Q60841 · RELN_MOUSE
- ProteinReelin
- GeneReln
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids3461 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 2061 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2074 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2179 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2264 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2397 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2399 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2460 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReelin
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ60841
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2101 | Fails 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. | ||||
Sequence: C → A | ||||||
Mutagenesis | 2360 | Abolishes ApoER2-binding. | ||||
Sequence: K → A | ||||||
Mutagenesis | 2467 | Abolishes ApoER2-binding. | ||||
Sequence: K → A |
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.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MERGCWAPRALVLAVLLLLATLRARA | ||||||
Chain | PRO_0000030305 | 27-3461 | Reelin | |||
Sequence: ATGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSIQSSQSIGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLSFVWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQGAPTEATAYSHLAEIHSDSVILRDDFDSYQQLELNPNIWVECSNCEMGEQCGTIMHGNAVTFCEPYGPRELTTTCLNTTTASVLQFSIGSGSCRFSYSDPSITVSYAKNNTADWIQLEKIRAPSNVSTVIHILYLPEEAKGESVQFQWKQDSLRVGEVYEACWALDNILVINSAHREVVLEDNLDPVDTGNWLFFPGATVKHSCQSDGNSIYFHGNEGSEFNFATTRDVDLSTEDIQEQWSEEFESQPTGWDILGAVVGADCGTVESGLSLVFLKDGERKLCTPYMDTTGYGNLRFYFVMGGICDPGVSHENDIILYAKIEGRKEHIALDTLTYSSYKVPSLVSVVINPELQTPATKFCLRQKSHQGYNRNVWAVDFFHVLPVLPSTMSHMIQFSINLGCGTHQPGNSVSLEFSTNHGRSWSLLHTECLPEICAGPHLPHSTVYSSENYSGWNRITIPLPNAALTRDTRIRWRQTGPILGNMWAIDNVYIGPSCLKFCSGRGQCTRHGCKCDPGFSGPACEMASQTFPMFISESFGSARLSSYHNFYSIRGAEVSFGCGVLASGKALVFNKDGRRQLITSFLDSSQSRFLQFTLRLGSKSVLSTCRAPDQPGEGVLLHYSYDNGITWKLLEHYSYVNYHEPRIISVELPDDARQFGIQFRWWQPYHSSQGEDVWAIDEIVMTSVLFNSISLDFTNLVEVTQSLGFYLGNVQPYCGHDWTLCFTGDSKLASSMRYVETQSMQIGASYMIQFSLVMGCGQKYTPHMDNQVKLEYSANHGLTWHLVQEECLPSMPSCQEFTSASIYHASEFTQWRRVTVVLPQKTWSGATRFRWSQSYYTAQDEWALDNIYIGQQCPNMCSGHGSCDHGVCRCDQGYQGTECHPEAALPSTIMSDFENPSSWESDWQEVIGGEVVKPEQGCGVVSSGSSLYFSKAGKRQLVSWDLDTSWVDFVQFYIQIGGESAACNKPDSREEGILLQYSNNGGIQWHLLAEMYFSDFSKPRFVYLELPAAAKTPCTRFRWWQPVFSGEDYDQWAVDDIIILSEKQKQVIPVVNPTLPQNFYEKPAFDYPMNQMSVWLMLANEGMAKNDSFCATTPSAMVFGKSDGDRFAVTRDLTLKPGYVLQFKLNIGCTSQFSSTAPVLLQYSHDAGMSWFLVKEGCFPASAGKGCEGNSRELSEPTVYYTGDFEEWTRITIAIPRSLASSKTRFRWIQESSSQKNVPPFGLDGVYISEPCPSYCSGHGDCISGVCFCDLGYTAAQGTCVSNTPNHSEMFDRFEGKLSPLWYKITGGQVGTGCGTLNDGRSLYFNGLGKREARTVPLDTRNIRLVQFYIQIGSKTSGITCIKPRARNEGLVVQYSNDNGILWHLLRELDFMSFLEPQIISIDLPREAKTPATAFRWWQPQHGKHSAQWALDDVLIGVNDSSQTGFQDKFDGSIDLQANWYRIQGGQVDIDCLSMDTALIFTENIGKPRYAETWDFHVSASSFLQFEMNMGCSKPFSGAHGIQLQYSLNNGKDWQLVTEECVPPTIGCVHYTESSTYTSERFQNWRRVTVYLPLATNSPRTRFRWIQTNYTVGADSWAIDNVILASGCPWMCSGRGICDSGRCVCDRGFGGPFCVPVVPLPSILKDDFNGNLHPDLWPEVYGAERGNLNGETIKSGTCLIFKGEGLRMLISRDLDCTNTMYVQFSLRFIAKGTPERSHSILLQFSVSGGVTWHLMDEFYFPQTTSILFINVPLPYGAQTNATRFRLWQPYNNGKKEEIWIIDDFIIDGNNLNNPVLLLDTFDFGPREDNWFFYPGGNIGLYCPYSSKGAPEEDSAMVFVSNEVGEHSITTRDLSVNENTIIQFEINVGCSTDSSSADPVRLEFSRDFGATWHLLLPLCYHSSSLVSSLCSTEHHPSSTYYAGTTQGWRREVVHFGKLHLCGSVRFRWYQGFYPAGSQPVTWAIDNVYIGPQCEEMCYGHGSCINGTKCICDPGYSGPTCKISTKNPDFLKDDFEGQLESDRFLLMSGGKPSRKCGILSSGNNLFFNEDGLRMLVTRDLDLSHARFVQFFMRLGCGKGVPDPRSQPVLLQYSLNGGLSWSLLQEFLFSNSSNVGRYIALEMPLKARSGSTRLRWWQPSENGHFYSPWVIDQILIGGNISGNTVLEDDFSTLDSRKWLLHPGGTKMPVCGSTGDALVFIEKASTRYVVTTDIAVNEDSFLQIDFAASCSVTDSCYAIELEYSVDLGLSWHPLVRDCLPTNVECSRYHLQRILVSDTFNKWTRITLPLPSYTRSQATRFRWHQPAPFDKQQTWAIDNVYIGDGCLDMCSGHGRCVQGSCVCDEQWGGLYCDEPETSLPTQLKDNFNRAPSNQNWLTVSGGKLSTVCGAVASGLALHFSGGCSRLLVTVDLNLTNAEFIQFYFMYGCLITPSNRNQGVLLEYSVNGGITWNLLMEIFYDQYSKPGFVNILLPPDAKEIATRFRWWQPRHDGLDQNDWAIDNVLISGSADQRTVMLDTFSSAPVPQHERSPADAGPVGRIAFEMFLEDKTSVNENWLFHDDCTVERFCDSPDGVMLCGSHDGREVYAVTHDLTPTENWIMQFKISVGCKVPEKIAQNQIHVQFSTDFGVSWSYLVPQCLPADPKCSGSVSQPSVFFPTEGWKRITYPLPESLTGNPVRFRFYQKYSDVQWAIDNFYLGPGCLDNCGGHGDCLKEQCICDPGYSGPNCYLTHSLKTFLKERFDSEEIKPDLWMSLEGGSTCTECGVLAENTALYFGGSTVRQAITQDLDLRGAKFLQYWGRIGSENNMTSCHRPVCRKEGVLLDFSTDGGITWTLLHEMDFQKYISVRHDYILLPEGALTNTTRLRWWQPFVISNGLVVSGVERAQWALDNILIGGAEINPSQLVDTFDDEGSSHEENWSFYPNAVRTAGFCGNPSFHLYWPNKKKDKTHNALSSRELIIQPGYMMQFKIVVGCEATSCGDLHSVMLEYTKDARSDSWQLVQTQCLPSSSNSIGCSPFQFHEATIYNAVNSSSWKRITIQLPDHVSSSATQFRWIQKGEETEKQSWAIDHVYIGEACPKLCSGHGYCTTGAVCICDESFQGDDCSVFSHELPSYIKDNFESARVTEANWETIQGGVIGSGCGQLAPYAHGDSLYFNGCQIRQAATKPLDLTRASKIMFVLQIGSPAQTDSCNSDLSGPHTVDKAVLLQYSVNNGITWHVIAQHQPKDFTQAQRVSYNVPLEARMKGVLLRWWQPRHNGTGHDQWALDHVEVVLVSTRKQNYMMNFSRQHGLRHFYNRRRRSLRRYP | ||||||
Disulfide bond | 41↔127 | |||||
Sequence: CTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSIQSSQSIGGSSAFGFGIMSDHQFGNQFMC | ||||||
Glycosylation | 141 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 155↔179 | |||||
Sequence: CVNFMATATHRGQVIFKDALAQQLC | ||||||
Glycosylation | 258 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 290 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 306 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 540↔581 | |||||
Sequence: CLRQKSHQGYNRNVWAVDFFHVLPVLPSTMSHMIQFSINLGC | ||||||
Disulfide bond | 609↔614 | |||||
Sequence: CLPEIC | ||||||
Glycosylation | 629 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 675↔685 | |||||
Sequence: CLKFCSGRGQC | ||||||
Disulfide bond | 692↔701 | |||||
Sequence: CDPGFSGPAC | ||||||
Disulfide bond | 895↔937 | |||||
Sequence: CGHDWTLCFTGDSKLASSMRYVETQSMQIGASYMIQFSLVMGC | ||||||
Disulfide bond | 968↔975 | |||||
Sequence: CLPSMPSC | ||||||
Disulfide bond | 1034↔1044 | |||||
Sequence: CPNMCSGHGSC | ||||||
Disulfide bond | 1051↔1060 | |||||
Sequence: CDQGYQGTEC | ||||||
Glycosylation | 1267 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1339↔1348 | |||||
Sequence: CFPASAGKGC | ||||||
Disulfide bond | 1413↔1423 | |||||
Sequence: CPSYCSGHGDC | ||||||
Disulfide bond | 1417↔1428 | |||||
Sequence: CSGHGDCISGVC | ||||||
Disulfide bond | 1430↔1441 | |||||
Sequence: CDLGYTAAQGTC | ||||||
Glycosylation | 1447 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1475↔1522 | |||||
Sequence: CGTLNDGRSLYFNGLGKREARTVPLDTRNIRLVQFYIQIGSKTSGITC | ||||||
Glycosylation | 1600 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1633↔1673 | |||||
Sequence: CLSMDTALIFTENIGKPRYAETWDFHVSASSFLQFEMNMGC | ||||||
Disulfide bond | 1702↔1709 | |||||
Sequence: CVPPTIGC | ||||||
Glycosylation | 1750 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1921 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1983↔2030 | |||||
Sequence: CPYSSKGAPEEDSAMVFVSNEVGEHSITTRDLSVNENTIIQFEINVGC | ||||||
Disulfide bond | 2059↔2070 | |||||
Sequence: CYHSSSLVSSLC | ||||||
Disulfide bond | 2101 | Interchain | ||||
Sequence: C | ||||||
Disulfide bond | 2133↔2143 | |||||
Sequence: CEEMCYGHGSC | ||||||
Disulfide bond | 2137↔2149 | |||||
Sequence: CYGHGSCINGTKC | ||||||
Glycosylation | 2145 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2151↔2160 | |||||
Sequence: CDPGYSGPTC | ||||||
Disulfide bond | 2195↔2235 | |||||
Sequence: CGILSSGNNLFFNEDGLRMLVTRDLDLSHARFVQFFMRLGC | ||||||
Glycosylation | 2269 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2317 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2348↔2387 | |||||
Sequence: CGSTGDALVFIEKASTRYVVTTDIAVNEDSFLQIDFAASC | ||||||
Disulfide bond | 2393↔2559 | |||||
Sequence: CYAIELEYSVDLGLSWHPLVRDCLPTNVECSRYHLQRILVSDTFNKWTRITLPLPSYTRSQATRFRWHQPAPFDKQQTWAIDNVYIGDGCLDMCSGHGRCVQGSCVCDEQWGGLYCDEPETSLPTQLKDNFNRAPSNQNWLTVSGGKLSTVCGAVASGLALHFSGGC | ||||||
Disulfide bond | 2482↔2492 | |||||
Sequence: CLDMCSGHGRC | ||||||
Disulfide bond | 2486↔2497 | |||||
Sequence: CSGHGRCVQGSC | ||||||
Disulfide bond | 2499↔2508 | |||||
Sequence: CDEQWGGLYC | ||||||
Disulfide bond | 2544↔2584 | |||||
