RELN_MOUSE
ID RELN_MOUSE Reviewed; 3461 AA.
AC Q60841; E9PZ78; Q9CUA6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Reelin;
DE EC=3.4.21.-;
DE AltName: Full=Reeler protein;
DE Flags: Precursor;
GN Name=Reln; Synonyms=Rl;
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), AND INVOLVEMENT IN RL.
RC TISSUE=Cerebellum;
RX PubMed=7715726; DOI=10.1038/374719a0;
RA D'Arcangelo G., Miao G.G., Chen S.-C., Soares H.D., Morgan J.I., Curran T.;
RT "A protein related to extracellular matrix proteins deleted in the mouse
RT mutant reeler.";
RL Nature 374:719-723(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=9417911; DOI=10.1006/geno.1997.4983;
RA Royaux I., Lambert de Rouvroit C., D'Arcangelo G., Demirov D.,
RA Goffinet A.M.;
RT "Genomic organization of the mouse reelin gene.";
RL Genomics 46:240-250(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2152-3461 (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7647795; DOI=10.1038/ng0595-77;
RA Hirotsune S., Takahara T., Sasaki N., Hirose K., Yoshiki A., Ohashi T.,
RA Kusakabe M., Murakami Y., Muramatsu M., Watanabe S., Nakao K., Katsuki M.,
RA Hayashizaki Y.;
RT "The reeler gene encodes a protein with an EGF-like motif expressed by
RT pioneer neurons.";
RL Nat. Genet. 10:77-83(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3044-3461 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP CHARACTERIZATION.
RX PubMed=8987733; DOI=10.1523/jneurosci.17-01-00023.1997;
RA D'Arcangelo G., Nakajima K., Miyata T., Ogawa M., Mikoshiba K., Curran T.;
RT "Reelin is a secreted glycoprotein recognized by the CR-50 monoclonal
RT antibody.";
RL J. Neurosci. 17:23-31(1997).
RN [7]
RP CHARACTERIZATION.
RX PubMed=11689558; DOI=10.1074/jbc.m106996200;
RA Quattrocchi C.C., Wannenes F., Persico A.M., Ciafre S.A., D'Arcangelo G.,
RA Farace M.G., Keller F.;
RT "Reelin is a serine protease of the extracellular matrix.";
RL J. Biol. Chem. 277:303-309(2002).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=9182958; DOI=10.1111/j.1460-9568.1997.tb01456.x;
RA Schiffmann S.N., Bernier B., Goffinet A.M.;
RT "Reelin mRNA expression during mouse brain development.";
RL Eur. J. Neurosci. 9:1055-1071(1997).
RN [9]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=10328932; DOI=10.1006/exnr.1999.7019;
RA Lambert de Rouvroit C., Bernier B., Royaux I., de Bergeyck V.,
RA Goffinet A.M.;
RT "Evolutionarily conserved, alternative splicing of reelin during brain
RT development.";
RL Exp. Neurol. 156:229-238(1999).
RN [10]
RP INTERACTION WITH VLDLR AND APOER2.
RX PubMed=10571241; DOI=10.1016/s0896-6273(00)80861-2;
RA Hiesberger T., Trommsdorff M., Howell B.W., Goffinet A.M., Mumby M.C.,
RA Cooper J.A., Herz J.;
RT "Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces
RT tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation.";
RL Neuron 24:481-489(1999).
RN [11]
RP FUNCTION.
RX PubMed=10880573; DOI=10.1073/pnas.150040497;
RA Yip J.W., Yip Y.P.L., Nakajima K., Capriotti C.;
RT "Reelin controls position of autonomic neurons in the spinal cord.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8612-8616(2000).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 SUBUNIT, INTERCHAIN DISULFIDE BOND, AND MUTAGENESIS OF CYS-2101.
RX PubMed=21844191; DOI=10.1074/jbc.m111.242719;
RA Yasui N., Kitago Y., Beppu A., Kohno T., Morishita S., Gomi H., Nagae M.,
RA Hattori M., Takagi J.;
RT "Functional importance of covalent homodimer of reelin protein linked via
RT its central region.";
RL J. Biol. Chem. 286:35247-35256(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1222-1597, DISULFIDE BONDS, AND
RP CALCIUM-BINDING.
RX PubMed=16858396; DOI=10.1038/sj.emboj.7601240;
RA Nogi T., Yasui N., Hattori M., Iwasaki K., Takagi J.;
RT "Structure of a signaling-competent reelin fragment revealed by X-ray
RT crystallography and electron tomography.";
RL EMBO J. 25:3675-3683(2006).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1948-2662, DISULFIDE BONDS,
RP GLYCOSYLATION AT ASN-2145; ASN-2269; ASN-2317 AND ASN-2569,
RP CALCIUM-BINDING, ZINC-BINDING SITES, AND MUTAGENESIS OF LYS-2360 AND
RP LYS-2467.
RX PubMed=17548821; DOI=10.1073/pnas.0700438104;
RA Yasui N., Nogi T., Kitao T., Nakano Y., Hattori M., Takagi J.;
RT "Structure of a receptor-binding fragment of reelin and mutational analysis
RT reveal a recognition mechanism similar to endocytic receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9988-9993(2007).
CC -!- FUNCTION: Extracellular matrix serine protease that plays a role in
CC layering of neurons in the cerebral cortex and cerebellum. Regulates
CC microtubule function in neurons and neuronal migration. Affects
CC migration of sympathetic preganglionic neurons in the spinal cord,
CC where it seems to act as a barrier to neuronal migration. Enzymatic
CC activity is important for the modulation of cell adhesion. Binding to
CC the extracellular domains of lipoprotein receptors VLDLR and
CC LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of
CC TAU phosphorylation. {ECO:0000269|PubMed:10880573}.
CC -!- SUBUNIT: Oligomer of disulfide-linked homodimers. Binds to the
CC ectodomains of VLDLR and LRP8/APOER2. {ECO:0000269|PubMed:16858396,
CC ECO:0000269|PubMed:17548821, ECO:0000269|PubMed:21844191}.
CC -!- INTERACTION:
CC Q60841; Q924X6: Lrp8; NbExp=4; IntAct=EBI-9248666, EBI-432319;
CC Q60841; Q14114: LRP8; Xeno; NbExp=10; IntAct=EBI-9248666, EBI-2681187;
CC Q60841; P98155: VLDLR; Xeno; NbExp=7; IntAct=EBI-9248666, EBI-9004309;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q60841-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60841-2; Sequence=VSP_005577;
CC Name=3;
CC IsoId=Q60841-3; Sequence=VSP_005578;
CC -!- TISSUE SPECIFICITY: The major isoform 1 is neuron-specific. It is
CC abundantly produced during brain ontogenesis by the Cajal-Retzius cells
CC and other pioneer neurons located in the telencephalic marginal zone
CC and by granule cells of the external granular layer of the cerebellum.
CC Expression is located in deeper layers in the developing hippocampus
CC and olfactory bulb, low levels of expression are also detected in the
CC immature striatum. At early developmental stages, expressed also in
CC hypothalamic differentiation fields, tectum and spinal cord. A moderate
CC to low level of expression occurs in the septal area, striatal fields,
CC habenular nuclei, some thalamic nuclei, particularly the lateral
CC geniculate, the retina and some nuclei of the reticular formation in
CC the central field of the medulla. Very low levels found in liver and
CC kidney. No expression in radial glial cells, cortical plate, Purkinje
CC cells and inferior olivary neurons. The minor isoform 2 is only
CC expressed in non neuronal cells. The minor isoform 3 is found in the
CC same cells as isoform 1, but is almost undetectable in retina and brain
CC stem. {ECO:0000269|PubMed:10328932, ECO:0000269|PubMed:9182958}.
CC -!- DEVELOPMENTAL STAGE: First detected at embryonic day 11.5. Expression
CC increases up to birth and remains high from postnatal day 2 to 11 in
CC both cerebellum and fore/midbrain. Expression declines thereafter and
CC is largely brain specific in the adult.
CC -!- DOMAIN: The basic C-terminal region is essential for secretion.
CC -!- PTM: N-glycosylated and to a lesser extent also O-glycosylated.
CC {ECO:0000269|PubMed:17548821}.
CC -!- DISEASE: Note=Defects in Reln are the cause of the autosomal recessive
CC reeler (rl) phenotype which is characterized by impaired motor
CC coordination, tremors and ataxia. Neurons in affected mice fail to
CC reach their correct locations in the developing brain, disrupting the
CC organization of the cerebellar and cerebral cortices and other
CC laminated regions. {ECO:0000269|PubMed:7715726}.
CC -!- SIMILARITY: Belongs to the reelin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09788.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U24703; AAB91599.1; -; mRNA.
DR EMBL; AC113028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC119906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D63520; BAA09788.1; ALT_INIT; mRNA.
DR EMBL; AK017094; BAB30592.1; -; mRNA.
DR CCDS; CCDS39023.1; -. [Q60841-1]
DR CCDS; CCDS80217.1; -. [Q60841-2]
DR PIR; S58870; S58870.
DR RefSeq; NP_001297393.1; NM_001310464.1. [Q60841-2]
DR RefSeq; NP_035391.2; NM_011261.2. [Q60841-1]
DR PDB; 2DDU; X-ray; 2.05 A; A=1222-1597.
DR PDB; 2E26; X-ray; 2.00 A; A=1948-2661.
DR PDB; 3A7Q; X-ray; 2.60 A; A=1948-2661.
DR PDB; 5B4X; X-ray; 3.20 A; A/C=1948-2662.
DR PDB; 6A48; X-ray; 2.00 A; A=195-864.
DR PDBsum; 2DDU; -.
DR PDBsum; 2E26; -.
DR PDBsum; 3A7Q; -.
DR PDBsum; 5B4X; -.
DR PDBsum; 6A48; -.
DR SMR; Q60841; -.
DR BioGRID; 202855; 13.
DR ComplexPortal; CPX-4524; Reelin complex.
DR DIP; DIP-40924N; -.
DR IntAct; Q60841; 6.
DR STRING; 10090.ENSMUSP00000124052; -.
DR GlyConnect; 2678; 6 N-Linked glycans (2 sites).
DR GlyGen; Q60841; 20 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; Q60841; -.
DR PhosphoSitePlus; Q60841; -.
DR jPOST; Q60841; -.
DR MaxQB; Q60841; -.
DR PaxDb; Q60841; -.
DR PeptideAtlas; Q60841; -.
DR PRIDE; Q60841; -.
DR ProteomicsDB; 253205; -. [Q60841-1]
DR ProteomicsDB; 253206; -. [Q60841-2]
DR ProteomicsDB; 253207; -. [Q60841-3]
DR Antibodypedia; 3876; 229 antibodies from 28 providers.
DR DNASU; 19699; -.
DR Ensembl; ENSMUST00000062372; ENSMUSP00000058025; ENSMUSG00000042453. [Q60841-2]
DR Ensembl; ENSMUST00000161356; ENSMUSP00000124052; ENSMUSG00000042453. [Q60841-1]
DR GeneID; 19699; -.
DR KEGG; mmu:19699; -.
DR UCSC; uc008wpi.1; mouse. [Q60841-1]
DR CTD; 5649; -.
DR MGI; MGI:103022; Reln.
DR VEuPathDB; HostDB:ENSMUSG00000042453; -.
DR eggNOG; ENOG502QSIP; Eukaryota.
DR GeneTree; ENSGT00580000081623; -.
DR HOGENOM; CLU_000468_0_0_1; -.
DR InParanoid; Q60841; -.
DR OMA; MGGGDCD; -.
DR OrthoDB; 9177at2759; -.
DR PhylomeDB; Q60841; -.
DR TreeFam; TF106479; -.
DR Reactome; R-MMU-8866376; Reelin signalling pathway.
DR BioGRID-ORCS; 19699; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Reln; mouse.
DR EvolutionaryTrace; Q60841; -.
DR PRO; PR:Q60841; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q60841; protein.
DR Bgee; ENSMUSG00000042453; Expressed in ciliary body and 317 other tissues.
DR ExpressionAtlas; Q60841; baseline and differential.
DR Genevisible; Q60841; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:ComplexPortal.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0110157; C:reelin complex; ISO:MGI.
DR GO; GO:0070325; F:lipoprotein particle receptor binding; IPI:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; IPI:BHF-UCL.
DR GO; GO:0008306; P:associative learning; IDA:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0021800; P:cerebral cortex tangential migration; IMP:MGI.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0021542; P:dentate gyrus development; ISO:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IDA:BHF-UCL.
DR GO; GO:1904936; P:interneuron migration; IMP:MGI.
DR GO; GO:0097477; P:lateral motor column neuron migration; IMP:UniProtKB.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
DR GO; GO:0007612; P:learning; IMP:CACAO.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0007616; P:long-term memory; IDA:BHF-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:CACAO.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:BHF-UCL.
DR GO; GO:0097475; P:motor neuron migration; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; IMP:BHF-UCL.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; IDA:BHF-UCL.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IDA:BHF-UCL.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:BHF-UCL.
DR GO; GO:1902078; P:positive regulation of lateral motor column neuron migration; IMP:BHF-UCL.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IDA:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:BHF-UCL.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IDA:MGI.
DR GO; GO:0090129; P:positive regulation of synapse maturation; IDA:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IDA:BHF-UCL.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IDA:BHF-UCL.
DR GO; GO:0097107; P:postsynaptic density assembly; IC:BHF-UCL.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; IMP:BHF-UCL.
DR GO; GO:0035418; P:protein localization to synapse; IMP:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0097120; P:receptor localization to synapse; IMP:BHF-UCL.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050795; P:regulation of behavior; IMP:BHF-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0045664; P:regulation of neuron differentiation; IC:ComplexPortal.
DR GO; GO:2001222; P:regulation of neuron migration; IC:ComplexPortal.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:BHF-UCL.
DR GO; GO:0060025; P:regulation of synaptic activity; IC:ComplexPortal.
DR GO; GO:0048265; P:response to pain; IMP:MGI.
DR GO; GO:0021511; P:spinal cord patterning; IMP:MGI.
DR GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
DR CDD; cd08544; Reeler; 1.
DR Gene3D; 2.60.40.4060; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR041161; EGF_Tenascin.
DR InterPro; IPR002861; Reeler_dom.
DR InterPro; IPR042307; Reeler_sf.
DR InterPro; IPR034968; Reelin.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR11841; PTHR11841; 12.
DR Pfam; PF18720; EGF_Tenascin; 1.
DR Pfam; PF02014; Reeler; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF50939; SSF50939; 3.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS51019; REELIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion;
KW Developmental protein; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..3461
FT /note="Reelin"
FT /id="PRO_0000030305"
FT DOMAIN 27..191
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT REPEAT 593..604
FT /note="BNR 1"
FT DOMAIN 671..702
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 799..810
FT /note="BNR 2"
FT REPEAT 952..963
FT /note="BNR 3"
FT DOMAIN 1030..1061
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1157..1168
FT /note="BNR 4"
FT REPEAT 1323..1334
FT /note="BNR 5"
FT DOMAIN 1409..1442
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1535..1546
FT /note="BNR 6"
FT REPEAT 1686..1697
FT /note="BNR 7"
FT DOMAIN 1765..1796
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1884..1895
FT /note="BNR 8"
FT REPEAT 2043..2054
FT /note="BNR 9"
FT DOMAIN 2129..2161
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 2250..2261
FT /note="BNR 10"
FT REPEAT 2399..2410
FT /note="BNR 11"
FT DOMAIN 2478..2509
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 2598..2609
FT /note="BNR 12"
FT REPEAT 2778..2789
FT /note="BNR 13"
FT DOMAIN 2853..2884
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 2979..2990
FT /note="BNR 14"
FT REPEAT 3143..3155
FT /note="BNR 15"
FT DOMAIN 3228..3260
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 3363..3374
FT /note="BNR 16"
FT BINDING 2061
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 2074
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 2179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 2264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 2397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 2399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 2460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17548821"
FT CARBOHYD 2269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17548821"
FT CARBOHYD 2317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17548821"
FT CARBOHYD 2569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17548821"
FT CARBOHYD 2962
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3016
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3073
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 155..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 540..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 609..614
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 675..685
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 692..701
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 895..937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 968..975
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1034..1044
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1051..1060
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1271..1310
FT DISULFID 1339..1348
FT DISULFID 1633..1673
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1702..1709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1983..2030
FT DISULFID 2059..2070
FT DISULFID 2101
FT /note="Interchain"
FT DISULFID 2133..2143
FT DISULFID 2137..2149
FT DISULFID 2151..2160
FT DISULFID 2195..2235
FT DISULFID 2348..2387
FT DISULFID 2393..2559
FT DISULFID 2482..2492
FT DISULFID 2486..2497
FT DISULFID 2499..2508
FT DISULFID 2544..2584
FT DISULFID 2794..2801
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2919..2966
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3160..3170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3232..3242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3236..3248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3250..3259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3296..3346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 3429..3461
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005578"
FT VAR_SEQ 3429..3430
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_005577"
FT MUTAGEN 2101
FT /note="C->A: Fails to assemble into disulfide-bonded
FT multimers, while still exhibiting non-covalently associated
FT high molecular weight oligomeric states in solution;
FT retains binding to LRP8 and VLDR receptors but fails to
FT show signaling activity."
FT /evidence="ECO:0000269|PubMed:21844191"
FT MUTAGEN 2360
FT /note="K->A: Abolishes ApoER2-binding."
FT /evidence="ECO:0000269|PubMed:17548821"
FT MUTAGEN 2467
FT /note="K->A: Abolishes ApoER2-binding."
FT /evidence="ECO:0000269|PubMed:17548821"
FT CONFLICT 1191
FT /note="A -> G (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1202
FT /note="Q -> K (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1335
FT /note="V -> L (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1345
FT /note="G -> A (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1505
FT /note="R -> S (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1522..1524
FT /note="CIK -> YIT (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1529
FT /note="N -> Y (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1593
FT /note="D -> G (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1611
FT /note="F -> L (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1648
FT /note="K -> N (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1661
FT /note="A -> E (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1667
FT /note="F -> W (in Ref. 1; AAB91599)"
FT /evidence="ECO:0000305"
FT CONFLICT 3066
FT /note="Missing (in Ref. 5; BAB30592)"
FT /evidence="ECO:0000305"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:6A48"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:6A48"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 322..331
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 344..356
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6A48"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 474..482
FT /evidence="ECO:0007829|PDB:6A48"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 495..501
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:6A48"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 522..527
FT /evidence="ECO:0007829|PDB:6A48"
FT HELIX 530..532
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 534..544
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 554..562
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 571..583
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 589..597
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:6A48"
FT TURN 611..613
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 623..626
FT /evidence="ECO:0007829|PDB:6A48"
FT TURN 627..629
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 632..639
FT /evidence="ECO:0007829|PDB:6A48"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 646..655
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 664..673
FT /evidence="ECO:0007829|PDB:6A48"
FT HELIX 676..681
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 682..686
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 689..692
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 703..706
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:6A48"
FT HELIX 721..723
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 727..732
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 734..737
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 742..745
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 747..750
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 756..760
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 770..777
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 795..803
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 809..814
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 823..828
FT /evidence="ECO:0007829|PDB:6A48"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 836..844
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 849..851
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 855..862
FT /evidence="ECO:0007829|PDB:6A48"
FT STRAND 1301..1310
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1320..1327
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1333..1335
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1345..1348
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1359..1361
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1370..1375
FT /evidence="ECO:0007829|PDB:2DDU"
FT HELIX 1378..1380
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1386..1390
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1408..1411
FT /evidence="ECO:0007829|PDB:2DDU"
FT HELIX 1414..1419
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1420..1424
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1427..1430
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1434..1437
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1440..1445
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1451..1453
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1456..1458
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1463..1472
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1478..1481
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1483..1486
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1493..1496
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1506..1513
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1516..1518
FT /evidence="ECO:0007829|PDB:2DDU"
FT HELIX 1528..1530
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1531..1539
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1545..1550
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1559..1564
FT /evidence="ECO:0007829|PDB:2DDU"
FT HELIX 1567..1569
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1571..1579
FT /evidence="ECO:0007829|PDB:2DDU"
FT HELIX 1584..1586
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1590..1597
FT /evidence="ECO:0007829|PDB:2DDU"
FT STRAND 1958..1960
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 1963..1965
FT /evidence="ECO:0007829|PDB:2E26"
FT HELIX 1968..1970
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 1971..1973
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 1978..1980
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 1996..1999
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2001..2003
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 2005..2011
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2014..2016
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2020..2032
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2040..2047
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2053..2056
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2059..2061
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2078..2080
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2089..2095
FT /evidence="ECO:0007829|PDB:2E26"
FT TURN 2096..2099
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2102..2113
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2122..2131
FT /evidence="ECO:0007829|PDB:2E26"
FT HELIX 2134..2139
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2140..2144
FT /evidence="ECO:0007829|PDB:2E26"
FT TURN 2145..2147
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2148..2151
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2155..2157
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2170..2172
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2174..2176
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2178..2187
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2189..2193
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2197..2201
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2203..2206
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2208..2210
FT /evidence="ECO:0007829|PDB:3A7Q"
FT STRAND 2212..2216
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2226..2233
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2236..2238
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2247..2254
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2260..2265
FT /evidence="ECO:0007829|PDB:2E26"
FT TURN 2269..2272
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2275..2280
FT /evidence="ECO:0007829|PDB:2E26"
FT HELIX 2283..2285
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2287..2296
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2299..2301
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2307..2315
FT /evidence="ECO:0007829|PDB:2E26"
FT TURN 2318..2320
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 2324..2326
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2328..2330
FT /evidence="ECO:0007829|PDB:2E26"
FT TURN 2333..2335
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2336..2338
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2343..2345
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2354..2357
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2364..2368
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2371..2373
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2378..2384
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2387..2389
FT /evidence="ECO:0007829|PDB:3A7Q"
FT STRAND 2395..2403
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2409..2412
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2419..2422
FT /evidence="ECO:0007829|PDB:2E26"
FT TURN 2433..2436
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2440..2445
FT /evidence="ECO:0007829|PDB:2E26"
FT HELIX 2448..2450
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2452..2461
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2471..2480
FT /evidence="ECO:0007829|PDB:2E26"
FT HELIX 2484..2488
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2489..2493
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2496..2499
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2503..2505
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2510..2513
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2519..2521
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2523..2526
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 2529..2531
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2532..2542
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2547..2550
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2552..2555
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2562..2565
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2575..2582
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2584..2586
FT /evidence="ECO:0007829|PDB:2E26"
FT HELIX 2591..2593
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2594..2602
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2608..2613
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2615..2617
FT /evidence="ECO:0007829|PDB:3A7Q"
FT STRAND 2622..2627
FT /evidence="ECO:0007829|PDB:2E26"
FT HELIX 2630..2632
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2634..2642
FT /evidence="ECO:0007829|PDB:2E26"
FT STRAND 2654..2661
FT /evidence="ECO:0007829|PDB:2E26"
SQ 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
