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Q60841 (RELN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Reelin

EC=3.4.21.-
Alternative name(s):
Reeler protein
Gene names
Name:Reln
Synonyms:Rl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation. Ref.11

Subunit structure

Oligomer of disulfide-linked homodimers. Binds to the ectodomains of VLDLR and LRP8/APOER2. Ref.10 Ref.12 Ref.13 Ref.14

Subcellular location

Secretedextracellular spaceextracellular matrix.

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. Ref.8 Ref.9

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.

Domain

The basic C-terminal region is essential for secretion.

Post-translational modification

N-glycosylated and to a lesser extent also O-glycosylated. Ref.14

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.

Sequence similarities

Belongs to the reelin family.

Contains 16 BNR repeats.

Contains 8 EGF-like domains.

Contains 1 reelin domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionDevelopmental protein
Hydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-methyl-D-aspartate receptor clustering

Inferred from mutant phenotype PubMed 21664258. Source: BHF-UCL

associative learning

Inferred from direct assay PubMed 21852430. Source: BHF-UCL

axon guidance

Inferred from mutant phenotype PubMed 16324103. Source: MGI

brain development

Inferred from mutant phenotype PubMed 12223565. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from mutant phenotype PubMed 17694053. Source: MGI

cell morphogenesis involved in differentiation

Inferred from mutant phenotype PubMed 12925587. Source: MGI

central nervous system development

Inferred from mutant phenotype PubMed 11900467. Source: MGI

cerebral cortex development

Inferred from mutant phenotype PubMed 21491433. Source: MGI

cerebral cortex tangential migration

Inferred from mutant phenotype PubMed 16901480. Source: MGI

dendrite development

Inferred from mutant phenotype PubMed 14715136. Source: MGI

forebrain development

Inferred from mutant phenotype PubMed 17694053. Source: MGI

glial cell differentiation

Inferred from mutant phenotype PubMed 12925587. Source: MGI

hippocampus development

Inferred from direct assay PubMed 17229826. Source: BHF-UCL

lateral motor column neuron migration

Inferred from mutant phenotype PubMed 20711475. Source: UniProtKB

layer formation in cerebral cortex

Inferred from mutant phenotype PubMed 20847152. Source: MGI

long-term memory

Inferred from direct assay PubMed 21852430. Source: BHF-UCL

neuron migration

Inferred from mutant phenotype PubMed 12223565PubMed 12724835PubMed 14980731PubMed 15703280. Source: MGI

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 12526740. Source: MGI

positive regulation of CREB transcription factor activity

Inferred from direct assay PubMed 21852430. Source: BHF-UCL

positive regulation of TOR signaling

Inferred from direct assay PubMed 21664258. Source: BHF-UCL

positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity

Inferred from direct assay PubMed 17229826. Source: BHF-UCL

positive regulation of dendritic spine morphogenesis

Inferred from direct assay PubMed 21852430. Source: BHF-UCL

positive regulation of excitatory postsynaptic membrane potential

Inferred from direct assay PubMed 17229826. Source: BHF-UCL

positive regulation of lateral motor column neuron migration

Inferred from mutant phenotype PubMed 20711475. Source: BHF-UCL

positive regulation of long-term synaptic potentiation

Inferred from direct assay PubMed 21852430. Source: BHF-UCL

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 17229826. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 10571240PubMed 21852430. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 21664258. Source: BHF-UCL

