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

 LRP2_PIG                Reviewed;        4652 AA.
C0HL13;
25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
25-OCT-2017, sequence version 1.
23-MAY-2018, entry version 5.
RecName: Full=Low-density lipoprotein receptor-related protein 2 {ECO:0000303|PubMed:9228033};
Short=LRP-2 {ECO:0000303|PubMed:9228033};
AltName: Full=Glycoprotein 330 {ECO:0000250|UniProtKB:P98158};
Short=gp330 {ECO:0000250|UniProtKB:P98158};
AltName: Full=Megalin {ECO:0000303|PubMed:9228033};
Flags: Precursor;
Name=LRP2 {ECO:0000250|UniProtKB:P98164};
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Porcine genome sequencing project;
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000305}
FUNCTION, AND INTERACTION WITH BETA-AMYLOID PEPTIDE 40 IN COMPLEX WITH
CLU.
PubMed=9228033;
Hammad S.M., Ranganathan S., Loukinova E., Twal W.O., Argraves W.S.;
"Interaction of apolipoprotein J-amyloid beta-peptide complex with low
density lipoprotein receptor-related protein-2/megalin. A mechanism to
prevent pathological accumulation of amyloid beta-peptide.";
J. Biol. Chem. 272:18644-18649(1997).
[3] {ECO:0000305}
INTERACTION WITH SHH.
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).
-!- FUNCTION: Multiligand endocytic receptor (By similarity). 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
(By similarity). 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 (By similarity). 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 (By
similarity). 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 (By
similarity). Together with CUBN, mediates renal reabsorption of
myoglobin (By similarity). Mediates renal uptake and subsequent
lysosomal degradation of APOM (By similarity). 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 (By similarity). Mediates
endocytosis of Sonic hedgehog protein N-product (ShhN), the active
product of SHH (By similarity). Also mediates ShhN transcytosis
(By similarity). 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 (By similarity). 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 (By similarity). Mediates endocytosis
of angiotensin-2 (By similarity). Also mediates endocytosis of
angiotensis 1-7 (By similarity). Binds to the complex composed of
beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis
and lysosomal degradation (PubMed:9228033). Required for embryonic
heart development (By similarity). Required for normal hearing,
possibly through interaction with estrogen in the inner ear (By
similarity). {ECO:0000250|UniProtKB:A2ARV4,
ECO:0000250|UniProtKB:P98158, ECO:0000250|UniProtKB:P98164,
ECO:0000269|PubMed:9228033}.
-!- 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 (By similarity). Forms a
multimeric complex together with LRPAP1 (By similarity). Interacts
(via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (By
similarity). Interacts with LRP2BP (By similarity). Interacts (via
NPXY motif) with DAB2; the interaction is not affected by tyrosine
phosphorylation of the NPXY motif (By similarity). Interacts with
MB (By similarity). Interacts with BMP4 (By similarity). Interacts
with the Sonic hedgehog protein N-product which is the active
product of SHH (PubMed:11964399). Interacts with CST3 in a
calcium-dependent manner (By similarity). Interacts with the
vitamin-D binding protein GC/DBP (By similarity). Interacts with
sex hormone-binding protein SHBG (By similarity). 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 (By
similarity). Interacts with ALB (By similarity). Interacts with
the antiapoptotic protein BIRC5/survivin (By similarity).
Interacts with matrix metalloproteinase MMP2 in complex with
metalloproteinase inhibitor TIMP1 (By similarity). 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 (By similarity). Does not interact
with beta-amyloid protein 40 alone but interacts with the complex
composed of beta-amyloid protein 40 and CLU/APOJ (PubMed:9228033).
{ECO:0000250|UniProtKB:A2ARV4, ECO:0000250|UniProtKB:P98158,
ECO:0000250|UniProtKB:P98164, ECO:0000269|PubMed:11964399,
ECO:0000269|PubMed:9228033}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000250|UniProtKB:P98158}; Single-pass type I membrane
protein {ECO:0000255}. Endosome lumen
{ECO:0000250|UniProtKB:P98158}. 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. In the endolymphatic sac of the inner
ear, located in the lumen of endosomes as a soluble form.
