Names & Taxonomy

Uniprot ID:
P78509
Entry Name:
RELN_HUMAN
Status:
reviewed
Protein Names:
Reelin (EC 3.4.21.-)
Gene Names:
RELN
Gene Names Primary:
RELN
Organism:
Homo sapiens (Human)

Structure

Length:
3460
Sequence:
MERSGWARQTFLLALLLGATLRARAAAGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSVQASQSIGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLSFIWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQGAPTDVTVHPHLAEIHSDSIILRDDFDSYHQLQLNPNIWVECNNCETGEQCGAIMHGNAVTFCEPYGPRELITTGLNTTTASVLQFSIGSGSCRFSYSDPSIIVLYAKNNSADWIQLEKIRAPSNVSTIIHILYLPEDAKGENVQFQWKQENLRVGEVYEACWALDNILIINSAHRQVVLEDSLDPVDTGNWLFFPGATVKHSCQSDGNSIYFHGNEGSEFNFATTRDVDLSTEDIQEQWSEEFESQPTGWDVLGAVIGTECGTIESGLSMVFLKDGERKLCTPSMDTTGYGNLRFYFVMGGICDPGNSHENDIILYAKIEGRKEHITLDTLSYSSYKVPSLVSVVINPELQTPATKFCLRQKNHQGHNRNVWAVDFFHVLPVLPSTMSHMIQFSINLGCGTHQPGNSVSLEFSTNHGRSWSLLHTECLPEICAGPHLPHSTVYSSENYSGWNRITIPLPNAALTRNTRIRWRQTGPILGNMWAIDNVYIGPSCLKFCSGRGQCTRHGCKCDPGFSGPACEMASQTFPMFISESFGSSRLSSYHNFYSIRGAEVSFGCGVLASGKALVFNKDGRRQLITSFLDSSQSRFLQFTLRLGSKSVLSTCRAPDQPGEGVLLHYSYDNGITWKLLEHYSYLSYHEPRIISVELPGDAKQFGIQFRWWQPYHSSQREDVWAIDEIIMTSVLFNSISLDFTNLVEVTQSLGFYLGNVQPYCGHDWTLCFTGDSKLASSMRYVETQSMQIGASYMIQFSLVMGCGQKYTPHMDNQVKLEYSTNHGLTWHLVQEECLPSMPSCQEFTSASIYHASEFTQWRRVIVLLPQKTWSSATRFRWSQSYYTAQDEWALDSIYIGQQCPNMCSGHGSCDHGICRCDQGYQGTECHPEAALPSTIMSDFENQNGWESDWQEVIGGEIVKPEQGCGVISSGSSLYFSKAGKRQLVSWDLDTSWVDFVQFYIQIGGESASCNKPDSREEGVLLQYSNNGGIQWHLLAEMYFSDFSKPRFVYLELPAAAKTPCTRFRWWQPVFSGEDYDQWAVDDIIILSEKQKQIIPVINPTLPQNFYEKPAFDYPMNQMSVWLMLANEGMVKNETFCAATPSAMIFGKSDGDRFAVTRDLTLKPGYVLQFKLNIGCANQFSSTAPVLLQYSHDAGMSWFLVKEGCYPASAGKGCEGNSRELSEPTMYHTGDFEEWTRITIVIPRSLASSKTRFRWIQESSSQKNVPPFGLDGVYISEPCPSYCSGHGDCISGVCFCDLGYTAAQGTCVSNVPNHNEMFDRFEGKLSPLWYKITGAQVGTGCGTLNDGKSLYFNGPGKREARTVPLDTRNIRLVQFYIQIGSKTSGITCIKPRTRNEGLIVQYSNDNGILWHLLRELDFMSFLEPQIISIDLPQDAKTPATAFRWWQPQHGKHSAQWALDDVLIGMNDSSQTGFQDKFDGSIDLQANWYRIQGGQVDIDCLSMDTALIFTENIGKPRYAETWDFHVSASTFLQFEMSMGCSKPFSNSHSVQLQYSLNNGKDWHLVTEECVPPTIGCLHYTESSIYTSERFQNWKRITVYLPLSTISPRTRFRWIQANYTVGADSWAIDNVVLASGCPWMCSGRGICDAGRCVCDRGFGGPYCVPVVPLPSILKDDFNGNLHPDLWPEVYGAERGNLNGETIKSGTSLIFKGEGLRMLISRDLDCTNTMYVQFSLRFIAKSTPERSHSILLQFSISGGITWHLMDEFYFPQTTNILFINVPLPYTAQTNATRFRLWQPYNNGKKEEIWIVDDFIIDGNNVNNPVMLLDTFDFGPREDNWFFYPGGNIGLYCPYSSKGAPEEDSAMVFVSNEVGEHSITTRDLNVNENTIIQFEINVGCSTDSSSADPVRLEFSRDFGATWHLLLPLCYHSSSHVSSLCSTEHHPSSTYYAGTMQGWRREVVHFGKLHLCGSVRFRWYQGFYPAGSQPVTWAIDNVYIGPQCEEMCNGQGSCINGTKCICDPGYSGPTCKISTKNPDFLKDDFEGQLESDRFLLMSGGKPSRKCGILSSGNNLFFNEDGLRMLMTRDLDLSHARFVQFFMRLGCGKGVPDPRSQPVLLQYSLNGGLSWSLLQEFLFSNSSNVGRYIALEIPLKARSGSTRLRWWQPSENGHFYSPWVIDQILIGGNISGNTVLEDDFTTLDSRKWLLHPGGTKMPVCGSTGDALVFIEKASTRYVVSTDVAVNEDSFLQIDFAASCSVTDSCYAIELEYSVDLGLSWHPLVRDCLPTNVECSRYHLQRILVSDTFNKWTRITLPLPPYTRSQATRFRWHQPAPFDKQQTWAIDNVYIGDGCIDMCSGHGRCIQGNCVCDEQWGGLYCDDPETSLPTQLKDNFNRAPSSQNWLTVNGGKLSTVCGAVASGMALHFSGGCSRLLVTVDLNLTNAEFIQFYFMYGCLITPNNRNQGVLLEYSVNGGITWNLLMEIFYDQYSKPGFVNILLPPDAKEIATRFRWWQPRHDGLDQNDWAIDNVLISGSADQRTVMLDTFSSAPVPQHERSPADAGPVGRIAFDMFMEDKTSVNEHWLFHDDCTVERFCDSPDGVMLCGSHDGREVYAVTHDLTPTEGWIMQFKISVGCKVSEKIAQNQIHVQYSTDFGVSWNYLVPQCLPADPKCSGSVSQPSVFFPTKGWKRITYPLPESLVGNPVRFRFYQKYSDMQWAIDNFYLGPGCLDNCRGHGDCLREQCICDPGYSGPNCYLTHTLKTFLKERFDSEEIKPDLWMSLEGGSTCTECGILAEDTALYFGGSTVRQAVTQDLDLRGAKFLQYWGRIGSENNMTSCHRPICRKEGVLLDYSTDGGITWTLLHEMDYQKYISVRHDYILLPEDALTNTTRLRWWQPFVISNGIVVSGVERAQWALDNILIGGAEINPSQLVDTFDDEGTSHEENWSFYPNAVRTAGFCGNPSFHLYWPNKKKDKTHNALSSRELIIQPGYMMQFKIVVGCEATSCGDLHSVMLEYTKDARSDSWQLVQTQCLPSSSNSIGCSPFQFHEATIYNSVNSSSWKRITIQLPDHVSSSATQFRWIQKGEETEKQSWAIDHVYIGEACPKLCSGHGYCTTGAICICDESFQGDDCSVFSHDLPSYIKDNFESARVTEANWETIQGGVIGSGCGQLAPYAHGDSLYFNGCQIRQAATKPLDLTRASKIMFVLQIGSMSQTDSCNSDLSGPHAVDKAVLLQYSVNNGITWHVIAQHQPKDFTQAQRVSYNVPLEARMKGVLLRWWQPRHNGTGHDQWALDHVEVVLVSTRKQNYMMNFSRQHGLRHFYNRRRRSLRRYP
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Secreted, extracellular space, extracellular matrix

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).
Gene Ontology Go:
cytoplasm
dendrite
extracellular space
proteinaceous extracellular matrix
lipoprotein particle receptor binding
metal ion binding
protein serine/threonine/tyrosine kinase activity
serine-type peptidase activity
very-low-density lipoprotein particle receptor binding
associative learning
axon guidance
brain development
cell adhesion
cell morphogenesis involved in differentiation
central nervous system development
cerebral cortex tangential migration
dendrite development
glial cell differentiation
hippocampus development
lateral motor column neuron migration
layer formation in cerebral cortex
long-term memory
long-term synaptic potentiation
modulation of synaptic transmission
neuron migration
NMDA glutamate receptor clustering
peptidyl-tyrosine phosphorylation
positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity
positive regulation of CREB transcription factor activity
positive regulation of dendritic spine morphogenesis
positive regulation of excitatory postsynaptic potential
positive regulation of lateral motor column neuron migration
positive regulation of long-term synaptic potentiation
positive regulation of neuron projection development
positive regulation of peptidyl-tyrosine phosphorylation
positive regulation of phosphatidylinositol 3-kinase signaling
positive regulation of protein kinase activity
positive regulation of protein tyrosine kinase activity
positive regulation of small GTPase mediated signal transduction
positive regulation of synapse maturation
positive regulation of synaptic transmission, glutamatergic
positive regulation of TOR signaling
postsynaptic density protein 95 clustering
receptor localization to synapse
reelin-mediated signaling pathway
regulation of behavior
regulation of N-methyl-D-aspartate selective glutamate receptor activity
response to pain
spinal cord patterning
ventral spinal cord development
Gene Ontology Biological Process:
associative learning
axon guidance
brain development
cell adhesion
cell morphogenesis involved in differentiation
central nervous system development
cerebral cortex tangential migration
dendrite development
glial cell differentiation
hippocampus development
lateral motor column neuron migration
layer formation in cerebral cortex
long-term memory
long-term synaptic potentiation
modulation of synaptic transmission
neuron migration
NMDA glutamate receptor clustering
peptidyl-tyrosine phosphorylation
positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity
positive regulation of CREB transcription factor activity
positive regulation of dendritic spine morphogenesis
positive regulation of excitatory postsynaptic potential
positive regulation of lateral motor column neuron migration
positive regulation of long-term synaptic potentiation
positive regulation of neuron projection development
positive regulation of peptidyl-tyrosine phosphorylation
positive regulation of phosphatidylinositol 3-kinase signaling
positive regulation of protein kinase activity
positive regulation of protein tyrosine kinase activity
positive regulation of small GTPase mediated signal transduction
positive regulation of synapse maturation
positive regulation of synaptic transmission, glutamatergic
positive regulation of TOR signaling
postsynaptic density protein 95 clustering
receptor localization to synapse
reelin-mediated signaling pathway
regulation of behavior
regulation of N-methyl-D-aspartate selective glutamate receptor activity
response to pain
spinal cord patterning
ventral spinal cord development
Gene Ontology Molecular Function:
lipoprotein particle receptor binding
metal ion binding
protein serine/threonine/tyrosine kinase activity
serine-type peptidase activity
very-low-density lipoprotein particle receptor binding
Gene Ontology Cellular Component:
cytoplasm
dendrite
extracellular space
proteinaceous extracellular matrix
Keywords:
Alternative splicing
Calcium
Cell adhesion
Complete proteome
Developmental protein
Disease mutation
Disulfide bond
EGF-like domain
Epilepsy
Extracellular matrix
Glycoprotein
Hydrolase
Lissencephaly
Metal-binding
Polymorphism
Protease
Reference proteome
Repeat
Secreted
Serine protease
Signal
Zinc

Publication

PubMed ID:
9049633 12853948 12690205 10328932 9861036 10973257 11317216 19159218 26046367