positive regulation of protein kinase activity

Inferred from direct assay PubMed 12526740. Source: MGI

positive regulation of protein tyrosine kinase activity

Inferred from direct assay PubMed 21852430. Source: BHF-UCL

positive regulation of small GTPase mediated signal transduction

Inferred from direct assay PubMed 15062102. Source: MGI

positive regulation of synapse maturation

Inferred from direct assay PubMed 17229826. Source: BHF-UCL

positive regulation of synaptic transmission, glutamatergic

Inferred from direct assay PubMed 17229826. Source: BHF-UCL

postsynaptic density assembly

Inferred by curator PubMed 21664258. Source: BHF-UCL

postsynaptic density protein 95 clustering

Inferred from mutant phenotype PubMed 21664258. Source: BHF-UCL

protein localization to synapse

Inferred from mutant phenotype PubMed 21664258. Source: BHF-UCL

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

receptor localization to synapse

Inferred from mutant phenotype PubMed 21664258. Source: BHF-UCL

reelin-mediated signaling pathway

Inferred from direct assay PubMed 10571240PubMed 21852430. Source: BHF-UCL

regulation of N-methyl-D-aspartate selective glutamate receptor activity

Inferred from mutant phenotype PubMed 20357114. Source: BHF-UCL

regulation of behavior

Inferred from mutant phenotype PubMed 20357114. Source: BHF-UCL

regulation of gene expression

Inferred from mutant phenotype PubMed 15255972. Source: MGI

regulation of synaptic transmission

Inferred from mutant phenotype PubMed 18778775. Source: BHF-UCL

response to pain

Inferred from mutant phenotype PubMed 16580148. Source: MGI

spinal cord patterning

Inferred from mutant phenotype PubMed 16580148. Source: MGI

ventral spinal cord development

Inferred from expression pattern PubMed 20711475. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15525772PubMed 19409883. Source: MGI

dendrite

Inferred from direct assay PubMed 15677725. Source: MGI

extracellular space

Inferred from direct assay PubMed 12526740PubMed 12724835. Source: MGI

proteinaceous extracellular matrix

Traceable author statement PubMed 11900467. Source: MGI

   Molecular_functionlipoprotein particle receptor binding

Inferred from physical interaction PubMed 10571240. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

very-low-density lipoprotein particle receptor binding

Inferred from physical interaction PubMed 10571240. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: 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.
Isoform 2 (identifier: Q60841-2)

The sequence of this isoform differs from the canonical sequence as follows:
     3429-3430: Missing.
Isoform 3 (identifier: Q60841-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 34613435Reelin
PRO_0000030305

Regions

Domain27 – 191165Reelin
Repeat593 – 60412BNR 1
Domain671 – 70232EGF-like 1
Repeat799 – 81012BNR 2
Repeat952 – 96312BNR 3
Domain1030 – 106132EGF-like 2
Repeat1157 – 116812BNR 4
Repeat1323 – 133412BNR 5
Domain1409 – 144234EGF-like 3
Repeat1535 – 154612BNR 6
Repeat1686 – 169712BNR 7
Domain1765 – 179632EGF-like 4
Repeat1884 – 189512BNR 8
Repeat2043 – 205412BNR 9
Domain2129 – 216133EGF-like 5
Repeat2250 – 226112BNR 10
Repeat2399 – 241012BNR 11
Domain2478 – 250932EGF-like 6
Repeat2598 – 260912BNR 12
Repeat2778 – 278912BNR 13
Domain2853 – 288432EGF-like 7
Repeat2979 – 299012BNR 14
Repeat3143 – 315513BNR 15
Domain3228 – 326033EGF-like 8
Repeat3363 – 337412BNR 16
Compositional bias3432 – 346130Arg-rich (basic)

Sites

Metal binding20611Zinc 1
Metal binding20741Zinc 1
Metal binding21791Zinc 1
Metal binding22641Zinc 1
Metal binding23971Zinc 2
Metal binding23991Zinc 2
Metal binding24601Zinc 2

