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P78509 (RELN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Reelin

EC=3.4.21.-
Gene names
Name:RELN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3460 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 By similarity.

Subunit structure

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

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

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. In adult brain, preferentially expressed in GABAergic interneurons of prefrontal cortices, temporal cortex, hippocampus and glutamatergic granule cells of cerebellum. Expression is reduced to about 50% in patients with schizophrenia. Also expressed in fetal and adult liver. Ref.5

Developmental stage

Expressed in fetal and postnatal brain and liver. Expression in postnatal human brain is high in the cerebellum.

Domain

The basic C-terminal region is essential for secretion By similarity.

Polymorphism

A polymorphic GGC triplet repeat located in the 5'-UTR region of RELN gene, which harbors in the normal population 8 to 10 repeats, is significantly increased in autistic patients to carry 4 to 23 additional repeats.

Involvement in disease

Lissencephaly 2 (LIS2) [MIM:257320]: A classic type lissencephaly associated with ataxia, mental retardation, seizures and abnormalities of the cerebellum, hippocampus and brainstem.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Sequence similarities

Belongs to the reelin family.

Contains 16 BNR repeats.

Contains 8 EGF-like domains.

Contains 1 reelin domain.

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

associative learning

Inferred from electronic annotation. Source: Ensembl

axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

brain development

Inferred from sequence or structural similarity. Source: UniProtKB

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell morphogenesis involved in differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

central nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

cerebral cortex tangential migration

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite development

Inferred from electronic annotation. Source: Ensembl

glial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

hippocampus development

Inferred from sequence or structural similarity. Source: BHF-UCL

lateral motor column neuron migration

Inferred from electronic annotation. Source: Ensembl

long-term memory

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of CREB transcription factor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of TOR signaling

Inferred from electronic annotation. Source: Ensembl

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

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of lateral motor column neuron migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of long-term synaptic potentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of neuron projection development

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity PubMed 10571240. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of small GTPase mediated signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synapse maturation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of synaptic transmission, glutamatergic

Inferred from sequence or structural similarity. Source: BHF-UCL

postsynaptic density protein 95 clustering

Inferred from electronic annotation. Source: Ensembl

receptor localization to synapse

Inferred from electronic annotation. Source: Ensembl

reelin-mediated signaling pathway

Inferred from sequence or structural similarity PubMed 10571240. Source: BHF-UCL

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

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of behavior

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of synaptic transmission

Inferred from sequence or structural similarity. Source: BHF-UCL

response to pain

Inferred from sequence or structural similarity. Source: UniProtKB

spinal cord patterning

Inferred from sequence or structural similarity. Source: UniProtKB

ventral spinal cord development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlipoprotein particle receptor binding

Inferred from sequence or structural similarity PubMed 10571240. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine/tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

serine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

very-low-density lipoprotein particle receptor binding

Inferred from sequence or structural similarity PubMed 10571240. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78509-1)

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: P78509-2)

The sequence of this isoform differs from the canonical sequence as follows:
     3428-3429: Missing.
Isoform 3 (identifier: P78509-3)

The sequence of this isoform differs from the canonical sequence as follows:
     3428-3460: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 34603435Reelin
PRO_0000030304

Regions

Domain26 – 190165Reelin
Repeat592 – 60312BNR 1
Domain670 – 70132EGF-like 1
Repeat798 – 80912BNR 2
Repeat951 – 96212BNR 3
Domain1029 – 106032EGF-like 2
Repeat1156 – 116712BNR 4
Repeat1322 – 133312BNR 5
Domain1408 – 144134EGF-like 3
Repeat1534 – 154512BNR 6
Repeat1685 – 169612BNR 7
Domain1764 – 179532EGF-like 4
Repeat1883 – 189412BNR 8
Repeat2042 – 205312BNR 9
Domain2128 – 216033EGF-like 5
Repeat2249 – 226012BNR 10
Repeat2398 – 240912BNR 11
Domain2477 – 250832EGF-like 6
Repeat2597 – 260812BNR 12
Repeat2777 – 278812BNR 13
Domain2852 – 288332EGF-like 7
Repeat2978 – 298912BNR 14
Repeat3142 – 315413BNR 15
Domain3227 – 325933EGF-like 8
Repeat3362 – 337312BNR 16
Compositional bias3431 – 346030Arg-rich (basic)