{ECO:0000250|UniProtKB:P98158}.
-!- DOMAIN: Two overlapping PxLPxI/L motifs mediate interaction with
ankyrin repeats of ANKRA2. {ECO:0000250|UniProtKB:P98158}.
-!- DOMAIN: The cytoplasmic domain is required for sorting to the
apical cell membrane. {ECO:0000250|UniProtKB:P98158}.
-!- 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:0000250|UniProtKB:P98158}.
-!- 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; GL881906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
UniGene; Ssc.4289; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:ARUK-UCL.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0035258; F:steroid hormone receptor binding; ISS:UniProtKB.
GO; GO:0060982; P:coronary artery morphogenesis; ISS:UniProtKB.
GO; GO:1904447; P:folate import across plasma membrane; ISS:UniProtKB.
GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
GO; GO:0030001; P:metal ion transport; ISS:UniProtKB.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
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:1905167; P:positive regulation of lysosomal protein catabolic process; IDA:ARUK-UCL.
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; IGI:ARUK-UCL.
GO; GO:0003139; P:secondary heart field specification; ISS:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
GO; GO:0060068; P:vagina development; ISS:UniProtKB.
GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:UniProtKB.
CDD; cd00112; LDLa; 35.
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; 1.
Pfam; PF07645; EGF_CA; 2.
Pfam; PF00057; Ldl_recept_a; 35.
Pfam; PF00058; Ldl_recept_b; 15.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 27.
SMART; SM00179; EGF_CA; 10.
SMART; SM00192; LDLa; 36.
SMART; SM00135; LY; 38.
SUPFAM; SSF57184; SSF57184; 4.
SUPFAM; SSF57424; SSF57424; 36.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 5.
PROSITE; PS01187; EGF_CA; 3.
PROSITE; PS01209; LDLRA_1; 29.
PROSITE; PS50068; LDLRA_2; 36.
PROSITE; PS51120; LDLRB; 35.
1: Evidence at protein level;
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 4652 Low-density lipoprotein receptor-related
protein 2. {ECO:0000255}.
/FTId=PRO_0000441957.
TOPO_DOM 26 4422 Extracellular. {ECO:0000305}.
TRANSMEM 4423 4443 Helical. {ECO:0000255}.
TOPO_DOM 4444 4652 Cytoplasmic. {ECO:0000305}.
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 108 144 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 142 181 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 183 219 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 223 259 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 267 308 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 348 386 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 436 478 LDL-receptor class B 1.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 479 521 LDL-receptor class B 2.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 522 568 LDL-receptor class B 3.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 569 613 LDL-receptor class B 4.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 753 795 LDL-receptor class B 5.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 796 837 LDL-receptor class B 6.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 838 881 LDL-receptor class B 7.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 882 925 LDL-receptor class B 8.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 1025 1061 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1066 1104 LDL-receptor class A 9.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1110 1146 LDL-receptor class A 10.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1150 1186 LDL-receptor class A 11.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1188 1225 LDL-receptor class A 12.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1231 1269 LDL-receptor class A 13.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1272 1308 LDL-receptor class A 14.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1313 1351 LDL-receptor class A 15.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
REPEAT 1480 1522 LDL-receptor class B 9.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1523 1565 LDL-receptor class B 10.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1568 1611 LDL-receptor class B 11.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1612 1654 LDL-receptor class B 12.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1655 1696 LDL-receptor class B 13.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1789 1831 LDL-receptor class B 14.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1832 1881 LDL-receptor class B 15.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1882 1929 LDL-receptor class B 16.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1930 1971 LDL-receptor class B 17.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1972 2012 LDL-receptor class B 18.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2105 2154 LDL-receptor class B 19.