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Q60841

- RELN_MOUSE

UniProt

Q60841 - RELN_MOUSE

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Protein

Reelin

Gene

Reln

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi2061 – 20611Zinc 1
Metal bindingi2074 – 20741Zinc 1
Metal bindingi2179 – 21791Zinc 1
Metal bindingi2264 – 22641Zinc 1
Metal bindingi2397 – 23971Zinc 2
Metal bindingi2399 – 23991Zinc 2
Metal bindingi2460 – 24601Zinc 2

GO - Molecular functioni

  1. lipoprotein particle receptor binding Source: BHF-UCL
  2. metal ion binding Source: UniProtKB-KW
  3. serine-type peptidase activity Source: UniProtKB-KW
  4. very-low-density lipoprotein particle receptor binding Source: BHF-UCL

GO - Biological processi

  1. associative learning Source: BHF-UCL
  2. axon guidance Source: MGI
  3. brain development Source: MGI
  4. cell adhesion Source: UniProtKB-KW
  5. cell migration Source: MGI
  6. cell morphogenesis involved in differentiation Source: MGI
  7. central nervous system development Source: MGI
  8. cerebral cortex development Source: MGI
  9. cerebral cortex tangential migration Source: MGI
  10. dendrite development Source: MGI
  11. forebrain development Source: MGI
  12. glial cell differentiation Source: MGI
  13. hippocampus development Source: BHF-UCL
  14. lateral motor column neuron migration Source: UniProtKB
  15. layer formation in cerebral cortex Source: MGI
  16. long-term memory Source: BHF-UCL
  17. neuron migration Source: MGI
  18. N-methyl-D-aspartate receptor clustering Source: BHF-UCL
  19. peptidyl-tyrosine phosphorylation Source: MGI
  20. positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: BHF-UCL
  21. positive regulation of CREB transcription factor activity Source: BHF-UCL
  22. positive regulation of dendritic spine morphogenesis Source: BHF-UCL
  23. positive regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
  24. positive regulation of lateral motor column neuron migration Source: BHF-UCL
  25. positive regulation of long-term synaptic potentiation Source: BHF-UCL
  26. positive regulation of neuron projection development Source: BHF-UCL
  27. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  28. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  29. positive regulation of protein kinase activity Source: MGI
  30. positive regulation of protein tyrosine kinase activity Source: BHF-UCL
  31. positive regulation of small GTPase mediated signal transduction Source: MGI
  32. positive regulation of synapse maturation Source: BHF-UCL
  33. positive regulation of synaptic transmission, glutamatergic Source: BHF-UCL
  34. positive regulation of TOR signaling Source: BHF-UCL
  35. postsynaptic density assembly Source: BHF-UCL
  36. postsynaptic density protein 95 clustering Source: BHF-UCL
  37. protein localization to synapse Source: BHF-UCL
  38. receptor localization to synapse Source: BHF-UCL
  39. reelin-mediated signaling pathway Source: BHF-UCL
  40. regulation of behavior Source: BHF-UCL
  41. regulation of gene expression Source: MGI
  42. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: BHF-UCL
  43. regulation of synaptic transmission Source: BHF-UCL
  44. response to pain Source: MGI
  45. spinal cord patterning Source: MGI
  46. ventral spinal cord development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Serine protease

