Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Reelin

Gene

Reln

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi2061Zinc 11
Metal bindingi2074Zinc 11
Metal bindingi2179Zinc 11
Metal bindingi2264Zinc 11
Metal bindingi2397Zinc 21
Metal bindingi2399Zinc 21
Metal bindingi2460Zinc 21

GO - Molecular functioni

  • lipoprotein particle receptor binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • serine-type peptidase activity Source: UniProtKB-KW
  • very-low-density lipoprotein particle receptor binding Source: BHF-UCL

GO - Biological processi

  • associative learning Source: BHF-UCL
  • axon guidance Source: MGI
  • brain development Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • cell migration Source: MGI
  • cell morphogenesis involved in differentiation Source: MGI
  • central nervous system development Source: MGI
  • cerebral cortex development Source: MGI
  • cerebral cortex tangential migration Source: MGI
  • dendrite development Source: MGI
  • forebrain development Source: MGI
  • glial cell differentiation Source: MGI
  • hippocampus development Source: BHF-UCL
  • lateral motor column neuron migration Source: UniProtKB
  • layer formation in cerebral cortex Source: MGI
  • learning Source: CACAO
  • long-term memory Source: BHF-UCL
  • long-term synaptic potentiation Source: CACAO
  • modulation of synaptic transmission Source: BHF-UCL
  • neuron migration Source: MGI
  • NMDA glutamate receptor clustering Source: BHF-UCL
  • peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: BHF-UCL
  • positive regulation of CREB transcription factor activity Source: BHF-UCL
  • positive regulation of dendritic spine morphogenesis Source: BHF-UCL
  • positive regulation of excitatory postsynaptic potential Source: BHF-UCL
  • positive regulation of lateral motor column neuron migration Source: BHF-UCL
  • positive regulation of long-term synaptic potentiation Source: BHF-UCL
  • positive regulation of neuron projection development Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  • positive regulation of protein kinase activity Source: MGI
  • positive regulation of protein tyrosine kinase activity Source: BHF-UCL
  • positive regulation of small GTPase mediated signal transduction Source: MGI
  • positive regulation of synapse maturation Source: BHF-UCL
  • positive regulation of synaptic transmission, glutamatergic Source: BHF-UCL
  • positive regulation of TOR signaling Source: BHF-UCL
  • postsynaptic density assembly Source: BHF-UCL
  • postsynaptic density protein 95 clustering Source: BHF-UCL
  • protein localization to synapse Source: BHF-UCL
  • receptor localization to synapse Source: BHF-UCL
  • reelin-mediated signaling pathway Source: BHF-UCL
  • regulation of behavior Source: BHF-UCL
  • regulation of gene expression Source: MGI
  • regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: BHF-UCL
  • response to pain Source: MGI
  • spinal cord patterning Source: MGI
  • 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

Enzyme and pathway databases

ReactomeiR-MMU-8866376. Reelin signalling pathway.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:103022. Reln.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • dendrite Source: MGI
  • extracellular space Source: MGI
  • plasma membrane Source: GOC
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi2101C → 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 Publication1
Mutagenesisi2360K → A: Abolishes ApoER2-binding. 1 Publication1
Mutagenesisi2467K → A: Abolishes ApoER2-binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000003030527 – 3461ReelinAdd BLAST3435

