| IED ID | IndEnz0002008409 |
| Enzyme Type ID | protease008409 |
| Protein Name |
Reelin EC 3.4.21.- Fragment |
| Gene Name | RELN |
| Organism | Gallus gallus (Chicken) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
| Enzyme Sequence | TNGLNTTTASVLQFSLGSGSCRFSYSDPSITVSYSKNSSADWTQLEKISAPSNVSTIIHILYLPEDAKGENVHFQWKQDYLHAGEVYEACWALDNILIINAAHRKVVLEDNLDPVDTGNWLFFPGATVKHSCQSDGNSIYFHGTEGSEFNFATTRDVDLSTEDAQEQWAEEFESQPKGWDILGAVIGTECGTLESGSSMVFLRDGERKICTPYMDTTGYGNLRFYFSMGGNCDSGESHENDVILYAKIEGRREHIALDTLTYAAYKVPSLVSVVISPDLQTPATKFCLKQKSHQGHNRNVWAVDYFHVLPVLPSTVTHMIQFSINLGCGTYQPGNSVSLEFSTNHGRSWSLLHTECLPEICAGPHLPHSTVYASENYSGWNRITTPVPNAALTSDTRIRWRQTGPIHGNMWAIDNIYIGPSCLKFCSGRGQCTRNGCKCDPGFSGPACETASQTFPMFISESFASSRLSSYHNFYSIRGAEVSFGCGVLASGKALVFNKDGRRQLITAFLDSSQSRFLQFTLRLGSKSVLSTCKAPDQPGEGVLLHYSYDNGITWKLLEHYSYLNYHEPRIISVELPEDARQIGIQFRWWQPYHSSQGEDVWAIDEIVMTSVLFNSISLDFTNLVEVTQSLGFYLGNVQPYCGHDWTLCFTGDSKLTSSMRYVETQSMQIGASYMIQFNLVMGCGQKFTPHMDNQVKLEYSTNHGLTWHLVQEECLPSMPSCQEFTSASIYHSNEFTQWRRITVLLPQKTWSSATRFRWSQCYYTAPDEWALDNIYIGQQCPNMCSGHGWCDHGVCRCDSGFRGTECQPENPLPSTVMSDFENPDVLKTEWQEIIGGEIVKPEEGCGVISSGSSLYFNKAGKRQLVSWDLDTTWVDFVQFYIQIGGESSSCNRPDSREEGVLLQYSNNGGINWQLLAEMYFSDFSKPRFVYLELPAAAKTPCTRFRWWQPVFSGEGYDQWAIDDIIILSEKQKHIIPVVNPTLPQNFYEKPAFDYPMNQLSVWLILANEGMTKNESFCSATPSAMLFGKSDGDRFAVTRDLTLKPGYVLQFKLNIGCTNQYSSSAPVLLQYSHDAGLFWSLVKEGCYPASPGTKGCEGSSRELSEPTVYHTGDFEDWTRITIVIPRSLAASKTRFRWIQESSSHKSVPPFGLDGVYISEPCPNYCNGHGDCVSGVCFCDLGYTASHGTCVSNVPNHSEMFDRFERKLSPLWYKITGGQVGTGCGVLSDGKSLYFNGPGKREARTVPLDTTNIRLVQFYVQIGSKATGNSCNRPRSRNEGLIVQYTNDNGITWHLLRELDFMSYLEPQVVSIDLPREAKTSATAFRWWQPQHGKHSAQWALDDVLIGMNDSSQTGFQDKFDGTVDLQASWYRIQGGQVDIDCLSMDTALMFSENIEKPRYAETWDFHVSASTFLQFELSMGCSKPYSNSHSIHLQYSLNNGRDWHLVTEECVPPTIGCQHYTESSIYTSERFQNWKRITAYLPPITNSPRTRFRWIQYNYASGVDSWAIDNVVLATGCPWMCSGHGICDAGHCVCDRGFGGPYCVHVNPLPSVLKDDFNGNLHPDLWPEVYGAERGNLNGDTIKSGTALIFKGEGLRMLVSRDLDCTNTVYIQFSFKFIAKGTPERSHSILLQYSVNGGITWHLIDEFYFTQTTDVLFINVPLPYTAQSNATRFRLWQPYNSGKKEEIWIIDDFIIDGNNLKNPIILLDTFDFGPKEDNWFFYPGGNIGLYCPYSSKGAPEEDSAMVFVSNEVGEHSITTRDLSVNENTIIQFEINIGCTTDSSSADPVKLEFSRDLGATWHLLLPLCYSSSSHLSSLCSTEHHPSSTYYTGTTQGWRREVIHFGKLHLCGLTRFRWYQGFYPAGSQPVTWAIDNVYIGPQCEEMCNGHGSCINGTKCICDPGYSGPTCKISTKNSDSLKDDFEGQLESDRFLLVSGGKPSRKCGIMSGGNNLFFNEEGLRMLMTRDLDLSQARFVQFFMRLGCGKGVPDPRSQLSXLQYSLNGGLTWSLLQEFLFSNSSNVGRYIALEIPMKARSSSTRLRWWQPSENGHFYSPWVIDQILIGGNISGSTVLEDDFTTLDSRKWLLHPGGTKMPVCGSTGDALVFIEKASTRYVVTTDIVVNEDSFLQIDFAASCSVTGSCYAIELEYSVDLGITWHPILRDCLPTNVECNRYHLQRILISDTFNKWTRITLPLPPYTRSQATRFRWHQPAPFDKQQTWAIDNVYIGDGCIDMCSGHGKCTQDNCVCDEHWGGLYCDEPETPLPTQLKDNFNRSPSNQNWLTVNGGKLSTVCGAVASGMALHFSGGCSRMLVTVDLNLTNAEFIQFYFMYGCLITPNNRNQGVLLEYSVNGGITWSPLMEIFYDQFSKPGFVNILLPYDAKTIGTRFRWWQPKHDGLDQNDWAIDNVLISGSTDQRTVMLDTFSSAPLPQHERSPADAGPTGRIAFDMFMEDKTTVNEHWLFHDDCSIERFCDSPDGVMICGSHDGREVYAVTHDLTPTEGWIMQFKVSVGCKTSEKLAQNQVHVQYSTDFGVSWSYLVPQCLPADPKCSGSVSQPSVFFPTKGWKRVTYSLPENLVGNPVRFRFYQKYSDVQWAIDNFYLGPGCLENCRGHGDCLKEQCICDPGYSGPNCYLTQTLKTFLKERFDNEEIKPDLWMSLEGGNTCTECGILAEDTTLYFGGQTVRQAVTQDLDLRGAKFLQYWGRIGSENNMTTCHRPTCRKEGVLLDYSIDGGITWTLLHEMDYQKYISVRHDYILLPEHALTNTTRLRWWQPFTISNGIVVSGPDRAQWALDNILIGGAEINPSQLVDTFDDEGTSHEENWSSYPNAVRTAGFCGNPSFHLYWPNKKKDKTHNILSSRELIIQPGYMMQFKIVVGCEASSCGDLHSVMLEYTKDARTDSWQLVQTHCLPSSSNSIGCSPFQFHEATIYNSVNSSMWRRITIQLPDHVSSSATQFRWIQKGEELEKQSWAIDHVYIGEACPKLCSGRGYCSTGAICICDEGYQGDDCSVFSHDLPSYIKDNFESERVTEINWETIQGGVIGNGCGQLAPYAHGDSLYFNGCQVRQAVTKPLDLTRASKIMFVLQIGSISQTDSCNTNLIDPNTVDKAVLLQYSVNNGITWQVIAQHQPKDFIQAQRVSYNVPLEARMKGVLLRWWQPRHNGTGHDQWALDHVEVVLISTRKQNYMMNFSRQHGLRHFYNRRRRSLRRYP |
| Enzyme Length | 3209 |
| Uniprot Accession Number | O93574 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (25); Domain (8); Glycosylation (18); Metal binding (6); Non-terminal residue (1); Repeat (16) |
| Keywords | Calcium;Cell adhesion;Developmental protein;Disulfide bond;EGF-like domain;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Repeat;Secreted;Serine protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18448255; 20606009; 21452229; 23438760; 24030152; 24519818; 24573679; |
| Motif | |
| Gene Encoded By | |
| Mass | 361,294 |
| Kinetics | |
| Metal Binding | METAL 1822; /note=Zinc 1; /evidence=ECO:0000250; METAL 1927; /note=Zinc 1; /evidence=ECO:0000250; METAL 2012; /note=Zinc 1; /evidence=ECO:0000250; METAL 2145; /note=Zinc 2; /evidence=ECO:0000250; METAL 2147; /note=Zinc 2; /evidence=ECO:0000250; METAL 2208; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |