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
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi2062Zinc 1By similarity1
Metal bindingi2075Zinc 1By similarity1
Metal bindingi2180Zinc 1By similarity1
Metal bindingi2265Zinc 1By similarity1
Metal bindingi2398Zinc 2By similarity1
Metal bindingi2400Zinc 2By similarity1
Metal bindingi2461Zinc 2By similarity1

GO - Molecular functioni

GO - Biological processi

  • axon guidance Source: UniProtKB
  • brain development Source: UniProtKB
  • cell adhesion Source: UniProtKB-KW
  • cell morphogenesis involved in differentiation Source: UniProtKB
  • cellular response to dexamethasone stimulus Source: RGD
  • central nervous system development Source: UniProtKB
  • cerebral cortex development Source: RGD
  • cerebral cortex tangential migration Source: UniProtKB
  • dentate gyrus development Source: RGD
  • glial cell differentiation Source: UniProtKB
  • hypothalamus development Source: RGD
  • locomotory behavior Source: RGD
  • memory Source: RGD
  • midgut development Source: RGD
  • neuron migration Source: UniProtKB
  • orbitofrontal cortex development Source: RGD
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of small GTPase mediated signal transduction Source: UniProtKB
  • response to amino acid Source: RGD
  • response to axon injury Source: RGD
  • response to corticosterone Source: RGD
  • response to drug Source: RGD
  • response to electrical stimulus Source: RGD
  • response to ethanol Source: RGD
  • response to fatty acid Source: RGD
  • response to hormone Source: RGD
  • response to insecticide Source: RGD
  • response to lithium ion Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to pain Source: UniProtKB
  • response to progesterone Source: RGD
  • response to toxic substance Source: RGD
  • social behavior Source: RGD
  • spinal cord patterning Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Serine protease

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Reelin (EC:3.4.21.-)
Gene namesi
Name:Reln
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3553. Reln.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • cytoplasm Source: UniProtKB
  • dendrite Source: UniProtKB
  • extracellular space Source: UniProtKB
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • perikaryon Source: RGD
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in Reln are the cause of the creeping phenotype, which is characterized by tremor, gait ataxia, cerebellar hypoplasia and abnormal neuronal migration (particularly in the cerebral cortex and hippocampus). The mutation is due to a nucleotide insertion at codon 1892 which results in a translational frameshift and truncation of the protein.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000003030628 – 3462ReelinAdd BLAST3435

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi42 ↔ 128PROSITE-ProRule annotation
Glycosylationi142N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi156 ↔ 180PROSITE-ProRule annotation
Glycosylationi259N-linked (GlcNAc...)Sequence analysis1
Glycosylationi291N-linked (GlcNAc...)Sequence analysis1
Glycosylationi307N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi541 ↔ 582PROSITE-ProRule annotation
Disulfide bondi610 ↔ 615PROSITE-ProRule annotation
Glycosylationi630N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi676 ↔ 686PROSITE-ProRule annotation
Disulfide bondi693 ↔ 702PROSITE-ProRule annotation
Disulfide bondi896 ↔ 938PROSITE-ProRule annotation
Disulfide bondi969 ↔ 976PROSITE-ProRule annotation
Disulfide bondi1035 ↔ 1045PROSITE-ProRule annotation
Disulfide bondi1052 ↔ 1061PROSITE-ProRule annotation
Glycosylationi1268N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1272 ↔ 1311PROSITE-ProRule annotation
Disulfide bondi1340 ↔ 1349PROSITE-ProRule annotation
Glycosylationi1448N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1601N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1634 ↔ 1674PROSITE-ProRule annotation
Disulfide bondi1703 ↔ 1710PROSITE-ProRule annotation
Glycosylationi1751N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1922N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2102InterchainPROSITE-ProRule annotation
Disulfide bondi2134 ↔ 2144PROSITE-ProRule annotation
Disulfide bondi2138 ↔ 2150PROSITE-ProRule annotation
Glycosylationi2146N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2152 ↔ 2161PROSITE-ProRule annotation
Disulfide bondi2196 ↔ 2236PROSITE-ProRule annotation
Glycosylationi2270N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2318N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2349 ↔ 2388PROSITE-ProRule annotation
Disulfide bondi2394 ↔ 2560PROSITE-ProRule annotation
Disulfide bondi2483 ↔ 2493PROSITE-ProRule annotation
Disulfide bondi2487 ↔ 2498PROSITE-ProRule annotation
Disulfide bondi2500 ↔ 2509PROSITE-ProRule annotation
Disulfide bondi2545 ↔ 2585PROSITE-ProRule annotation
Glycosylationi2570N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2795 ↔ 2802PROSITE-ProRule annotation
Disulfide bondi2920 ↔ 2967PROSITE-ProRule annotation
Glycosylationi2963N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3017N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3074N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3161 ↔ 3171PROSITE-ProRule annotation
Glycosylationi3186N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3233 ↔ 3243PROSITE-ProRule annotation
Disulfide bondi3237 ↔ 3249PROSITE-ProRule annotation
Disulfide bondi3251 ↔ 3260PROSITE-ProRule annotation
Disulfide bondi3297 ↔ 3347PROSITE-ProRule annotation
Glycosylationi3413N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3440N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP58751.
PRIDEiP58751.

PTM databases

iPTMnetiP58751.
PhosphoSitePlusiP58751.

Expressioni

Tissue specificityi

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.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi246846. 1 interactor.
STRINGi10116.ENSRNOP00000058574.

Structurei

3D structure databases

ProteinModelPortaliP58751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 192ReelinPROSITE-ProRule annotationAdd BLAST165
Repeati594 – 605BNR 1Add BLAST12
Domaini672 – 703EGF-like 1PROSITE-ProRule annotationAdd BLAST32
Repeati800 – 811BNR 2Add BLAST12
Repeati953 – 964BNR 3Add BLAST12
Domaini1031 – 1062EGF-like 2PROSITE-ProRule annotationAdd BLAST32
Repeati1158 – 1169BNR 4Add BLAST12
Repeati1324 – 1335BNR 5Add BLAST12
Domaini1410 – 1443EGF-like 3PROSITE-ProRule annotationAdd BLAST34
Repeati1536 – 1547BNR 6Add BLAST12
Repeati1687 – 1698BNR 7Add BLAST12
Domaini1766 – 1797EGF-like 4PROSITE-ProRule annotationAdd BLAST32
Repeati1885 – 1896BNR 8Add BLAST12
Repeati2044 – 2055BNR 9Add BLAST12
Domaini2130 – 2162EGF-like 5PROSITE-ProRule annotationAdd BLAST33
Repeati2251 – 2262BNR 10Add BLAST12
Repeati2400 – 2411BNR 11Add BLAST12
Domaini2479 – 2510EGF-like 6PROSITE-ProRule annotationAdd BLAST32
Repeati2599 – 2610BNR 12Add BLAST12
Repeati2779 – 2790BNR 13Add BLAST12
Domaini2854 – 2885EGF-like 7PROSITE-ProRule annotationAdd BLAST32
Repeati2980 – 2991BNR 14Add BLAST12
Repeati3144 – 3156BNR 15Add BLAST13
Domaini3229 – 3261EGF-like 8PROSITE-ProRule annotationAdd BLAST33
Repeati3364 – 3375BNR 16Add BLAST12

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi3433 – 3462Arg-rich (basic)Add BLAST30

Domaini

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

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.
HOGENOMiHOG000252908.
HOVERGENiHBG023117.
InParanoidiP58751.
KOiK06249.
PhylomeDBiP58751.

