Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Reelin (EC 3.4.21.-) (Reeler protein)

 RELN_MOUSE              Reviewed;        3461 AA.
Q60841; E9PZ78; Q9CUA6;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
23-MAY-2018, entry version 167.
RecName: Full=Reelin;
EC=3.4.21.-;
AltName: Full=Reeler protein;
Flags: Precursor;
Name=Reln; Synonyms=Rl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN RL.
TISSUE=Cerebellum;
PubMed=7715726; DOI=10.1038/374719a0;
D'Arcangelo G., Miao G.G., Chen S.-C., Soares H.D., Morgan J.I.,
Curran T.;
"A protein related to extracellular matrix proteins deleted in the
mouse mutant reeler.";
Nature 374:719-723(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
PubMed=9417911; DOI=10.1006/geno.1997.4983;
Royaux I., Lambert de Rouvroit C., D'Arcangelo G., Demirov D.,
Goffinet A.M.;
"Genomic organization of the mouse reelin gene.";
Genomics 46:240-250(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 2152-3461 (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=7647795; DOI=10.1038/ng0595-77;
Hirotsune S., Takahara T., Sasaki N., Hirose K., Yoshiki A.,
Ohashi T., Kusakabe M., Murakami Y., Muramatsu M., Watanabe S.,
Nakao K., Katsuki M., Hayashizaki Y.;
"The reeler gene encodes a protein with an EGF-like motif expressed by
pioneer neurons.";
Nat. Genet. 10:77-83(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3044-3461 (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
CHARACTERIZATION.
PubMed=8987733;
D'Arcangelo G., Nakajima K., Miyata T., Ogawa M., Mikoshiba K.,
Curran T.;
"Reelin is a secreted glycoprotein recognized by the CR-50 monoclonal
antibody.";
J. Neurosci. 17:23-31(1997).
[7]
CHARACTERIZATION.
PubMed=11689558; DOI=10.1074/jbc.M106996200;
Quattrocchi C.C., Wannenes F., Persico A.M., Ciafre S.A.,
D'Arcangelo G., Farace M.G., Keller F.;
"Reelin is a serine protease of the extracellular matrix.";
J. Biol. Chem. 277:303-309(2002).
[8]
TISSUE SPECIFICITY.
PubMed=9182958; DOI=10.1111/j.1460-9568.1997.tb01456.x;
Schiffmann S.N., Bernier B., Goffinet A.M.;
"Reelin mRNA expression during mouse brain development.";
Eur. J. Neurosci. 9:1055-1071(1997).
[9]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=10328932; DOI=10.1006/exnr.1999.7019;
Lambert de Rouvroit C., Bernier B., Royaux I., de Bergeyck V.,
Goffinet A.M.;
"Evolutionarily conserved, alternative splicing of reelin during brain
development.";
Exp. Neurol. 156:229-238(1999).
[10]
INTERACTION WITH VLDLR AND APOER2.
PubMed=10571241; DOI=10.1016/S0896-6273(00)80861-2;
Hiesberger T., Trommsdorff M., Howell B.W., Goffinet A.M., Mumby M.C.,
Cooper J.A., Herz J.;
"Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces
tyrosine phosphorylation of disabled-1 and modulates tau
phosphorylation.";
Neuron 24:481-489(1999).
[11]
FUNCTION.
PubMed=10880573; DOI=10.1073/pnas.150040497;
Yip J.W., Yip Y.P.L., Nakajima K., Capriotti C.;
"Reelin controls position of autonomic neurons in the spinal cord.";
Proc. Natl. Acad. Sci. U.S.A. 97:8612-8616(2000).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
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]
SUBUNIT, INTERCHAIN DISULFIDE BOND, AND MUTAGENESIS OF CYS-2101.
PubMed=21844191; DOI=10.1074/jbc.M111.242719;
Yasui N., Kitago Y., Beppu A., Kohno T., Morishita S., Gomi H.,
Nagae M., Hattori M., Takagi J.;
"Functional importance of covalent homodimer of reelin protein linked
via its central region.";
J. Biol. Chem. 286:35247-35256(2011).
[14]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1222-1597, DISULFIDE BONDS,
AND CALCIUM-BINDING.
PubMed=16858396; DOI=10.1038/sj.emboj.7601240;
Nogi T., Yasui N., Hattori M., Iwasaki K., Takagi J.;
"Structure of a signaling-competent reelin fragment revealed by X-ray
crystallography and electron tomography.";
EMBO J. 25:3675-3683(2006).