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 127PROSITE-ProRule annotation
Glycosylationi141N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi155 ↔ 179PROSITE-ProRule annotation
Glycosylationi258N-linked (GlcNAc...)Sequence analysis1
Glycosylationi290N-linked (GlcNAc...)Sequence analysis1
Glycosylationi306N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi540 ↔ 581PROSITE-ProRule annotation
Disulfide bondi609 ↔ 614PROSITE-ProRule annotation
Glycosylationi629N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi1267N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1271 ↔ 1310
Disulfide bondi1339 ↔ 1348
Glycosylationi1447N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1600N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1633 ↔ 1673PROSITE-ProRule annotation
Disulfide bondi1702 ↔ 1709PROSITE-ProRule annotation
Glycosylationi1750N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1921N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1983 ↔ 2030
Disulfide bondi2059 ↔ 2070
Disulfide bondi2101Interchain
Disulfide bondi2133 ↔ 2143
Disulfide bondi2137 ↔ 2149
Glycosylationi2145N-linked (GlcNAc...)1 Publication1
Disulfide bondi2151 ↔ 2160
Disulfide bondi2195 ↔ 2235
Glycosylationi2269N-linked (GlcNAc...)1 Publication1
Glycosylationi2317N-linked (GlcNAc...)1 Publication1
Disulfide bondi2348 ↔ 2387
Disulfide bondi2393 ↔ 2559
Disulfide bondi2482 ↔ 2492
Disulfide bondi2486 ↔ 2497
Disulfide bondi2499 ↔ 2508
Disulfide bondi2544 ↔ 2584
Glycosylationi2569N-linked (GlcNAc...)1 Publication1
Disulfide bondi2794 ↔ 2801PROSITE-ProRule annotation
Disulfide bondi2919 ↔ 2966PROSITE-ProRule annotation
Glycosylationi2962N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3016N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3073N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3160 ↔ 3170PROSITE-ProRule annotation
Glycosylationi3185N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3232 ↔ 3242PROSITE-ProRule annotation
Disulfide bondi3236 ↔ 3248PROSITE-ProRule annotation
Disulfide bondi3250 ↔ 3259PROSITE-ProRule annotation
Disulfide bondi3296 ↔ 3346PROSITE-ProRule annotation
Glycosylationi3412N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3439N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ60841.
PeptideAtlasiQ60841.
PRIDEiQ60841.

PTM databases

iPTMnetiQ60841.
PhosphoSitePlusiQ60841.

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

BgeeiENSMUSG00000042453.
CleanExiMM_RELN.
ExpressionAtlasiQ60841. baseline and differential.
GenevisibleiQ60841. MM.

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.

GO - Molecular functioni

  • lipoprotein particle receptor binding Source: BHF-UCL
  • very-low-density lipoprotein particle receptor binding Source: BHF-UCL

Protein-protein interaction databases

DIPiDIP-40924N.
IntActiQ60841. 2 interactors.
MINTiMINT-111528.
STRINGi10090.ENSMUSP00000124052.

Structurei

Secondary structure

13461
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1301 – 1310Combined sources10
Beta strandi1320 – 1327Combined sources8
Beta strandi1333 – 1335Combined sources3
Beta strandi1345 – 1348Combined sources4
Beta strandi1359 – 1361Combined sources3
Beta strandi1370 – 1375Combined sources6
Helixi1378 – 1380Combined sources3
Beta strandi1386 – 1390Combined sources5
Beta strandi1408 – 1411Combined sources4
Helixi1414 – 1419Combined sources6
Beta strandi1420 – 1424Combined sources5
Beta strandi1427 – 1430Combined sources4
Beta strandi1434 – 1437Combined sources4
Beta strandi1440 – 1445Combined sources6
Beta strandi1451 – 1453Combined sources3
Beta strandi1456 – 1458Combined sources3
Beta strandi1463 – 1472Combined sources10
Beta strandi1478 – 1481Combined sources4
Beta strandi1483 – 1486Combined sources4
Beta strandi1493 – 1496Combined sources4
Beta strandi1506 – 1513Combined sources8
Beta strandi1516 – 1518Combined sources3
Helixi1528 – 1530Combined sources3
Beta strandi1531 – 1539Combined sources9
Beta strandi1545 – 1550Combined sources6
Beta strandi1559 – 1564Combined sources6
Helixi1567 – 1569Combined sources3
Beta strandi1571 – 1579Combined sources9
Helixi1584 – 1586Combined sources3
Beta strandi1590 – 1597Combined sources8
Beta strandi1958 – 1960Combined sources3
Beta strandi1963 – 1965Combined sources3
Helixi1968 – 1970Combined sources3
Beta strandi1971 – 1973Combined sources3
Beta strandi1978 – 1980Combined sources3
Beta strandi1996 – 1999Combined sources4
Beta strandi2005 – 2011Combined sources7
Beta strandi2014 – 2016Combined sources3
Beta strandi2020 – 2032Combined sources13
Beta strandi2040 – 2047Combined sources8
Beta strandi2053 – 2056Combined sources4
Beta strandi2059 – 2061Combined sources3
Beta strandi2078 – 2080Combined sources3
Beta strandi2089 – 2095Combined sources7
Turni2096 – 2099Combined sources4
Beta strandi2102 – 2113Combined sources12
Beta strandi2122 – 2131Combined sources10
Helixi2134 – 2139Combined sources6
Beta strandi2140 – 2144Combined sources5
Turni2145 – 2147Combined sources3
Beta strandi2148 – 2151Combined sources4
Beta strandi2155 – 2157Combined sources3
Beta strandi2170 – 2172Combined sources3
Beta strandi2174 – 2176Combined sources3
Beta strandi2178 – 2187Combined sources10
Beta strandi2189 – 2193Combined sources5
Beta strandi2197 – 2201Combined sources5
Beta strandi2203 – 2206Combined sources4
Beta strandi2208 – 2210Combined sources3
Beta strandi2212 – 2216Combined sources5
Beta strandi2226 – 2233Combined sources8
Beta strandi2236 – 2238Combined sources3
Beta strandi2247 – 2254Combined sources8
Beta strandi2260 – 2265Combined sources6
Turni2269 – 2272Combined sources4
Beta strandi2275 – 2280Combined sources6
Helixi2283 – 2285Combined sources3
Beta strandi2287 – 2296Combined sources10
Beta strandi2299 – 2301Combined sources3
Beta strandi2307 – 2315Combined sources9
Beta strandi2324 – 2326Combined sources3
Beta strandi2328 – 2330Combined sources3
Turni2333 – 2335Combined sources3
Beta strandi2336 – 2338Combined sources3
Beta strandi2343 – 2345Combined sources3
Beta strandi2354 – 2357Combined sources4
Beta strandi2364 – 2368Combined sources5
Beta strandi2371 – 2373Combined sources3
Beta strandi2378 – 2384Combined sources7
Beta strandi2387 – 2389Combined sources3
Beta strandi2395 – 2403Combined sources9
Beta strandi2409 – 2412Combined sources4
Beta strandi2419 – 2422Combined sources4
Turni2433 – 2436Combined sources4
Beta strandi2440 – 2445Combined sources6
Helixi2448 – 2450Combined sources3
Beta strandi2452 – 2461Combined sources10
Beta strandi2471 – 2480Combined sources10
Helixi2484 – 2488Combined sources5
Beta strandi2489 – 2493Combined sources5
Beta strandi2496 – 2499Combined sources4
Beta strandi2503 – 2505Combined sources3
Beta strandi2510 – 2513Combined sources4
Beta strandi2519 – 2521Combined sources3
Turni2529 – 2531Combined sources3
Beta strandi2532 – 2542Combined sources11
Beta strandi2547 – 2550Combined sources4
Beta strandi2552 – 2555Combined sources4
Beta strandi2562 – 2565Combined sources4
Beta strandi2575 – 2582Combined sources8
Beta strandi2584 – 2586Combined sources3
Helixi2591 – 2593Combined sources3
Beta strandi2594 – 2602Combined sources9
Beta strandi2608 – 2613Combined sources6
Beta strandi2615 – 2617Combined sources3
Beta strandi2622 – 2627Combined sources6
Helixi2630 – 2632Combined sources3
Beta strandi2634 – 2642Combined sources9
Beta strandi2654 – 2661Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ60841.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 191ReelinPROSITE-ProRule annotationAdd BLAST165
Repeati593 – 604BNR 1Add BLAST12
Domaini671 – 702EGF-like 1PROSITE-ProRule annotationAdd BLAST32
Repeati799 – 810BNR 2Add BLAST12
Repeati952 – 963BNR 3Add BLAST12
Domaini1030 – 1061EGF-like 2PROSITE-ProRule annotationAdd BLAST32
Repeati1157 – 1168BNR 4Add BLAST12
Repeati1323 – 1334BNR 5Add BLAST12
Domaini1409 – 1442EGF-like 3PROSITE-ProRule annotationAdd BLAST34
Repeati1535 – 1546BNR 6Add BLAST12
Repeati1686 – 1697BNR 7Add BLAST12
Domaini1765 – 1796EGF-like 4PROSITE-ProRule annotationAdd BLAST32
Repeati1884 – 1895BNR 8Add BLAST12
Repeati2043 – 2054BNR 9Add BLAST12
Domaini2129 – 2161EGF-like 5PROSITE-ProRule annotationAdd BLAST33
Repeati2250 – 2261BNR 10Add BLAST12
Repeati2399 – 2410BNR 11Add BLAST12
Domaini2478 – 2509EGF-like 6PROSITE-ProRule annotationAdd BLAST32
Repeati2598 – 2609BNR 12Add BLAST12
Repeati2778 – 2789BNR 13Add BLAST12
Domaini2853 – 2884EGF-like 7PROSITE-ProRule annotationAdd BLAST32
Repeati2979 – 2990BNR 14Add BLAST12
Repeati3143 – 3155BNR 15Add BLAST13
Domaini3228 – 3260EGF-like 8PROSITE-ProRule annotationAdd BLAST33
Repeati3363 – 3374BNR 16Add BLAST12

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi3432 – 3461Arg-rich (basic)Add BLAST30

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

eggNOGiENOG410IEXI. Eukaryota.
ENOG410XQKB. LUCA.
GeneTreeiENSGT00580000081623.
HOGENOMiHOG000252908.
HOVERGENiHBG023117.
InParanoidiQ60841.
KOiK06249.
OMAiNWFFYPG.
OrthoDBiEOG091G0016.
TreeFamiTF106479.

Family and domain databases

CDDicd08544. Reeler. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR002861. Reeler_dom.
IPR011040. Sialidases.
[Graphical view]
PfamiPF02014. Reeler. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 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. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1191A → G in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti1202Q → K in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti1335V → L in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti1345G → A in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti1505R → S in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti1522 – 1524CIK → YIT in AAB91599 (PubMed:7715726).Curated3
Sequence conflicti1529N → Y in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti1593D → G in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti1611F → L in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti1648K → N in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti1661A → E in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti1667F → W in AAB91599 (PubMed:7715726).Curated1
Sequence conflicti3066Missing in BAB30592 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0055783429 – 3461Missing in isoform 3. CuratedAdd BLAST33
Alternative sequenceiVSP_0055773429 – 3430Missing in isoform 2. 1 Publication2

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]
CCDS80217.1. [Q60841-2]
PIRiS58870.
RefSeqiNP_001297393.1. NM_001310464.1. [Q60841-2]
NP_035391.2. NM_011261.2. [Q60841-1]
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.
CCDSiCCDS39023.1. [Q60841-1]
CCDS80217.1. [Q60841-2]
PIRiS58870.
RefSeqiNP_001297393.1. NM_001310464.1. [Q60841-2]
NP_035391.2. NM_011261.2. [Q60841-1]
UniGeneiMm.425236.

3D structure databases

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

Protein-protein interaction databases

DIPiDIP-40924N.
IntActiQ60841. 2 interactors.
MINTiMINT-111528.
STRINGi10090.ENSMUSP00000124052.

PTM databases

iPTMnetiQ60841.
PhosphoSitePlusiQ60841.

Proteomic databases

PaxDbiQ60841.
PeptideAtlasiQ60841.
PRIDEiQ60841.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5649.
MGIiMGI:103022. Reln.

Phylogenomic databases

eggNOGiENOG410IEXI. Eukaryota.
ENOG410XQKB. LUCA.
GeneTreeiENSGT00580000081623.
HOGENOMiHOG000252908.
HOVERGENiHBG023117.
InParanoidiQ60841.
KOiK06249.
OMAiNWFFYPG.
OrthoDBiEOG091G0016.
TreeFamiTF106479.

Enzyme and pathway databases

ReactomeiR-MMU-8866376. Reelin signalling pathway.

Miscellaneous databases

ChiTaRSiReln. mouse.
EvolutionaryTraceiQ60841.
PROiQ60841.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000042453.
CleanExiMM_RELN.
ExpressionAtlasiQ60841. baseline and differential.
GenevisibleiQ60841. MM.

Family and domain databases

CDDicd08544. Reeler. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR002861. Reeler_dom.
IPR011040. Sialidases.
[Graphical view]
PfamiPF02014. Reeler. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 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]
ProtoNetiSearch...

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 2, 2016
This is version 155 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.