Family and domain databases

CDDicd08544. Reeler. 1 hit.
Gene3Di2.120.10.10. 3 hits.
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. 15 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: P58751-1) [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
MERGCWAPRT LVLAVLLLLL ATLRARAATG YYPRFSPFFF LCTHHGELEG
60 70 80 90 100
DGEQGEVLIS LHIAGNPTYY VPGQEYHVTI STSTFFDGLL VTGLYTSTSI
110 120 130 140 150
QSSQSIGGSS AFGFGIMSDH QFGNQFMCSV VASHVSHLPT TNLSFVWIAP
160 170 180 190 200
PAGTGCVNFM ATATHRGQVI FKDALAQQLC EQGAPTEATA YSHLAEIHSD
210 220 230 240 250
SVILRDDFDS YHQLELNPNI WAECSNCDTG EQCGTIMHGN AVTFCEPYGP
260 270 280 290 300
RELTTTYLNT TTASVLQFSI GSGSCRFSYS DPSIIVSYAK NNTADWIQLE
310 320 330 340 350
KIRAPSNVST IIHILYLPED AKGENVQFQW KQDSLHVGEV YEACWALDNI
360 370 380 390 400
LVINSAHRQV ILEDSLDPVD TGNWLFFPGA TVKHSCQSDG NAIYFHGNEG
410 420 430 440 450
SQLNFATTRD VDLSTEDIQE QWSEEFESQP TGWDILGAVV GSECGTIESG
460 470 480 490 500
LSLVFLKDGE RKLCTPYMDT TGYGNLRFYF AMGGTCDPGD SHENDVILYA
510 520 530 540 550
KIEGKKEHIA LDTLSYSSYK VPTLVSVVIN PELQTPATKF CLRQKNHQGH
560 570 580 590 600
NQNVWAVDFF HVLPILPSTM SHMIQFSINL GCGTHQPGNS VSLEFSTNHG
610 620 630 640 650
RSWSLLHTEC LPEICAGPHL PHSTIYSSEN YSGWNRVTIP LPNAALTRDT
660 670 680 690 700
RIRWRQTGPI LGNMWAIDNV YIGPSCLKFC SGRGQCTRHG CKCDPGFSGP
710 720 730 740 750
ACEMASQTFP MFISESFGSS RLSSYHNFYS IRGAEVSFGC GVLASGKALV
760 770 780 790 800
FNKDGRRQLI TSFLDSSQSR FLQFTLRLGS KSVLSTCRAP DQPGEGVLLH
810 820 830 840 850
YSYDNGITWK LLEHYSYLNY HEPRIISVEL PDDAKQFGIQ FRWWQPYHSS
860 870 880 890 900
QGEDVWAIDE ILMTSVLFNS ISLDFTNLVE VTQSLGFYLG NIQPYCGHDW
910 920 930 940 950
TLCFTGDSKL ASSMRYVETQ SMQIGASYMI QFSLVMGCGQ KYTPHMDNQV
960 970 980 990 1000
KLEYSTNHGL TWHLVQDECL PSMPSCQEFT SASIYHASEF TQWRRVTVIL
1010 1020 1030 1040 1050
PQKTWSGATR FRWSQSYYTA QDEWALDDIY IGQQCPNMCS GHGSCDHGVC
1060 1070 1080 1090 1100
RCDQGYQGTE CHPEAALPST IMSDFENPSS WDSDWQEVIG GEVVKPEQGC
1110 1120 1130 1140 1150
GVVSSGSSLY FSKAGKRQLV SWDLDTSWVD FVQFYIQIGG ESAACNKPDS
1160 1170 1180 1190 1200
REEGVLLQYS NNGGIQWHLL AEMYFSDFGK PRFVYLELPA AAKTPCTRFR
1210 1220 1230 1240 1250
WWQPVFSGED YDQWAVDDII ILSEKQKQVI PVVNPTLPQN FYEKPAFDYP
1260 1270 1280 1290 1300
INQMSVWLML ANEGMAKNDS FCATTPSAMV FGKSDGDRFA VTRDLTLKPG
1310 1320 1330 1340 1350
YVLQFKLNIG CASQFSSTAP VLLQYSHDAG MSWFLVKEGC FPASAGKGCE
1360 1370 1380 1390 1400
GNSRELSEPT VYYTGDFEEW TRVTIAIPRS LASSKTRFRW IQESSSQKNV
1410 1420 1430 1440 1450
PPFGLDGVYI SEPCPSYCSG HGDCISGVCF CDLGYTAAQG TCVSNIPNHS
1460 1470 1480 1490 1500
EMFDRFEGKL SPLWYKISGG QVGTGCGTLS DGRSLYFNGL GKREARTVPL
1510 1520 1530 1540 1550
DTRNIRLVQF YIQIGSKTSG ITCIKPRARN EGLVVQYSND NGILWHLLRE
1560 1570 1580 1590 1600
LDFLSFLEPQ IISIDLPREA KTPATAFRWW QPQHGKHSAQ WALDDVLIGV
1610 1620 1630 1640 1650
NDSSQTGFQD KFDGSIDLQA NWYRIQGGQV DIDCLSMDTA LIFTENIGKP
1660 1670 1680 1690 1700
RYAETWDFHV SASSFLQFDM SMGCSKPFSA THSVQLQYSL NNGKDWHPVT
1710 1720 1730 1740 1750
EECVPPTIGC VHYTESSTYT SERFQNWRRV TVYLPLATNS PRTRFRWIQA
1760 1770 1780 1790 1800
NYTMGADAWA IDNVLLASGC PWLCSGRGIC DSGRCVCDRG FGGPFCVPVV
1810 1820 1830 1840 1850
PLPSILKDDF NGNLHPDLWP EVYGAERGNL NGETIKSGTS LIFKGEGLRM
1860 1870 1880 1890 1900
LISRDLDCTN TMYVQFSLRF IAKGTPERSH SILLQSSING GVTWRLMDEF
1910 1920 1930 1940 1950
YFPQTTSILF INVPLPYSAQ TNATRFRLWQ PYNNGKKEEI WIIDDFIIDG
1960 1970 1980 1990 2000
DNLNNPVMLL DTFDFGPRED NWFFYPGGNI GLYCPYSSKG APEEDSAMVF
2010 2020 2030 2040 2050
VSNEIGEHSI TTRDLSVNEN TIIQFEINVG CSTDSSSADP VRLEFSRDFG
2060 2070 2080 2090 2100
ATWHLLLPLC YHSSSLVSSL CSTEHHPSST YYAGTTQGWR REVVHFGKLH
2110 2120 2130 2140 2150
LCGSVRFRWY QGFYPAGSQP VTWAIDNVYI GPQCEEMCCG HGSCVNGTKC
2160 2170 2180 2190 2200
ICDPGYSGPT CKISTKNPDF LKDDFEGQLE SDRFLLMSGG KPSRKCGILS
2210 2220 2230 2240 2250
SGNNLFFNED GLRMLVTRDL DLSHARFVQF FMRLGCGKGV PDPRSQPVLL
2260 2270 2280 2290 2300
QYSLNGGLSW SLLQEFLFSN SSNVGRYIAL EMPLKARSGS TRLRWWQPSE
2310 2320 2330 2340 2350
NGHFYSPWVI DQILIGGNIS GNTVLEDDFS TLDSRKWLLH PGGTKMPVCG
2360 2370 2380 2390 2400
STGDALVFIE KASTRYVVTT DIAVNEDSFL QIDFAASCSV TDSCYAIELE
2410 2420 2430 2440 2450
YSVDLGLSWH PLVRDCLPTN VECSRYHLQR ILVSDTFNKW TRITLPLPAY
2460 2470 2480 2490 2500
TRSQATRFRW HQPAPFDKQQ TWAIDNVYIG DGCLDMCSGH GRCIQGSCVC
2510 2520 2530 2540 2550
DEQWGGLYCD EPETSLPTQL KDNFNRAPSN QNWLTVNGGK LSTVCGAVAS
2560 2570 2580 2590 2600
GLALHFSGGC SRLLVTVDLN LTNAEFIQFY FMYGCLITPS NRNQGVLLEY
2610 2620 2630 2640 2650
SVNGGITWTL LMEIFYDQYS KPGFVNILLP PDAKEIGTRF RWWQPRHDGL
2660 2670 2680 2690 2700
DQNDWAIDNV LISGSADQRT VMLDTFSSAP VPQHERSPAD AGPVGRIAFD
2710 2720 2730 2740 2750
MFMEDKTSVN ENWVFHDDCT VERFCDSPDG VMLCGSHDGR EVYAVTHDLT
2760 2770 2780 2790 2800
PTENWIMQFK ISVGCKVPEK IAQNQIHVQF STDFGVSWSY LVPQCLPADP
2810 2820 2830 2840 2850
KCSGTVSQPS VFFPTKGWKR ITYPLPESLM GNPVRFRFYQ KYSDVQWAID
2860 2870 2880 2890 2900
NFYLGPGCLD NCGGHGDCLK EQCICDPGYS GPHCYLTHTL KTFLKERFDS
2910 2920 2930 2940 2950
EEIKPDLWMS LEGGSTCTEC GILAENTALY FGGSTVRQAI TQDLDLRGAK
2960 2970 2980 2990 3000
FLQYWGRIGS ENNMTSCHRP VCRKEGVLLD YSKDGGITWT LLHEMDFQKY
3010 3020 3030 3040 3050
ISVRHDYILL PEGALTNTTR LRWWQPFVIS NGLVVSGVER AQWALDNILI
3060 3070 3080 3090 3100
GGAEINPSQL VDTFDDEGSS HEENWSFYPN AVRTAGFCGN PSFHLYWPNK
3110 3120 3130 3140 3150
KKDKTHNALS SRELIIQPGY MMQFKIVVGC EATSCGDLHS VMLEYTKDAR
3160 3170 3180 3190 3200
SDSWQLVQTQ CLPSSSNSIG CSPFQFHEAT IYNAVNSSSW KRITIQLPDH
3210 3220 3230 3240 3250
VSSSATQFRW IQKGEETEKQ SWAIDHVYIG EACPRLCSGH GYCTTGAVCI
3260 3270 3280 3290 3300
CDESFQGDDC SVFSHELPSY IKDNFESARV TEANWETIQG GAIGSGCGQL
3310 3320 3330 3340 3350
APYAHGDSLY FNGCQIRQAA TKPLDLTRAS KIMFVLQIGS TAQTDSCNSD
3360 3370 3380 3390 3400
LSGPHTVDKA VLLQYSVNNG ITWHVIAQHQ PKDFTQAQRV SYNVPLEARM
3410 3420 3430 3440 3450
KGVLLRWWQP RHNGTGHDQW ALDHVEVVLV STRKQNYMMN FSRQHGLRHF
3460
YNRRRRSLRR YP
Length:3,462
Mass (Da):387,531
Last modified:March 27, 2002 - v1
Checksum:iFCCF89B090E035F6
GO
Isoform 2 (identifier: P58751-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3430-3431: Missing.

Show »
Length:3,460
Mass (Da):387,345
Checksum:i610A71EBC643226D
GO
Isoform 3 (identifier: P58751-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3430-3462: Missing.

Show »
Length:3,429
Mass (Da):383,236
Checksum:i22F3FFBBDF2E088B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti336H → R in BAC75467 (PubMed:12670697).Curated1
Sequence conflicti2714V → L in BAC75467 (PubMed:12670697).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0055803430 – 3462Missing in isoform 3. CuratedAdd BLAST33
Alternative sequenceiVSP_0055793430 – 3431Missing in isoform 2. Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049473 mRNA. Translation: BAB78470.1.
AB062680 mRNA. Translation: BAC75467.1.
RefSeqiNP_536319.2. NM_080394.2.
UniGeneiRn.98353.

Genome annotation databases

GeneIDi24718.
KEGGirno:24718.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049473 mRNA. Translation: BAB78470.1.
AB062680 mRNA. Translation: BAC75467.1.
RefSeqiNP_536319.2. NM_080394.2.
UniGeneiRn.98353.

3D structure databases

ProteinModelPortaliP58751.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246846. 1 interactor.
STRINGi10116.ENSRNOP00000058574.

PTM databases

iPTMnetiP58751.
PhosphoSitePlusiP58751.

Proteomic databases

PaxDbiP58751.
PRIDEiP58751.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24718.
KEGGirno:24718.

Organism-specific databases

CTDi5649.
RGDi3553. Reln.

Phylogenomic databases

eggNOGiENOG410IEXI. Eukaryota.
ENOG410XQKB. LUCA.
HOGENOMiHOG000252908.
HOVERGENiHBG023117.
InParanoidiP58751.
KOiK06249.
PhylomeDBiP58751.

Miscellaneous databases

PROiP58751.

Family and domain databases

CDDicd08544. Reeler. 1 hit.
Gene3Di2.120.10.10. 3 hits.
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. 15 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_RAT
AccessioniPrimary (citable) accession number: P58751
Secondary accession number(s): Q80T65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: November 2, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.