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Q60841

- RELN_MOUSE

UniProt

Q60841 - RELN_MOUSE

Protein

Reelin

Gene

Reln

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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

    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

    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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MERGCWAPRA LVLAVLLLLA TLRARAATGY YPRFSPFFFL CTHHGELEGD     50
    GEQGEVLISL HIAGNPTYYV PGQEYHVTIS TSTFFDGLLV TGLYTSTSIQ 100
    SSQSIGGSSA FGFGIMSDHQ FGNQFMCSVV ASHVSHLPTT NLSFVWIAPP 150
    AGTGCVNFMA TATHRGQVIF KDALAQQLCE QGAPTEATAY SHLAEIHSDS 200
    VILRDDFDSY QQLELNPNIW VECSNCEMGE QCGTIMHGNA VTFCEPYGPR 250
    ELTTTCLNTT TASVLQFSIG SGSCRFSYSD PSITVSYAKN NTADWIQLEK 300
    IRAPSNVSTV IHILYLPEEA KGESVQFQWK QDSLRVGEVY EACWALDNIL 350
    VINSAHREVV LEDNLDPVDT GNWLFFPGAT VKHSCQSDGN SIYFHGNEGS 400
    EFNFATTRDV DLSTEDIQEQ WSEEFESQPT GWDILGAVVG ADCGTVESGL 450
    SLVFLKDGER KLCTPYMDTT GYGNLRFYFV MGGICDPGVS HENDIILYAK 500
    IEGRKEHIAL DTLTYSSYKV PSLVSVVINP ELQTPATKFC LRQKSHQGYN 550
    RNVWAVDFFH VLPVLPSTMS HMIQFSINLG CGTHQPGNSV SLEFSTNHGR 600
    SWSLLHTECL PEICAGPHLP HSTVYSSENY SGWNRITIPL PNAALTRDTR 650
    IRWRQTGPIL GNMWAIDNVY IGPSCLKFCS GRGQCTRHGC KCDPGFSGPA 700
    CEMASQTFPM FISESFGSAR LSSYHNFYSI RGAEVSFGCG VLASGKALVF 750
    NKDGRRQLIT SFLDSSQSRF LQFTLRLGSK SVLSTCRAPD QPGEGVLLHY 800
    SYDNGITWKL LEHYSYVNYH EPRIISVELP DDARQFGIQF RWWQPYHSSQ 850
    GEDVWAIDEI VMTSVLFNSI SLDFTNLVEV TQSLGFYLGN VQPYCGHDWT 900
    LCFTGDSKLA SSMRYVETQS MQIGASYMIQ FSLVMGCGQK YTPHMDNQVK 950
    LEYSANHGLT WHLVQEECLP SMPSCQEFTS ASIYHASEFT QWRRVTVVLP 1000
    QKTWSGATRF RWSQSYYTAQ DEWALDNIYI GQQCPNMCSG HGSCDHGVCR 1050
    CDQGYQGTEC HPEAALPSTI MSDFENPSSW ESDWQEVIGG EVVKPEQGCG 1100
    VVSSGSSLYF SKAGKRQLVS WDLDTSWVDF VQFYIQIGGE SAACNKPDSR 1150
    EEGILLQYSN NGGIQWHLLA EMYFSDFSKP RFVYLELPAA AKTPCTRFRW 1200
    WQPVFSGEDY DQWAVDDIII LSEKQKQVIP VVNPTLPQNF YEKPAFDYPM 1250
    NQMSVWLMLA NEGMAKNDSF CATTPSAMVF GKSDGDRFAV TRDLTLKPGY 1300
    VLQFKLNIGC TSQFSSTAPV LLQYSHDAGM SWFLVKEGCF PASAGKGCEG 1350
    NSRELSEPTV YYTGDFEEWT RITIAIPRSL ASSKTRFRWI QESSSQKNVP 1400
    PFGLDGVYIS EPCPSYCSGH GDCISGVCFC DLGYTAAQGT CVSNTPNHSE 1450
    MFDRFEGKLS PLWYKITGGQ VGTGCGTLND GRSLYFNGLG KREARTVPLD 1500
    TRNIRLVQFY IQIGSKTSGI TCIKPRARNE GLVVQYSNDN GILWHLLREL 1550
    DFMSFLEPQI ISIDLPREAK TPATAFRWWQ PQHGKHSAQW ALDDVLIGVN 1600
    DSSQTGFQDK FDGSIDLQAN WYRIQGGQVD IDCLSMDTAL IFTENIGKPR 1650
    YAETWDFHVS ASSFLQFEMN MGCSKPFSGA HGIQLQYSLN NGKDWQLVTE 1700
