LRP8_MOUSE
ID LRP8_MOUSE Reviewed; 996 AA.
AC Q924X6; Q8CAK9; Q8CDF5; Q921B6;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Low-density lipoprotein receptor-related protein 8;
DE Short=LRP-8;
DE AltName: Full=Apolipoprotein E receptor 2;
DE Flags: Precursor;
GN Name=Lrp8; Synonyms=Apoer2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9685741; DOI=10.1093/oxfordjournals.jbchem.a022134;
RA Kim H.-J., Kim D.-H., Magoori K., Saeki S., Yamamoto T.;
RT "Evolution of the apolipoprotein E receptor 2 gene by exon loss.";
RL J. Biochem. 124:451-456(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND
RP INTERACTION WITH REELIN AND ALPHA2-MACROGLOBULIN.
RX PubMed=11294845; DOI=10.1074/jbc.m102662200;
RA Brandes C., Kahr L., Stockinger W., Hiesberger T., Schneider W.J.,
RA Nimpf J.;
RT "Alternative splicing in the ligand binding domain of mouse ApoE receptor-2
RT produces receptor variants binding reelin but not alpha2-macroglobulin.";
RL J. Biol. Chem. 276:22160-22169(2001).
RN [3]
RP INTERACTION WITH SNX17.
RX PubMed=12169628; DOI=10.1093/emboj/cdf435;
RA Stockinger W., Sailler B., Strasser V., Recheis B., Fasching D., Kahr L.,
RA Schneider W.J., Nimpf J.;
RT "The PX-domain protein SNX17 interacts with members of the LDL receptor
RT family and modulates endocytosis of the LDL receptor.";
RL EMBO J. 21:4259-4267(2002).
RN [4]
RP ALTERNATIVE SPLICING, GLYCOSYLATION, AND PROTEOLYTIC PROCESSING.
RX PubMed=12871934; DOI=10.1074/jbc.m305858200;
RA May P., Bock H.H., Nimpf J., Herz J.;
RT "Differential glycosylation regulates processing of lipoprotein receptors
RT by gamma-secretase.";
RL J. Biol. Chem. 278:37386-37392(2003).
RN [5]
RP ALTERNATIVE SPLICING, AND PROTEOLYTIC PROCESSING.
RX PubMed=12426372; DOI=10.1093/emboj/cdf599;
RA Koch S., Strasser V., Hauser C., Fasching D., Brandes C., Bajari T.M.,
RA Schneider W.J., Nimpf J.;
RT "A secreted soluble form of ApoE receptor 2 acts as a dominant-negative
RT receptor and inhibits Reelin signaling.";
RL EMBO J. 21:5996-6004(2002).
RN [6]
RP FUNCTION IN SPERM DEVELOPMENT.
RX PubMed=12695510; DOI=10.1074/jbc.m302157200;
RA Andersen O.M., Yeung C.H., Vorum H., Wellner M., Andreassen T.K.,
RA Erdmann B., Mueller E.C., Herz J., Otto A., Cooper T.G., Willnow T.E.;
RT "Essential role of the apolipoprotein E receptor-2 in sperm development.";
RL J. Biol. Chem. 278:23989-23995(2003).
RN [7]
RP INTERACTION WITH DAB1, AND DISRUPTION PHENOTYPE.
RX PubMed=10380922; DOI=10.1016/s0092-8674(00)80782-5;
RA Trommsdorff M., Gotthardt M., Hiesberger T., Shelton J., Stockinger W.,
RA Nimpf J., Hammer R.E., Richardson J.A., Herz J.;
RT "Reeler/Disabled-like disruption of neuronal migration in knockout mice
RT lacking the VLDL receptor and ApoE receptor 2.";
RL Cell 97:689-701(1999).
RN [8]
RP INTERACTION WITH JNK-INTERACTING PROTEINS, AND TISSUE SPECIFICITY.
RX PubMed=10827199; DOI=10.1074/jbc.m004119200;
RA Stockinger W., Brandes C., Fasching D., Hermann M., Gotthardt M., Herz J.,
RA Schneider W.J., Nimpf J.;
RT "The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2.";
RL J. Biol. Chem. 275:25625-25632(2000).
RN [9]
RP INTERACTION WITH RAP AND REELIN, STOICHIOMETRY, AND MUTAGENESIS.
RX PubMed=12899622; DOI=10.1021/bi034475p;
RA Andersen O.M., Benhayon D., Curran T., Willnow T.E.;
RT "Differential binding of ligands to the apolipoprotein E receptor 2.";
RL Biochemistry 42:9355-9364(2003).
RN [10]
RP INTERACTION WITH MDK.
RX PubMed=12573468; DOI=10.1016/s0168-0102(02)00226-2;
RA Sakaguchi N., Muramatsu H., Ichihara-Tanaka K., Maeda N., Noda M.,
RA Yamamoto T., Michikawa M., Ikematsu S., Sakuma S., Muramatsu T.;
RT "Receptor-type protein tyrosine phosphatase zeta as a component of the
RT signaling receptor complex for midkine-dependent survival of embryonic
RT neurons.";
RL Neurosci. Res. 45:219-224(2003).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18174160; DOI=10.1074/jbc.m709945200;
RA Olson G.E., Winfrey V.P., Hill K.E., Burk R.F.;
RT "Megalin mediates selenoprotein P uptake by kidney proximal tubule
RT epithelial cells.";
RL J. Biol. Chem. 283:6854-6860(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION.
RX PubMed=29336888; DOI=10.1016/j.cell.2017.12.026;
RA Tavazoie M.F., Pollack I., Tanqueco R., Ostendorf B.N., Reis B.S.,
RA Gonsalves F.C., Kurth I., Andreu-Agullo C., Derbyshire M.L., Posada J.,
RA Takeda S., Tafreshian K.N., Rowinsky E., Szarek M., Waltzman R.J.,
RA Mcmillan E.A., Zhao C., Mita M., Mita A., Chmielowski B., Postow M.A.,
RA Ribas A., Mucida D., Tavazoie S.F.;
RT "LXR/ApoE Activation Restricts Innate Immune Suppression in Cancer.";
RL Cell 172:825-840(2018).
CC -!- FUNCTION: Cell surface receptor for Reelin (RELN) and apolipoprotein E
CC (apoE)-containing ligands. LRP8 participates in transmitting the
CC extracellular Reelin signal to intracellular signaling processes, by
CC binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL
CC receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and
CC microtubule function in neurons. LRP8 has higher affinity for Reelin
CC than VLDLR. LRP8 is thus a key component of the Reelin pathway which
CC governs neuronal layering of the forebrain during embryonic brain
CC development. Binds the endoplasmic reticulum resident receptor-
CC associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may
CC be involved in the suppression of platelet aggregation in the
CC vasculature. Highly expressed in the initial segment of the epididymis,
CC where it affects the functional expression of clusterin and
CC phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins
CC required for sperm maturation (PubMed:12695510). May also function as
CC an endocytic receptor. Not required for endocytic uptake of SEPP1 in
CC the kidney which is mediated by LRP2 (PubMed:18174160). Together with
CC its ligand, apolipoprotein E (apoE), may indirectly play a role in the
CC suppression of the innate immune response by controlling the survival
CC of myeloid-derived suppressor cells (PubMed:29336888).
CC {ECO:0000269|PubMed:12695510, ECO:0000269|PubMed:18174160,
CC ECO:0000269|PubMed:29336888}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with VLDLR (By
CC similarity). Reelin associates with two or more receptor molecules.
CC Interacts with DAB1 and JNK-interacting proteins. Interacts with SNX17.
CC Interacts with PCSK9 (By similarity). Interacts with MDK; this
CC interaction is calcium dependent (PubMed:12573468). Interacts with CLU
CC (By similarity). {ECO:0000250|UniProtKB:Q14114,
CC ECO:0000269|PubMed:12573468}.
CC -!- INTERACTION:
CC Q924X6; Q62108: Dlg4; NbExp=3; IntAct=EBI-432319, EBI-300895;
CC Q924X6; P35438: Grin1; NbExp=4; IntAct=EBI-432319, EBI-400084;
CC Q924X6; Q60841: Reln; NbExp=4; IntAct=EBI-432319, EBI-9248666;
CC Q924X6; P02749: APOH; Xeno; NbExp=2; IntAct=EBI-432319, EBI-2114682;
CC Q924X6; Q99068: Lrpap1; Xeno; NbExp=2; IntAct=EBI-432319, EBI-919734;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Secreted. Note=Isoforms that contain
CC the exon coding for a furin-type cleavage site are proteolytically
CC processed, leading to a secreted receptor fragment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q924X6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924X6-2; Sequence=VSP_010309;
CC Name=3; Synonyms=ApoER2delta4-6,8-F;
CC IsoId=Q924X6-5; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed in neurons throughout the brain, with
CC strong expression in pyramidal neurons of the hippocampus, granule
CC cells of the dentate gyrus, cortical neurons and Purkinje cells of the
CC cerebellum. Also expressed in the epithelium of the choroid plexus and
CC of the blood vessels (apical expression), as well as in the epididymis.