Amino acid modifications

Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation3061N-linked (GlcNAc...) Potential
Glycosylation6291N-linked (GlcNAc...) Potential
Glycosylation12671N-linked (GlcNAc...) Potential
Glycosylation14471N-linked (GlcNAc...) Potential
Glycosylation16001N-linked (GlcNAc...) Potential
Glycosylation17501N-linked (GlcNAc...) Potential
Glycosylation19211N-linked (GlcNAc...) Potential
Glycosylation21451N-linked (GlcNAc...) Ref.14
Glycosylation22691N-linked (GlcNAc...) Ref.14
Glycosylation23171N-linked (GlcNAc...) Ref.14
Glycosylation25691N-linked (GlcNAc...) Ref.14
Glycosylation29621N-linked (GlcNAc...) Potential
Glycosylation30161N-linked (GlcNAc...) Potential
Glycosylation30731N-linked (GlcNAc...) Potential
Glycosylation31851N-linked (GlcNAc...) Potential
Glycosylation34121N-linked (GlcNAc...) Potential
Glycosylation34391N-linked (GlcNAc...) Potential
Disulfide bond41 ↔ 127 By similarity
Disulfide bond155 ↔ 179 By similarity
Disulfide bond540 ↔ 581 By similarity
Disulfide bond609 ↔ 614 By similarity
Disulfide bond675 ↔ 685 By similarity
Disulfide bond692 ↔ 701 By similarity
Disulfide bond895 ↔ 937 By similarity
Disulfide bond968 ↔ 975 By similarity
Disulfide bond1034 ↔ 1044 By similarity
Disulfide bond1051 ↔ 1060 By similarity
Disulfide bond1271 ↔ 1310 Ref.12 Ref.13 Ref.14
Disulfide bond1339 ↔ 1348 Ref.12 Ref.13 Ref.14
Disulfide bond1633 ↔ 1673 By similarity
Disulfide bond1702 ↔ 1709 By similarity
Disulfide bond1983 ↔ 2030 Ref.12 Ref.13 Ref.14
Disulfide bond2059 ↔ 2070 Ref.12 Ref.13 Ref.14
Disulfide bond2101Interchain Ref.12 Ref.13 Ref.14
Disulfide bond2133 ↔ 2143 Ref.12 Ref.13 Ref.14
Disulfide bond2137 ↔ 2149 Ref.12 Ref.13 Ref.14
Disulfide bond2151 ↔ 2160 Ref.12 Ref.13 Ref.14
Disulfide bond2195 ↔ 2235 Ref.12 Ref.13 Ref.14
Disulfide bond2348 ↔ 2387 Ref.12 Ref.13 Ref.14
Disulfide bond2393 ↔ 2559 Ref.12 Ref.13 Ref.14
Disulfide bond2482 ↔ 2492 Ref.12 Ref.13 Ref.14
Disulfide bond2486 ↔ 2497 Ref.12 Ref.13 Ref.14
Disulfide bond2499 ↔ 2508 Ref.12 Ref.13 Ref.14
Disulfide bond2544 ↔ 2584 Ref.12 Ref.13 Ref.14
Disulfide bond2794 ↔ 2801 By similarity
Disulfide bond2919 ↔ 2966 By similarity
Disulfide bond3160 ↔ 3170 By similarity
Disulfide bond3232 ↔ 3242 By similarity
Disulfide bond3236 ↔ 3248 By similarity
Disulfide bond3250 ↔ 3259 By similarity
Disulfide bond3296 ↔ 3346 By similarity

Natural variations

Alternative sequence3429 – 346133Missing in isoform 3.
VSP_005578
Alternative sequence3429 – 34302Missing in isoform 2.
VSP_005577

Experimental info

Mutagenesis21011C → 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. Ref.12
Mutagenesis23601K → A: Abolishes ApoER2-binding. Ref.14
Mutagenesis24671K → A: Abolishes ApoER2-binding. Ref.14
Sequence conflict11911A → G in AAB91599. Ref.1
Sequence conflict12021Q → K in AAB91599. Ref.1
Sequence conflict13351V → L in AAB91599. Ref.1
Sequence conflict13451G → A in AAB91599. Ref.1
Sequence conflict15051R → S in AAB91599. Ref.1
Sequence conflict1522 – 15243CIK → YIT in AAB91599. Ref.1
Sequence conflict15291N → Y in AAB91599. Ref.1
Sequence conflict15931D → G in AAB91599. Ref.1
Sequence conflict16111F → L in AAB91599. Ref.1
Sequence conflict16481K → N in AAB91599. Ref.1
Sequence conflict16611A → E in AAB91599. Ref.1
Sequence conflict16671F → W in AAB91599. Ref.1
Sequence conflict30661Missing in BAB30592. Ref.5

Secondary structure

................................................................................................................................................................................................................ 3461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 1CCE64C845160F2E

FASTA3,461387,495
        10         20         30         40         50         60 
MERGCWAPRA LVLAVLLLLA TLRARAATGY YPRFSPFFFL CTHHGELEGD GEQGEVLISL 

        70         80         90        100        110        120 
HIAGNPTYYV PGQEYHVTIS TSTFFDGLLV TGLYTSTSIQ SSQSIGGSSA FGFGIMSDHQ 

       130        140        150        160        170        180 
FGNQFMCSVV ASHVSHLPTT NLSFVWIAPP AGTGCVNFMA TATHRGQVIF KDALAQQLCE 

       190        200        210        220        230        240 
QGAPTEATAY SHLAEIHSDS VILRDDFDSY QQLELNPNIW VECSNCEMGE QCGTIMHGNA 

       250        260        270        280        290        300 
VTFCEPYGPR ELTTTCLNTT TASVLQFSIG SGSCRFSYSD PSITVSYAKN NTADWIQLEK 

       310        320        330        340        350        360 
IRAPSNVSTV IHILYLPEEA KGESVQFQWK QDSLRVGEVY EACWALDNIL VINSAHREVV 

       370        380        390        400        410        420 
LEDNLDPVDT GNWLFFPGAT VKHSCQSDGN SIYFHGNEGS EFNFATTRDV DLSTEDIQEQ 

       430        440        450        460        470        480 
WSEEFESQPT GWDILGAVVG ADCGTVESGL SLVFLKDGER KLCTPYMDTT GYGNLRFYFV 

       490        500        510        520        530        540 
MGGICDPGVS HENDIILYAK IEGRKEHIAL DTLTYSSYKV PSLVSVVINP ELQTPATKFC 

       550        560        570        580        590        600 
LRQKSHQGYN RNVWAVDFFH VLPVLPSTMS HMIQFSINLG CGTHQPGNSV SLEFSTNHGR 

       610        620        630        640        650        660 
SWSLLHTECL PEICAGPHLP HSTVYSSENY SGWNRITIPL PNAALTRDTR IRWRQTGPIL 

       670        680        690        700        710        720 
GNMWAIDNVY IGPSCLKFCS GRGQCTRHGC KCDPGFSGPA CEMASQTFPM FISESFGSAR 

       730        740        750        760        770        780 
LSSYHNFYSI RGAEVSFGCG VLASGKALVF NKDGRRQLIT SFLDSSQSRF LQFTLRLGSK 

       790        800        810        820        830        840 
SVLSTCRAPD QPGEGVLLHY SYDNGITWKL LEHYSYVNYH EPRIISVELP DDARQFGIQF 

       850        860        870        880        890        900 
RWWQPYHSSQ GEDVWAIDEI VMTSVLFNSI SLDFTNLVEV TQSLGFYLGN VQPYCGHDWT 

       910        920        930        940        950        960 
LCFTGDSKLA SSMRYVETQS MQIGASYMIQ FSLVMGCGQK YTPHMDNQVK LEYSANHGLT 

       970        980        990       1000       1010       1020 
WHLVQEECLP SMPSCQEFTS ASIYHASEFT QWRRVTVVLP QKTWSGATRF RWSQSYYTAQ 

      1030       1040       1050       1060       1070       1080 
DEWALDNIYI GQQCPNMCSG HGSCDHGVCR CDQGYQGTEC HPEAALPSTI MSDFENPSSW 

      1090       1100       1110       1120       1130       1140 
ESDWQEVIGG EVVKPEQGCG VVSSGSSLYF SKAGKRQLVS WDLDTSWVDF VQFYIQIGGE 

      1150       1160       1170       1180       1190       1200 
SAACNKPDSR EEGILLQYSN NGGIQWHLLA EMYFSDFSKP RFVYLELPAA AKTPCTRFRW 

      1210       1220       1230       1240       1250       1260 
WQPVFSGEDY DQWAVDDIII LSEKQKQVIP VVNPTLPQNF YEKPAFDYPM NQMSVWLMLA 

      1270       1280       1290       1300       1310       1320 
NEGMAKNDSF CATTPSAMVF GKSDGDRFAV TRDLTLKPGY VLQFKLNIGC TSQFSSTAPV 

      1330       1340       1350       1360       1370       1380 
LLQYSHDAGM SWFLVKEGCF PASAGKGCEG NSRELSEPTV YYTGDFEEWT RITIAIPRSL 

      1390       1400       1410       1420       1430       1440 
ASSKTRFRWI QESSSQKNVP PFGLDGVYIS EPCPSYCSGH GDCISGVCFC DLGYTAAQGT 

      1450       1460       1470       1480       1490       1500 
CVSNTPNHSE MFDRFEGKLS PLWYKITGGQ VGTGCGTLND GRSLYFNGLG KREARTVPLD 

      1510       1520       1530       1540       1550       1560 
TRNIRLVQFY IQIGSKTSGI TCIKPRARNE GLVVQYSNDN GILWHLLREL DFMSFLEPQI 

      1570       1580       1590       1600       1610       1620 
ISIDLPREAK TPATAFRWWQ PQHGKHSAQW ALDDVLIGVN DSSQTGFQDK FDGSIDLQAN 

      1630       1640       1650       1660       1670       1680 
WYRIQGGQVD IDCLSMDTAL IFTENIGKPR YAETWDFHVS ASSFLQFEMN MGCSKPFSGA 

      1690       1700       1710       1720       1730       1740 
HGIQLQYSLN NGKDWQLVTE ECVPPTIGCV HYTESSTYTS ERFQNWRRVT VYLPLATNSP 