[15]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1948-2662, DISULFIDE BONDS,
GLYCOSYLATION AT ASN-2145; ASN-2269; ASN-2317 AND ASN-2569,
CALCIUM-BINDING, ZINC-BINDING SITES, AND MUTAGENESIS OF LYS-2360 AND
LYS-2467.
PubMed=17548821; DOI=10.1073/pnas.0700438104;
Yasui N., Nogi T., Kitao T., Nakano Y., Hattori M., Takagi J.;
"Structure of a receptor-binding fragment of reelin and mutational
analysis reveal a recognition mechanism similar to endocytic
receptors.";
Proc. Natl. Acad. Sci. U.S.A. 104:9988-9993(2007).
-!- FUNCTION: Extracellular matrix serine protease that plays a role
in layering of neurons in the cerebral cortex and cerebellum.
Regulates microtubule function in neurons and neuronal migration.
Affects migration of sympathetic preganglionic neurons in the
spinal cord, where it seems to act as a barrier to neuronal
migration. Enzymatic activity is important for the modulation of
cell adhesion. Binding to the extracellular domains of lipoprotein
receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation
of DAB1 and modulation of TAU phosphorylation.
{ECO:0000269|PubMed:10880573}.
-!- SUBUNIT: Oligomer of disulfide-linked homodimers. Binds to the
ectodomains of VLDLR and LRP8/APOER2.
{ECO:0000269|PubMed:16858396, ECO:0000269|PubMed:17548821,
ECO:0000269|PubMed:21844191}.
-!- INTERACTION:
Q14114:LRP8 (xeno); NbExp=10; IntAct=EBI-9248666, EBI-2681187;
Q924X6:Lrp8; NbExp=4; IntAct=EBI-9248666, EBI-432319;
P98155:VLDLR (xeno); NbExp=7; IntAct=EBI-9248666, EBI-9004309;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q60841-1; Sequence=Displayed;
Name=2;
IsoId=Q60841-2; Sequence=VSP_005577;
Name=3;
IsoId=Q60841-3; Sequence=VSP_005578;
-!- TISSUE SPECIFICITY: The major isoform 1 is neuron-specific. It is
abundantly produced during brain ontogenesis by the Cajal-Retzius
cells and other pioneer neurons located in the telencephalic
marginal zone and by granule cells of the external granular layer
of the cerebellum. Expression is located in deeper layers in the
developing hippocampus and olfactory bulb, low levels of
expression are also detected in the immature striatum. At early
developmental stages, expressed also in hypothalamic
differentiation fields, tectum and spinal cord. A moderate to low
level of expression occurs in the septal area, striatal fields,
habenular nuclei, some thalamic nuclei, particularly the lateral
geniculate, the retina and some nuclei of the reticular formation
in the central field of the medulla. Very low levels found in
liver and kidney. No expression in radial glial cells, cortical
plate, Purkinje cells and inferior olivary neurons. The minor
isoform 2 is only expressed in non neuronal cells. The minor
isoform 3 is found in the same cells as isoform 1, but is almost
undetectable in retina and brain stem.
{ECO:0000269|PubMed:10328932, ECO:0000269|PubMed:9182958}.
-!- DEVELOPMENTAL STAGE: First detected at embryonic day 11.5.
Expression increases up to birth and remains high from postnatal
day 2 to 11 in both cerebellum and fore/midbrain. Expression
declines thereafter and is largely brain specific in the adult.
-!- DOMAIN: The basic C-terminal region is essential for secretion.
-!- PTM: N-glycosylated and to a lesser extent also O-glycosylated.
{ECO:0000269|PubMed:17548821}.
-!- DISEASE: Note=Defects in Reln are the cause of the autosomal
recessive reeler (rl) phenotype which is characterized by impaired
motor coordination, tremors and ataxia. Neurons in affected mice
fail to reach their correct locations in the developing brain,
disrupting the organization of the cerebellar and cerebral
cortices and other laminated regions.
{ECO:0000269|PubMed:7715726}.
-!- SIMILARITY: Belongs to the reelin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA09788.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U24703; AAB91599.1; -; mRNA.
EMBL; AC113028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC116404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC119906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC121878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D63520; BAA09788.1; ALT_INIT; mRNA.
EMBL; AK017094; BAB30592.1; -; mRNA.
CCDS; CCDS39023.1; -. [Q60841-1]
CCDS; CCDS80217.1; -. [Q60841-2]
PIR; S58870; S58870.
RefSeq; NP_001297393.1; NM_001310464.1. [Q60841-2]
RefSeq; NP_035391.2; NM_011261.2. [Q60841-1]
UniGene; Mm.425236; -.
PDB; 2DDU; X-ray; 2.05 A; A=1222-1597.
PDB; 2E26; X-ray; 2.00 A; A=1948-2661.
PDB; 3A7Q; X-ray; 2.60 A; A=1948-2661.
PDB; 5B4X; X-ray; 3.20 A; A/C=1948-2662.
PDBsum; 2DDU; -.
PDBsum; 2E26; -.
PDBsum; 3A7Q; -.
PDBsum; 5B4X; -.
ProteinModelPortal; Q60841; -.
SMR; Q60841; -.
DIP; DIP-40924N; -.
IntAct; Q60841; 6.
STRING; 10090.ENSMUSP00000124052; -.
iPTMnet; Q60841; -.
PhosphoSitePlus; Q60841; -.
PaxDb; Q60841; -.
PeptideAtlas; Q60841; -.
PRIDE; Q60841; -.
Ensembl; ENSMUST00000062372; ENSMUSP00000058025; ENSMUSG00000042453. [Q60841-2]
Ensembl; ENSMUST00000161356; ENSMUSP00000124052; ENSMUSG00000042453. [Q60841-1]
GeneID; 19699; -.
KEGG; mmu:19699; -.
UCSC; uc008wpi.1; mouse. [Q60841-1]
CTD; 5649; -.
MGI; MGI:103022; Reln.
eggNOG; ENOG410IEXI; Eukaryota.
eggNOG; ENOG410XQKB; LUCA.
GeneTree; ENSGT00580000081623; -.
HOGENOM; HOG000252908; -.
HOVERGEN; HBG023117; -.
InParanoid; Q60841; -.
KO; K06249; -.
OMA; NWFFYPG; -.
OrthoDB; EOG091G0016; -.
TreeFam; TF106479; -.
Reactome; R-MMU-8866376; Reelin signalling pathway.
ChiTaRS; Reln; mouse.
EvolutionaryTrace; Q60841; -.
PRO; PR:Q60841; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000042453; -.
CleanEx; MM_RELN; -.
ExpressionAtlas; Q60841; baseline and differential.
Genevisible; Q60841; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IEA:GOC.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0070325; F:lipoprotein particle receptor binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; IPI:BHF-UCL.
GO; GO:0008306; P:associative learning; IDA:BHF-UCL.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IMP:MGI.
GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
GO; GO:0007417; P:central nervous system development; IMP:MGI.
GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
GO; GO:0021800; P:cerebral cortex tangential migration; IMP:MGI.
GO; GO:0016358; P:dendrite development; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
GO; GO:0021766; P:hippocampus development; IDA:BHF-UCL.
GO; GO:0097477; P:lateral motor column neuron migration; IMP:UniProtKB.
GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
GO; GO:0007612; P:learning; IMP:CACAO.
GO; GO:0007616; P:long-term memory; IDA:BHF-UCL.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:CACAO.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:BHF-UCL.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:0097114; P:NMDA glutamate receptor clustering; IMP:BHF-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:2000969; P:positive regulation of AMPA receptor activity; IDA:BHF-UCL.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:BHF-UCL.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IDA:BHF-UCL.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:BHF-UCL.
GO; GO:1902078; P:positive regulation of lateral motor column neuron migration; IMP:BHF-UCL.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IDA:BHF-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:MGI.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:BHF-UCL.
GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IDA:MGI.
GO; GO:0090129; P:positive regulation of synapse maturation; IDA:BHF-UCL.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IDA:BHF-UCL.
GO; GO:0032008; P:positive regulation of TOR signaling; IDA:BHF-UCL.
GO; GO:0097107; P:postsynaptic density assembly; IC:BHF-UCL.
GO; GO:0097119; P:postsynaptic density protein 95 clustering; IMP:BHF-UCL.
GO; GO:0035418; P:protein localization to synapse; IMP:BHF-UCL.
GO; GO:0097120; P:receptor localization to synapse; IMP:BHF-UCL.
GO; GO:0038026; P:reelin-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0050795; P:regulation of behavior; IMP:BHF-UCL.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:BHF-UCL.
GO; GO:0048265; P:response to pain; IMP:MGI.
GO; GO:0021511; P:spinal cord patterning; IMP:MGI.
GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
CDD; cd08544; Reeler; 1.
Gene3D; 2.60.120.260; -; 19.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR002861; Reeler_dom.
InterPro; IPR034968; Reelin.
InterPro; IPR036278; Sialidase_sf.
PANTHER; PTHR11841; PTHR11841; 1.
Pfam; PF02014; Reeler; 1.
SMART; SM00181; EGF; 8.
SUPFAM; SSF50939; SSF50939; 14.
PROSITE; PS00022; EGF_1; 7.
PROSITE; PS01186; EGF_2; 6.
PROSITE; PS50026; EGF_3; 5.
PROSITE; PS51019; REELIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion;
Complete proteome; Developmental protein; Disulfide bond;
EGF-like domain; Extracellular matrix; Glycoprotein; Hydrolase;
Metal-binding; Protease; Reference proteome; Repeat; Secreted;
Serine protease; Signal; Zinc.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 3461 Reelin.
/FTId=PRO_0000030305.
DOMAIN 27 191 Reelin. {ECO:0000255|PROSITE-
ProRule:PRU00363}.
REPEAT 593 604 BNR 1.
DOMAIN 671 702 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 799 810 BNR 2.
REPEAT 952 963 BNR 3.
DOMAIN 1030 1061 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1157 1168 BNR 4.
REPEAT 1323 1334 BNR 5.
DOMAIN 1409 1442 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1535 1546 BNR 6.
REPEAT 1686 1697 BNR 7.
DOMAIN 1765 1796 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1884 1895 BNR 8.
REPEAT 2043 2054 BNR 9.
DOMAIN 2129 2161 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 2250 2261 BNR 10.
REPEAT 2399 2410 BNR 11.
DOMAIN 2478 2509 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 2598 2609 BNR 12.
REPEAT 2778 2789 BNR 13.
DOMAIN 2853 2884 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 2979 2990 BNR 14.
REPEAT 3143 3155 BNR 15.
DOMAIN 3228 3260 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 3363 3374 BNR 16.
COMPBIAS 3432 3461 Arg-rich (basic).
METAL 2061 2061 Zinc 1.
METAL 2074 2074 Zinc 1.
METAL 2179 2179 Zinc 1.
METAL 2264 2264 Zinc 1.
METAL 2397 2397 Zinc 2.
METAL 2399 2399 Zinc 2.
METAL 2460 2460 Zinc 2.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 629 629 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1267 1267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1447 1447 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1600 1600 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1750 1750 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1921 1921 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2145 2145 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17548821}.
CARBOHYD 2269 2269 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17548821}.
CARBOHYD 2317 2317 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17548821}.
CARBOHYD 2569 2569 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17548821}.
CARBOHYD 2962 2962 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3016 3016 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3073 3073 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3185 3185 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3412 3412 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3439 3439 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 127 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 155 179 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 540 581 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 609 614 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 675 685 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 692 701 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 895 937 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 968 975 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1034 1044 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1051 1060 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1271 1310
DISULFID 1339 1348
DISULFID 1633 1673 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1702 1709 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1983 2030
DISULFID 2059 2070
DISULFID 2101 2101 Interchain.
DISULFID 2133 2143
DISULFID 2137 2149
DISULFID 2151 2160
DISULFID 2195 2235
DISULFID 2348 2387
DISULFID 2393 2559
DISULFID 2482 2492
DISULFID 2486 2497
DISULFID 2499 2508
DISULFID 2544 2584
DISULFID 2794 2801 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2919 2966 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3160 3170 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3232 3242 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3236 3248 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3250 3259 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3296 3346 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VAR_SEQ 3429 3461 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_005578.
VAR_SEQ 3429 3430 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_005577.
MUTAGEN 2101 2101 C->A: Fails to assemble into disulfide-
bonded multimers, while still exhibiting
non-covalently associated high molecular
weight oligomeric states in solution;
retains binding to LRP8 and VLDR
receptors but fails to show signaling
activity. {ECO:0000269|PubMed:21844191}.
MUTAGEN 2360 2360 K->A: Abolishes ApoER2-binding.
{ECO:0000269|PubMed:17548821}.
MUTAGEN 2467 2467 K->A: Abolishes ApoER2-binding.
{ECO:0000269|PubMed:17548821}.
CONFLICT 1191 1191 A -> G (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1202 1202 Q -> K (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1335 1335 V -> L (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1345 1345 G -> A (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1505 1505 R -> S (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1522 1524 CIK -> YIT (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1529 1529 N -> Y (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1593 1593 D -> G (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1611 1611 F -> L (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1648 1648 K -> N (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1661 1661 A -> E (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 1667 1667 F -> W (in Ref. 1; AAB91599).
{ECO:0000305}.
CONFLICT 3066 3066 Missing (in Ref. 5; BAB30592).
{ECO:0000305}.
STRAND 1301 1310 {ECO:0000244|PDB:2DDU}.
STRAND 1320 1327 {ECO:0000244|PDB:2DDU}.
STRAND 1333 1335 {ECO:0000244|PDB:2DDU}.
STRAND 1345 1348 {ECO:0000244|PDB:2DDU}.
STRAND 1359 1361 {ECO:0000244|PDB:2DDU}.
STRAND 1370 1375 {ECO:0000244|PDB:2DDU}.
HELIX 1378 1380 {ECO:0000244|PDB:2DDU}.
STRAND 1386 1390 {ECO:0000244|PDB:2DDU}.
STRAND 1408 1411 {ECO:0000244|PDB:2DDU}.
HELIX 1414 1419 {ECO:0000244|PDB:2DDU}.
STRAND 1420 1424 {ECO:0000244|PDB:2DDU}.
STRAND 1427 1430 {ECO:0000244|PDB:2DDU}.
STRAND 1434 1437 {ECO:0000244|PDB:2DDU}.
STRAND 1440 1445 {ECO:0000244|PDB:2DDU}.
STRAND 1451 1453 {ECO:0000244|PDB:2DDU}.
STRAND 1456 1458 {ECO:0000244|PDB:2DDU}.
STRAND 1463 1472 {ECO:0000244|PDB:2DDU}.
STRAND 1478 1481 {ECO:0000244|PDB:2DDU}.
STRAND 1483 1486 {ECO:0000244|PDB:2DDU}.
STRAND 1493 1496 {ECO:0000244|PDB:2DDU}.
STRAND 1506 1513 {ECO:0000244|PDB:2DDU}.
STRAND 1516 1518 {ECO:0000244|PDB:2DDU}.
HELIX 1528 1530 {ECO:0000244|PDB:2DDU}.
STRAND 1531 1539 {ECO:0000244|PDB:2DDU}.
STRAND 1545 1550 {ECO:0000244|PDB:2DDU}.
STRAND 1559 1564 {ECO:0000244|PDB:2DDU}.
HELIX 1567 1569 {ECO:0000244|PDB:2DDU}.
STRAND 1571 1579 {ECO:0000244|PDB:2DDU}.
HELIX 1584 1586 {ECO:0000244|PDB:2DDU}.
STRAND 1590 1597 {ECO:0000244|PDB:2DDU}.
STRAND 1958 1960 {ECO:0000244|PDB:2E26}.
STRAND 1963 1965 {ECO:0000244|PDB:2E26}.
HELIX 1968 1970 {ECO:0000244|PDB:2E26}.
STRAND 1971 1973 {ECO:0000244|PDB:2E26}.
STRAND 1978 1980 {ECO:0000244|PDB:2E26}.
STRAND 1996 1999 {ECO:0000244|PDB:2E26}.
STRAND 2001 2003 {ECO:0000244|PDB:5B4X}.
STRAND 2005 2011 {ECO:0000244|PDB:2E26}.
STRAND 2014 2016 {ECO:0000244|PDB:2E26}.
STRAND 2020 2032 {ECO:0000244|PDB:2E26}.
STRAND 2040 2047 {ECO:0000244|PDB:2E26}.
STRAND 2053 2056 {ECO:0000244|PDB:2E26}.
STRAND 2059 2061 {ECO:0000244|PDB:2E26}.
STRAND 2078 2080 {ECO:0000244|PDB:2E26}.
STRAND 2089 2095 {ECO:0000244|PDB:2E26}.
TURN 2096 2099 {ECO:0000244|PDB:2E26}.
STRAND 2102 2113 {ECO:0000244|PDB:2E26}.
STRAND 2122 2131 {ECO:0000244|PDB:2E26}.
HELIX 2134 2139 {ECO:0000244|PDB:2E26}.
STRAND 2140 2144 {ECO:0000244|PDB:2E26}.
TURN 2145 2147 {ECO:0000244|PDB:2E26}.
STRAND 2148 2151 {ECO:0000244|PDB:2E26}.
STRAND 2155 2157 {ECO:0000244|PDB:2E26}.
STRAND 2170 2172 {ECO:0000244|PDB:2E26}.
STRAND 2174 2176 {ECO:0000244|PDB:2E26}.
STRAND 2178 2187 {ECO:0000244|PDB:2E26}.
STRAND 2189 2193 {ECO:0000244|PDB:2E26}.
STRAND 2197 2201 {ECO:0000244|PDB:2E26}.
STRAND 2203 2206 {ECO:0000244|PDB:2E26}.
STRAND 2208 2210 {ECO:0000244|PDB:3A7Q}.
STRAND 2212 2216 {ECO:0000244|PDB:2E26}.
STRAND 2226 2233 {ECO:0000244|PDB:2E26}.
STRAND 2236 2238 {ECO:0000244|PDB:2E26}.
STRAND 2247 2254 {ECO:0000244|PDB:2E26}.
STRAND 2260 2265 {ECO:0000244|PDB:2E26}.
TURN 2269 2272 {ECO:0000244|PDB:2E26}.
STRAND 2275 2280 {ECO:0000244|PDB:2E26}.
HELIX 2283 2285 {ECO:0000244|PDB:2E26}.
STRAND 2287 2296 {ECO:0000244|PDB:2E26}.
STRAND 2299 2301 {ECO:0000244|PDB:2E26}.
STRAND 2307 2315 {ECO:0000244|PDB:2E26}.
TURN 2318 2320 {ECO:0000244|PDB:5B4X}.
STRAND 2324 2326 {ECO:0000244|PDB:2E26}.
STRAND 2328 2330 {ECO:0000244|PDB:2E26}.
TURN 2333 2335 {ECO:0000244|PDB:2E26}.
STRAND 2336 2338 {ECO:0000244|PDB:2E26}.
STRAND 2343 2345 {ECO:0000244|PDB:2E26}.
STRAND 2354 2357 {ECO:0000244|PDB:2E26}.
STRAND 2364 2368 {ECO:0000244|PDB:2E26}.
STRAND 2371 2373 {ECO:0000244|PDB:2E26}.
STRAND 2378 2384 {ECO:0000244|PDB:2E26}.
STRAND 2387 2389 {ECO:0000244|PDB:3A7Q}.
STRAND 2395 2403 {ECO:0000244|PDB:2E26}.
STRAND 2409 2412 {ECO:0000244|PDB:2E26}.
STRAND 2419 2422 {ECO:0000244|PDB:2E26}.
TURN 2433 2436 {ECO:0000244|PDB:2E26}.
STRAND 2440 2445 {ECO:0000244|PDB:2E26}.
HELIX 2448 2450 {ECO:0000244|PDB:2E26}.
STRAND 2452 2461 {ECO:0000244|PDB:2E26}.
STRAND 2471 2480 {ECO:0000244|PDB:2E26}.
HELIX 2484 2488 {ECO:0000244|PDB:2E26}.
STRAND 2489 2493 {ECO:0000244|PDB:2E26}.
STRAND 2496 2499 {ECO:0000244|PDB:2E26}.
STRAND 2503 2505 {ECO:0000244|PDB:2E26}.
STRAND 2510 2513 {ECO:0000244|PDB:2E26}.
STRAND 2519 2521 {ECO:0000244|PDB:2E26}.
STRAND 2523 2526 {ECO:0000244|PDB:5B4X}.
TURN 2529 2531 {ECO:0000244|PDB:2E26}.
STRAND 2532 2542 {ECO:0000244|PDB:2E26}.
STRAND 2547 2550 {ECO:0000244|PDB:2E26}.
STRAND 2552 2555 {ECO:0000244|PDB:2E26}.
STRAND 2562 2565 {ECO:0000244|PDB:2E26}.
STRAND 2575 2582 {ECO:0000244|PDB:2E26}.
STRAND 2584 2586 {ECO:0000244|PDB:2E26}.
HELIX 2591 2593 {ECO:0000244|PDB:2E26}.
STRAND 2594 2602 {ECO:0000244|PDB:2E26}.
STRAND 2608 2613 {ECO:0000244|PDB:2E26}.
STRAND 2615 2617 {ECO:0000244|PDB:3A7Q}.
STRAND 2622 2627 {ECO:0000244|PDB:2E26}.
HELIX 2630 2632 {ECO:0000244|PDB:2E26}.
STRAND 2634 2642 {ECO:0000244|PDB:2E26}.
STRAND 2654 2661 {ECO:0000244|PDB:2E26}.
SEQUENCE 3461 AA; 387495 MW; 1CCE64C845160F2E CRC64;
MERGCWAPRA LVLAVLLLLA TLRARAATGY YPRFSPFFFL CTHHGELEGD GEQGEVLISL
HIAGNPTYYV PGQEYHVTIS TSTFFDGLLV TGLYTSTSIQ SSQSIGGSSA FGFGIMSDHQ
FGNQFMCSVV ASHVSHLPTT NLSFVWIAPP AGTGCVNFMA TATHRGQVIF KDALAQQLCE
QGAPTEATAY SHLAEIHSDS VILRDDFDSY QQLELNPNIW VECSNCEMGE QCGTIMHGNA
VTFCEPYGPR ELTTTCLNTT TASVLQFSIG SGSCRFSYSD PSITVSYAKN NTADWIQLEK
IRAPSNVSTV IHILYLPEEA KGESVQFQWK QDSLRVGEVY EACWALDNIL VINSAHREVV
LEDNLDPVDT GNWLFFPGAT VKHSCQSDGN SIYFHGNEGS EFNFATTRDV DLSTEDIQEQ
WSEEFESQPT GWDILGAVVG ADCGTVESGL SLVFLKDGER KLCTPYMDTT GYGNLRFYFV
MGGICDPGVS HENDIILYAK IEGRKEHIAL DTLTYSSYKV PSLVSVVINP ELQTPATKFC
LRQKSHQGYN RNVWAVDFFH VLPVLPSTMS HMIQFSINLG CGTHQPGNSV SLEFSTNHGR
SWSLLHTECL PEICAGPHLP HSTVYSSENY SGWNRITIPL PNAALTRDTR IRWRQTGPIL
GNMWAIDNVY IGPSCLKFCS GRGQCTRHGC KCDPGFSGPA CEMASQTFPM FISESFGSAR
LSSYHNFYSI RGAEVSFGCG VLASGKALVF NKDGRRQLIT SFLDSSQSRF LQFTLRLGSK
SVLSTCRAPD QPGEGVLLHY SYDNGITWKL LEHYSYVNYH EPRIISVELP DDARQFGIQF
RWWQPYHSSQ GEDVWAIDEI VMTSVLFNSI SLDFTNLVEV TQSLGFYLGN VQPYCGHDWT
LCFTGDSKLA SSMRYVETQS MQIGASYMIQ FSLVMGCGQK YTPHMDNQVK LEYSANHGLT
WHLVQEECLP SMPSCQEFTS ASIYHASEFT QWRRVTVVLP QKTWSGATRF RWSQSYYTAQ
DEWALDNIYI GQQCPNMCSG HGSCDHGVCR CDQGYQGTEC HPEAALPSTI MSDFENPSSW
ESDWQEVIGG EVVKPEQGCG VVSSGSSLYF SKAGKRQLVS WDLDTSWVDF VQFYIQIGGE
SAACNKPDSR EEGILLQYSN NGGIQWHLLA EMYFSDFSKP RFVYLELPAA AKTPCTRFRW
WQPVFSGEDY DQWAVDDIII LSEKQKQVIP VVNPTLPQNF YEKPAFDYPM NQMSVWLMLA
NEGMAKNDSF CATTPSAMVF GKSDGDRFAV TRDLTLKPGY VLQFKLNIGC TSQFSSTAPV
LLQYSHDAGM SWFLVKEGCF PASAGKGCEG NSRELSEPTV YYTGDFEEWT RITIAIPRSL
ASSKTRFRWI QESSSQKNVP PFGLDGVYIS EPCPSYCSGH GDCISGVCFC DLGYTAAQGT
CVSNTPNHSE MFDRFEGKLS PLWYKITGGQ VGTGCGTLND GRSLYFNGLG KREARTVPLD
TRNIRLVQFY IQIGSKTSGI TCIKPRARNE GLVVQYSNDN GILWHLLREL DFMSFLEPQI
ISIDLPREAK TPATAFRWWQ PQHGKHSAQW ALDDVLIGVN DSSQTGFQDK FDGSIDLQAN
WYRIQGGQVD IDCLSMDTAL IFTENIGKPR YAETWDFHVS ASSFLQFEMN MGCSKPFSGA
HGIQLQYSLN NGKDWQLVTE ECVPPTIGCV HYTESSTYTS ERFQNWRRVT VYLPLATNSP
RTRFRWIQTN YTVGADSWAI DNVILASGCP WMCSGRGICD SGRCVCDRGF GGPFCVPVVP
LPSILKDDFN GNLHPDLWPE VYGAERGNLN GETIKSGTCL IFKGEGLRML ISRDLDCTNT
MYVQFSLRFI AKGTPERSHS ILLQFSVSGG VTWHLMDEFY FPQTTSILFI NVPLPYGAQT
NATRFRLWQP YNNGKKEEIW IIDDFIIDGN NLNNPVLLLD TFDFGPREDN WFFYPGGNIG
LYCPYSSKGA PEEDSAMVFV SNEVGEHSIT TRDLSVNENT IIQFEINVGC STDSSSADPV
RLEFSRDFGA TWHLLLPLCY HSSSLVSSLC STEHHPSSTY YAGTTQGWRR EVVHFGKLHL
CGSVRFRWYQ GFYPAGSQPV TWAIDNVYIG PQCEEMCYGH GSCINGTKCI CDPGYSGPTC
KISTKNPDFL KDDFEGQLES DRFLLMSGGK PSRKCGILSS GNNLFFNEDG LRMLVTRDLD
LSHARFVQFF MRLGCGKGVP DPRSQPVLLQ YSLNGGLSWS LLQEFLFSNS SNVGRYIALE
MPLKARSGST RLRWWQPSEN GHFYSPWVID QILIGGNISG NTVLEDDFST LDSRKWLLHP
GGTKMPVCGS TGDALVFIEK ASTRYVVTTD IAVNEDSFLQ IDFAASCSVT DSCYAIELEY
SVDLGLSWHP LVRDCLPTNV ECSRYHLQRI LVSDTFNKWT RITLPLPSYT RSQATRFRWH
QPAPFDKQQT WAIDNVYIGD GCLDMCSGHG RCVQGSCVCD EQWGGLYCDE PETSLPTQLK
DNFNRAPSNQ NWLTVSGGKL STVCGAVASG LALHFSGGCS RLLVTVDLNL TNAEFIQFYF
MYGCLITPSN RNQGVLLEYS VNGGITWNLL MEIFYDQYSK PGFVNILLPP DAKEIATRFR
WWQPRHDGLD QNDWAIDNVL ISGSADQRTV MLDTFSSAPV PQHERSPADA GPVGRIAFEM
FLEDKTSVNE NWLFHDDCTV ERFCDSPDGV MLCGSHDGRE VYAVTHDLTP TENWIMQFKI
SVGCKVPEKI AQNQIHVQFS TDFGVSWSYL VPQCLPADPK CSGSVSQPSV FFPTEGWKRI
TYPLPESLTG NPVRFRFYQK YSDVQWAIDN FYLGPGCLDN CGGHGDCLKE QCICDPGYSG
PNCYLTHSLK TFLKERFDSE EIKPDLWMSL EGGSTCTECG VLAENTALYF GGSTVRQAIT
QDLDLRGAKF LQYWGRIGSE NNMTSCHRPV CRKEGVLLDF STDGGITWTL LHEMDFQKYI
SVRHDYILLP EGALTNTTRL RWWQPFVISN GLVVSGVERA QWALDNILIG GAEINPSQLV
DTFDDEGSSH EENWSFYPNA VRTAGFCGNP SFHLYWPNKK KDKTHNALSS RELIIQPGYM
MQFKIVVGCE ATSCGDLHSV MLEYTKDARS DSWQLVQTQC LPSSSNSIGC SPFQFHEATI
YNAVNSSSWK RITIQLPDHV SSSATQFRWI QKGEETEKQS WAIDHVYIGE ACPKLCSGHG
YCTTGAVCIC DESFQGDDCS VFSHELPSYI KDNFESARVT EANWETIQGG VIGSGCGQLA
PYAHGDSLYF NGCQIRQAAT KPLDLTRASK IMFVLQIGSP AQTDSCNSDL SGPHTVDKAV
LLQYSVNNGI TWHVIAQHQP KDFTQAQRVS YNVPLEARMK GVLLRWWQPR HNGTGHDQWA
LDHVEVVLVS TRKQNYMMNF SRQHGLRHFY NRRRRSLRRY P


Related products :

Catalog number Product name Quantity
E2134m ELISA Mouse,Mus musculus,Reeler protein,Reelin,Reln,Rl 96T
U2134m CLIA Mouse,Mus musculus,Reeler protein,Reelin,Reln,Rl 96T
U2134m CLIA kit Mouse,Mus musculus,Reeler protein,Reelin,Reln,Rl 96T
E2134m ELISA kit Mouse,Mus musculus,Reeler protein,Reelin,Reln,Rl 96T
GTX18570 Reelin 25 µl
32540002 Reelin 100 µg
DL-RL-Ra Rat Reelin (RL) ELISA Kit 96T
EH2121 Reelin Elisa Kit 96T
orb129357 Reelin antibody (PE-Cy3) 100 ul
orb124836 Reelin antibody (PE) 100 ul
201-11-1484 Rat Reelin (RL)ELISA kit 96T
DL-RL-Mu Mouse Reelin (RL) ELISA Kit 96T
orb123852 Reelin antibody (Cy7) 100 ul
orb122868 Reelin antibody (Cy5) 100 ul
GTX18570 Reelin _ RELN 25 µl
orb114827 Reelin antibody (Cy3) 100 ul
orb110395 Reelin antibody (HRP) 100 ul
DL-RL-Hu Human Reelin (RL) ELISA Kit 96T
orb130115 Reelin antibody (PE-Cy5) 100 ul
orb130607 Reelin antibody (PE-Cy5.5) 100 ul
32540002 Reelin _ RELN 100 µg
201-11-1484 Rat Reelin(RL)ELISA kit 96T
G6952 Reelin (RL), Rat, ELISA Kit 96T
orb123360 Reelin antibody (Cy5.5) 100 ul
QY-E10161 Rat Reelin(RL)ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur