GenomeNet

Database: UniProt
Entry: Q924X6
LinkDB: Q924X6
Original site: Q924X6 
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   31-JUL-2019, entry version 165.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   receptor-2 produces receptor variants binding reelin but not alpha2-
RT   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.,
RA   Kahr L., Schneider W.J., Nimpf J.;
RT   "The PX-domain protein SNX17 interacts with members of the LDL
RT   receptor 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
RT   receptors 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-
RT   negative 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
RT   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.,
RA   Stockinger W., Nimpf J., Hammer R.E., Richardson J.A., Herz J.;
RT   "Reeler/Disabled-like disruption of neuronal migration in knockout
RT   mice 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.,
RA   Herz J., Schneider W.J., Nimpf J.;
RT   "The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and
RT   -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;
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
RT   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.,
RA   Posada J., Takeda S., Tafreshian K.N., Rowinsky E., Szarek M.,
RA   Waltzman R.J., Mcmillan E.A., Zhao C., Mita M., Mita A.,
RA   Chmielowski B., Postow M.A., 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
CC       apolipoprotein E (apoE)-containing ligands. LRP8 participates in
CC       transmitting the extracellular Reelin signal to intracellular
CC       signaling processes, by binding to DAB1 on its cytoplasmic tail.
CC       Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to
CC       regulate DAB1 tyrosine phosphorylation and microtubule function in
CC       neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is
CC       thus a key component of the Reelin pathway which governs neuronal
CC       layering of the forebrain during embryonic brain development.
CC       Binds the endoplasmic reticulum resident receptor-associated
CC       protein (RAP). Binds dimers of beta 2-glycoprotein I and may be
CC       involved in the suppression of platelet aggregation in the
CC       vasculature. Highly expressed in the initial segment of the
CC       epididymis, where it affects the functional expression of
CC       clusterin and phospholipid hydroperoxide glutathione peroxidase
CC       (PHGPx), two proteins required for sperm maturation
CC       (PubMed:12695510). May also function as an endocytic receptor. Not
CC       required for endocytic uptake of SEPP1 in the kidney which is
CC       mediated by LRP2 (PubMed:18174160). Together with its ligand,
CC       apolipoprotein E (apoE), may indirectly play a role in the
CC       suppression of the innate immune response by controlling the
CC       survival of myeloid-derived suppressor cells (PubMed:29336888).
CC       {ECO:0000269|PubMed:12695510, ECO:0000269|PubMed:18174160,
CC       ECO:0000269|PubMed:29336888}.
CC   -!- SUBUNIT: Reelin associates with two or more receptor molecules.
CC       Interacts with DAB1 and JNK-interacting proteins. Interacts with
CC       SNX17. Interacts with PCSK9 (By similarity). Interacts with MDK;
CC       this interaction is calcium dependent (PubMed:12573468).
CC       {ECO:0000250, ECO:0000269|PubMed:12573468}.
CC   -!- INTERACTION:
CC       P02749:APOH (xeno); NbExp=2; IntAct=EBI-432319, EBI-2114682;
CC       Q62108:Dlg4; NbExp=3; IntAct=EBI-432319, EBI-300895;
CC       P35438:Grin1; NbExp=4; IntAct=EBI-432319, EBI-400084;
CC       Q99068:Lrpap1 (xeno); NbExp=2; IntAct=EBI-432319, EBI-919734;
CC       Q60841:Reln; NbExp=4; IntAct=EBI-432319, EBI-9248666;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       type I membrane protein {ECO:0000305}. Secreted. Note=Isoforms
CC       that contain the exon coding for a furin-type cleavage site are
CC       proteolytically processed, leading to a secreted receptor
CC       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         Note=No experimental confirmation available.;
CC       Name=3; Synonyms=ApoER2delta4-6,8-F;
CC         IsoId=Q924X6-5; Sequence=Not described;
CC         Note=Contains a 18 aa insert in the extracellular part which
CC         carries a furin cleavage site.;
CC   -!- TISSUE SPECIFICITY: Expressed in neurons throughout the brain,
CC       with strong expression in pyramidal neurons of the hippocampus,
CC       granule cells of the dentate gyrus, cortical neurons and Purkinje
CC       cells of the cerebellum. Also expressed in the epithelium of the
CC       choroid plexus and of the blood vessels (apical expression), as
CC       well as in the epididymis. {ECO:0000269|PubMed:10827199}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from 12 dpc to 16 dpc. Mice which
CC       are deficient in LRP8 have neuronal migration defect.
CC   -!- DOMAIN: The cytoplasmic domain is involved in the binding of DAB1
CC       and in the recruitment of JNK-interacting proteins. Isoforms,
CC       which lack part of the cytoplasmic domain, are unable to recruit
CC       members of the family of JNK interacting proteins (JIP) to the
CC       cytoplasmic tail.
CC   -!- PTM: O-glycosylated. Some alternatively spliced isoforms lack the
CC       O-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
CC       the entire ligand-binding domain as a soluble polypeptide and in
CC       the intracellular domain (ICD) release into the cytoplasm. The
CC       gamma-secretase-dependent proteolytical processing occurs after
CC       the bulk of the extracellular domain has been shed, in a furin-
CC       dependent manner, in alternatively spliced isoforms carrying the
CC       furin cleavage site. Hypoglycosylation (mainly hypo-O-
CC       glycosylation) leads to increased extracellular cleavage, which in
CC       turn results in accelerating release of the intracellular domain
CC       (ICD) by the gamma-secretase. The resulting receptor fragment is
CC       able to inhibit Reelin signaling and in particular the Reelin-
CC       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
CC       LRP8 and VLVLR together results in a phenotype virtually
CC       indistinguishable from that seen in "reeler" and "scrambler" mice.
CC       Subtle effects of VLDLR deletion are found mainly in the
CC       cerebellum, whereas lack of LRP8 predominantly affects the
CC       positioning of the neurons in the neocortex. Besides brain
CC       formation defects, LRP8-deficient mice also exhibit male
CC       infertility. {ECO:0000269|PubMed:10380922,
CC       ECO:0000269|PubMed:18174160}.
CC   -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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   SMR; Q924X6; -.
DR   CORUM; Q924X6; -.
DR   DIP; DIP-33284N; -.
DR   IntAct; Q924X6; 9.
DR   STRING; 10090.ENSMUSP00000102343; -.
DR   TCDB; 9.B.87.1.9; the selenoprotein p receptor (selp-receptor) family.
DR   GlyConnect; 2487; -.
DR   iPTMnet; Q924X6; -.
DR   PhosphoSitePlus; Q924X6; -.
DR   PRIDE; Q924X6; -.
DR   Ensembl; ENSMUST00000143601; ENSMUSP00000115854; ENSMUSG00000028613. [Q924X6-1]
DR   GeneID; 16975; -.
DR   CTD; 7804; -.
DR   MGI; MGI:1340044; Lrp8.
DR   GeneTree; ENSGT00940000154819; -.
DR   HOGENOM; HOG000115656; -.
DR   InParanoid; Q924X6; -.
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   PRO; PR:Q924X6; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000028613; Expressed in 186 organ(s), highest expression level in brain blood vessel.
DR   ExpressionAtlas; Q924X6; baseline and differential.
DR   Genevisible; Q924X6; MM.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0005901; C:caveola; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
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:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005875; C:microtubule associated complex; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0019894; F:kinesin binding; ISO:MGI.
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: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: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; IPR013032; EGF-like_CS.
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; Complete proteome;
KW   Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted;
KW   Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   CHAIN        29    996       Low-density lipoprotein receptor-related
FT                                protein 8.
FT                                /FTId=PRO_0000017333.
FT   TOPO_DOM     29    858       Extracellular. {ECO:0000255}.
FT   TRANSMEM    859    881       Helical. {ECO:0000255}.
FT   TOPO_DOM    882    996       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       40     76       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN       79    117       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      120    158       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      160    196       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      199    238       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      250    287       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      290    326       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      330    369       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      364    408       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      409    448       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT      495    541       LDL-receptor class B 1.
FT   REPEAT      542    584       LDL-receptor class B 2.
FT   REPEAT      585    628       LDL-receptor class B 3.
FT   REPEAT      629    671       LDL-receptor class B 4.
FT   REPEAT      672    714       LDL-receptor class B 5.
FT   REGION      773    831       Clustered O-linked oligosaccharides.
FT   CARBOHYD    170    170       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    551    551       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    805    805       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    840    840       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     41     53       {ECO:0000250}.
FT   DISULFID     48     66       {ECO:0000250}.
FT   DISULFID     60     75       {ECO:0000250}.
FT   DISULFID     80     92       {ECO:0000250}.
FT   DISULFID     87    105       {ECO:0000250}.
FT   DISULFID     99    116       {ECO:0000250}.
FT   DISULFID    121    135       {ECO:0000250}.
FT   DISULFID    128    148       {ECO:0000250}.
FT   DISULFID    142    157       {ECO:0000250}.
FT   DISULFID    161    173       {ECO:0000250}.
FT   DISULFID    168    186       {ECO:0000250}.
FT   DISULFID    180    195       {ECO:0000250}.
FT   DISULFID    200    213       {ECO:0000250}.
FT   DISULFID    207    226       {ECO:0000250}.
FT   DISULFID    220    237       {ECO:0000250}.
FT   DISULFID    251    264       {ECO:0000250}.
FT   DISULFID    259    277       {ECO:0000250}.
FT   DISULFID    271    286       {ECO:0000250}.
FT   DISULFID    291    303       {ECO:0000250}.
FT   DISULFID    298    316       {ECO:0000250}.
FT   DISULFID    310    325       {ECO:0000250}.
FT   DISULFID    331    344       {ECO:0000250}.
FT   DISULFID    339    357       {ECO:0000250}.
FT   DISULFID    351    368       {ECO:0000250}.
FT   DISULFID    373    384       {ECO:0000250}.
FT   DISULFID    380    393       {ECO:0000250}.
FT   DISULFID    395    407       {ECO:0000250}.
FT   DISULFID    413    423       {ECO:0000250}.
FT   DISULFID    419    432       {ECO:0000250}.
FT   DISULFID    434    447       {ECO:0000250}.
FT   VAR_SEQ     160    285       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11294845}.
FT                                /FTId=VSP_010309.
FT   MUTAGEN      61     61       D->N: Lower affinity for RAP. Abolishes
FT                                binding to Reelin.
FT                                {ECO:0000269|PubMed:12899622}.
FT   MUTAGEN     102    102       E->Q: Same affinity for RAP. Same
FT                                affinity for Reelin.
FT                                {ECO:0000269|PubMed:12899622}.
FT   MUTAGEN     145    145       E->Q: Same affinity for RAP. Lower
FT                                affinity for Reelin.
FT                                {ECO:0000269|PubMed:12899622}.
FT   CONFLICT     32     32       P -> L (in Ref. 1; BAB46965).
FT                                {ECO:0000305}.
FT   CONFLICT    286    287       CS -> SA (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    610    610       T -> P (in Ref. 2; CAC38356).
FT                                {ECO:0000305}.
FT   CONFLICT    672    673       DK -> VQ (in Ref. 2; CAC38356).
FT                                {ECO:0000305}.
FT   CONFLICT    715    716       KQ -> NE (in Ref. 2; CAC38356).
FT                                {ECO:0000305}.
FT   CONFLICT    750    750       Y -> F (in Ref. 2; CAC38356).
FT                                {ECO:0000305}.
FT   CONFLICT    766    766       R -> K (in Ref. 2; CAC38356).
FT                                {ECO:0000305}.
FT   CONFLICT    802    802       T -> A (in Ref. 2; CAC38356).
FT                                {ECO:0000305}.
FT   CONFLICT    815    817       AAA -> VAV (in Ref. 2; CAC38356).
FT                                {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
//
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