Sites

Metal binding20601Zinc 1 By similarity
Metal binding20731Zinc 1 By similarity
Metal binding21781Zinc 1 By similarity
Metal binding22631Zinc 1 By similarity
Metal binding23961Zinc 2 By similarity
Metal binding23981Zinc 2 By similarity
Metal binding24591Zinc 2 By similarity

Amino acid modifications

Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation2571N-linked (GlcNAc...) Potential
Glycosylation2891N-linked (GlcNAc...) Potential
Glycosylation3051N-linked (GlcNAc...) Ref.9
Glycosylation6281N-linked (GlcNAc...) Potential
Glycosylation12661N-linked (GlcNAc...) Potential
Glycosylation15991N-linked (GlcNAc...) Potential
Glycosylation17491N-linked (GlcNAc...) Potential
Glycosylation19201N-linked (GlcNAc...) Ref.9
Glycosylation21441N-linked (GlcNAc...) Potential
Glycosylation22681N-linked (GlcNAc...) Potential
Glycosylation23161N-linked (GlcNAc...) Potential
Glycosylation25681N-linked (GlcNAc...) Potential
Glycosylation29611N-linked (GlcNAc...) Potential
Glycosylation30151N-linked (GlcNAc...) Ref.9
Glycosylation30721N-linked (GlcNAc...) Potential
Glycosylation31841N-linked (GlcNAc...) Potential
Glycosylation34111N-linked (GlcNAc...) Potential
Glycosylation34381N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 126 By similarity
Disulfide bond154 ↔ 178 By similarity
Disulfide bond539 ↔ 580 By similarity
Disulfide bond608 ↔ 613 By similarity
Disulfide bond674 ↔ 684 By similarity
Disulfide bond691 ↔ 700 By similarity
Disulfide bond894 ↔ 936 By similarity
Disulfide bond967 ↔ 974 By similarity
Disulfide bond1033 ↔ 1043 By similarity
Disulfide bond1050 ↔ 1059 By similarity
Disulfide bond1270 ↔ 1309 By similarity
Disulfide bond1338 ↔ 1347 By similarity
Disulfide bond1632 ↔ 1672 By similarity
Disulfide bond1701 ↔ 1708 By similarity
Disulfide bond2100Interchain By similarity
Disulfide bond2132 ↔ 2142 By similarity
Disulfide bond2136 ↔ 2148 By similarity
Disulfide bond2150 ↔ 2159 By similarity
Disulfide bond2194 ↔ 2234 By similarity
Disulfide bond2347 ↔ 2386 By similarity
Disulfide bond2392 ↔ 2558 By similarity
Disulfide bond2543 ↔ 2583 By similarity
Disulfide bond2793 ↔ 2800 By similarity
Disulfide bond2856 ↔ 2866 By similarity
Disulfide bond2860 ↔ 2871 By similarity
Disulfide bond2873 ↔ 2882 By similarity
Disulfide bond2918 ↔ 2965 By similarity
Disulfide bond3159 ↔ 3169 By similarity
Disulfide bond3231 ↔ 3241 By similarity
Disulfide bond3235 ↔ 3247 By similarity
Disulfide bond3249 ↔ 3258 By similarity
Disulfide bond3295 ↔ 3345 By similarity

Natural variations

Alternative sequence3428 – 346033Missing in isoform 3.
VSP_005576
Alternative sequence3428 – 34292Missing in isoform 2.
VSP_005575
Natural variant9781T → A.
Corresponds to variant rs3025962 [ dbSNP | Ensembl ].
VAR_047977
Natural variant9971L → V.
Corresponds to variant rs362691 [ dbSNP | Ensembl ].
VAR_047978
Natural variant17031P → R.
Corresponds to variant rs2229860 [ dbSNP | Ensembl ].
VAR_057712

Experimental info

Sequence conflict7521D → E in AAC51105. Ref.1

Sequences

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

Last modified May 18, 2010. Version 3.
Checksum: 9A398EC17FA4EE1B

FASTA3,460388,388
        10         20         30         40         50         60 
MERSGWARQT FLLALLLGAT LRARAAAGYY PRFSPFFFLC THHGELEGDG EQGEVLISLH 

        70         80         90        100        110        120 
IAGNPTYYVP GQEYHVTIST STFFDGLLVT GLYTSTSVQA SQSIGGSSAF GFGIMSDHQF 

       130        140        150        160        170        180 
GNQFMCSVVA SHVSHLPTTN LSFIWIAPPA GTGCVNFMAT ATHRGQVIFK DALAQQLCEQ 

       190        200        210        220        230        240 
GAPTDVTVHP HLAEIHSDSI ILRDDFDSYH QLQLNPNIWV ECNNCETGEQ CGAIMHGNAV 

       250        260        270        280        290        300 
TFCEPYGPRE LITTGLNTTT ASVLQFSIGS GSCRFSYSDP SIIVLYAKNN SADWIQLEKI 

       310        320        330        340        350        360 
RAPSNVSTII HILYLPEDAK GENVQFQWKQ ENLRVGEVYE ACWALDNILI INSAHRQVVL 

       370        380        390        400        410        420 
EDSLDPVDTG NWLFFPGATV KHSCQSDGNS IYFHGNEGSE FNFATTRDVD LSTEDIQEQW 

       430        440        450        460        470        480 
SEEFESQPTG WDVLGAVIGT ECGTIESGLS MVFLKDGERK LCTPSMDTTG YGNLRFYFVM 

       490        500        510        520        530        540 
GGICDPGNSH ENDIILYAKI EGRKEHITLD TLSYSSYKVP SLVSVVINPE LQTPATKFCL 

       550        560        570        580        590        600 
RQKNHQGHNR NVWAVDFFHV LPVLPSTMSH MIQFSINLGC GTHQPGNSVS LEFSTNHGRS 

       610        620        630        640        650        660 
WSLLHTECLP EICAGPHLPH STVYSSENYS GWNRITIPLP NAALTRNTRI RWRQTGPILG 

       670        680        690        700        710        720 
NMWAIDNVYI GPSCLKFCSG RGQCTRHGCK CDPGFSGPAC EMASQTFPMF ISESFGSSRL 

       730        740        750        760        770        780 
SSYHNFYSIR GAEVSFGCGV LASGKALVFN KDGRRQLITS FLDSSQSRFL QFTLRLGSKS 

       790        800        810        820        830        840 
VLSTCRAPDQ PGEGVLLHYS YDNGITWKLL EHYSYLSYHE PRIISVELPG DAKQFGIQFR 

       850        860        870        880        890        900 
WWQPYHSSQR EDVWAIDEII MTSVLFNSIS LDFTNLVEVT QSLGFYLGNV QPYCGHDWTL 

       910        920        930        940        950        960 
CFTGDSKLAS SMRYVETQSM QIGASYMIQF SLVMGCGQKY TPHMDNQVKL EYSTNHGLTW 

       970        980        990       1000       1010       1020 
HLVQEECLPS MPSCQEFTSA SIYHASEFTQ WRRVIVLLPQ KTWSSATRFR WSQSYYTAQD 

      1030       1040       1050       1060       1070       1080 
EWALDSIYIG QQCPNMCSGH GSCDHGICRC DQGYQGTECH PEAALPSTIM SDFENQNGWE 

      1090       1100       1110       1120       1130       1140 
SDWQEVIGGE IVKPEQGCGV ISSGSSLYFS KAGKRQLVSW DLDTSWVDFV QFYIQIGGES 

      1150       1160       1170       1180       1190       1200 
ASCNKPDSRE EGVLLQYSNN GGIQWHLLAE MYFSDFSKPR FVYLELPAAA KTPCTRFRWW 

      1210       1220       1230       1240       1250       1260 
QPVFSGEDYD QWAVDDIIIL SEKQKQIIPV INPTLPQNFY EKPAFDYPMN QMSVWLMLAN 