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2155 2199 LDL-receptor class B 20.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2200 2243 LDL-receptor class B 21.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2244 2287 LDL-receptor class B 22.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2429 2475 LDL-receptor class B 23.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2476 2516 LDL-receptor class B 24.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2517 2560 LDL-receptor class B 25.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2561 2602 LDL-receptor class B 26.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2603 2644 LDL-receptor class B 27.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 2696 2734 LDL-receptor class A 16.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2737 2773 LDL-receptor class A 17.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2776 2815 LDL-receptor class A 18.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2818 2857 LDL-receptor class A 19.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2860 2897 LDL-receptor class A 20.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2902 2941 LDL-receptor class A 21.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2944 2986 LDL-receptor class A 22.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2989 3025 LDL-receptor class A 23.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3028 3066 LDL-receptor class A 24.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3071 3107 LDL-receptor class A 25.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3149 3189 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 3236 3278 LDL-receptor class B 28.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3279 3321 LDL-receptor class B 29.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3330 3373 LDL-receptor class B 30.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3374 3417 LDL-receptor class B 31.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3418 3458 LDL-receptor class B 32.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 3509 3547 LDL-receptor class A 26.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3550 3588 LDL-receptor class A 27.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3591 3629 LDL-receptor class A 28.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3632 3670 LDL-receptor class A 29.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3675 3713 LDL-receptor class A 30.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3716 3753 LDL-receptor class A 31.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3756 3792 LDL-receptor class A 32.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3795 3831 LDL-receptor class A 33.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3839 3877 LDL-receptor class A 34.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3880 3919 LDL-receptor class A 35.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3925 3961 LDL-receptor class A 36.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3964 4004 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4005 4046 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 4152 4194 LDL-receptor class B 33.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 4195 4238 LDL-receptor class B 34.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 4240 4281 LDL-receptor class B 35.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 4375 4409 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 4588 4601 Interaction with DAB2.
{ECO:0000250|UniProtKB:P98164}.
MOTIF 4450 4459 SH3-binding. {ECO:0000255}.
MOTIF 4453 4458 PxLPxI/L motif 1; mediates interaction
with ANKRA2.
{ECO:0000250|UniProtKB:P98158}.
MOTIF 4456 4461 PxLPxI/L motif 2; mediates interaction
with ANKRA2.
{ECO:0000250|UniProtKB:P98158}.
MOTIF 4518 4523 Endocytosis signal. {ECO:0000255}.
MOTIF 4594 4597 NPXY motif. {ECO:0000255}.
MOTIF 4597 4600 SH2-binding. {ECO:0000255}.
MOTIF 4610 4621 SH3-binding. {ECO:0000255}.
METAL 1128 1128 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98164}.
METAL 1131 1131 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1133 1133 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98164}.
METAL 1135 1135 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1141 1141 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1142 1142 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1207 1207 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98158}.
METAL 1210 1210 Calcium. {ECO:0000250|UniProtKB:P98158}.
METAL 1212 1212 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98158}.
METAL 1214 1214 Calcium. {ECO:0000250|UniProtKB:P98158}.
METAL 1220 1220 Calcium. {ECO:0000250|UniProtKB:P98158}.
METAL 1221 1221 Calcium. {ECO:0000250|UniProtKB:P98158}.
MOD_RES 4460 4460 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4568 4568 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4615 4615 Phosphoserine.
{ECO:0000250|UniProtKB:P98158}.
MOD_RES 4629 4629 Phosphothreonine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4650 4650 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARV4}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 388 388 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 771 771 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 866 866 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1015 1015 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1064 1064 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1102 1102 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1188 1188 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1329 1329 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1385 1385 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1452 1452 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1498 1498 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1552 1552 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1677 1677 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1809 1809 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2053 2053 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2175 2175 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2222 2222 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2485 2485 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2698 2698 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2778 2778 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2806 2806 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2807 2807 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2944 2944 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2984 2984 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2989 2989 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3122 3122 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3208 3208 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3254 3254 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3312 3312 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3352 3352 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3435 3435 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3444 3444 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3562 3562 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3678 3678 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3878 3878 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 3976 3976 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 4066 4066 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 4325 4325 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
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 109 121 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 116 134 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 128 143 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 143 158 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 153 171 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 165 180 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 184 196 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 191 209 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 203 218 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 224 236 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 231 249 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 243 258 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 268 281 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 275 294 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 288 307 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 352 362 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 358 371 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 373 385 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1026 1038 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1033 1051 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1045 1060 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1067 1081 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1074 1094 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1088 1103 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1111 1123 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1118 1136 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1130 1145 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1151 1163 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1158 1176 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1170 1185 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1189 1202 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1196 1215 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1209 1224 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1232 1245 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1239 1258 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1252 1268 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1273 1285 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1280 1298 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1292 1307 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1314 1327 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1321 1340 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1334 1350 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2697 2709 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2704 2722 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2716 2733 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2738 2750 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2745 2763 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2757 2772 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2777 2790 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2785 2803 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2797 2814 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2819 2832 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2826 2845 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2839 2856 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2861 2873 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2868 2886 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2880 2896 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2903 2915 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2910 2928 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2922 2940 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2945 2962 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2952 2975 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2969 2985 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2990 3002 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2997 3015 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3009 3024 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3029 3041 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3036 3054 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3048 3065 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3072 3084 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3079 3097 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3091 3106 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3153 3164 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3160 3173 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3175 3188 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3510 3523 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3517 3536 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3530 3546 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3551 3563 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3558 3576 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3570 3587 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3592 3604 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3599 3617 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3611 3628 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3633 3645 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3640 3658 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3652 3669 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3676 3690 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3684 3703 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3697 3712 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3717 3730 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3725 3743 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3737 3752 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3757 3769 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3764 3782 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3776 3791 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3796 3808 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3803 3821 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3815 3830 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3840 3852 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3847 3865 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3859 3876 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3881 3894 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3889 3907 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3901 3918 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3926 3938 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3933 3951 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3945 3960 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3968 3977 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3973 3987 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3989 4003 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4009 4019 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4015 4028 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4030 4045 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4379 4387 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4381 4397 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4399 4408 {ECO:0000255|PROSITE-ProRule:PRU00076}.
SEQUENCE 4652 AA; 521302 MW; A512AC3DEDFC535C CRC64;
MERWAAAAAC TLLLAFAACL APASGRECLG NEFRCSNGHC ITESWRCDGT RDCLDGSDEI
GCPPSTCGST QFHCENEDVC IPLYWVCDGE EDCSNGADEH QRCPPGRTCS SHHFTCTNGE
CIPVEYRCDH STDCLDGTDE INCRYPVCQQ QTCHNGACYN TSQRCDGEID CRDASDELNC
TQRCLRNEFQ CGSGECIPRD YVCDHDPDCS DSSDEHSCSV YQPCKGNEFA CSNGFCINQN
WVCDGMADCL DNSDEDGCES SIIRTHECYP NEWACPEDGK CIPLSRVCDG IADCPRGGDE
NKQGRVCDVN MCPSLGCEYQ CHKSPSGGTC NCPPGFIVNK NNTRSCVDFN DCQIWGICDH
FCEDRIGHHQ CFCAEGYVLE HEQHCRANSS SGQAFVIFSN GRNLLLGDIQ GQSFEYLVRS
QNRGSPVGVD FHYRLSKVFW TDTMQNKVFS LDIDGLVIRE VLSVSIEDPE NLAVDWINNK
LYIVETNVNR IDLANLDGSH RITLITENLG RPRGIALDPT VGYLFFSDWQ SISGQPKIER
AYMDGSNRKD LVKIKLGWPG GITLDLVAKR VYWVDARFDY IETVTYDGTQ RKTVLQGGSN
IPHPFGITLF EDNLFFTDWT KFSVMKANKF TETNPRVYFR SSTRPFGVTV YHAIRQPSVR
NPCGNNNGGC EHICVLSHRT DNGGLGYRCK CKLGYIPGLD DYSCVATKQF LFFSTDVAVR
GIPLTPSNQK DVILPVTGSP SVFVGIDFDA KENAIFFSDT SKDMIFRQKI NGTGREIITA
NRVPSVESLS FDWISRNLYW TDASYRSVTV MRLADKSRRT IVQNLNNPRS IVVHPIAGYI
FFTDWFRPAK ILRAWSDGSH MLPIVNTTLG WPNGLAIDWG SSRLYWVDAF LDKIEHTTFD
GLDRRALNHL QQMTHPFGLT VFGEYVYFTD WRQRSIVRVR KTDGGEMTIL RNGVGNVMRV
KIFETSIQVG SNACNRPTNP NGDCSHFCFP VPNLQRVCGC PYGMRLASNR LNCVNDSSRE
PPMEQCGALS FPCNNGRCVP LHYRCDGVDD CHDNSDEVQC GAFNTSCAPS AFACGHGGGE
CIPSYWRCDN HNDCVDGSDE QNCSSQAQTS CRADYFTCDN HMCIPKNWLC DTDNDCGDGS
DEKRCDLGET CSPTQFHCPN HRCIDLAFVC DGDKDCADGS DESACVINCT DSQFKCVGSN
KCISNTYRCD GVSDCSDHSD EIDCPTRPPG MCRQDEFQCR EDGICIPDSW ECDGHPDCLT
GSDEHSGCPP RTCPXSRFLC ANGNCIFRDW LCDGDNDCRD MSDEKDCPTQ PFLCPSWQWQ
CPGHSICVNL SSVCDGISDC PHGTDESPLC NQESCLHSNG GCTHLCIQGP FGAQCECPLG
YRLANDSKTC EDIDECRIPG FCSQHCYNMR GSFRCWCDIE YSLEADQRTC KATASESLLL
VVANQNQLIA DNITKSMDHM RALIQDGSHI VAVDFDSVRG RIFWSDKTLG KIFSAFQNGT
DRKPVFNSGN IMTESIAVDW VGRNLYWADF ALETIEVSKL DGTLRTVLLS ENVTSPRGIV
LDPRVNDRVI FWTNWGSYPR IERASMDGEM RTVIVQQKIF WPNGLAIDYP TRLLYFADGN
LDHIHFCKYD GSNRKQVISS GEGSGHLFAI TIFEDSIYWT DRNSQDVRKA NKWHGGNESV
VLSASQPLGI VAVHPARQPT ARNPCTIARC SHLCLLSSER LYSCACPSGW SLSQDSMTCV
RDDDAFLIVV RRTTIFGISL NPEVNTDNAM VPISGMESGY DVEVDYSEQF LYYADYPGEI
YKVKTDGTNR TLFDPLTKVG STTTLALDWL SRNLYYTDSE ARSIKVLTLR GNVRYRKTLI
TNDGTTLGIG VPVSITVDPA KGKLYWSDLG IEGRVPAKIA CANMDGTSRK NLFTGHLENV
GFITLDIQEQ KLYWTVRSYI SIERGNVDGT DRMSLVNSLP RPRGIAVYGP YLYYADEQNQ
VIERVDKATG ANKVVVREGL PNLRALRIYR RRGSESSNGC SNNINACQQI CLPVPGGLFT
CACAVGFKLN PDNRTCSSHD SFIVVSMLTA IRGYSLDVSD HSEAMVPVEL EGQNTLHVDV
DVSSGFVYWA DFNRNVQTDN AIRRIKIDGS GFADIITDGI GKDGIRGIAV DWVAGNLYFI
NAFVSETLIE VLRINTTHRR VLLKTTEDVP RDIVVDPKNR YLFWSDIGQT PKIERSFLDC
TNRTVLVSEM VASPRGLALD HNSGYIYWVD DSLDLIARVS IHGGNSETIR FGSSYPTPYA
IAVFGNSIIW VDRDLKTIFQ ASKEPFKTDP PTVIRNNINW LRDVTVFDKQ AQPRSPAEVN
YNPCLQNNGG CTHFCFALPQ LRTPKCGCAF GVLQGDGRSC AISREDFLIY ALDNSVRSLH
FDPEDYNVPF TAISVEETAV AVDYDSIDNR IYFTQVLASG KGQISYISLN SRSHSPTVVI
SNLGSPDGIA FDWIGRRIYY SDYTNQTIQS MNMDGSRRTV VARVTKPRAI VLDPCQGYMY
WTDWSTNAQI ERATMAGNFR NSIVNRDLVW PNGLTLDYKE NLLYWADASL QKIERSSVTG
TGREVIVSRA NAPFGLTVYG QYIYWTDWLT QKIYRANKYD GSGQTAMTTA LPFLPNGIRA
VVNNQELCHN PCGRFNGGCS HVCAPGPNGP ECKCPHEGRW YLANNNKYCI VDDGKRCNST
QFTCLSGYCI LESLKCNDID ECGDSSDELE TLCAYHTCPP TSFTCANGRC IQRHFRCDHY
NDCGDNSDES GCRFRSCNIT TEFSCNNGKC LPLQLVCDGI DHCNDNNTSD EKNCAQHTCL
PDYIKCANSN VCIPRLFLCD GDNDCGDMSD ENPIYCVSPT CKNNEFQCTS GSCIPELWHC
DGERDCDDGS DEPATCVYSP STCSSDEFKC DNNRCIQMEW ICDGDNDCGD MSDEDGRHHC
ENHNCSSYAF HCVNSAPPSR RCIPLSWVCD GDADCSDAYD EHQNCTRRNC SGTEFRCSNG
LCIPNWFRCD RRNDCGDYSD ERNCKYPACD ENLFTCQNGI CTYKSYICDG ENDCGDNSDE
LEHLCHKEET TCPPHQFRCN NGNCIEMVKV CNHQADCSDN SDEERCGVNE CNDPLLSGCD
QNCTDTLTSF YCSCKPGYRL LPDKRTCVDI DECKETPSVC SQKCENLLGS YICKCAPGYT
REPDGRSCRQ NTNIEPYLIF SNRYYLRNLT IDGHIYSLIL QGLGNAVALD FDRVEERLYW
LDIENKVIER MFLNKTNREA VIKYNIPGTE SLAVDWVTRK LYWSDSYLNC LSVSDLNGRY
RRKLAEHCVD VNNTFCFDKP RGIALHPRYG YVYWADWTDR AYIGRVGMDG RNKSLIISSK
IKWPNGITID YTNDLLYWTD AHLGYIEYSD LEGSHRHTVY ETGTLSHPFA VTIFEDTIYW
TDWNTKTVEK GNKYNGSNRE VLVNTTHRPY DIHVYHPYRQ PFVSNPCGTN NGGCSHLCLI
KAGGNGFTCE CPDNFYTIQH GDTTQCLPMC SSTQFLCANN EMCIPIWWKC DGQKDCLDGS
DEPNTCPQRF CRLGQFQCSD GNCTSSNFIC NARQDCPDGS DEDAVLCEHH RCESNQWQCA
NKRCIPESWQ CDSLNDCGDN SDEDSSHCAR RTCLPGYFKC ANGHCIPQSW KCDVDNDCGD
YSDEPLQECM GPAYRCDNYT EFDCKTNYRC IPKWAVCNGF DDCRDNSDEQ NCESLTCKPS
GEFRCTNHHC IPLRWRCDGH NDCGDNSDEE NCVPRQCSES EFRCDDQTCI PSRWICDQNN
DCGDNSDERD CEVMTCHPGY FQCSSGHCIP DQMRCDGFAD CLDASDEATC PTRFPNGAYC
PATLFECKNH VCVQPSWKCD GDNDCGDGSD EELHLCLNIT CDLTNRFRCD NNRCIYRHEL
CNHEDDCGDG SDEKKENCLA PTPRPCTEGE FKCSNGHCIS QHLVCDDVDD CGDHFDETGC
NTGEERSCAE NLCEHNCTQL IGGGFICSCR PGFKASSLNR NSCEDINECE QFGVCPQNCH
NTKGSYECTC AEGFRSMSEH YGERCAAEGN PPLLLLPENV RVRKYNLSSE KFSDYLEDQE
RIQALDYDWD PEGTGLSVVY YTVLGHGSKF GAIKRAYIPN FESGSNNPVK EVNLGLKYIV
QPDGIAVDWV GRHIYWSDAK TQRIEVAELD GRYRKWLITT LLDQPAAIVV NPKQGLMYWT
DWGKNPKIEI AWMDGQHRKV LVQEDLGWPT GLSIDYVNSD RIYWSDLKED VIETIKHDGT
DRKVVVTAAM NPYSLDIFES QLYWISKDKG EIWVQDKFER DRKEKLLIVN PWLTQVRIFH
QRRYNQSVPN RCKKVCSHLC LLKPEGYTCA CPQGSRFIAG SVTECDAAIE SPVTMPPPCR
CMNEGNCYFD KNNLPKCKCP SGYMGEYCEI GLSKGISPGT TVAVLVTLIL IIIIGGLVAL
GFFHYRKTGS ILISMPRLPS LSNLSKYTEN GNGVTFRSGE DVNMDIGVSG FGPESAIDRS
MAMSEHFAMD LEKPPIIFEN PMYTSKDGTI RMAQPTTTQV SESGNVYNKN YGSPVNPDEL
APDTKPASPS ADETQVTKWN IFKRKPKQNT NFENPIYAET ENEPKVGAAV TPPPSPSPPA
KKTQKKGTTP AYSATEDTFK DTANLVREDS EA


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YHB0684Ra Rat low-density lipoprotein-receptor-related protein,LRP-1 ELISA Kit 96T
ER1132 Low-Density Lipoprotein-Receptor-Related Protein Elisa Kit 96T
E06L0278 Goat low-density lipoprotein receptor-related protein 1 96 Tests/kit
E06L0279 Goat low-density lipoprotein-receptor-related protein 6 96 Tests/kit
E14945h Rat ELISA Kit FOR Low-density lipoprotein receptor-related protein 3 96T
SL0454Ra Rat low-density lipoprotein-receptor-related protein,LRP-1 ELISA Kit 96T
KN0398Ra Rat low-density lipoprotein-receptor-related protein,LRP-1 ELISA Kit 96 WELLS
ER215 Low-density lipoprotein receptor-related protein 2 Elisa Kit 96T
EH1247 Low-density lipoprotein receptor-related protein 4 Elisa Kit 96T
YHB0684Ra Rat low-density lipoprotein-receptor-related protein,LRP-1 ELISA Kit 48T
E07L0278 Porcine low-density lipoprotein receptor-related protein 1 96 Tests/kit
E07L0279 Porcine low-density lipoprotein-receptor-related protein 6 96 Tests/kit
E12411281 Rat low-density lipoprotein-receptor-related protein(LRP-6) ELISA KIT 1
C389 Low-Density Lipoprotein Receptor-Related Protein 12 LRP12 500
E02S0268 Rat Soluble low density lipoprotein receptor related protein 1 96T/kit
E03L0279 Mouse low-density lipoprotein-receptor-related protein 6 96 Tests/kit
E03L0278 Mouse low-density lipoprotein receptor-related protein 1 96 Tests/kit
EH1183 Low-density lipoprotein receptor-related protein 11 Elisa Kit 96T


 

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