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Reelin (EC:3.4.21.-)
Alternative name(s):
Reeler protein
Gene namesi
Name:Reln
Synonyms:Rl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:103022. Reln.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. dendrite Source: MGI
  3. extracellular space Source: MGI
  4. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2101 – 21011C → A: 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. 1 Publication
Mutagenesisi2360 – 23601K → A: Abolishes ApoER2-binding. 1 Publication
Mutagenesisi2467 – 24671K → A: Abolishes ApoER2-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 34613435ReelinPRO_0000030305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 127PROSITE-ProRule annotation
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi155 ↔ 179PROSITE-ProRule annotation
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi540 ↔ 581PROSITE-ProRule annotation
Disulfide bondi609 ↔ 614PROSITE-ProRule annotation
Glycosylationi629 – 6291N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi675 ↔ 685PROSITE-ProRule annotation
Disulfide bondi692 ↔ 701PROSITE-ProRule annotation
Disulfide bondi895 ↔ 937PROSITE-ProRule annotation
Disulfide bondi968 ↔ 975PROSITE-ProRule annotation
Disulfide bondi1034 ↔ 1044PROSITE-ProRule annotation
Disulfide bondi1051 ↔ 1060PROSITE-ProRule annotation
Glycosylationi1267 – 12671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1271 ↔ 1310
Disulfide bondi1339 ↔ 1348
Glycosylationi1447 – 14471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1600 – 16001N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1633 ↔ 1673PROSITE-ProRule annotation
Disulfide bondi1702 ↔ 1709PROSITE-ProRule annotation
Glycosylationi1750 – 17501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1921 – 19211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1983 ↔ 2030
Disulfide bondi2059 ↔ 2070
Disulfide bondi2101 – 2101Interchain
Disulfide bondi2133 ↔ 2143
Disulfide bondi2137 ↔ 2149
Glycosylationi2145 – 21451N-linked (GlcNAc...)1 Publication
Disulfide bondi2151 ↔ 2160
Disulfide bondi2195 ↔ 2235
Glycosylationi2269 – 22691N-linked (GlcNAc...)1 Publication
Glycosylationi2317 – 23171N-linked (GlcNAc...)1 Publication
Disulfide bondi2348 ↔ 2387
Disulfide bondi2393 ↔ 2559
Disulfide bondi2482 ↔ 2492
Disulfide bondi2486 ↔ 2497
Disulfide bondi2499 ↔ 2508
Disulfide bondi2544 ↔ 2584
Glycosylationi2569 – 25691N-linked (GlcNAc...)1 Publication
Disulfide bondi2794 ↔ 2801PROSITE-ProRule annotation
Disulfide bondi2919 ↔ 2966PROSITE-ProRule annotation
Glycosylationi2962 – 29621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3016 – 30161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3073 – 30731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3160 ↔ 3170PROSITE-ProRule annotation
Glycosylationi3185 – 31851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3232 ↔ 3242PROSITE-ProRule annotation
Disulfide bondi3236 ↔ 3248PROSITE-ProRule annotation
Disulfide bondi3250 ↔ 3259PROSITE-ProRule annotation
Disulfide bondi3296 ↔ 3346PROSITE-ProRule annotation
Glycosylationi3412 – 34121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3439 – 34391N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated and to a lesser extent also O-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ60841.
PaxDbiQ60841.
PRIDEiQ60841.

PTM databases

PhosphoSiteiQ60841.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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

BgeeiQ60841.
CleanExiMM_RELN.
GenevestigatoriQ60841.

Interactioni

Subunit structurei

Oligomer of disulfide-linked homodimers. Binds to the ectodomains of VLDLR and LRP8/APOER2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Lrp8Q924X64EBI-9248666,EBI-432319
VLDLRP981554EBI-9248666,EBI-9004309From a different organism.

Protein-protein interaction databases

DIPiDIP-40924N.
IntActiQ60841. 2 interactions.
MINTiMINT-111528.