Sequence: CGAVASGLALHFSGGCSRLLVTVDLNLTNAEFIQFYFMYGC | ||||||
Glycosylation | 2569 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2794↔2801 | |||||
Sequence: CLPADPKC | ||||||
Disulfide bond | 2919↔2966 | |||||
Sequence: CGVLAENTALYFGGSTVRQAITQDLDLRGAKFLQYWGRIGSENNMTSC | ||||||
Glycosylation | 2962 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3016 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3073 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3160↔3170 | |||||
Sequence: CLPSSSNSIGC | ||||||
Glycosylation | 3185 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3232↔3242 | |||||
Sequence: CPKLCSGHGYC | ||||||
Disulfide bond | 3236↔3248 | |||||
Sequence: CSGHGYCTTGAVC | ||||||
Disulfide bond | 3250↔3259 | |||||
Sequence: CDESFQGDDC | ||||||
Disulfide bond | 3296↔3346 | |||||
Sequence: CGQLAPYAHGDSLYFNGCQIRQAATKPLDLTRASKIMFVLQIGSPAQTDSC | ||||||
Glycosylation | 3412 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3439 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated and to a lesser extent also O-glycosylated.
Keywords
- PTM
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q60841 | Lrp8 Q924X6 | 4 | EBI-9248666, EBI-432319 | |
XENO | Q60841 | LRP8 Q14114 | 10 | EBI-9248666, EBI-2681187 | |
XENO | Q60841 | VLDLR P98155 | 7 | EBI-9248666, EBI-9004309 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-191 | Reelin | ||||
Sequence: ATGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSIQSSQSIGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLSFVWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQGAPTEATAYS | ||||||
Repeat | 593-604 | BNR 1 | ||||
Sequence: EFSTNHGRSWSL | ||||||
Domain | 671-702 | EGF-like 1 | ||||
Sequence: IGPSCLKFCSGRGQCTRHGCKCDPGFSGPACE | ||||||
Repeat | 799-810 | BNR 2 | ||||
Sequence: HYSYDNGITWKL | ||||||
Repeat | 952-963 | BNR 3 | ||||
Sequence: EYSANHGLTWHL | ||||||
Domain | 1030-1061 | EGF-like 2 | ||||
Sequence: IGQQCPNMCSGHGSCDHGVCRCDQGYQGTECH | ||||||
Repeat | 1157-1168 | BNR 4 | ||||
Sequence: QYSNNGGIQWHL | ||||||
Repeat | 1323-1334 | BNR 5 | ||||
Sequence: QYSHDAGMSWFL | ||||||
Domain | 1409-1442 | EGF-like 3 | ||||
Sequence: ISEPCPSYCSGHGDCISGVCFCDLGYTAAQGTCV | ||||||
Repeat | 1535-1546 | BNR 6 | ||||
Sequence: QYSNDNGILWHL | ||||||
Repeat | 1686-1697 | BNR 7 | ||||
Sequence: QYSLNNGKDWQL | ||||||
Domain | 1765-1796 | EGF-like 4 | ||||
Sequence: LASGCPWMCSGRGICDSGRCVCDRGFGGPFCV | ||||||
Repeat | 1884-1895 | BNR 8 | ||||
Sequence: QFSVSGGVTWHL | ||||||
Repeat | 2043-2054 | BNR 9 | ||||
Sequence: EFSRDFGATWHL | ||||||
Domain | 2129-2161 | EGF-like 5 | ||||