      1270       1280       1290       1300       1310       1320 
EGMVKNETFC AATPSAMIFG KSDGDRFAVT RDLTLKPGYV LQFKLNIGCA NQFSSTAPVL 

      1330       1340       1350       1360       1370       1380 
LQYSHDAGMS WFLVKEGCYP ASAGKGCEGN SRELSEPTMY HTGDFEEWTR ITIVIPRSLA 

      1390       1400       1410       1420       1430       1440 
SSKTRFRWIQ ESSSQKNVPP FGLDGVYISE PCPSYCSGHG DCISGVCFCD LGYTAAQGTC 

      1450       1460       1470       1480       1490       1500 
VSNVPNHNEM FDRFEGKLSP LWYKITGAQV GTGCGTLNDG KSLYFNGPGK REARTVPLDT 

      1510       1520       1530       1540       1550       1560 
RNIRLVQFYI QIGSKTSGIT CIKPRTRNEG LIVQYSNDNG ILWHLLRELD FMSFLEPQII 

      1570       1580       1590       1600       1610       1620 
SIDLPQDAKT PATAFRWWQP QHGKHSAQWA LDDVLIGMND SSQTGFQDKF DGSIDLQANW 

      1630       1640       1650       1660       1670       1680 
YRIQGGQVDI DCLSMDTALI FTENIGKPRY AETWDFHVSA STFLQFEMSM GCSKPFSNSH 

      1690       1700       1710       1720       1730       1740 
SVQLQYSLNN GKDWHLVTEE CVPPTIGCLH YTESSIYTSE RFQNWKRITV YLPLSTISPR 

      1750       1760       1770       1780       1790       1800 
TRFRWIQANY TVGADSWAID NVVLASGCPW MCSGRGICDA GRCVCDRGFG GPYCVPVVPL 

      1810       1820       1830       1840       1850       1860 
PSILKDDFNG NLHPDLWPEV YGAERGNLNG ETIKSGTSLI FKGEGLRMLI SRDLDCTNTM 

      1870       1880       1890       1900       1910       1920 
YVQFSLRFIA KSTPERSHSI LLQFSISGGI TWHLMDEFYF PQTTNILFIN VPLPYTAQTN 

      1930       1940       1950       1960       1970       1980 
ATRFRLWQPY NNGKKEEIWI VDDFIIDGNN VNNPVMLLDT FDFGPREDNW FFYPGGNIGL 

      1990       2000       2010       2020       2030       2040 
YCPYSSKGAP EEDSAMVFVS NEVGEHSITT RDLNVNENTI IQFEINVGCS TDSSSADPVR 

      2050       2060       2070       2080       2090       2100 
LEFSRDFGAT WHLLLPLCYH SSSHVSSLCS TEHHPSSTYY AGTMQGWRRE VVHFGKLHLC 

      2110       2120       2130       2140       2150       2160 
GSVRFRWYQG FYPAGSQPVT WAIDNVYIGP QCEEMCNGQG SCINGTKCIC DPGYSGPTCK 

      2170       2180       2190       2200       2210       2220 
ISTKNPDFLK DDFEGQLESD RFLLMSGGKP SRKCGILSSG NNLFFNEDGL RMLMTRDLDL 

      2230       2240       2250       2260       2270       2280 
SHARFVQFFM RLGCGKGVPD PRSQPVLLQY SLNGGLSWSL LQEFLFSNSS NVGRYIALEI 

      2290       2300       2310       2320       2330       2340 
PLKARSGSTR LRWWQPSENG HFYSPWVIDQ ILIGGNISGN TVLEDDFTTL DSRKWLLHPG 

      2350       2360       2370       2380       2390       2400 
GTKMPVCGST GDALVFIEKA STRYVVSTDV AVNEDSFLQI DFAASCSVTD SCYAIELEYS 

      2410       2420       2430       2440       2450       2460 
VDLGLSWHPL VRDCLPTNVE CSRYHLQRIL VSDTFNKWTR ITLPLPPYTR SQATRFRWHQ 

      2470       2480       2490       2500       2510       2520 
PAPFDKQQTW AIDNVYIGDG CIDMCSGHGR CIQGNCVCDE QWGGLYCDDP ETSLPTQLKD 

      2530       2540       2550       2560       2570       2580 
NFNRAPSSQN WLTVNGGKLS TVCGAVASGM ALHFSGGCSR LLVTVDLNLT NAEFIQFYFM 

      2590       2600       2610       2620       2630       2640 
YGCLITPNNR NQGVLLEYSV NGGITWNLLM EIFYDQYSKP GFVNILLPPD AKEIATRFRW 

      2650       2660       2670       2680       2690       2700 
WQPRHDGLDQ NDWAIDNVLI SGSADQRTVM LDTFSSAPVP QHERSPADAG PVGRIAFDMF 

      2710       2720       2730       2740       2750       2760 
MEDKTSVNEH WLFHDDCTVE RFCDSPDGVM LCGSHDGREV YAVTHDLTPT EGWIMQFKIS 

      2770       2780       2790       2800       2810       2820 
VGCKVSEKIA QNQIHVQYST DFGVSWNYLV PQCLPADPKC SGSVSQPSVF FPTKGWKRIT 

      2830       2840       2850       2860       2870       2880 
YPLPESLVGN PVRFRFYQKY SDMQWAIDNF YLGPGCLDNC RGHGDCLREQ CICDPGYSGP 

      2890       2900       2910       2920       2930       2940 
NCYLTHTLKT FLKERFDSEE IKPDLWMSLE GGSTCTECGI LAEDTALYFG GSTVRQAVTQ 

      2950       2960       2970       2980       2990       3000 
DLDLRGAKFL QYWGRIGSEN NMTSCHRPIC RKEGVLLDYS TDGGITWTLL HEMDYQKYIS 

      3010       3020       3030       3040       3050       3060 
VRHDYILLPE DALTNTTRLR WWQPFVISNG IVVSGVERAQ WALDNILIGG AEINPSQLVD 

      3070       3080       3090       3100       3110       3120 
TFDDEGTSHE ENWSFYPNAV RTAGFCGNPS FHLYWPNKKK DKTHNALSSR ELIIQPGYMM 

      3130       3140       3150       3160       3170       3180 
QFKIVVGCEA TSCGDLHSVM LEYTKDARSD SWQLVQTQCL PSSSNSIGCS PFQFHEATIY 

      3190       3200       3210       3220       3230       3240 
NSVNSSSWKR ITIQLPDHVS SSATQFRWIQ KGEETEKQSW AIDHVYIGEA CPKLCSGHGY 

      3250       3260       3270       3280       3290       3300 
CTTGAICICD ESFQGDDCSV FSHDLPSYIK DNFESARVTE ANWETIQGGV IGSGCGQLAP 

      3310       3320       3330       3340       3350       3360 
YAHGDSLYFN GCQIRQAATK PLDLTRASKI MFVLQIGSMS QTDSCNSDLS GPHAVDKAVL 

      3370       3380       3390       3400       3410       3420 
LQYSVNNGIT WHVIAQHQPK DFTQAQRVSY NVPLEARMKG VLLRWWQPRH NGTGHDQWAL 

      3430       3440       3450       3460 
DHVEVVLVST RKQNYMMNFS RQHGLRHFYN RRRRSLRRYP 

« Hide

Isoform 2 [UniParc].

Checksum: A67B9EAF1DAE6F69
Show »

FASTA3,458388,201
Isoform 3 [UniParc].

Checksum: E9DF2AE0AC29DB8C
Show »

FASTA3,427384,093

References

« Hide 'large scale' references
[1]"The human reelin gene: isolation, sequencing, and mapping on chromosome 7."
DeSilva U., D'Arcangelo G., Braden V.V., Chen J., Miao G.G., Curran T., Green E.D.
Genome Res. 7:157-164(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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.
[5]"A decrease of reelin expression as a putative vulnerability factor in schizophrenia."
Impagnatiello F., Guidotti A.R., Pesold C., Dwivedi Y., Caruncho H., Pisu M.G., Uzunov D.P., Smalheiser N.R., Davis J.M., Pandey G.N., Pappas G.D., Tueting P., Sharma R.P., Costa E.
Proc. Natl. Acad. Sci. U.S.A. 95:15718-15723(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Autosomal recessive lissencephaly with cerebellar hypoplasia is associated with human RELN mutations."
Hong S.E., Shugart Y.Y., Huang D.T., Shahwan S.A., Grant P.E., Hourihane J.O.B., Martin N.D.T., Walsh C.A.
Nat. Genet. 26:93-96(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LIS2.
[7]Erratum
Hong S.E., Shugart Y.Y., Huang D.T., Shahwan S.A., Grant P.E., Hourihane J.O.B., Martin N.D.T., Walsh C.A.
Nat. Genet. 27:225-225(2001)
[8]"Reelin gene alleles and haplotypes as a factor predisposing to autistic disorder."
Persico A.M., D'Agruma L., Maiorano N., Totaro A., Militerni R., Bravaccio C., Wassink T.H., Schneider C., Melmed R., Trillo S., Montecchi F., Palermo M., Pascucci T., Puglisi-Allegra S., Reichelt K.-L., Conciatori M., Marino R., Quattrocchi C.C. expand/collapse author list , Baldi A., Zelante L., Gasparini P., Keller F.
Mol. Psychiatry 6:150-159(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-305; ASN-1920 AND ASN-3015.
Tissue: Liver.
+Additional computationally mapped references.

Web resources

Wikipedia

Reelin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U79716 mRNA. Translation: AAC51105.1.
AC002067 Genomic DNA. Translation: AAM49151.1.
AC006981 Genomic DNA. No translation available.
AC073208 Genomic DNA. Translation: AAP22355.1.
AC005101 Genomic DNA. Translation: AAP22330.1.
AC000121 Genomic DNA. Translation: AAB46357.2.
AC006316 Genomic DNA. Translation: AAD29127.1.
AC005064 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24410.1.
CH236947 Genomic DNA. Translation: EAL24411.1.
CCDSCCDS34722.1. [P78509-2]
CCDS47680.1. [P78509-1]
RefSeqNP_005036.2. NM_005045.3. [P78509-1]
NP_774959.1. NM_173054.2. [P78509-2]
UniGeneHs.655654.

3D structure databases

ProteinModelPortalP78509.
SMRP78509. Positions 1293-1596, 1955-2661.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111630. 5 interactions.
MINTMINT-155986.
STRING9606.ENSP00000392423.

PTM databases

PhosphoSiteP78509.

Polymorphism databases

DMDM296452988.

Proteomic databases

MaxQBP78509.
PaxDbP78509.
PRIDEP78509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343529; ENSP00000345694; ENSG00000189056. [P78509-2]
ENST00000428762; ENSP00000392423; ENSG00000189056. [P78509-1]
GeneID5649.
KEGGhsa:5649.
UCSCuc010liz.3. human. [P78509-2]
uc022ajq.1. human. [P78509-1]

Organism-specific databases

CTD5649.
GeneCardsGC07M103112.
H-InvDBHIX0033998.
HIX0201200.
HGNCHGNC:9957. RELN.
HPACAB004556.
MIM257320. phenotype.
600514. gene.
neXtProtNX_P78509.
Orphanet89844. Lissencephaly syndrome, Norman-Roberts type.
PharmGKBPA34323.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45680.
HOVERGENHBG023117.
InParanoidP78509.
KOK06249.
OMANWFFYPG.
OrthoDBEOG7P2XR4.
PhylomeDBP78509.
TreeFamTF106479.

Gene expression databases

ArrayExpressP78509.
BgeeP78509.
CleanExHS_RELN.
GenevestigatorP78509.

Family and domain databases

Gene3D2.120.10.10. 2 hits.
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. 17 hits.
PROSITEPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 6 hits.
PS50026. EGF_3. 5 hits.
PS51019. REELIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiReelin.
GenomeRNAi5649.
NextBio21946.
PROP78509.
SOURCESearch...

Entry information

Entry nameRELN_HUMAN
AccessionPrimary (citable) accession number: P78509
Secondary accession number(s): A4D0P9 expand/collapse secondary AC list , A4D0Q0, Q86UJ0, Q86UJ8, Q8NDV0, Q9UDQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM