Q60841 · RELN_MOUSE

Function

function

Extracellular matrix serine protease secreted by pioneer neurons that plays a role in layering of neurons in the cerebral cortex and cerebellum by coordinating cell positioning during neurodevelopment (PubMed:10880573, PubMed:11689558, PubMed:7715726, PubMed:8987733).
Regulates microtubule function in neurons and neuronal migration (PubMed:10880573, PubMed:7715726, PubMed:8987733).
Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation (PubMed:10571241).
Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration (PubMed:11689558, PubMed:7715726, PubMed:8987733).
Enzymatic activity is important for the modulation of cell adhesion (PubMed:11689558, PubMed:8987733).

Features

Showing features for binding site.

134615001,0001,5002,0002,5003,000
TypeIDPosition(s)Description
Binding site2061Zn2+ 1 (UniProtKB | ChEBI)
Binding site2074Zn2+ 1 (UniProtKB | ChEBI)
Binding site2179Zn2+ 1 (UniProtKB | ChEBI)
Binding site2264Zn2+ 1 (UniProtKB | ChEBI)
Binding site2397Zn2+ 2 (UniProtKB | ChEBI)
Binding site2399Zn2+ 2 (UniProtKB | ChEBI)
Binding site2460Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentaxon
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentcytoplasm
Cellular Componentdendrite
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Cellular Componentneuron projection
Cellular Componentneuronal cell body
Cellular Componentperikaryon
Cellular Componentplasma membrane
Cellular Componentreelin complex
Molecular Functionlipoprotein particle receptor binding
Molecular Functionmetal ion binding
Molecular Functionreceptor ligand activity
Molecular Functionserine-type peptidase activity
Molecular Functionvery-low-density lipoprotein particle receptor binding
Biological Processassociative learning
Biological Processaxon guidance
Biological Processbrain development
Biological Processcell adhesion
Biological Processcell migration
Biological Processcell morphogenesis
Biological Processcentral nervous system development
Biological Processcerebral cortex development
Biological Processcerebral cortex tangential migration
Biological Processdendrite development
Biological Processdentate gyrus development
Biological Processforebrain development
Biological Processglial cell differentiation
Biological Processhippocampus development
Biological Processinterneuron migration
Biological Processlateral motor column neuron migration
Biological Processlayer formation in cerebral cortex
Biological Processlearning
Biological Processlocomotory behavior
Biological Processlong-term memory
Biological Processlong-term synaptic potentiation
Biological Processmodulation of chemical synaptic transmission
Biological Processmotor neuron migration
Biological Processneuron migration
Biological ProcessNMDA glutamate receptor clustering
Biological Processpositive regulation of AMPA receptor activity
Biological Processpositive regulation of CREB transcription factor activity
Biological Processpositive regulation of dendritic spine morphogenesis
Biological Processpositive regulation of excitatory postsynaptic potential
Biological Processpositive regulation of lateral motor column neuron migration
Biological Processpositive regulation of long-term synaptic potentiation
Biological Processpositive regulation of neuron projection development
Biological Processpositive regulation of peptidyl-tyrosine phosphorylation
Biological Processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Processpositive regulation of protein phosphorylation
Biological Processpositive regulation of protein tyrosine kinase activity
Biological Processpositive regulation of small GTPase mediated signal transduction
Biological Processpositive regulation of synapse maturation
Biological Processpositive regulation of synaptic transmission, glutamatergic
Biological Processpositive regulation of TOR signaling
Biological Processpostsynaptic density assembly
Biological Processpostsynaptic density protein 95 clustering
Biological Processprotein localization to synapse
Biological Processproteolysis
Biological Processreceptor localization to synapse
Biological Processreelin-mediated signaling pathway
Biological Processregulation of behavior
Biological Processregulation of gene expression
Biological Processregulation of neuron differentiation
Biological Processregulation of neuron migration
Biological Processregulation of NMDA receptor activity
Biological Processregulation of synapse maturation
Biological Processregulation of synaptic activity
Biological Processresponse to pain
Biological Processspinal cord patterning
Biological Processventral spinal cord development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Reelin
  • EC number
  • Alternative names
    • Reeler protein

