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Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]

 LRP1_MOUSE              Reviewed;        4545 AA.
Q91ZX7; Q61291; Q920Y4;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
05-DEC-2018, entry version 143.
RecName: Full=Prolow-density lipoprotein receptor-related protein 1;
Short=LRP-1;
AltName: Full=Alpha-2-macroglobulin receptor;
Short=A2MR;
AltName: CD_antigen=CD91;
Contains:
RecName: Full=Low-density lipoprotein receptor-related protein 1 85 kDa subunit;
Short=LRP-85;
Contains:
RecName: Full=Low-density lipoprotein receptor-related protein 1 515 kDa subunit;
Short=LRP-515;
Contains:
RecName: Full=Low-density lipoprotein receptor-related protein 1 intracellular domain;
Short=LRPICD;
Flags: Precursor;
Name=Lrp1 {ECO:0000312|EMBL:AAL09566.1};
Synonyms=A2mr {ECO:0000312|MGI:MGI:96828};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:CAA47817.1}
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver {ECO:0000312|EMBL:CAA47817.1};
PubMed=8485155; DOI=10.1016/0167-4781(93)90244-8;
Van Leuven F., Stas L., Raymakers L., Overbergh L., De Strooper B.,
Hilliker C., Lorent K., Fias E., Umans L., Torrekens S., Serneels L.,
Moechars D., Van den Berghe H.;
"Molecular cloning and sequencing of the murine alpha-2-macroglobulin
receptor cDNA.";
Biochim. Biophys. Acta 1173:71-74(1993).
[2] {ECO:0000312|EMBL:AAL09567.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/J {ECO:0000312|EMBL:AAL09567.1}, and
CBA/J {ECO:0000312|EMBL:AAL09566.1};
PubMed=12151109; DOI=10.1016/S0167-4781(02)00419-0;
Smeijers L., Willems S., Lauwers A., Thiry E., van Leuven F.,
Roebroek A.J.M.;
"Functional expression of murine LRP1 requires correction of Lrp1 cDNA
sequences.";
Biochim. Biophys. Acta 1577:155-158(2002).
[3]
FUNCTION AS A RECEPTOR FOR P.AERUGINOSA EXOA TOXIN.
PubMed=1618748;
Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J.,
Strickland D.K., Saelinger C.B.;
"The alpha 2-macroglobulin receptor/low density lipoprotein receptor-
related protein binds and internalizes Pseudomonas exotoxin A.";
J. Biol. Chem. 267:12420-12423(1992).
[4]
INTERACTION WITH DAB2.
PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x;
Morris S.M., Cooper J.A.;
"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and
interacts with AP-2.";
Traffic 2:111-123(2001).
[5] {ECO:0000305}
INTERACTION WITH MAFB.
PubMed=15135046; DOI=10.1016/j.febslet.2004.03.069;
Petersen H.H., Hilpert J., Jacobsen C., Lauwers A., Roebroek A.J.M.,
Willnow T.E.;
"Low-density lipoprotein receptor-related protein interacts with MafB,
a regulator of hindbrain development.";
FEBS Lett. 565:23-27(2004).
[6] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=1423604; DOI=10.1016/0092-8674(92)90511-A;
Herz J., Clouthier D.E., Hammer R.E.;
"LDL receptor-related protein internalizes and degrades uPA-PAI-1
complexes and is essential for embryo implantation.";
Cell 71:411-421(1992).
[7]
ERRATUM.
PubMed=8490961; DOI=10.1016/0092-8674(93)90130-I;
Herz J., Couthier D.E., Hammer R.E.;
Cell 73:428-428(1993).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4524, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-730; ASN-2128 AND
ASN-3049.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-447.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[11]
FUNCTION AS A RECEPTOR FOR CHOLIX TOXIN.
PubMed=18276581; DOI=10.1074/jbc.M710008200;
Jorgensen R., Purdy A.E., Fieldhouse R.J., Kimber M.S., Bartlett D.H.,
Merrill A.R.;
"Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae.";
J. Biol. Chem. 283:10671-10678(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2010, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Endocytic receptor involved in endocytosis and in
phagocytosis of apoptotic cells. Required for early embryonic
development (PubMed:1423604). Involved in cellular lipid
homeostasis. Involved in the plasma clearance of chylomicron
remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as
the local metabolism of complexes between plasminogen activators
and their endogenous inhibitors. May modulate cellular events,
such as APP metabolism, kinase-dependent intracellular signaling,
neuronal calcium signaling as well as neurotransmission. Acts as
an alpha-2-macroglobulin receptor (By similarity).