CC {ECO:0000269|PubMed:10827199}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 12 dpc to 16 dpc. Mice which are
CC deficient in LRP8 have neuronal migration defect.
CC -!- DOMAIN: The cytoplasmic domain is involved in the binding of DAB1 and
CC in the recruitment of JNK-interacting proteins. Isoforms, which lack
CC part of the cytoplasmic domain, are unable to recruit members of the
CC family of JNK interacting proteins (JIP) to the cytoplasmic tail.
CC -!- PTM: O-glycosylated. Some alternatively spliced isoforms lack the O-
CC linked sugar domain. {ECO:0000269|PubMed:12871934}.
CC -!- PTM: Undergoes sequential, furin and gamma-secretase dependent,
CC proteolytic processing, resulting in the extracellular release of the
CC entire ligand-binding domain as a soluble polypeptide and in the
CC intracellular domain (ICD) release into the cytoplasm. The gamma-
CC secretase-dependent proteolytical processing occurs after the bulk of
CC the extracellular domain has been shed, in a furin-dependent manner, in
CC alternatively spliced isoforms carrying the furin cleavage site.
CC Hypoglycosylation (mainly hypo-O-glycosylation) leads to increased
CC extracellular cleavage, which in turn results in accelerating release
CC of the intracellular domain (ICD) by the gamma-secretase. The resulting
CC receptor fragment is able to inhibit Reelin signaling and in particular
CC the Reelin-induced DAB1 phosphorylation. {ECO:0000269|PubMed:12426372,
CC ECO:0000269|PubMed:12871934}.
CC -!- PTM: Tyrosine phosphorylated upon apoE binding. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by MYLIP leading to degradation. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Does not affect endocytosis of SEPP1 in the
CC kidney proximal tubule (PubMed:18174160). Targeted disruption of LRP8
CC and VLVLR together results in a phenotype virtually indistinguishable
CC from that seen in 'reeler' and 'scrambler' mice. Subtle effects of
CC VLDLR deletion are found mainly in the cerebellum, whereas lack of LRP8
CC predominantly affects the positioning of the neurons in the neocortex.
CC Besides brain formation defects, LRP8-deficient mice also exhibit male
CC infertility. {ECO:0000269|PubMed:10380922,
CC ECO:0000269|PubMed:18174160}.
CC -!- MISCELLANEOUS: [Isoform 3]: Contains a 18 aa insert in the
CC extracellular part which carries a furin cleavage site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR EMBL; D85463; BAB46965.1; -; mRNA.
DR EMBL; AJ312058; CAC38356.1; -; mRNA.
DR CCDS; CCDS51255.1; -. [Q924X6-2]
DR PIR; JE0237; JE0237.
DR RefSeq; XP_011238759.1; XM_011240457.2.
DR AlphaFoldDB; Q924X6; -.
DR SMR; Q924X6; -.
DR CORUM; Q924X6; -.
DR DIP; DIP-33284N; -.
DR IntAct; Q924X6; 9.
DR TCDB; 9.B.87.1.9; the selenoprotein p receptor (selp-receptor) family.
DR GlyConnect; 2487; 2 N-Linked glycans (2 sites).
DR GlyGen; Q924X6; 4 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q924X6; -.
DR PhosphoSitePlus; Q924X6; -.
DR EPD; Q924X6; -.
DR MaxQB; Q924X6; -.
DR PRIDE; Q924X6; -.
DR ProteomicsDB; 292363; -. [Q924X6-1]
DR ProteomicsDB; 292364; -. [Q924X6-2]
DR Antibodypedia; 33078; 410 antibodies from 33 providers.
DR Ensembl; ENSMUST00000143601; ENSMUSP00000115854; ENSMUSG00000028613. [Q924X6-1]
DR Ensembl; ENSMUST00000238569; ENSMUSP00000158644; ENSMUSG00000028613. [Q924X6-1]
DR MGI; MGI:1340044; Lrp8.