Structurei

Secondary structure

1
3461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1301 – 131010Combined sources
Beta strandi1320 – 13278Combined sources
Beta strandi1333 – 13353Combined sources
Beta strandi1345 – 13484Combined sources
Beta strandi1359 – 13613Combined sources
Beta strandi1370 – 13756Combined sources
Helixi1378 – 13803Combined sources
Beta strandi1386 – 13905Combined sources
Beta strandi1408 – 14114Combined sources
Helixi1414 – 14196Combined sources
Beta strandi1420 – 14245Combined sources
Beta strandi1427 – 14304Combined sources
Beta strandi1434 – 14374Combined sources
Beta strandi1440 – 14456Combined sources
Beta strandi1451 – 14533Combined sources
Beta strandi1456 – 14583Combined sources
Beta strandi1463 – 147210Combined sources
Beta strandi1478 – 14814Combined sources
Beta strandi1483 – 14864Combined sources
Beta strandi1493 – 14964Combined sources
Beta strandi1506 – 15138Combined sources
Beta strandi1516 – 15183Combined sources
Helixi1528 – 15303Combined sources
Beta strandi1531 – 15399Combined sources
Beta strandi1545 – 15506Combined sources
Beta strandi1559 – 15646Combined sources
Helixi1567 – 15693Combined sources
Beta strandi1571 – 15799Combined sources
Helixi1584 – 15863Combined sources
Beta strandi1590 – 15978Combined sources
Beta strandi1958 – 19603Combined sources
Beta strandi1963 – 19653Combined sources
Helixi1968 – 19703Combined sources
Beta strandi1971 – 19733Combined sources
Beta strandi1978 – 19803Combined sources
Beta strandi1996 – 19994Combined sources
Beta strandi2005 – 20117Combined sources
Beta strandi2014 – 20163Combined sources
Beta strandi2020 – 203213Combined sources
Beta strandi2040 – 20478Combined sources
Beta strandi2053 – 20564Combined sources
Beta strandi2059 – 20613Combined sources
Beta strandi2078 – 20803Combined sources
Beta strandi2089 – 20957Combined sources
Turni2096 – 20994Combined sources
Beta strandi2102 – 211312Combined sources
Beta strandi2122 – 213110Combined sources
Helixi2134 – 21396Combined sources
Beta strandi2140 – 21445Combined sources
Turni2145 – 21473Combined sources
Beta strandi2148 – 21514Combined sources
Beta strandi2155 – 21573Combined sources
Beta strandi2170 – 21723Combined sources
Beta strandi2174 – 21763Combined sources
Beta strandi2178 – 218710Combined sources
Beta strandi2189 – 21935Combined sources
Beta strandi2197 – 22015Combined sources
Beta strandi2203 – 22064Combined sources
Beta strandi2208 – 22103Combined sources
Beta strandi2212 – 22165Combined sources
Beta strandi2226 – 22338Combined sources
Beta strandi2236 – 22383Combined sources
Beta strandi2247 – 22548Combined sources
Beta strandi2260 – 22656Combined sources
Turni2269 – 22724Combined sources
Beta strandi2275 – 22806Combined sources
Helixi2283 – 22853Combined sources
Beta strandi2287 – 229610Combined sources
Beta strandi2299 – 23013Combined sources
Beta strandi2307 – 23159Combined sources
Beta strandi2324 – 23263Combined sources
Beta strandi2328 – 23303Combined sources
Turni2333 – 23353Combined sources
Beta strandi2336 – 23383Combined sources
Beta strandi2343 – 23453Combined sources
Beta strandi2354 – 23574Combined sources
Beta strandi2364 – 23685Combined sources
Beta strandi2371 – 23733Combined sources
Beta strandi2378 – 23847Combined sources
Beta strandi2387 – 23893Combined sources
Beta strandi2395 – 24039Combined sources
Beta strandi2409 – 24124Combined sources
Beta strandi2419 – 24224Combined sources
Turni2433 – 24364Combined sources
Beta strandi2440 – 24456Combined sources
Helixi2448 – 24503Combined sources
Beta strandi2452 – 246110Combined sources
Beta strandi2471 – 248010Combined sources
Helixi2484 – 24885Combined sources
Beta strandi2489 – 24935Combined sources
Beta strandi2496 – 24994Combined sources
Beta strandi2503 – 25053Combined sources
Beta strandi2510 – 25134Combined sources
Beta strandi2519 – 25213Combined sources
Turni2529 – 25313Combined sources
Beta strandi2532 – 254211Combined sources
Beta strandi2547 – 25504Combined sources
Beta strandi2552 – 25554Combined sources
Beta strandi2562 – 25654Combined sources
Beta strandi2575 – 25828Combined sources
Beta strandi2584 – 25863Combined sources
Helixi2591 – 25933Combined sources
Beta strandi2594 – 26029Combined sources
Beta strandi2608 – 26136Combined sources
Beta strandi2615 – 26173Combined sources
Beta strandi2622 – 26276Combined sources
Helixi2630 – 26323Combined sources
Beta strandi2634 – 26429Combined sources
Beta strandi2654 – 26618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DDUX-ray2.05A1222-1597[»]
2E26X-ray2.00A1948-2661[»]
3A7QX-ray2.60A1948-2661[»]
ProteinModelPortaliQ60841.
SMRiQ60841. Positions 1294-1597, 1956-2662.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60841.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 191165ReelinPROSITE-ProRule annotationAdd
BLAST
Repeati593 – 60412BNR 1Add
BLAST
Domaini671 – 70232EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Repeati799 – 81012BNR 2Add
BLAST
Repeati952 – 96312BNR 3Add
BLAST
Domaini1030 – 106132EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Repeati1157 – 116812BNR 4Add
BLAST
Repeati1323 – 133412BNR 5Add
BLAST
Domaini1409 – 144234EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Repeati1535 – 154612BNR 6Add
BLAST
Repeati1686 – 169712BNR 7Add
BLAST
Domaini1765 – 179632EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Repeati1884 – 189512BNR 8Add
BLAST
Repeati2043 – 205412BNR 9Add
BLAST
Domaini2129 – 216133EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Repeati2250 – 226112BNR 10Add
BLAST
Repeati2399 – 241012BNR 11Add
BLAST
Domaini2478 – 250932EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Repeati2598 – 260912BNR 12Add
BLAST
Repeati2778 – 278912BNR 13Add
BLAST
Domaini2853 – 288432EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Repeati2979 – 299012BNR 14Add
BLAST
Repeati3143 – 315513BNR 15Add
BLAST
Domaini3228 – 326033EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Repeati3363 – 337412BNR 16Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3432 – 346130Arg-rich (basic)Add
BLAST