{ECO:0000250|UniProtKB:Q07954, ECO:0000269|PubMed:1423604}.
-!- FUNCTION: (Microbial infection) Functions as a receptor for Vibrio
cholerae cholix toxin and for Pseudomonas aeruginosa exotoxin A.
{ECO:0000269|PubMed:1618748, ECO:0000269|PubMed:18276581}.
-!- SUBUNIT: Heterodimer of an 85-kDa membrane-bound carboxyl subunit
and a non-covalently attached 515-kDa N-terminal subunit. Found in
a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with SNX17,
PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with
SHC1, GULP1 and DAB1. Interacts with LRPAP1 (By similarity).
Intracellular domain interacts with MAFB. Can weakly interact (via
NPXY motif) with DAB2 (via PID domain); the interaction is
enhanced by tyrosine phosphorylation of the NPXY motif. Interacts
with bacterial exotoxins. {ECO:0000250,
ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:15135046}.
-!- INTERACTION:
P97318:Dab1; NbExp=2; IntAct=EBI-300955, EBI-81680;
Q62108:Dlg4; NbExp=4; IntAct=EBI-300955, EBI-300895;
P48356:Lepr; NbExp=2; IntAct=EBI-300955, EBI-2257257;
Q9WVI9:Mapk8ip1; NbExp=2; IntAct=EBI-300955, EBI-74515;
Q9ERE9:Mapk8ip2; NbExp=2; IntAct=EBI-300955, EBI-74576;
-!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
protein 1 85 kDa subunit: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Membrane, coated pit
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
protein 1 515 kDa subunit: Cell membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}.
Membrane, coated pit {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
protein 1 intracellular domain: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=After cleavage, the intracellular domain
(LRPICD) is detected both in the cytoplasm and in the nucleus.
{ECO:0000250}.
-!- PTM: Phosphorylated on serine and threonine residues.
{ECO:0000250}.
-!- PTM: Phosphorylated on tyrosine residues upon stimulation with
PDGF. Tyrosine phosphorylation promotes interaction with SHC1 (By
similarity). {ECO:0000250}.
-!- PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and
a 515 kDa large extracellular domain (LRP-515) that remains non-
covalently associated. Gamma-secretase-dependent cleavage of LRP-
85 releases the intracellular domain from the membrane (By
similarity). {ECO:0000250|UniProtKB:Q07954}.
-!- DISRUPTION PHENOTYPE: Death during early embryogenesis around 14
dpc. {ECO:0000269|PubMed:1423604}.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000255}.
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EMBL; X67469; CAA47817.1; ALT_SEQ; mRNA.
EMBL; AF367720; AAL09566.1; -; mRNA.
EMBL; AF369477; AAL09567.1; -; Genomic_DNA.
EMBL; AF369389; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369390; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369391; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369392; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369393; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369394; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369395; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369396; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369397; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369398; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369399; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369400; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369401; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369402; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369403; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369404; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369405; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369406; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369407; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369408; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369409; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369410; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369411; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369412; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369413; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369414; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369415; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369416; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369417; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369418; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369419; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369420; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369421; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369422; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369423; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369424; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369425; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369426; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369427; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369428; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369429; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369430; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369431; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369432; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369433; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369434; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369435; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369436; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369437; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369438; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369439; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369440; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369441; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369442; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369443; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369444; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369445; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369446; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369447; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369448; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369449; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369450; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369451; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369452; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369453; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369454; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369455; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369456; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369457; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369458; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369459; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369460; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369461; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369462; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369463; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369464; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369465; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369466; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369467; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369468; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369469; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369470; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369471; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369472; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369473; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369474; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369475; AAL09567.1; JOINED; Genomic_DNA.
EMBL; AF369476; AAL09567.1; JOINED; Genomic_DNA.
CCDS; CCDS24245.1; -.
PIR; S25111; S25111.
RefSeq; NP_032538.2; NM_008512.2.
UniGene; Mm.271854; -.
ProteinModelPortal; Q91ZX7; -.
SMR; Q91ZX7; -.
BioGrid; 201201; 9.
CORUM; Q91ZX7; -.
DIP; DIP-47785N; -.
IntAct; Q91ZX7; 15.
MINT; Q91ZX7; -.
STRING; 10090.ENSMUSP00000044004; -.
iPTMnet; Q91ZX7; -.
PhosphoSitePlus; Q91ZX7; -.
SwissPalm; Q91ZX7; -.
MaxQB; Q91ZX7; -.
PaxDb; Q91ZX7; -.
PeptideAtlas; Q91ZX7; -.
PRIDE; Q91ZX7; -.
GeneID; 16971; -.
KEGG; mmu:16971; -.
UCSC; uc007hjx.1; mouse.
CTD; 4035; -.
MGI; MGI:96828; Lrp1.
eggNOG; KOG1215; Eukaryota.
eggNOG; ENOG410XP34; LUCA.
HOGENOM; HOG000230574; -.
HOVERGEN; HBG006292; -.
InParanoid; Q91ZX7; -.
KO; K04550; -.
PhylomeDB; Q91ZX7; -.
TreeFam; TF315253; -.
PRO; PR:Q91ZX7; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0016964; F:alpha-2 macroglobulin receptor activity; ISS:UniProtKB.
GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0032050; F:clathrin heavy chain binding; ISO:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0097242; P:amyloid-beta clearance; IMP:BHF-UCL.
GO; GO:0035909; P:aorta morphogenesis; IMP:BHF-UCL.
GO; GO:0043277; P:apoptotic cell clearance; IMP:MGI.
GO; GO:0003279; P:cardiac septum development; IMP:MGI.
GO; GO:0008283; P:cell proliferation; ISO:MGI.
GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; IMP:BHF-UCL.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IMP:BHF-UCL.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:MGI.
GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
GO; GO:0032370; P:positive regulation of lipid transport; IMP:BHF-UCL.
GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; ISO:MGI.
GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
GO; GO:0051222; P:positive regulation of protein transport; ISO:MGI.
GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:BHF-UCL.
GO; GO:0032374; P:regulation of cholesterol transport; IMP:BHF-UCL.
GO; GO:0032429; P:regulation of phospholipase A2 activity; IMP:BHF-UCL.
GO; GO:0045056; P:transcytosis; ISO:MGI.
CDD; cd00112; LDLa; 31.
Gene3D; 2.120.10.30; -; 8.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR026823; cEGF.
InterPro; IPR032485; DUF5050.
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; 1.
Pfam; PF16472; DUF5050; 1.
Pfam; PF00008; EGF; 1.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00057; Ldl_recept_a; 30.
Pfam; PF00058; Ldl_recept_b; 12.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 26.
SMART; SM00179; EGF_CA; 7.
SMART; SM00192; LDLa; 31.
SMART; SM00135; LY; 35.
SUPFAM; SSF57184; SSF57184; 4.
SUPFAM; SSF57424; SSF57424; 30.
PROSITE; PS00010; ASX_HYDROXYL; 3.
PROSITE; PS00022; EGF_1; 5.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 6.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS01209; LDLRA_1; 27.
PROSITE; PS50068; LDLRA_2; 31.
PROSITE; PS51120; LDLRB; 34.
1: Evidence at protein level;
Acetylation; Calcium; Cell membrane; Coated pit; Complete proteome;
Cytoplasm; Developmental protein; Disulfide bond; EGF-like domain;
Endocytosis; Glycoprotein; Membrane; Metal-binding; Nucleus;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 4545 Prolow-density lipoprotein receptor-
related protein 1.
/FTId=PRO_0000273273.
CHAIN 20 ?3944 Low-density lipoprotein receptor-related
protein 1 515 kDa subunit.
/FTId=PRO_0000302753.
CHAIN ?3945 4545 Low-density lipoprotein receptor-related
protein 1 85 kDa subunit.
/FTId=PRO_0000302754.
CHAIN ?4442 4545 Low-density lipoprotein receptor-related
protein 1 intracellular domain.
/FTId=PRO_0000302755.
TOPO_DOM 20 4424 Extracellular. {ECO:0000255}.
TRANSMEM 4425 4445 Helical. {ECO:0000255}.
TOPO_DOM 4446 4545 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 67 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 71 111 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 112 150 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 151 190 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 293 335 LDL-receptor class B 1. {ECO:0000255}.
REPEAT 336 379 LDL-receptor class B 2. {ECO:0000255}.
REPEAT 380 423 LDL-receptor class B 3. {ECO:0000255}.
DOMAIN 475 521 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 572 614 LDL-receptor class B 4. {ECO:0000255}.
REPEAT 615 660 LDL-receptor class B 5. {ECO:0000255}.
REPEAT 661 711 LDL-receptor class B 6. {ECO:0000255}.
REPEAT 712 755 LDL-receptor class B 7. {ECO:0000255}.
DOMAIN 804 844 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 853 893 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 894 934 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 935 974 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 975 1014 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1014 1054 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1061 1100 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1103 1143 LDL-receptor class A 9.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1144 1183 LDL-receptor class A 10.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1184 1223 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1224 1263 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1310 1356 LDL-receptor class B 8. {ECO:0000255}.
REPEAT 1357 1399 LDL-receptor class B 9. {ECO:0000255}.
REPEAT 1400 1446 LDL-receptor class B 10. {ECO:0000255}.
REPEAT 1447 1491 LDL-receptor class B 11. {ECO:0000255}.
REPEAT 1492 1532 LDL-receptor class B 12. {ECO:0000255}.
DOMAIN 1537 1580 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1628 1670 LDL-receptor class B 13. {ECO:0000255}.
REPEAT 1671 1714 LDL-receptor class B 14. {ECO:0000255}.
REPEAT 1715 1754 LDL-receptor class B 15. {ECO:0000255}.
REPEAT 1755 1799 LDL-receptor class B 16. {ECO:0000255}.
DOMAIN 1847 1888 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1935 1977 LDL-receptor class B 17. {ECO:0000255}.
REPEAT 1978 2020 LDL-receptor class B 18. {ECO:0000255}.
REPEAT 2021 2064 LDL-receptor class B 19. {ECO:0000255}.
REPEAT 2065 2108 LDL-receptor class B 20. {ECO:0000255}.
DOMAIN 2156 2196 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 2254 2295 LDL-receptor class B 21. {ECO:0000255}.
REPEAT 2296 2344 LDL-receptor class B 22. {ECO:0000255}.
REPEAT 2345 2389 LDL-receptor class B 23. {ECO:0000255}.
REPEAT 2390 2432 LDL-receptor class B 24. {ECO:0000255}.
REPEAT 2433 2474 LDL-receptor class B 25. {ECO:0000255}.
DOMAIN 2479 2519 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2523 2564 LDL-receptor class A 11.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2565 2603 LDL-receptor class A 12.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2604 2642 LDL-receptor class A 13.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2643 2691 LDL-receptor class A 14.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2695 2733 LDL-receptor class A 15.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2733 2772 LDL-receptor class A 16.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2773 2815 LDL-receptor class A 17.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2817 2856 LDL-receptor class A 18.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2857 2900 LDL-receptor class A 19.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2903 2941 LDL-receptor class A 20.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2942 2982 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2983 3023 EGF-like 12; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 3070 3114 LDL-receptor class B 26. {ECO:0000255}.
REPEAT 3115 3157 LDL-receptor class B 27. {ECO:0000255}.
REPEAT 3158 3201 LDL-receptor class B 28. {ECO:0000255}.
REPEAT 3202 3244 LDL-receptor class B 29. {ECO:0000255}.
REPEAT 3245 3285 LDL-receptor class B 30. {ECO:0000255}.
DOMAIN 3291 3332 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3333 3372 LDL-receptor class A 21.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3373 3411 LDL-receptor class A 22.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3412 3451 LDL-receptor class A 23.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3452 3492 LDL-receptor class A 24.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3493 3534 LDL-receptor class A 25.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3535 3573 LDL-receptor class A 26.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3574 3612 LDL-receptor class A 27.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3612 3650 LDL-receptor class A 28.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3653 3693 LDL-receptor class A 29.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3694 3734 LDL-receptor class A 30.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3740 3779 LDL-receptor class A 31.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3782 3824 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3825 3862 EGF-like 15. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 3913 3955 LDL-receptor class B 31. {ECO:0000255}.
REPEAT 3971 4013 LDL-receptor class B 32. {ECO:0000255}.
REPEAT 4014 4057 LDL-receptor class B 33. {ECO:0000255}.
REPEAT 4058 4102 LDL-receptor class B 34. {ECO:0000255}.
DOMAIN 4148 4184 EGF-like 16. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4197 4233 EGF-like 17. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4233 4269 EGF-like 18. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4269 4305 EGF-like 19. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4305 4341 EGF-like 20. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4341 4376 EGF-like 21. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4374 4410 EGF-like 22. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 4446 4545 Interaction with MAFB.
{ECO:0000269|PubMed:15135046}.
MOTIF 3941 3944 Recognition site for proteolytical
processing. {ECO:0000255}.
MOTIF 4503 4508 NPXY motif.
METAL 872 872 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 875 875 Calcium 1. {ECO:0000250}.
METAL 877 877 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 879 879 Calcium 1. {ECO:0000250}.
METAL 885 885 Calcium 1. {ECO:0000250}.
METAL 886 886 Calcium 1. {ECO:0000250}.
METAL 1033 1033 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 1036 1036 Calcium 2. {ECO:0000250}.
METAL 1038 1038 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 1040 1040 Calcium 2. {ECO:0000250}.
METAL 1046 1046 Calcium 2. {ECO:0000250}.
METAL 1047 1047 Calcium 2. {ECO:0000250}.
METAL 1081 1081 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 1084 1084 Calcium 3. {ECO:0000250}.
METAL 1086 1086 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 1088 1088 Calcium 3. {ECO:0000250}.
METAL 1094 1094 Calcium 3. {ECO:0000250}.
METAL 1095 1095 Calcium 3. {ECO:0000250}.
MOD_RES 2010 2010 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 4461 4461 Phosphothreonine.
{ECO:0000250|UniProtKB:Q07954}.
MOD_RES 4508 4508 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q07954}.
MOD_RES 4518 4518 Phosphoserine.
{ECO:0000250|UniProtKB:Q07954}.
MOD_RES 4521 4521 Phosphoserine.
{ECO:0000250|UniProtKB:Q07954}.
MOD_RES 4524 4524 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 447 447 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 730 730 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 929 929 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1051 1051 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1155 1155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1156 1156 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1196 1196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1219 1219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1512 1512 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1559 1559 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1576 1576 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1617 1617 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1646 1646 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1724 1724 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1734 1734 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1764 1764 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1826 1826 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1934 1934 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1996 1996 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2049 2049 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2118 2118 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2128 2128 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 2473 2473 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2503 2503 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2522 2522 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2602 2602 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2621 2621 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2639 2639 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2816 2816 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2906 2906 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3049 3049 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 3090 3090 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3265 3265 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3334 3334 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3489 3489 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3663 3663 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3789 3789 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3840 3840 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3954 3954 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4076 4076 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4126 4126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4180 4180 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4279 4279 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4280 4280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4365 4365 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 41 {ECO:0000250|UniProtKB:P01130}.
DISULFID 35 54 {ECO:0000250|UniProtKB:P01130}.
DISULFID 48 65 {ECO:0000250|UniProtKB:P01130}.
DISULFID 73 86 {ECO:0000250|UniProtKB:P01130}.
DISULFID 80 99 {ECO:0000250|UniProtKB:P01130}.
DISULFID 93 109 {ECO:0000250|UniProtKB:P01130}.
DISULFID 116 125 {ECO:0000250|UniProtKB:P01130}.
DISULFID 121 134 {ECO:0000250|UniProtKB:P01130}.
DISULFID 136 149 {ECO:0000250|UniProtKB:P01130}.
DISULFID 155 165 {ECO:0000250|UniProtKB:P01130}.
DISULFID 161 174 {ECO:0000250|UniProtKB:P01130}.
DISULFID 176 189 {ECO:0000250|UniProtKB:P01130}.
DISULFID 479 494 {ECO:0000250|UniProtKB:P01130}.
DISULFID 490 505 {ECO:0000250|UniProtKB:P01130}.
DISULFID 507 520 {ECO:0000250|UniProtKB:P01130}.
DISULFID 808 819 {ECO:0000250|UniProtKB:P01130}.
DISULFID 815 828 {ECO:0000250|UniProtKB:P01130}.
DISULFID 830 843 {ECO:0000250|UniProtKB:P01130}.
DISULFID 855 867 {ECO:0000250|UniProtKB:Q07954}.
DISULFID 862 880 {ECO:0000250|UniProtKB:Q07954}.
DISULFID 874 891 {ECO:0000250|UniProtKB:Q07954}.
DISULFID 896 908 {ECO:0000250|UniProtKB:P01130}.
DISULFID 903 921 {ECO:0000250|UniProtKB:P01130}.
DISULFID 915 932 {ECO:0000250|UniProtKB:P01130}.
DISULFID 937 949 {ECO:0000250|UniProtKB:P01130}.
DISULFID 944 962 {ECO:0000250|UniProtKB:P01130}.
DISULFID 956 972 {ECO:0000250|UniProtKB:P01130}.
DISULFID 977 990 {ECO:0000250|UniProtKB:P01130}.
DISULFID 985 1003 {ECO:0000250|UniProtKB:P01130}.
DISULFID 997 1012 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1016 1028 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1023 1041 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1035 1052 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1063 1076 {ECO:0000250|UniProtKB:Q07954}.
DISULFID 1070 1089 {ECO:0000250|UniProtKB:Q07954}.
DISULFID 1083 1098 {ECO:0000250|UniProtKB:Q07954}.
DISULFID 1105 1119 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1113 1132 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1126 1141 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1146 1160 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1153 1173 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1167 1183 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1186 1197 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1193 1207 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1209 1222 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1228 1238 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1234 1247 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1249 1262 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1541 1554 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1550 1564 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1566 1579 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1851 1862 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1858 1872 {ECO:0000250|UniProtKB:P01130}.
DISULFID 1874 1887 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2160 2171 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2167 2181 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2183 2195 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2483 2494 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2490 2504 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2506 2518 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2525 2538 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2533 2551 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2545 2562 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2567 2579 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2574 2592 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2586 2601 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2606 2618 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2613 2631 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2625 2640 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2645 2667 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2661 2680 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2674 2689 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2697 2709 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2704 2722 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2716 2731 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2735 2747 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2742 2760 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2754 2770 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2775 2788 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2782 2801 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2795 2813 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2819 2831 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2826 2844 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2838 2854 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2859 2871 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2866 2885 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2879 2898 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2905 2918 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2913 2931 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2925 2940 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2945 2957 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2953 2966 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2968 2981 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2987 2997 {ECO:0000250|UniProtKB:P01130}.
DISULFID 2993 3006 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3008 3022 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3295 3306 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3302 3316 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3318 3331 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3335 3347 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3342 3360 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3354 3370 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3375 3387 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3382 3400 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3394 3409 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3414 3427 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3421 3440 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3434 3449 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3454 3467 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3461 3480 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3474 3490 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3495 3508 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3502 3521 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3515 3532 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3537 3549 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3544 3562 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3556 3571 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3576 3588 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3583 3601 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3595 3610 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3614 3626 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3621 3639 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3633 3648 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3655 3667 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3662 3680 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3674 3691 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3696 3710 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3704 3723 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3717 3732 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3742 3755 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3750 3768 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3762 3777 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3786 3799 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3793 3808 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3810 3823 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3829 3839 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3835 3848 {ECO:0000250|UniProtKB:P01130}.
DISULFID 3850 3861 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4152 4161 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4157 4170 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4172 4183 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4201 4211 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4205 4221 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4223 4232 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4237 4247 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4241 4257 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4259 4268 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4273 4283 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4277 4293 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4295 4304 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4309 4319 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4313 4329 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4331 4340 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4345 4353 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4348 4364 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4366 4375 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4378 4388 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4382 4398 {ECO:0000250|UniProtKB:P01130}.
DISULFID 4400 4409 {ECO:0000250|UniProtKB:P01130}.
CONFLICT 2642 2642 A -> T (in Ref. 2; AAL09567).
{ECO:0000305}.
SEQUENCE 4545 AA; 504742 MW; 9904CF5DF5EE333E CRC64;
MLTPPLLLLL PLLSALVSGA TMDAPKTCSP KQFACRDQIT CISKGWRCDG ERDCPDGSDE
APEICPQSKA QRCPPNEHSC LGTELCVPMS RLCNGIQDCM DGSDEGAHCR ELRANCSRMG
CQHHCVPTPS GPTCYCNSSF QLQADGKTCK DFDECSVYGT CSQLCTNTDG SFTCGCVEGY
LLQPDNRSCK AKNEPVDRPP VLLIANSQNI LATYLSGAQV STITPTSTRQ TTAMDFSYAN
ETVCWVHVGD SAAQTQLKCA RMPGLKGFVD EHTINISLSL HHVEQMAIDW LTGNFYFVDD
IDDRIFVCNR NGDTCVTLLD LELYNPKGIA LDPAMGKVFF TDYGQIPKVE RCDMDGQNRT
KLVDSKIVFP HGITLDLVSR LVYWADAYLD YIEVVDYEGK GRQTIIQGIL IEHLYGLTVF
ENYLYATNSD NANTQQKTSV IRVNRFNSTE YQVVTRVDKG GALHIYHQRR QPRVRSHACE
NDQYGKPGGC SDICLLANSH KARTCRCRSG FSLGSDGKSC KKPEHELFLV YGKGRPGIIR
GMDMGAKVPD EHMIPIENLM NPRALDFHAE TGFIYFADTT SYLIGRQKID GTERETILKD
GIHNVEGVAV DWMGDNLYWT DDGPKKTISV ARLEKAAQTR KTLIEGKMTH PRAIVVDPLN
GWMYWTDWEE DPKDSRRGRL ERAWMDGSHR DIFVTSKTVL WPNGLSLDIP AGRLYWVDAF
YDRIETILLN GTDRKIVYEG PELNHAFGLC HHGNYLFWTE YRSGSVYRLE RGVAGAPPTV
TLLRSERPPI FEIRMYDAQQ QQVGTNKCRV NNGGCSSLCL ATPGSRQCAC AEDQVLDTDG
VTCLANPSYV PPPQCQPGEF ACANNRCIQE RWKCDGDNDC LDNSDEAPAL CHQHTCPSDR
FKCENNRCIP NRWLCDGDND CGNSEDESNA TCSARTCPPN QFSCASGRCI PISWTCDLDD
DCGDRSDESA SCAYPTCFPL TQFTCNNGRC ININWRCDND NDCGDNSDEA GCSHSCSSTQ
FKCNSGRCIP EHWTCDGDND CGDYSDETHA NCTNQATRPP GGCHSDEFQC RLDGLCIPLR
WRCDGDTDCM DSSDEKSCEG VTHVCDPNVK FGCKDSARCI SKAWVCDGDS DCEDNSDEEN
CEALACRPPS HPCANNTSVC LPPDKLCDGK DDCGDGSDEG ELCDQCSLNN GGCSHNCSVA
PGEGIVCSCP LGMELGSDNH TCQIQSYCAK HLKCSQKCDQ NKFSVKCSCY EGWVLEPDGE
SCRSLDPFKP FIIFSNRHEI RRIDLHKGDY SVLVPGLRNT IALDFHLSQS ALYWTDVVED
KIYRGKLLDN GALTSFEVVI QYGLATPEGL AVDWIAGNIY WVESNLDQIE VAKLDGTLRT
TLLAGDIEHP RAIALDPRDG ILFWTDWDAS LPRIEAASMS GAGRRTIHRE TGSGGWPNGL
TVDYLEKRIL WIDARSDAIY SARYDGSGHM EVLRGHEFLS HPFAVTLYGG EVYWTDWRTN
TLAKANKWTG HNVTVVQRTN TQPFDLQVYH PSRQPMAPNP CEANGGRGPC SHLCLINYNR
TVSCACPHLM KLHKDNTTCY EFKKFLLYAR QMEIRGVDLD APYYNYIISF TVPDIDNVTV
LDYDAREQRV YWSDVRTQAI KRAFINGTGV ETVVSADLPN AHGLAVDWVS RNLFWTSYDT
NKKQINVARL DGSFKNAVVQ GLEQPHGLVV HPLRGKLYWT DGDNISMANM DGSNHTLLFS
GQKGPVGLAI DFPESKLYWI SSGNHTINRC NLDGSELEVI DTMRSQLGKA TALAIMGDKL
WWADQVSEKM GTCNKADGSG SVVLRNSTTL VMHMKVYDES IQLEHEGTNP CSVNNGDCSQ
LCLPTSETTR SCMCTAGYSL RSGQQACEGV GSFLLYSVHE GIRGIPLDPN DKSDALVPVS
GTSLAVGIDF HAENDTIYWV DMGLSTISRA KRDQTWREDV VTNGIGRVEG IAVDWIAGNI
YWTDQGFDVI EVARLNGSFR YVVISQGLDK PRAITVHPEK GYLFWTEWGH YPRIERSRLD
GTERVVLVNV SISWPNGISV DYQGGKLYWC DARMDKIERI DLETGENREV VLSSNNMDMF
SVSVFEDFIY WSDRTHANGS IKRGCKDNAT DSVPLRTGIG VQLKDIKVFN RDRQKGTNVC
AVANGGCQQL CLYRGGGQRA CACAHGMLAE DGASCREYAG YLLYSERTIL KSIHLSDERN
LNAPVQPFED PEHMKNVIAL AFDYRAGTSP GTPNRIFFSD IHFGNIQQIN DDGSGRTTIV
ENVGSVEGLA YHRGWDTLYW TSYTTSTITR HTVDQTRPGA FERETVITMS GDDHPRAFVL
DECQNLMFWT NWNELHPSIM RAALSGANVL TLIEKDIRTP NGLAIDHRAE KLYFSDATLD
KIERCEYDGS HRYVILKSEP VHPFGLAVYG EHIFWTDWVR RAVQRANKYV GSDMKLLRVD
IPQQPMGIIA VANDTNSCEL SPCRINNGGC QDLCLLTHQG HVNCSCRGGR ILQEDFTCRA
VNSSCRAQDE FECANGECIS FSLTCDGVSH CKDKSDEKPS YCNSRRCKKT FRQCNNGRCV
SNMLWCNGVD DCGDGSDEIP CNKTACGVGE FRCRDGSCIG NSSRCNQFVD CEDASDEMNC
SATDCSSYFR LGVKGVLFQP CERTSLCYAP SWVCDGANDC GDYSDERDCP GVKRPRCPLN
YFACPSGRCI PMSWTCDKED DCENGEDETH CNKFCSEAQF ECQNHRCISK QWLCDGSDDC
GDGSDEAAHC EGKTCGPSSF SCPGTHVCVP ERWLCDGDKD CTDGADESVT AGCLYNSTCD
DREFMCQNRL CIPKHFVCDH DRDCADGSDE SPECEYPTCG PNEFRCANGR CLSSRQWECD
GENDCHDHSD EAPKNPHCTS PEHKCNASSQ FLCSSGRCVA EALLCNGQDD CGDGSDERGC
HVNECLSRKL SGCSQDCEDL KIGFKCRCRP GFRLKDDGRT CADLDECSTT FPCSQLCINT
HGSYKCLCVE GYAPRGGDPH SCKAVTDEEP FLIFANRYYL RKLNLDGSNY TLLKQGLNNA
VALDFDYREQ MIYWTDVTTQ GSMIRRMHLN GSNVQVLHRT GLSNPDGLAV DWVGGNLYWC
DKGRDTIEVS KLNGAYRTVL VSSGLREPRA LVVDVQNGYL YWTDWGDHSL IGRIGMDGSG
RSIIVDTKIT WPNGLTVDYV TERIYWADAR EDYIEFASLD GSNRHVVLSQ DIPHIFALTL
FEDYVYWTDW ETKSINRAHK TTGANKTLLI STLHRPMDLH VFHALRQPDV PNHPCKVNNG
GCSNLCLLSP GGGHKCACPT NFYLGGDGRT CVSNCTASQF VCKNDKCIPF WWKCDTEDDC
GDHSDEPPDC PEFKCRPGQF QCSTGICTNP AFICDGDNDC QDNSDEANCD IHVCLPSQFK
CTNTNRCIPG IFRCNGQDNC GDGEDERDCP EVTCAPNQFQ CSITKRCIPR VWVCDRDNDC
VDGSDEPANC TQMTCGVDEF RCKDSGRCIP ARWKCDGEDD CGDGSDEPKE ECDERTCEPY
QFRCKNNRCV PGRWQCDYDN DCGDNSDEES CTPRPCSESE FSCANGRCIA GRWKCDGDHD
CADGSDEKDC TPRCDMDQFQ CKSGHCIPLR WRCDADADCM DGSDEEACGT GVRTCPLDEF
QCNNTLCKPL AWKCDGEDDC GDNSDENPEE CARFICPPNR PFRCKNDRVC LWIGRQCDGV
DNCGDGTDEE DCEPPTAQNP HCKDKKEFLC RNQRCLSSSL RCNMFDDCGD GSDEEDCSID
PKLTSCATNA SMCGDEARCV RTEKAAYCAC RSGFHTVPGQ PGCQDINECL RFGTCSQLCN
NTKGGHLCSC ARNFMKTHNT CKAEGSEYQV LYIADDNEIR SLFPGHPHSA YEQTFQGDES
VRIDAMDVHV KAGRVYWTNW HTGTISYRSL PPAAPPTTSN RHRRQIDRGV THLNISGLKM
PRGIAIDWVA GNVYWTDSGR DVIEVAQMKG ENRKTLISGM IDEPHAIVVD PLRGTMYWSD
WGNHPKIETA AMDGTLRETL VQDNIQWPTG LAVDYHNERL YWADAKLSVI GSIRLNGTDP
IVAADSKRGL SHPFSIDVFE DYIYGVTYIN NRVFKIHKFG HSPLINLTGG LSHASDVVLY
HQHKQPEVTN PCDRKKCEWL CLLSPSGPVC TCPNGKRLDN GTCVPVPSPT PPPDAPRPGT
CTLQCFNGGS CFLNARRQPK CRCQPRYTGD KCELDQCWEY CHNGGTCAAS PSGMPTCRCP
TGFTGPKCTA QVCAGYCSNN STCTVNQGNQ PQCRCLPGFL GDRCQYRQCS GFCENFGTCQ
MAADGSRQCR CTVYFEGPRC EVNKCSRCLQ GACVVNKQTG DVTCNCTDGR VAPSCLTCID
HCSNGGSCTM NSKMMPECQC PPHMTGPRCE EQVVSQQQPG HMASILIPLL LLLLLLLVAG
VVFWYKRRVR GAKGFQHQRM TNGAMNVEIG NPTYKMYEGG EPDDVGGLLD ADFALDPDKP
TNFTNPVYAT LYMGGHGSRH SLASTDEKRE LLGRGPEDEI GDPLA


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