DR VEuPathDB; HostDB:ENSMUSG00000028613; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000154819; -.
DR InParanoid; Q924X6; -.
DR OMA; ANERTCD; -.
DR OrthoDB; 359795at2759; -.
DR PhylomeDB; Q924X6; -.
DR Reactome; R-MMU-432142; Platelet sensitization by LDL.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 16975; 3 hits in 29 CRISPR screens.
DR ChiTaRS; Lrp8; mouse.
DR PRO; PR:Q924X6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q924X6; protein.
DR Bgee; ENSMUSG00000028613; Expressed in embryonic brain and 168 other tissues.
DR ExpressionAtlas; Q924X6; baseline and differential.
DR Genevisible; Q924X6; MM.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:MGI.
DR GO; GO:0034185; F:apolipoprotein binding; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:BHF-UCL.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; TAS:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:MGI.
DR GO; GO:0038025; F:reelin receptor activity; IMP:BHF-UCL.
DR GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; ISO:MGI.
DR GO; GO:0021541; P:ammon gyrus development; IMP:BHF-UCL.
DR GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:CACAO.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:CACAO.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IGI:MGI.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IGI:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:BHF-UCL.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IMP:BHF-UCL.
DR GO; GO:1900006; P:positive regulation of dendrite development; IGI:BHF-UCL.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IGI:MGI.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:BHF-UCL.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 4.10.400.10; -; 8.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57424; SSF57424; 8.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 8.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Disulfide bond;
KW EGF-like domain; Endocytosis; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..996
FT /note="Low-density lipoprotein receptor-related protein 8"
FT /id="PRO_0000017333"
FT TOPO_DOM 29..858
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 882..996
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..76
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 79..117
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 120..158
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 160..196
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 199..238
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 250..287
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 290..326
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 330..369
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 364..408
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 409..448
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 495..541
FT /note="LDL-receptor class B 1"
FT REPEAT 542..584
FT /note="LDL-receptor class B 2"
FT REPEAT 585..628
FT /note="LDL-receptor class B 3"
FT REPEAT 629..671
FT /note="LDL-receptor class B 4"
FT REPEAT 672..714
FT /note="LDL-receptor class B 5"
FT REGION 773..831
FT /note="Clustered O-linked oligosaccharides"
FT REGION 778..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q14114"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q14114"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q14114"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q14114"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q14114"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q14114"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..53
FT /evidence="ECO:0000250|UniProtKB:Q14114"
FT DISULFID 48..66
FT /evidence="ECO:0000250|UniProtKB:Q14114"
FT DISULFID 60..75
FT /evidence="ECO:0000250|UniProtKB:Q14114"
FT DISULFID 80..92
FT /evidence="ECO:0000250"
FT DISULFID 87..105
FT /evidence="ECO:0000250"
FT DISULFID 99..116
FT /evidence="ECO:0000250"
FT DISULFID 121..135
FT /evidence="ECO:0000250"
FT DISULFID 128..148
FT /evidence="ECO:0000250"
FT DISULFID 142..157
FT /evidence="ECO:0000250"
FT DISULFID 161..173
FT /evidence="ECO:0000250"
FT DISULFID 168..186
FT /evidence="ECO:0000250"
FT DISULFID 180..195
FT /evidence="ECO:0000250"
FT DISULFID 200..213
FT /evidence="ECO:0000250"
FT DISULFID 207..226
FT /evidence="ECO:0000250"
FT DISULFID 220..237
FT /evidence="ECO:0000250"
FT DISULFID 251..264
FT /evidence="ECO:0000250"
FT DISULFID 259..277
FT /evidence="ECO:0000250"
FT DISULFID 271..286
FT /evidence="ECO:0000250"
FT DISULFID 291..303
FT /evidence="ECO:0000250"
FT DISULFID 298..316
FT /evidence="ECO:0000250"
FT DISULFID 310..325
FT /evidence="ECO:0000250"
FT DISULFID 331..344
FT /evidence="ECO:0000250"
FT DISULFID 339..357
FT /evidence="ECO:0000250"
FT DISULFID 351..368
FT /evidence="ECO:0000250"
FT DISULFID 373..384
FT /evidence="ECO:0000250"
FT DISULFID 380..393
FT /evidence="ECO:0000250"
FT DISULFID 395..407
FT /evidence="ECO:0000250"
FT DISULFID 413..423
FT /evidence="ECO:0000250"
FT DISULFID 419..432
FT /evidence="ECO:0000250"
FT DISULFID 434..447
FT /evidence="ECO:0000250"
FT VAR_SEQ 160..285
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11294845"
FT /id="VSP_010309"
FT MUTAGEN 61
FT /note="D->N: Lower affinity for RAP. Abolishes binding to
FT Reelin."
FT /evidence="ECO:0000269|PubMed:12899622"
FT MUTAGEN 102
FT /note="E->Q: Same affinity for RAP. Same affinity for
FT Reelin."
FT /evidence="ECO:0000269|PubMed:12899622"
FT MUTAGEN 145
FT /note="E->Q: Same affinity for RAP. Lower affinity for
FT Reelin."
FT /evidence="ECO:0000269|PubMed:12899622"
FT CONFLICT 32
FT /note="P -> L (in Ref. 1; BAB46965)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..287
FT /note="CS -> SA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="T -> P (in Ref. 2; CAC38356)"
FT /evidence="ECO:0000305"
FT CONFLICT 672..673
FT /note="DK -> VQ (in Ref. 2; CAC38356)"
FT /evidence="ECO:0000305"
FT CONFLICT 715..716
FT /note="KQ -> NE (in Ref. 2; CAC38356)"
FT /evidence="ECO:0000305"
FT CONFLICT 750
FT /note="Y -> F (in Ref. 2; CAC38356)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="R -> K (in Ref. 2; CAC38356)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="T -> A (in Ref. 2; CAC38356)"
FT /evidence="ECO:0000305"
FT CONFLICT 815..817
FT /note="AAA -> VAV (in Ref. 2; CAC38356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 996 AA; 109818 MW; BA1AF0132A964EBA CRC64;
MGRPELGALR PLALLLLLLL QLQHLSAADP LPGGQGPVKE CEEDQFRCRN ERCIPLVWRC
DEDNDCSDNS DEDDCPKRTC ADSDFTCDNG HCIPERWKCD GEEECPDGSD ESKATCSSEE
CPAEKLSCGP TSHKCVPASW RCDGEKDCEG GADEAGCPTL CAPHEFQCSN RSCLASVFVC
DGDDDCGDGS DERGCSDPAC PPREFRCGGG GTCIPERWVC DRQFDCEDRS DEAAELCGRA
GQGTTATPAA CAPTAQFTCR SGECIHLGWR CDGDRDCKDK SDEADCSPGP CRENEFQCGD
GTCVLAIKRC NQERDCPDGS DEAGCLQEST CEGPRRFQCK SGECVDGGKV CDDQRDCRDW
SDEPQKVCGL NECLHNNGGC SHICTDLKIG FECTCPAGFQ LLDQKTCGDI DECQDPDACS
QICVNYKGYF KCECHPGYEM DTLTKNCKAV AGKSPSLIFT NRHEVRRIDL VKRDYSRLIP
MLKNVVALDV EVATNRIYWC DLSYRKIYSA HMDKASIPDE QVVLIDEQLH SPEGLAVDWV
HKHIYWTDSG NKTISVATTD GRRRCTLFSR ELSEPRAIAV DPLRGFMYWS DWGFQAKIEK
AGLNGADRQT LVSDNIEWPN GITLDLLSQR LYWVDSKLHQ LSSIDFNGGN RKMLIFSTDF
LSHPFGVAVF EDKVFWTDLE NEAIFSANRL NGLEIAILAE NLNNPHDIVI FHELKQPKAA
DACDLSAQPN GGCEYLCLPA PQISSHSPKY TCACPDTMWL GPDMKRCYRA PQSTSTTTLA
SAMTRTVPAT TRAPGTTIHD PTYQNHSTET PSQTAAAPHS VNVPRAPSTS PSTPSPATSN
HSQHYGNEGS QMGSTVTAAV IGVIVPIVVI ALLCMSGYLI WRNWKRKNTK SMNFDNPVYR
KTTEEEEEDE LHIGRTAQIG HVYPAAISNY DRPLWAEPCL GETRDLEDPA PALKELFVLP
GEPRSQLHQL PKNPLSELPV VKCKRVALSL EDDGLP