Domaini

The basic C-terminal region is essential for secretion.

Sequence similaritiesi

Belongs to the reelin family.Curated
Contains 16 BNR repeats.Curated
Contains 8 EGF-like domains.PROSITE-ProRule annotation
Contains 1 reelin domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG45680.
GeneTreeiENSGT00580000081623.
HOGENOMiHOG000252908.
HOVERGENiHBG023117.
InParanoidiQ60841.
KOiK06249.
OMAiNWFFYPG.
OrthoDBiEOG7P2XR4.
TreeFamiTF106479.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002861. Reeler_dom.
IPR011040. Sialidases.
[Graphical view]
PfamiPF12661. hEGF. 2 hits.
PF02014. Reeler. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 5 hits.
[Graphical view]
SUPFAMiSSF50939. SSF50939. 14 hits.
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 6 hits.
PS50026. EGF_3. 5 hits.
PS51019. REELIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q60841-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MERGCWAPRA LVLAVLLLLA TLRARAATGY YPRFSPFFFL CTHHGELEGD
60 70 80 90 100
GEQGEVLISL HIAGNPTYYV PGQEYHVTIS TSTFFDGLLV TGLYTSTSIQ
110 120 130 140 150
SSQSIGGSSA FGFGIMSDHQ FGNQFMCSVV ASHVSHLPTT NLSFVWIAPP
160 170 180 190 200
AGTGCVNFMA TATHRGQVIF KDALAQQLCE QGAPTEATAY SHLAEIHSDS
210 220 230 240 250
VILRDDFDSY QQLELNPNIW VECSNCEMGE QCGTIMHGNA VTFCEPYGPR
260 270 280 290 300
ELTTTCLNTT TASVLQFSIG SGSCRFSYSD PSITVSYAKN NTADWIQLEK
310 320 330 340 350
IRAPSNVSTV IHILYLPEEA KGESVQFQWK QDSLRVGEVY EACWALDNIL
360 370 380 390 400
VINSAHREVV LEDNLDPVDT GNWLFFPGAT VKHSCQSDGN SIYFHGNEGS
410 420 430 440 450
EFNFATTRDV DLSTEDIQEQ WSEEFESQPT GWDILGAVVG ADCGTVESGL
460 470 480 490 500
SLVFLKDGER KLCTPYMDTT GYGNLRFYFV MGGICDPGVS HENDIILYAK
510 520 530 540 550
IEGRKEHIAL DTLTYSSYKV PSLVSVVINP ELQTPATKFC LRQKSHQGYN
560 570 580 590 600
RNVWAVDFFH VLPVLPSTMS HMIQFSINLG CGTHQPGNSV SLEFSTNHGR
610 620 630 640 650
SWSLLHTECL PEICAGPHLP HSTVYSSENY SGWNRITIPL PNAALTRDTR
660 670 680 690 700
IRWRQTGPIL GNMWAIDNVY IGPSCLKFCS GRGQCTRHGC KCDPGFSGPA
710 720 730 740 750
CEMASQTFPM FISESFGSAR LSSYHNFYSI RGAEVSFGCG VLASGKALVF
760 770 780 790 800
NKDGRRQLIT SFLDSSQSRF LQFTLRLGSK SVLSTCRAPD QPGEGVLLHY
810 820 830 840 850
SYDNGITWKL LEHYSYVNYH EPRIISVELP DDARQFGIQF RWWQPYHSSQ
860 870 880 890 900
GEDVWAIDEI VMTSVLFNSI SLDFTNLVEV TQSLGFYLGN VQPYCGHDWT
910 920 930 940 950
LCFTGDSKLA SSMRYVETQS MQIGASYMIQ FSLVMGCGQK YTPHMDNQVK
960 970 980 990 1000
LEYSANHGLT WHLVQEECLP SMPSCQEFTS ASIYHASEFT QWRRVTVVLP
1010 1020 1030 1040 1050
QKTWSGATRF RWSQSYYTAQ DEWALDNIYI GQQCPNMCSG HGSCDHGVCR
1060 1070 1080 1090 1100
CDQGYQGTEC HPEAALPSTI MSDFENPSSW ESDWQEVIGG EVVKPEQGCG
1110 1120 1130 1140 1150
VVSSGSSLYF SKAGKRQLVS WDLDTSWVDF VQFYIQIGGE SAACNKPDSR
1160 1170 1180 1190 1200
EEGILLQYSN NGGIQWHLLA EMYFSDFSKP RFVYLELPAA AKTPCTRFRW
1210 1220 1230 1240 1250
WQPVFSGEDY DQWAVDDIII LSEKQKQVIP VVNPTLPQNF YEKPAFDYPM
1260 1270 1280 1290 1300
NQMSVWLMLA NEGMAKNDSF CATTPSAMVF GKSDGDRFAV TRDLTLKPGY
1310 1320 1330 1340 1350
VLQFKLNIGC TSQFSSTAPV LLQYSHDAGM SWFLVKEGCF PASAGKGCEG
1360 1370 1380 1390 1400
NSRELSEPTV YYTGDFEEWT RITIAIPRSL ASSKTRFRWI QESSSQKNVP
1410 1420 1430 1440 1450
PFGLDGVYIS EPCPSYCSGH GDCISGVCFC DLGYTAAQGT CVSNTPNHSE
1460 1470 1480 1490 1500
MFDRFEGKLS PLWYKITGGQ VGTGCGTLND GRSLYFNGLG KREARTVPLD
1510 1520 1530 1540 1550
TRNIRLVQFY IQIGSKTSGI TCIKPRARNE GLVVQYSNDN GILWHLLREL
1560 1570 1580 1590 1600
DFMSFLEPQI ISIDLPREAK TPATAFRWWQ PQHGKHSAQW ALDDVLIGVN
1610 1620 1630 1640 1650
DSSQTGFQDK FDGSIDLQAN WYRIQGGQVD IDCLSMDTAL IFTENIGKPR
1660 1670 1680 1690 1700
YAETWDFHVS ASSFLQFEMN MGCSKPFSGA HGIQLQYSLN NGKDWQLVTE
1710 1720 1730 1740 1750
ECVPPTIGCV HYTESSTYTS ERFQNWRRVT VYLPLATNSP RTRFRWIQTN
1760 1770 1780 1790 1800
YTVGADSWAI DNVILASGCP WMCSGRGICD SGRCVCDRGF GGPFCVPVVP
1810 1820 1830 1840 1850
LPSILKDDFN GNLHPDLWPE VYGAERGNLN GETIKSGTCL IFKGEGLRML
1860 1870 1880 1890 1900
ISRDLDCTNT MYVQFSLRFI AKGTPERSHS ILLQFSVSGG VTWHLMDEFY
1910 1920 1930 1940 1950
FPQTTSILFI NVPLPYGAQT NATRFRLWQP YNNGKKEEIW IIDDFIIDGN
1960 1970 1980 1990 2000
NLNNPVLLLD TFDFGPREDN WFFYPGGNIG LYCPYSSKGA PEEDSAMVFV
2010 2020 2030 2040 2050
SNEVGEHSIT TRDLSVNENT IIQFEINVGC STDSSSADPV RLEFSRDFGA
2060 2070 2080 2090 2100
TWHLLLPLCY HSSSLVSSLC STEHHPSSTY YAGTTQGWRR EVVHFGKLHL
2110 2120 2130 2140 2150
CGSVRFRWYQ GFYPAGSQPV TWAIDNVYIG PQCEEMCYGH GSCINGTKCI
2160 2170 2180 2190 2200
CDPGYSGPTC KISTKNPDFL KDDFEGQLES DRFLLMSGGK PSRKCGILSS
2210 2220 2230 2240 2250
GNNLFFNEDG LRMLVTRDLD LSHARFVQFF MRLGCGKGVP DPRSQPVLLQ
2260 2270 2280 2290 2300
YSLNGGLSWS LLQEFLFSNS SNVGRYIALE MPLKARSGST RLRWWQPSEN
2310 2320 2330 2340 2350
GHFYSPWVID QILIGGNISG NTVLEDDFST LDSRKWLLHP GGTKMPVCGS
2360 2370 2380 2390 2400
TGDALVFIEK ASTRYVVTTD IAVNEDSFLQ IDFAASCSVT DSCYAIELEY
2410 2420 2430 2440 2450
SVDLGLSWHP LVRDCLPTNV ECSRYHLQRI LVSDTFNKWT RITLPLPSYT
2460 2470 2480 2490 2500
RSQATRFRWH QPAPFDKQQT WAIDNVYIGD GCLDMCSGHG RCVQGSCVCD
2510 2520 2530 2540 2550
EQWGGLYCDE PETSLPTQLK DNFNRAPSNQ NWLTVSGGKL STVCGAVASG
2560 2570 2580 2590 2600
LALHFSGGCS RLLVTVDLNL TNAEFIQFYF MYGCLITPSN RNQGVLLEYS
2610 2620 2630 2640 2650
VNGGITWNLL MEIFYDQYSK PGFVNILLPP DAKEIATRFR WWQPRHDGLD
2660 2670 2680 2690 2700
QNDWAIDNVL ISGSADQRTV MLDTFSSAPV PQHERSPADA GPVGRIAFEM
2710 2720 2730 2740 2750
FLEDKTSVNE NWLFHDDCTV ERFCDSPDGV MLCGSHDGRE VYAVTHDLTP
2760 2770 2780 2790 2800
TENWIMQFKI SVGCKVPEKI AQNQIHVQFS TDFGVSWSYL VPQCLPADPK
2810 2820 2830 2840 2850
CSGSVSQPSV FFPTEGWKRI TYPLPESLTG NPVRFRFYQK YSDVQWAIDN
2860 2870 2880 2890 2900
FYLGPGCLDN CGGHGDCLKE QCICDPGYSG PNCYLTHSLK TFLKERFDSE
2910 2920 2930 2940 2950
EIKPDLWMSL EGGSTCTECG VLAENTALYF GGSTVRQAIT QDLDLRGAKF
2960 2970 2980 2990 3000
LQYWGRIGSE NNMTSCHRPV CRKEGVLLDF STDGGITWTL LHEMDFQKYI
3010 3020 3030 3040 3050
SVRHDYILLP EGALTNTTRL RWWQPFVISN GLVVSGVERA QWALDNILIG
3060 3070 3080 3090 3100
GAEINPSQLV DTFDDEGSSH EENWSFYPNA VRTAGFCGNP SFHLYWPNKK
3110 3120 3130 3140 3150
KDKTHNALSS RELIIQPGYM MQFKIVVGCE ATSCGDLHSV MLEYTKDARS
3160 3170 3180 3190 3200
DSWQLVQTQC LPSSSNSIGC SPFQFHEATI YNAVNSSSWK RITIQLPDHV
3210 3220 3230 3240 3250
SSSATQFRWI QKGEETEKQS WAIDHVYIGE ACPKLCSGHG YCTTGAVCIC
3260 3270 3280 3290 3300
DESFQGDDCS VFSHELPSYI KDNFESARVT EANWETIQGG VIGSGCGQLA
3310 3320 3330 3340 3350
PYAHGDSLYF NGCQIRQAAT KPLDLTRASK IMFVLQIGSP AQTDSCNSDL
3360 3370 3380 3390 3400
SGPHTVDKAV LLQYSVNNGI TWHVIAQHQP KDFTQAQRVS YNVPLEARMK
3410 3420 3430 3440 3450
GVLLRWWQPR HNGTGHDQWA LDHVEVVLVS TRKQNYMMNF SRQHGLRHFY
3460
NRRRRSLRRY P
Length:3,461
Mass (Da):387,495
Last modified:July 27, 2011 - v3
Checksum:i1CCE64C845160F2E
GO
Isoform 2 (identifier: Q60841-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3429-3430: Missing.

Show »
Length:3,459
Mass (Da):387,309
Checksum:iDC72A41DFC9B88C6
GO
Isoform 3 (identifier: Q60841-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3429-3461: Missing.

Show »
Length:3,428
Mass (Da):383,200
Checksum:iADA613A4F66D585A
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1191 – 11911A → G in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1202 – 12021Q → K in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1335 – 13351V → L in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1345 – 13451G → A in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1505 – 15051R → S in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1522 – 15243CIK → YIT in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1529 – 15291N → Y in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1593 – 15931D → G in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1611 – 16111F → L in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1648 – 16481K → N in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1661 – 16611A → E in AAB91599. (PubMed:7715726)Curated
Sequence conflicti1667 – 16671F → W in AAB91599. (PubMed:7715726)Curated
Sequence conflicti3066 – 30661Missing in BAB30592. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3429 – 346133Missing in isoform 3. CuratedVSP_005578Add
BLAST
Alternative sequencei3429 – 34302Missing in isoform 2. 1 PublicationVSP_005577

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24703 mRNA. Translation: AAB91599.1.
AC113028 Genomic DNA. No translation available.
AC116404 Genomic DNA. No translation available.
AC119906 Genomic DNA. No translation available.
AC121878 Genomic DNA. No translation available.
D63520 mRNA. Translation: BAA09788.1. Different initiation.
AK017094 mRNA. Translation: BAB30592.1.
CCDSiCCDS39023.1. [Q60841-1]
PIRiS58870.
RefSeqiNP_035391.2. NM_011261.2. [Q60841-1]
XP_006535709.1. XM_006535646.1. [Q60841-2]
UniGeneiMm.425236.

Genome annotation databases

EnsembliENSMUST00000062372; ENSMUSP00000058025; ENSMUSG00000042453. [Q60841-2]
ENSMUST00000161356; ENSMUSP00000124052; ENSMUSG00000042453. [Q60841-1]
GeneIDi19699.
KEGGimmu:19699.
UCSCiuc008wpi.1. mouse. [Q60841-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24703 mRNA. Translation: AAB91599.1 .
AC113028 Genomic DNA. No translation available.
AC116404 Genomic DNA. No translation available.
AC119906 Genomic DNA. No translation available.
AC121878 Genomic DNA. No translation available.
D63520 mRNA. Translation: BAA09788.1 . Different initiation.
AK017094 mRNA. Translation: BAB30592.1 .
CCDSi CCDS39023.1. [Q60841-1 ]
PIRi S58870.
RefSeqi NP_035391.2. NM_011261.2. [Q60841-1 ]
XP_006535709.1. XM_006535646.1. [Q60841-2 ]
UniGenei Mm.425236.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DDU X-ray 2.05 A 1222-1597 [» ]
2E26 X-ray 2.00 A 1948-2661 [» ]
3A7Q X-ray 2.60 A 1948-2661 [» ]
ProteinModelPortali Q60841.
SMRi Q60841. Positions 1294-1597, 1956-2662.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-40924N.
IntActi Q60841. 2 interactions.
MINTi MINT-111528.

PTM databases

PhosphoSitei Q60841.

Proteomic databases

MaxQBi Q60841.
PaxDbi Q60841.
PRIDEi Q60841.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000062372 ; ENSMUSP00000058025 ; ENSMUSG00000042453 . [Q60841-2 ]
ENSMUST00000161356 ; ENSMUSP00000124052 ; ENSMUSG00000042453 . [Q60841-1 ]
GeneIDi 19699.
KEGGi mmu:19699.
UCSCi uc008wpi.1. mouse. [Q60841-1 ]

Organism-specific databases

CTDi 5649.
MGIi MGI:103022. Reln.

Phylogenomic databases

eggNOGi NOG45680.
GeneTreei ENSGT00580000081623.
HOGENOMi HOG000252908.
HOVERGENi HBG023117.
InParanoidi Q60841.
KOi K06249.
OMAi NWFFYPG.
OrthoDBi EOG7P2XR4.
TreeFami TF106479.

Miscellaneous databases

ChiTaRSi Reln. mouse.
EvolutionaryTracei Q60841.
NextBioi 297056.
PROi Q60841.
SOURCEi Search...

Gene expression databases

Bgeei Q60841.
CleanExi MM_RELN.
Genevestigatori Q60841.

Family and domain databases

InterProi IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002861. Reeler_dom.
IPR011040. Sialidases.
[Graphical view ]
Pfami PF12661. hEGF. 2 hits.
PF02014. Reeler. 1 hit.
[Graphical view ]
SMARTi SM00181. EGF. 5 hits.
[Graphical view ]
SUPFAMi SSF50939. SSF50939. 14 hits.
PROSITEi PS00022. EGF_1. 7 hits.
PS01186. EGF_2. 6 hits.
PS50026. EGF_3. 5 hits.
PS51019. REELIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A protein related to extracellular matrix proteins deleted in the mouse mutant reeler."
    D'Arcangelo G., Miao G.G., Chen S.-C., Soares H.D., Morgan J.I., Curran T.
    Nature 374:719-723(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Cerebellum.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2152-3461 (ISOFORM 1).
    Strain: BALB/c.
    Tissue: Brain.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3044-3461 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  6. "Reelin is a secreted glycoprotein recognized by the CR-50 monoclonal antibody."
    D'Arcangelo G., Nakajima K., Miyata T., Ogawa M., Mikoshiba K., Curran T.
    J. Neurosci. 17:23-31(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. Cited for: CHARACTERIZATION.
  8. "Reelin mRNA expression during mouse brain development."
    Schiffmann S.N., Bernier B., Goffinet A.M.
    Eur. J. Neurosci. 9:1055-1071(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Evolutionarily conserved, alternative splicing of reelin during brain development."
    Lambert de Rouvroit C., Bernier B., Royaux I., de Bergeyck V., Goffinet A.M.
    Exp. Neurol. 156:229-238(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  10. "Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation."
    Hiesberger T., Trommsdorff M., Howell B.W., Goffinet A.M., Mumby M.C., Cooper J.A., Herz J.
    Neuron 24:481-489(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VLDLR AND APOER2.
  11. "Reelin controls position of autonomic neurons in the spinal cord."
    Yip J.W., Yip Y.P.L., Nakajima K., Capriotti C.
    Proc. Natl. Acad. Sci. U.S.A. 97:8612-8616(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Functional importance of covalent homodimer of reelin protein linked via its central region."
    Yasui N., Kitago Y., Beppu A., Kohno T., Morishita S., Gomi H., Nagae M., Hattori M., Takagi J.
    J. Biol. Chem. 286:35247-35256(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERCHAIN DISULFIDE BOND, MUTAGENESIS OF CYS-2101.
  13. "Structure of a signaling-competent reelin fragment revealed by X-ray crystallography and electron tomography."
    Nogi T., Yasui N., Hattori M., Iwasaki K., Takagi J.
    EMBO J. 25:3675-3683(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1222-1597, DISULFIDE BONDS, CALCIUM-BINDING.
  14. "Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptors."
    Yasui N., Nogi T., Kitao T., Nakano Y., Hattori M., Takagi J.
    Proc. Natl. Acad. Sci. U.S.A. 104:9988-9993(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1948-2662, DISULFIDE BONDS, GLYCOSYLATION AT ASN-2145; ASN-2269; ASN-2317 AND ASN-2569, CALCIUM-BINDING, ZINC-BINDING SITES, MUTAGENESIS OF LYS-2360 AND LYS-2467.

Entry informationi

Entry nameiRELN_MOUSE
AccessioniPrimary (citable) accession number: Q60841
Secondary accession number(s): E9PZ78, Q9CUA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3