Gene names

    • Name
      Reln
    • Synonyms
      Rl

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • BALB/cJ
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q60841
  • Secondary accessions
    • E9PZ78
    • Q9CUA6

Proteomes

Organism-specific databases

Phenotypes & Variants

Involvement in disease

  • Defects in Reln are the cause of the autosomal recessive reeler (rl) phenotype which is characterized by impaired motor coordination, tremors and ataxia. Neurons in affected mice fail to reach their correct locations in the developing brain, disrupting the organization of the cerebellar and cerebral cortices and other laminated regions

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis2101Fails to assemble into disulfide-bonded multimers, while still exhibiting non-covalently associated high molecular weight oligomeric states in solution; retains binding to LRP8 and VLDR receptors but fails to show signaling activity.
Mutagenesis2360Abolishes ApoER2-binding.
Mutagenesis2467Abolishes ApoER2-binding.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 144 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-26
ChainPRO_000003030527-3461Reelin
Disulfide bond41↔127
Glycosylation141N-linked (GlcNAc...) asparagine
Disulfide bond155↔179
Glycosylation258N-linked (GlcNAc...) asparagine
Glycosylation290N-linked (GlcNAc...) asparagine
Glycosylation306N-linked (GlcNAc...) asparagine
Disulfide bond540↔581
Disulfide bond609↔614
Glycosylation629N-linked (GlcNAc...) asparagine
Disulfide bond675↔685
Disulfide bond692↔701
Disulfide bond895↔937
Disulfide bond968↔975
Disulfide bond1034↔1044
Disulfide bond1051↔1060
Glycosylation1267N-linked (GlcNAc...) asparagine
Disulfide bond1339↔1348
Disulfide bond1413↔1423
Disulfide bond1417↔1428
Disulfide bond1430↔1441
Glycosylation1447N-linked (GlcNAc...) asparagine
Disulfide bond1475↔1522
Glycosylation1600N-linked (GlcNAc...) asparagine
Disulfide bond1633↔1673
Disulfide bond1702↔1709
Glycosylation1750N-linked (GlcNAc...) asparagine
Glycosylation1921N-linked (GlcNAc...) asparagine
Disulfide bond1983↔2030
Disulfide bond2059↔2070
Disulfide bond2101Interchain
Disulfide bond2133↔2143
Disulfide bond2137↔2149
Glycosylation2145N-linked (GlcNAc...) asparagine
Disulfide bond2151↔2160
Disulfide bond2195↔2235
Glycosylation2269N-linked (GlcNAc...) asparagine
Glycosylation2317N-linked (GlcNAc...) asparagine
Disulfide bond2348↔2387
Disulfide bond2393↔2559
Disulfide bond2482↔2492
Disulfide bond2486↔2497
Disulfide bond2499↔2508
Disulfide bond2544↔2584
Glycosylation2569N-linked (GlcNAc...) asparagine
Disulfide bond2794↔2801
Disulfide bond2919↔2966
Glycosylation2962N-linked (GlcNAc...) asparagine
Glycosylation3016N-linked (GlcNAc...) asparagine
Glycosylation3073N-linked (GlcNAc...) asparagine
Disulfide bond3160↔3170
Glycosylation3185N-linked (GlcNAc...) asparagine
Disulfide bond3232↔3242
Disulfide bond3236↔3248
Disulfide bond3250↔3259
Disulfide bond3296↔3346
Glycosylation3412N-linked (GlcNAc...) asparagine
Glycosylation3439N-linked (GlcNAc...) asparagine

Post-translational modification

N-glycosylated and to a lesser extent also O-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

The major isoform 1 is neuron-specific. It is abundantly produced during brain ontogenesis by the Cajal-Retzius cells and other pioneer neurons located in the telencephalic marginal zone and by granule cells of the external granular layer of the cerebellum. Expression is located in deeper layers in the developing hippocampus and olfactory bulb, low levels of expression are also detected in the immature striatum. At early developmental stages, expressed also in hypothalamic differentiation fields, tectum and spinal cord. A moderate to low level of expression occurs in the septal area, striatal fields, habenular nuclei, some thalamic nuclei, particularly the lateral geniculate, the retina and some nuclei of the reticular formation in the central field of the medulla. Very low levels found in liver and kidney. No expression in radial glial cells, cortical plate, Purkinje cells and inferior olivary neurons. The minor isoform 2 is only expressed in non neuronal cells. The minor isoform 3 is found in the same cells as isoform 1, but is almost undetectable in retina and brain stem.

Developmental stage

First detected at embryonic day 11.5. Expression increases up to birth and remains high from postnatal day 2 to 11 in both cerebellum and fore/midbrain. Expression declines thereafter and is largely brain specific in the adult.

Gene expression databases

Interaction

Subunit

Oligomer of disulfide-linked homodimers.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q60841Lrp8 Q924X64EBI-9248666, EBI-432319
XENO Q60841LRP8 Q1411410EBI-9248666, EBI-2681187
XENO Q60841VLDLR P981557EBI-9248666, EBI-9004309

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, repeat.

TypeIDPosition(s)Description
Domain27-191Reelin
Repeat593-604BNR 1
Domain671-702EGF-like 1
Repeat799-810BNR 2
Repeat952-963BNR 3
Domain1030-1061EGF-like 2
Repeat1157-1168BNR 4
Repeat1323-1334BNR 5
Domain1409-1442EGF-like 3
Repeat1535-1546BNR 6
Repeat1686-1697BNR 7
Domain1765-1796EGF-like 4
Repeat1884-1895BNR 8
Repeat2043-2054BNR 9
Domain2129-2161EGF-like 5
Repeat2250-2261BNR 10
Repeat2399-2410BNR 11
Domain2478-2509EGF-like 6
Repeat2598-2609BNR 12
Repeat2778-2789BNR 13
Domain2853-2884EGF-like 7
Repeat2979-2990BNR 14
Repeat3143-3155BNR 15
Domain3228-3260EGF-like 8
Repeat3363-3374BNR 16

Domain

The basic C-terminal region is essential for secretion.

Sequence similarities

Belongs to the reelin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 3 isoforms produced by Alternative splicing.

Q60841-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    3,461
  • Mass (Da)
    387,495
  • Last updated
    2011-07-27 v3
  • Checksum
    1CCE64C845160F2E
MERGCWAPRALVLAVLLLLATLRARAATGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSIQSSQSIGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLSFVWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQGAPTEATAYSHLAEIHSDSVILRDDFDSYQQLELNPNIWVECSNCEMGEQCGTIMHGNAVTFCEPYGPRELTTTCLNTTTASVLQFSIGSGSCRFSYSDPSITVSYAKNNTADWIQLEKIRAPSNVSTVIHILYLPEEAKGESVQFQWKQDSLRVGEVYEACWALDNILVINSAHREVVLEDNLDPVDTGNWLFFPGATVKHSCQSDGNSIYFHGNEGSEFNFATTRDVDLSTEDIQEQWSEEFESQPTGWDILGAVVGADCGTVESGLSLVFLKDGERKLCTPYMDTTGYGNLRFYFVMGGICDPGVSHENDIILYAKIEGRKEHIALDTLTYSSYKVPSLVSVVINPELQTPATKFCLRQKSHQGYNRNVWAVDFFHVLPVLPSTMSHMIQFSINLGCGTHQPGNSVSLEFSTNHGRSWSLLHTECLPEICAGPHLPHSTVYSSENYSGWNRITIPLPNAALTRDTRIRWRQTGPILGNMWAIDNVYIGPSCLKFCSGRGQCTRHGCKCDPGFSGPACEMASQTFPMFISESFGSARLSSYHNFYSIRGAEVSFGCGVLASGKALVFNKDGRRQLITSFLDSSQSRFLQFTLRLGSKSVLSTCRAPDQPGEGVLLHYSYDNGITWKLLEHYSYVNYHEPRIISVELPDDARQFGIQFRWWQPYHSSQGEDVWAIDEIVMTSVLFNSISLDFTNLVEVTQSLGFYLGNVQPYCGHDWTLCFTGDSKLASSMRYVETQSMQIGASYMIQFSLVMGCGQKYTPHMDNQVKLEYSANHGLTWHLVQEECLPSMPSCQEFTSASIYHASEFTQWRRVTVVLPQKTWSGATRFRWSQSYYTAQDEWALDNIYIGQQCPNMCSGHGSCDHGVCRCDQGYQGTECHPEAALPSTIMSDFENPSSWESDWQEVIGGEVVKPEQGCGVVSSGSSLYFSKAGKRQLVSWDLDTSWVDFVQFYIQIGGESAACNKPDSREEGILLQYSNNGGIQWHLLAEMYFSDFSKPRFVYLELPAAAKTPCTRFRWWQPVFSGEDYDQWAVDDIIILSEKQKQVIPVVNPTLPQNFYEKPAFDYPMNQMSVWLMLANEGMAKNDSFCATTPSAMVFGKSDGDRFAVTRDLTLKPGYVLQFKLNIGCTSQFSSTAPVLLQYSHDAGMSWFLVKEGCFPASAGKGCEGNSRELSEPTVYYTGDFEEWTRITIAIPRSLASSKTRFRWIQESSSQKNVPPFGLDGVYISEPCPSYCSGHGDCISGVCFCDLGYTAAQGTCVSNTPNHSEMFDRFEGKLSPLWYKITGGQVGTGCGTLNDGRSLYFNGLGKREARTVPLDTRNIRLVQFYIQIGSKTSGITCIKPRARNEGLVVQYSNDNGILWHLLRELDFMSFLEPQIISIDLPREAKTPATAFRWWQPQHGKHSAQWALDDVLIGVNDSSQTGFQDKFDGSIDLQANWYRIQGGQVDIDCLSMDTALIFTENIGKPRYAETWDFHVSASSFLQFEMNMGCSKPFSGAHGIQLQYSLNNGKDWQLVTEECVPPTIGCVHYTESSTYTSERFQNWRRVTVYLPLATNSPRTRFRWIQTNYTVGADSWAIDNVILASGCPWMCSGRGICDSGRCVCDRGFGGPFCVPVVPLPSILKDDFNGNLHPDLWPEVYGAERGNLNGETIKSGTCLIFKGEGLRMLISRDLDCTNTMYVQFSLRFIAKGTPERSHSILLQFSVSGGVTWHLMDEFYFPQTTSILFINVPLPYGAQTNATRFRLWQPYNNGKKEEIWIIDDFIIDGNNLNNPVLLLDTFDFGPREDNWFFYPGGNIGLYCPYSSKGAPEEDSAMVFVSNEVGEHSITTRDLSVNENTIIQFEINVGCSTDSSSADPVRLEFSRDFGATWHLLLPLCYHSSSLVSSLCSTEHHPSSTYYAGTTQGWRREVVHFGKLHLCGSVRFRWYQGFYPAGSQPVTWAIDNVYIGPQCEEMCYGHGSCINGTKCICDPGYSGPTCKISTKNPDFLKDDFEGQLESDRFLLMSGGKPSRKCGILSSGNNLFFNEDGLRMLVTRDLDLSHARFVQFFMRLGCGKGVPDPRSQPVLLQYSLNGGLSWSLLQEFLFSNSSNVGRYIALEMPLKARSGSTRLRWWQPSENGHFYSPWVIDQILIGGNISGNTVLEDDFSTLDSRKWLLHPGGTKMPVCGSTGDALVFIEKASTRYVVTTDIAVNEDSFLQIDFAASCSVTDSCYAIELEYSVDLGLSWHPLVRDCLPTNVECSRYHLQRILVSDTFNKWTRITLPLPSYTRSQATRFRWHQPAPFDKQQTWAIDNVYIGDGCLDMCSGHGRCVQGSCVCDEQWGGLYCDEPETSLPTQLKDNFNRAPSNQNWLTVSGGKLSTVCGAVASGLALHFSGGCSRLLVTVDLNLTNAEFIQFYFMYGCLITPSNRNQGVLLEYSVNGGITWNLLMEIFYDQYSKPGFVNILLPPDAKEIATRFRWWQPRHDGLDQNDWAIDNVLISGSADQRTVMLDTFSSAPVPQHERSPADAGPVGRIAFEMFLEDKTSVNENWLFHDDCTVERFCDSPDGVMLCGSHDGREVYAVTHDLTPTENWIMQFKISVGCKVPEKIAQNQIHVQFSTDFGVSWSYLVPQCLPADPKCSGSVSQPSVFFPTEGWKRITYPLPESLTGNPVRFRFYQKYSDVQWAIDNFYLGPGCLDNCGGHGDCLKEQCICDPGYSGPNCYLTHSLKTFLKERFDSEEIKPDLWMSLEGGSTCTECGVLAENTALYFGGSTVRQAITQDLDLRGAKFLQYWGRIGSENNMTSCHRPVCRKEGVLLDFSTDGGITWTLLHEMDFQKYISVRHDYILLPEGALTNTTRLRWWQPFVISNGLVVSGVERAQWALDNILIGGAEINPSQLVDTFDDEGSSHEENWSFYPNAVRTAGFCGNPSFHLYWPNKKKDKTHNALSSRELIIQPGYMMQFKIVVGCEATSCGDLHSVMLEYTKDARSDSWQLVQTQCLPSSSNSIGCSPFQFHEATIYNAVNSSSWKRITIQLPDHVSSSATQFRWIQKGEETEKQSWAIDHVYIGEACPKLCSGHGYCTTGAVCICDESFQGDDCSVFSHELPSYIKDNFESARVTEANWETIQGGVIGSGCGQLAPYAHGDSLYFNGCQIRQAATKPLDLTRASKIMFVLQIGSPAQTDSCNSDLSGPHTVDKAVLLQYSVNNGITWHVIAQHQPKDFTQAQRVSYNVPLEARMKGVLLRWWQPRHNGTGHDQWALDHVEVVLVSTRKQNYMMNFSRQHGLRHFYNRRRRSLRRYP

Q60841-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q60841-3

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F6U2B2F6U2B2_MOUSEReln47

Sequence caution

The sequence BAA09788.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict1191in Ref. 1; AAB91599
Sequence conflict1202in Ref. 1; AAB91599
Sequence conflict1335in Ref. 1; AAB91599
Sequence conflict1345in Ref. 1; AAB91599
Sequence conflict1505in Ref. 1; AAB91599
Sequence conflict1522-1524in Ref. 1; AAB91599
Sequence conflict1529in Ref. 1; AAB91599
Sequence conflict1593in Ref. 1; AAB91599
Sequence conflict1611in Ref. 1; AAB91599
Sequence conflict1648in Ref. 1; AAB91599
Sequence conflict1661in Ref. 1; AAB91599
Sequence conflict1667in Ref. 1; AAB91599
Sequence conflict3066in Ref. 5; BAB30592
Alternative sequenceVSP_0055773429-3430in isoform 2
Alternative sequenceVSP_0055783429-3461in isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U24703
EMBL· GenBank· DDBJ
AAB91599.1
EMBL· GenBank· DDBJ
mRNA
AC113028
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC116404
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC119906
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC121878
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
D63520
EMBL· GenBank· DDBJ
BAA09788.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK017094
EMBL· GenBank· DDBJ
BAB30592.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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