      1750       1760       1770       1780       1790       1800 
RTRFRWIQTN YTVGADSWAI DNVILASGCP WMCSGRGICD SGRCVCDRGF GGPFCVPVVP 

      1810       1820       1830       1840       1850       1860 
LPSILKDDFN GNLHPDLWPE VYGAERGNLN GETIKSGTCL IFKGEGLRML ISRDLDCTNT 

      1870       1880       1890       1900       1910       1920 
MYVQFSLRFI AKGTPERSHS ILLQFSVSGG VTWHLMDEFY FPQTTSILFI NVPLPYGAQT 

      1930       1940       1950       1960       1970       1980 
NATRFRLWQP YNNGKKEEIW IIDDFIIDGN NLNNPVLLLD TFDFGPREDN WFFYPGGNIG 

      1990       2000       2010       2020       2030       2040 
LYCPYSSKGA PEEDSAMVFV SNEVGEHSIT TRDLSVNENT IIQFEINVGC STDSSSADPV 

      2050       2060       2070       2080       2090       2100 
RLEFSRDFGA TWHLLLPLCY HSSSLVSSLC STEHHPSSTY YAGTTQGWRR EVVHFGKLHL 

      2110       2120       2130       2140       2150       2160 
CGSVRFRWYQ GFYPAGSQPV TWAIDNVYIG PQCEEMCYGH GSCINGTKCI CDPGYSGPTC 

      2170       2180       2190       2200       2210       2220 
KISTKNPDFL KDDFEGQLES DRFLLMSGGK PSRKCGILSS GNNLFFNEDG LRMLVTRDLD 

      2230       2240       2250       2260       2270       2280 
LSHARFVQFF MRLGCGKGVP DPRSQPVLLQ YSLNGGLSWS LLQEFLFSNS SNVGRYIALE 

      2290       2300       2310       2320       2330       2340 
MPLKARSGST RLRWWQPSEN GHFYSPWVID QILIGGNISG NTVLEDDFST LDSRKWLLHP 

      2350       2360       2370       2380       2390       2400 
GGTKMPVCGS TGDALVFIEK ASTRYVVTTD IAVNEDSFLQ IDFAASCSVT DSCYAIELEY 

      2410       2420       2430       2440       2450       2460 
SVDLGLSWHP LVRDCLPTNV ECSRYHLQRI LVSDTFNKWT RITLPLPSYT RSQATRFRWH 

      2470       2480       2490       2500       2510       2520 
QPAPFDKQQT WAIDNVYIGD GCLDMCSGHG RCVQGSCVCD EQWGGLYCDE PETSLPTQLK 

      2530       2540       2550       2560       2570       2580 
DNFNRAPSNQ NWLTVSGGKL STVCGAVASG LALHFSGGCS RLLVTVDLNL TNAEFIQFYF 

      2590       2600       2610       2620       2630       2640 
MYGCLITPSN RNQGVLLEYS VNGGITWNLL MEIFYDQYSK PGFVNILLPP DAKEIATRFR 

      2650       2660       2670       2680       2690       2700 
WWQPRHDGLD QNDWAIDNVL ISGSADQRTV MLDTFSSAPV PQHERSPADA GPVGRIAFEM 

      2710       2720       2730       2740       2750       2760 
FLEDKTSVNE NWLFHDDCTV ERFCDSPDGV MLCGSHDGRE VYAVTHDLTP TENWIMQFKI 

      2770       2780       2790       2800       2810       2820 
SVGCKVPEKI AQNQIHVQFS TDFGVSWSYL VPQCLPADPK CSGSVSQPSV FFPTEGWKRI 

      2830       2840       2850       2860       2870       2880 
TYPLPESLTG NPVRFRFYQK YSDVQWAIDN FYLGPGCLDN CGGHGDCLKE QCICDPGYSG 

      2890       2900       2910       2920       2930       2940 
PNCYLTHSLK TFLKERFDSE EIKPDLWMSL EGGSTCTECG VLAENTALYF GGSTVRQAIT 

      2950       2960       2970       2980       2990       3000 
QDLDLRGAKF LQYWGRIGSE NNMTSCHRPV CRKEGVLLDF STDGGITWTL LHEMDFQKYI 

      3010       3020       3030       3040       3050       3060 
SVRHDYILLP EGALTNTTRL RWWQPFVISN GLVVSGVERA QWALDNILIG GAEINPSQLV 

      3070       3080       3090       3100       3110       3120 
DTFDDEGSSH EENWSFYPNA VRTAGFCGNP SFHLYWPNKK KDKTHNALSS RELIIQPGYM 

      3130       3140       3150       3160       3170       3180 
MQFKIVVGCE ATSCGDLHSV MLEYTKDARS DSWQLVQTQC LPSSSNSIGC SPFQFHEATI 

      3190       3200       3210       3220       3230       3240 
YNAVNSSSWK RITIQLPDHV SSSATQFRWI QKGEETEKQS WAIDHVYIGE ACPKLCSGHG 

      3250       3260       3270       3280       3290       3300 
YCTTGAVCIC DESFQGDDCS VFSHELPSYI KDNFESARVT EANWETIQGG VIGSGCGQLA 

      3310       3320       3330       3340       3350       3360 
PYAHGDSLYF NGCQIRQAAT KPLDLTRASK IMFVLQIGSP AQTDSCNSDL SGPHTVDKAV 

      3370       3380       3390       3400       3410       3420 
LLQYSVNNGI TWHVIAQHQP KDFTQAQRVS YNVPLEARMK GVLLRWWQPR HNGTGHDQWA 

      3430       3440       3450       3460 
LDHVEVVLVS TRKQNYMMNF SRQHGLRHFY NRRRRSLRRY P 

« Hide

Isoform 2 [UniParc].

Checksum: DC72A41DFC9B88C6
Show »

FASTA3,459387,309
Isoform 3 [UniParc].

Checksum: ADA613A4F66D585A
Show »

FASTA3,428383,200

References

« Hide 'large scale' references
[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]"Genomic organization of the mouse reelin gene."
Royaux I., Lambert de Rouvroit C., D'Arcangelo G., Demirov D., Goffinet A.M.
Genomics 46:240-250(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The reeler gene encodes a protein with an EGF-like motif expressed by pioneer neurons."
Hirotsune S., Takahara T., Sasaki N., Hirose K., Yoshiki A., Ohashi T., Kusakabe M., Murakami Y., Muramatsu M., Watanabe S., Nakao K., Katsuki M., Hayashizaki Y.
Nat. Genet. 10:77-83(1995) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Reelin is a serine protease of the extracellular matrix."
Quattrocchi C.C., Wannenes F., Persico A.M., Ciafre S.A., D'Arcangelo G., Farace M.G., Keller F.
J. Biol. Chem. 277:303-309(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS58870.
RefSeqNP_035391.2. NM_011261.2.
XP_006535709.1. XM_006535646.1.
UniGeneMm.425236.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DDUX-ray2.05A1222-1597[»]
2E26X-ray2.00A1948-2662[»]
3A7QX-ray2.60A1948-2662[»]
ProteinModelPortalQ60841.
SMRQ60841. Positions 1294-1597, 1956-2662.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-40924N.
MINTMINT-111528.

PTM databases

PhosphoSiteQ60841.

Proteomic databases

PaxDbQ60841.
PRIDEQ60841.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000062372; ENSMUSP00000058025; ENSMUSG00000042453. [Q60841-2]
ENSMUST00000161356; ENSMUSP00000124052; ENSMUSG00000042453. [Q60841-1]
GeneID19699.
KEGGmmu:19699.
UCSCuc008wpi.1. mouse. [Q60841-1]

Organism-specific databases

CTD5649.
MGIMGI:103022. Reln.

Phylogenomic databases

eggNOGNOG45680.
GeneTreeENSGT00580000081623.
HOGENOMHOG000252908.
HOVERGENHBG023117.
InParanoidQ60841.
KOK06249.
OMANWFFYPG.
OrthoDBEOG7P2XR4.
TreeFamTF106479.

Gene expression databases

BgeeQ60841.
CleanExMM_RELN.
GenevestigatorQ60841.

Family and domain databases

InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002861. Reeler_dom.
IPR011040. Sialidases.
[Graphical view]
PfamPF12661. hEGF. 2 hits.
PF02014. Reeler. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 5 hits.
[Graphical view]
SUPFAMSSF50939. SSF50939. 14 hits.
PROSITEPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 6 hits.
PS50026. EGF_3. 5 hits.
PS51019. REELIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRELN. mouse.
EvolutionaryTraceQ60841.
NextBio297056.
PROQ60841.
SOURCESearch...

Entry information

Entry nameRELN_MOUSE
AccessionPrimary (citable) accession number: Q60841
Secondary accession number(s): E9PZ78, Q9CUA6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot