVND CLDNSDEDTS HCASRTCRPG QFKCNNGRCI PQSWKCDVDN
DCGDYSDEPI DECTTAAYNC DNHTEFSCKT NYRCIPQWAV CNGFDDCRDN SDEQGCESVP
CHPSGDFRCA NHHCIPLRWK CDGTDDCGDN SDEENCVPRE CSESEFRCAD QQCIPSRWVC
DQENDCGDNS DERDCEMKTC HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN
GTYCPAAMFE CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNIPCESPQR FRCDNSRCVY
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCISQHYVCD NVNDCGDLSD
ETGCNLGDNR TCAENICEQN CTQLSSGGFI CSCRPGFKPS TSDKNSCQDI NECEEFGICP
QSCRNSKGSY ECFCVDGFKS MSTHYGERCA ADGSPPLLLL PENVRIRKYN TSSEKFSEYL
EEEEHIQTID YDWDPEHIGL SVVYYTVLAQ GSQFGAIKRA YIPNFESGSN NPIREVDLGL
KYLMQPDGLA VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL
MFWTDQGKQP KIESAWMNGE HRSVLVSENL GWPNGLSIDY LNDDRVYWSD SKEDVIEAIK
YDGTDRRLII NEAMKPFSLD IFEDKLYWVA KEKGEVWRQN KFGKENKEKV LVVNPWLTQV
RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG YSCACPQGSD FVTGSTVQCD AASELPVTMP
PPCRCMHGGN CYFDENELPK CKCSSGYSGE YCEVGLSRGI PPGTTMAVLL TFVIVIIVGA
LVLVGLFHYR KTGSLLPTLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI
IDRSMAMNEH FVMEVGKQPV IFENPMYAAK DNTSKVALAV QGPSTGAQVT VPENVENQNY
GRPIDPSEIV PEPKPASPGA DEIQGKKWNI FKRKPKQTTN FENPIYAEMD SEVKDAVAVA
PPPSPSLPAK ASKRNLTPGY TATEDTFKDT ANLVKEDSDV


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