    ECVPPTIGCV HYTESSTYTS ERFQNWRRVT VYLPLATNSP RTRFRWIQTN 1750
    YTVGADSWAI DNVILASGCP WMCSGRGICD SGRCVCDRGF GGPFCVPVVP 1800
    LPSILKDDFN GNLHPDLWPE VYGAERGNLN GETIKSGTCL IFKGEGLRML 1850
    ISRDLDCTNT MYVQFSLRFI AKGTPERSHS ILLQFSVSGG VTWHLMDEFY 1900
    FPQTTSILFI NVPLPYGAQT NATRFRLWQP YNNGKKEEIW IIDDFIIDGN 1950
    NLNNPVLLLD TFDFGPREDN WFFYPGGNIG LYCPYSSKGA PEEDSAMVFV 2000
    SNEVGEHSIT TRDLSVNENT IIQFEINVGC STDSSSADPV RLEFSRDFGA 2050
    TWHLLLPLCY HSSSLVSSLC STEHHPSSTY YAGTTQGWRR EVVHFGKLHL 2100
    CGSVRFRWYQ GFYPAGSQPV TWAIDNVYIG PQCEEMCYGH GSCINGTKCI 2150
    CDPGYSGPTC KISTKNPDFL KDDFEGQLES DRFLLMSGGK PSRKCGILSS 2200
    GNNLFFNEDG LRMLVTRDLD LSHARFVQFF MRLGCGKGVP DPRSQPVLLQ 2250
    YSLNGGLSWS LLQEFLFSNS SNVGRYIALE MPLKARSGST RLRWWQPSEN 2300
    GHFYSPWVID QILIGGNISG NTVLEDDFST LDSRKWLLHP GGTKMPVCGS 2350
    TGDALVFIEK ASTRYVVTTD IAVNEDSFLQ IDFAASCSVT DSCYAIELEY 2400
    SVDLGLSWHP LVRDCLPTNV ECSRYHLQRI LVSDTFNKWT RITLPLPSYT 2450
    RSQATRFRWH QPAPFDKQQT WAIDNVYIGD GCLDMCSGHG RCVQGSCVCD 2500
    EQWGGLYCDE PETSLPTQLK DNFNRAPSNQ NWLTVSGGKL STVCGAVASG 2550
    LALHFSGGCS RLLVTVDLNL TNAEFIQFYF MYGCLITPSN RNQGVLLEYS 2600
    VNGGITWNLL MEIFYDQYSK PGFVNILLPP DAKEIATRFR WWQPRHDGLD 2650
    QNDWAIDNVL ISGSADQRTV MLDTFSSAPV PQHERSPADA GPVGRIAFEM 2700
    FLEDKTSVNE NWLFHDDCTV ERFCDSPDGV MLCGSHDGRE VYAVTHDLTP 2750
    TENWIMQFKI SVGCKVPEKI AQNQIHVQFS TDFGVSWSYL VPQCLPADPK 2800
    CSGSVSQPSV FFPTEGWKRI TYPLPESLTG NPVRFRFYQK YSDVQWAIDN 2850
    FYLGPGCLDN CGGHGDCLKE QCICDPGYSG PNCYLTHSLK TFLKERFDSE 2900
    EIKPDLWMSL EGGSTCTECG VLAENTALYF GGSTVRQAIT QDLDLRGAKF 2950
    LQYWGRIGSE NNMTSCHRPV CRKEGVLLDF STDGGITWTL LHEMDFQKYI 3000
    SVRHDYILLP EGALTNTTRL RWWQPFVISN GLVVSGVERA QWALDNILIG 3050
    GAEINPSQLV DTFDDEGSSH EENWSFYPNA VRTAGFCGNP SFHLYWPNKK 3100
    KDKTHNALSS RELIIQPGYM MQFKIVVGCE ATSCGDLHSV MLEYTKDARS 3150
    DSWQLVQTQC LPSSSNSIGC SPFQFHEATI YNAVNSSSWK RITIQLPDHV 3200
    SSSATQFRWI QKGEETEKQS WAIDHVYIGE ACPKLCSGHG YCTTGAVCIC 3250
    DESFQGDDCS VFSHELPSYI KDNFESARVT EANWETIQGG VIGSGCGQLA 3300
    PYAHGDSLYF NGCQIRQAAT KPLDLTRASK IMFVLQIGSP AQTDSCNSDL 3350
    SGPHTVDKAV LLQYSVNNGI TWHVIAQHQP KDFTQAQRVS YNVPLEARMK 3400
    GVLLRWWQPR HNGTGHDQWA LDHVEVVLVS TRKQNYMMNF SRQHGLRHFY 3450
    NRRRRSLRRY P 3461
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    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

    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: October 1, 2014
    This is version 139 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