Sequence: IGPQCEEMCYGHGSCINGTKCICDPGYSGPTCK | ||||||
Repeat | 2250-2261 | BNR 10 | ||||
Sequence: QYSLNGGLSWSL | ||||||
Repeat | 2399-2410 | BNR 11 | ||||
Sequence: EYSVDLGLSWHP | ||||||
Domain | 2478-2509 | EGF-like 6 | ||||
Sequence: IGDGCLDMCSGHGRCVQGSCVCDEQWGGLYCD | ||||||
Repeat | 2598-2609 | BNR 12 | ||||
Sequence: EYSVNGGITWNL | ||||||
Repeat | 2778-2789 | BNR 13 | ||||
Sequence: QFSTDFGVSWSY | ||||||
Domain | 2853-2884 | EGF-like 7 | ||||
Sequence: LGPGCLDNCGGHGDCLKEQCICDPGYSGPNCY | ||||||
Repeat | 2979-2990 | BNR 14 | ||||
Sequence: DFSTDGGITWTL | ||||||
Repeat | 3143-3155 | BNR 15 | ||||
Sequence: EYTKDARSDSWQL | ||||||
Domain | 3228-3260 | EGF-like 8 | ||||
Sequence: IGEACPKLCSGHGYCTTGAVCICDESFQGDDCS | ||||||
Repeat | 3363-3374 | BNR 16 | ||||
Sequence: QYSVNNGITWHV |
Domain
The basic C-terminal region is essential for secretion.
Sequence similarities
Belongs to the reelin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe 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.
- Name1
- Length3,461
- Mass (Da)387,495
- Last updated2011-07-27 v3
- Checksum1CCE64C845160F2E
Q60841-2
- Name2
- Differences from canonical
- 3429-3430: Missing
Q60841-3
- Name3
- Differences from canonical
- 3429-3461: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6U2B2 | F6U2B2_MOUSE | Reln | 47 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1191 | in Ref. 1; AAB91599 | ||||
Sequence: A → G | ||||||
Sequence conflict | 1202 | in Ref. 1; AAB91599 | ||||
Sequence: Q → K | ||||||
Sequence conflict | 1335 | in Ref. 1; AAB91599 | ||||
Sequence: V → L | ||||||
Sequence conflict | 1345 | in Ref. 1; AAB91599 | ||||
Sequence: G → A | ||||||
Sequence conflict | 1505 | in Ref. 1; AAB91599 | ||||
Sequence: R → S | ||||||
Sequence conflict | 1522-1524 | in Ref. 1; AAB91599 | ||||
Sequence: CIK → YIT | ||||||
Sequence conflict | 1529 | in Ref. 1; AAB91599 | ||||
Sequence: N → Y | ||||||
Sequence conflict | 1593 | in Ref. 1; AAB91599 | ||||
Sequence: D → G | ||||||
Sequence conflict | 1611 | in Ref. 1; AAB91599 | ||||
Sequence: F → L | ||||||
Sequence conflict | 1648 | in Ref. 1; AAB91599 | ||||
Sequence: K → N | ||||||
Sequence conflict | 1661 | in Ref. 1; AAB91599 | ||||
Sequence: A → E | ||||||
Sequence conflict | 1667 | in Ref. 1; AAB91599 | ||||
Sequence: F → W | ||||||
Sequence conflict | 3066 | in Ref. 5; BAB30592 | ||||
Sequence: Missing | ||||||
Alternative sequence | VSP_005577 | 3429-3430 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_005578 | 3429-3461 | in isoform 3 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |