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 29-MAY-2024, entry version 203. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7LYU; X-ray; 3.00 A; A/B=3052-3455. DR PDBsum; 2DDU; -. DR PDBsum; 2E26; -. DR PDBsum; 3A7Q; -. DR PDBsum; 5B4X; -. DR PDBsum; 6A48; -. DR PDBsum; 7LYU; -. 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 GlyCosmos; Q60841; 20 sites, 6 glycans. 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; 10090-ENSMUSP00000124052; -. DR PeptideAtlas; Q60841; -. DR ProteomicsDB; 253205; -. [Q60841-1] DR ProteomicsDB; 253206; -. [Q60841-2] DR ProteomicsDB; 253207; -. [Q60841-3] DR Antibodypedia; 3876; 255 antibodies from 28 providers. DR DNASU; 19699; -. DR Ensembl; ENSMUST00000062372.14; ENSMUSP00000058025.8; ENSMUSG00000042453.15. [Q60841-2] DR Ensembl; ENSMUST00000161356.8; ENSMUSP00000124052.2; ENSMUSG00000042453.15. [Q60841-1] DR GeneID; 19699; -. DR KEGG; mmu:19699; -. DR UCSC; uc008wpi.1; mouse. [Q60841-1] DR AGR; MGI:103022; -. 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; ATIKHAC; -. DR OrthoDB; 3107368at2759; -. DR PhylomeDB; Q60841; -. DR TreeFam; TF106479; -. DR Reactome; R-MMU-8866376; Reelin signalling pathway. DR BioGRID-ORCS; 19699; 3 hits in 79 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 320 other cell types or tissues. DR ExpressionAtlas; Q60841; baseline and differential. 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; IBA:GO_Central. 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:ComplexPortal. 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:0000902; P:cell morphogenesis; 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: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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:BHF-UCL. 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; NAS:ComplexPortal. DR GO; GO:2001222; P:regulation of neuron migration; NAS:ComplexPortal. DR GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:BHF-UCL. DR GO; GO:0060025; P:regulation of synaptic activity; NAS: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; cd00054; EGF_CA; 1. DR CDD; cd08544; Reeler; 1. DR CDD; cd10037; Reelin_repeat_1_subrepeat_1; 1. DR CDD; cd10045; Reelin_repeat_1_subrepeat_2; 1. DR CDD; cd10038; Reelin_repeat_2_subrepeat_1; 1. DR CDD; cd10046; Reelin_repeat_2_subrepeat_2; 1. DR CDD; cd10039; Reelin_repeat_3_subrepeat_1; 1. DR CDD; cd10047; Reelin_repeat_3_subrepeat_2; 1. DR CDD; cd10040; Reelin_repeat_4_subrepeat_1; 1. DR CDD; cd10048; Reelin_repeat_4_subrepeat_2; 1. DR CDD; cd10041; Reelin_repeat_5_subrepeat_1; 1. DR CDD; cd10049; Reelin_repeat_5_subrepeat_2; 1. DR CDD; cd10042; Reelin_repeat_6_subrepeat_1; 1. DR CDD; cd10050; Reelin_repeat_6_subrepeat_2; 1. DR CDD; cd10043; Reelin_repeat_7_subrepeat_1; 1. DR CDD; cd10051; Reelin_repeat_7_subrepeat_2; 1. DR CDD; cd10044; Reelin_repeat_8_subrepeat_1; 1. DR CDD; cd10052; Reelin_repeat_8_subrepeat_2; 1. DR CDD; cd10036; Reelin_subrepeat_Nt; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 19. DR Gene3D; 2.60.40.4060; Reeler domain; 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; IPR049419; Reelin_subrepeat-B. DR InterPro; IPR036278; Sialidase_sf. DR PANTHER; PTHR11841; REELIN; 1. DR PANTHER; PTHR11841:SF1; REELIN; 1. DR Pfam; PF18720; EGF_Tenascin; 1. DR Pfam; PF21471; Reelin_subrepeat-B; 18. DR SMART; SM00181; EGF; 8. DR SUPFAM; SSF50939; Sialidases; 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" FT STRAND 3059..3061 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3081..3084 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3091..3096 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3107..3109 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3113..3115 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3119..3128 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3140..3146 FT /evidence="ECO:0007829|PDB:7LYU" FT HELIX 3148..3150 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3153..3157 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3179..3181 FT /evidence="ECO:0007829|PDB:7LYU" FT TURN 3183..3185 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3190..3195 FT /evidence="ECO:0007829|PDB:7LYU" FT HELIX 3198..3200 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3202..3210 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3221..3230 FT /evidence="ECO:0007829|PDB:7LYU" FT HELIX 3233..3238 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3239..3243 FT /evidence="ECO:0007829|PDB:7LYU" FT TURN 3244..3246 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3247..3250 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3254..3259 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3261..3264 FT /evidence="ECO:0007829|PDB:7LYU" FT HELIX 3277..3283 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3284..3289 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3291..3293 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3307..3310 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3316..3320 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3330..3338 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3350..3352 FT /evidence="ECO:0007829|PDB:7LYU" FT TURN 3353..3358 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3359..3367 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3373..3378 FT /evidence="ECO:0007829|PDB:7LYU" FT HELIX 3380..3382 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3387..3392 FT /evidence="ECO:0007829|PDB:7LYU" FT HELIX 3395..3397 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3399..3408 FT /evidence="ECO:0007829|PDB:7LYU" FT STRAND 3419..3426 FT /evidence="ECO:0007829|PDB:7LYU" 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 //