CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009140
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Reelin 
Protein Synonyms/Alias
  
Gene Name
 Reln 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
2819FFPTKGWKRITYPLPubiquitination[1]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 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). 
Sequence Annotation
 DOMAIN 28 192 Reelin.
 REPEAT 594 605 BNR 1.
 DOMAIN 672 703 EGF-like 1.
 REPEAT 800 811 BNR 2.
 REPEAT 953 964 BNR 3.
 DOMAIN 1031 1062 EGF-like 2.
 REPEAT 1158 1169 BNR 4.
 REPEAT 1324 1335 BNR 5.
 DOMAIN 1410 1443 EGF-like 3.
 REPEAT 1536 1547 BNR 6.
 REPEAT 1687 1698 BNR 7.
 DOMAIN 1766 1797 EGF-like 4.
 REPEAT 1885 1896 BNR 8.
 REPEAT 2044 2055 BNR 9.
 DOMAIN 2130 2162 EGF-like 5.
 REPEAT 2251 2262 BNR 10.
 REPEAT 2400 2411 BNR 11.
 DOMAIN 2479 2510 EGF-like 6.
 REPEAT 2599 2610 BNR 12.
 REPEAT 2779 2790 BNR 13.
 DOMAIN 2854 2885 EGF-like 7.
 REPEAT 2980 2991 BNR 14.
 REPEAT 3144 3156 BNR 15.
 DOMAIN 3229 3261 EGF-like 8.
 REPEAT 3364 3375 BNR 16.
 METAL 2062 2062 Zinc 1 (By similarity).
 METAL 2075 2075 Zinc 1 (By similarity).
 METAL 2180 2180 Zinc 1 (By similarity).
 METAL 2265 2265 Zinc 1 (By similarity).
 METAL 2398 2398 Zinc 2 (By similarity).
 METAL 2400 2400 Zinc 2 (By similarity).
 METAL 2461 2461 Zinc 2 (By similarity).
 MOD_RES 1274 1274 Phosphothreonine (By similarity).
 CARBOHYD 142 142 N-linked (GlcNAc...) (Potential).
 CARBOHYD 259 259 N-linked (GlcNAc...) (Potential).
 CARBOHYD 291 291 N-linked (GlcNAc...) (Potential).
 CARBOHYD 307 307 N-linked (GlcNAc...) (Potential).
 CARBOHYD 630 630 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1268 1268 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1448 1448 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1601 1601 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1751 1751 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1922 1922 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2146 2146 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2270 2270 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2318 2318 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2570 2570 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2963 2963 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3017 3017 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3074 3074 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3186 3186 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3413 3413 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3440 3440 N-linked (GlcNAc...) (Potential).
 DISULFID 42 128 By similarity.
 DISULFID 156 180 By similarity.
 DISULFID 541 582 By similarity.
 DISULFID 610 615 By similarity.
 DISULFID 676 686 By similarity.
 DISULFID 693 702 By similarity.
 DISULFID 896 938 By similarity.
 DISULFID 969 976 By similarity.
 DISULFID 1035 1045 By similarity.
 DISULFID 1052 1061 By similarity.
 DISULFID 1272 1311 By similarity.
 DISULFID 1340 1349 By similarity.
 DISULFID 1634 1674 By similarity.
 DISULFID 1703 1710 By similarity.
 DISULFID 2134 2144 By similarity.
 DISULFID 2138 2150 By similarity.
 DISULFID 2152 2161 By similarity.
 DISULFID 2196 2236 By similarity.
 DISULFID 2349 2388 By similarity.
 DISULFID 2394 2560 By similarity.
 DISULFID 2483 2493 By similarity.
 DISULFID 2487 2498 By similarity.
 DISULFID 2500 2509 By similarity.
 DISULFID 2545 2585 By similarity.
 DISULFID 2795 2802 By similarity.
 DISULFID 2920 2967 By similarity.
 DISULFID 3161 3171 By similarity.
 DISULFID 3233 3243 By similarity.
 DISULFID 3237 3249 By similarity.
 DISULFID 3251 3260 By similarity.
 DISULFID 3297 3347 By similarity.  
Keyword
 Alternative splicing; Calcium; Cell adhesion; Complete proteome; Developmental protein; Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding; Phosphoprotein; Protease; Reference proteome; Repeat; Secreted; Serine protease; Signal; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3462 AA 
Protein Sequence
MERGCWAPRT LVLAVLLLLL ATLRARAATG YYPRFSPFFF LCTHHGELEG DGEQGEVLIS 60
LHIAGNPTYY VPGQEYHVTI STSTFFDGLL VTGLYTSTSI QSSQSIGGSS AFGFGIMSDH 120
QFGNQFMCSV VASHVSHLPT TNLSFVWIAP PAGTGCVNFM ATATHRGQVI FKDALAQQLC 180
EQGAPTEATA YSHLAEIHSD SVILRDDFDS YHQLELNPNI WAECSNCDTG EQCGTIMHGN 240
AVTFCEPYGP RELTTTYLNT TTASVLQFSI GSGSCRFSYS DPSIIVSYAK NNTADWIQLE 300
KIRAPSNVST IIHILYLPED AKGENVQFQW KQDSLHVGEV YEACWALDNI LVINSAHRQV 360
ILEDSLDPVD TGNWLFFPGA TVKHSCQSDG NAIYFHGNEG SQLNFATTRD VDLSTEDIQE 420
QWSEEFESQP TGWDILGAVV GSECGTIESG LSLVFLKDGE RKLCTPYMDT TGYGNLRFYF 480
AMGGTCDPGD SHENDVILYA KIEGKKEHIA LDTLSYSSYK VPTLVSVVIN PELQTPATKF 540
CLRQKNHQGH NQNVWAVDFF HVLPILPSTM SHMIQFSINL GCGTHQPGNS VSLEFSTNHG 600
RSWSLLHTEC LPEICAGPHL PHSTIYSSEN YSGWNRVTIP LPNAALTRDT RIRWRQTGPI 660
LGNMWAIDNV YIGPSCLKFC SGRGQCTRHG CKCDPGFSGP ACEMASQTFP MFISESFGSS 720
RLSSYHNFYS IRGAEVSFGC GVLASGKALV FNKDGRRQLI TSFLDSSQSR FLQFTLRLGS 780
KSVLSTCRAP DQPGEGVLLH YSYDNGITWK LLEHYSYLNY HEPRIISVEL PDDAKQFGIQ 840
FRWWQPYHSS QGEDVWAIDE ILMTSVLFNS ISLDFTNLVE VTQSLGFYLG NIQPYCGHDW 900
TLCFTGDSKL ASSMRYVETQ SMQIGASYMI QFSLVMGCGQ KYTPHMDNQV KLEYSTNHGL 960
TWHLVQDECL PSMPSCQEFT SASIYHASEF TQWRRVTVIL PQKTWSGATR FRWSQSYYTA 1020
QDEWALDDIY IGQQCPNMCS GHGSCDHGVC RCDQGYQGTE CHPEAALPST IMSDFENPSS 1080
WDSDWQEVIG GEVVKPEQGC GVVSSGSSLY FSKAGKRQLV SWDLDTSWVD FVQFYIQIGG 1140
ESAACNKPDS REEGVLLQYS NNGGIQWHLL AEMYFSDFGK PRFVYLELPA AAKTPCTRFR 1200
WWQPVFSGED YDQWAVDDII ILSEKQKQVI PVVNPTLPQN FYEKPAFDYP INQMSVWLML 1260
ANEGMAKNDS FCATTPSAMV FGKSDGDRFA VTRDLTLKPG YVLQFKLNIG CASQFSSTAP 1320
VLLQYSHDAG MSWFLVKEGC FPASAGKGCE GNSRELSEPT VYYTGDFEEW TRVTIAIPRS 1380
LASSKTRFRW IQESSSQKNV PPFGLDGVYI SEPCPSYCSG HGDCISGVCF CDLGYTAAQG 1440
TCVSNIPNHS EMFDRFEGKL SPLWYKISGG QVGTGCGTLS DGRSLYFNGL GKREARTVPL 1500
DTRNIRLVQF YIQIGSKTSG ITCIKPRARN EGLVVQYSND NGILWHLLRE LDFLSFLEPQ 1560
IISIDLPREA KTPATAFRWW QPQHGKHSAQ WALDDVLIGV NDSSQTGFQD KFDGSIDLQA 1620
NWYRIQGGQV DIDCLSMDTA LIFTENIGKP RYAETWDFHV SASSFLQFDM SMGCSKPFSA 1680
THSVQLQYSL NNGKDWHPVT EECVPPTIGC VHYTESSTYT SERFQNWRRV TVYLPLATNS 1740
PRTRFRWIQA NYTMGADAWA IDNVLLASGC PWLCSGRGIC DSGRCVCDRG FGGPFCVPVV 1800
PLPSILKDDF NGNLHPDLWP EVYGAERGNL NGETIKSGTS LIFKGEGLRM LISRDLDCTN 1860
TMYVQFSLRF IAKGTPERSH SILLQSSING GVTWRLMDEF YFPQTTSILF INVPLPYSAQ 1920
TNATRFRLWQ PYNNGKKEEI WIIDDFIIDG DNLNNPVMLL DTFDFGPRED NWFFYPGGNI 1980
GLYCPYSSKG APEEDSAMVF VSNEIGEHSI TTRDLSVNEN TIIQFEINVG CSTDSSSADP 2040
VRLEFSRDFG ATWHLLLPLC YHSSSLVSSL CSTEHHPSST YYAGTTQGWR REVVHFGKLH 2100
LCGSVRFRWY QGFYPAGSQP VTWAIDNVYI GPQCEEMCCG HGSCVNGTKC ICDPGYSGPT 2160
CKISTKNPDF LKDDFEGQLE SDRFLLMSGG KPSRKCGILS SGNNLFFNED GLRMLVTRDL 2220
DLSHARFVQF FMRLGCGKGV PDPRSQPVLL QYSLNGGLSW SLLQEFLFSN SSNVGRYIAL 2280
EMPLKARSGS TRLRWWQPSE NGHFYSPWVI DQILIGGNIS GNTVLEDDFS TLDSRKWLLH 2340
PGGTKMPVCG STGDALVFIE KASTRYVVTT DIAVNEDSFL QIDFAASCSV TDSCYAIELE 2400
YSVDLGLSWH PLVRDCLPTN VECSRYHLQR ILVSDTFNKW TRITLPLPAY TRSQATRFRW 2460
HQPAPFDKQQ TWAIDNVYIG DGCLDMCSGH GRCIQGSCVC DEQWGGLYCD EPETSLPTQL 2520
KDNFNRAPSN QNWLTVNGGK LSTVCGAVAS GLALHFSGGC SRLLVTVDLN LTNAEFIQFY 2580
FMYGCLITPS NRNQGVLLEY SVNGGITWTL LMEIFYDQYS KPGFVNILLP PDAKEIGTRF 2640
RWWQPRHDGL DQNDWAIDNV LISGSADQRT VMLDTFSSAP VPQHERSPAD AGPVGRIAFD 2700
MFMEDKTSVN ENWVFHDDCT VERFCDSPDG VMLCGSHDGR EVYAVTHDLT PTENWIMQFK 2760
ISVGCKVPEK IAQNQIHVQF STDFGVSWSY LVPQCLPADP KCSGTVSQPS VFFPTKGWKR 2820
ITYPLPESLM GNPVRFRFYQ KYSDVQWAID NFYLGPGCLD NCGGHGDCLK EQCICDPGYS 2880
GPHCYLTHTL KTFLKERFDS EEIKPDLWMS LEGGSTCTEC GILAENTALY FGGSTVRQAI 2940
TQDLDLRGAK FLQYWGRIGS ENNMTSCHRP VCRKEGVLLD YSKDGGITWT LLHEMDFQKY 3000
ISVRHDYILL PEGALTNTTR LRWWQPFVIS NGLVVSGVER AQWALDNILI GGAEINPSQL 3060
VDTFDDEGSS HEENWSFYPN AVRTAGFCGN PSFHLYWPNK KKDKTHNALS SRELIIQPGY 3120
MMQFKIVVGC EATSCGDLHS VMLEYTKDAR SDSWQLVQTQ CLPSSSNSIG CSPFQFHEAT 3180
IYNAVNSSSW KRITIQLPDH VSSSATQFRW IQKGEETEKQ SWAIDHVYIG EACPRLCSGH 3240
GYCTTGAVCI CDESFQGDDC SVFSHELPSY IKDNFESARV TEANWETIQG GAIGSGCGQL 3300
APYAHGDSLY FNGCQIRQAA TKPLDLTRAS KIMFVLQIGS TAQTDSCNSD LSGPHTVDKA 3360
VLLQYSVNNG ITWHVIAQHQ PKDFTQAQRV SYNVPLEARM KGVLLRWWQP RHNGTGHDQW 3420
ALDHVEVVLV STRKQNYMMN FSRQHGLRHF YNRRRRSLRR YP 3462 
Gene Ontology
 GO:0030424; C:axon; IDA:RGD.
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0030425; C:dendrite; ISS:UniProtKB.
 GO:0005615; C:extracellular space; ISS:UniProtKB.
 GO:0043204; C:perikaryon; IDA:RGD.
 GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISS:UniProtKB.
 GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
 GO:0007411; P:axon guidance; ISS:UniProtKB.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
 GO:0021800; P:cerebral cortex tangential migration; ISS:UniProtKB.
 GO:0021542; P:dentate gyrus development; IMP:RGD.
 GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
 GO:0021854; P:hypothalamus development; IEP:RGD.
 GO:0007626; P:locomotory behavior; IMP:RGD.
 GO:0007613; P:memory; IEP:RGD.
 GO:0007494; P:midgut development; IEP:RGD.
 GO:0001764; P:neuron migration; IMP:UniProtKB.
 GO:0021769; P:orbitofrontal cortex development; IEP:RGD.
 GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
 GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
 GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0043200; P:response to amino acid stimulus; IEP:RGD.
 GO:0048678; P:response to axon injury; IEP:RGD.
 GO:0051412; P:response to corticosterone stimulus; IEP:RGD.
 GO:0042493; P:response to drug; IEP:RGD.
 GO:0051602; P:response to electrical stimulus; IEP:RGD.
 GO:0045471; P:response to ethanol; IEP:RGD.
 GO:0070542; P:response to fatty acid; IEP:RGD.
 GO:0017085; P:response to insecticide; IEP:RGD.
 GO:0010226; P:response to lithium ion; IEP:RGD.
 GO:0009612; P:response to mechanical stimulus; IEP:RGD.
 GO:0048265; P:response to pain; ISS:UniProtKB.
 GO:0032570; P:response to progesterone stimulus; IEP:RGD.
 GO:0035176; P:social behavior; IEP:RGD.
 GO:0021511; P:spinal cord patterning; ISS:UniProtKB. 
Interpro
 IPR000742; EG-like_dom.
 IPR013032; EGF-like_CS.
 IPR002861; Reeler_dom.
 IPR011040; Sialidases. 
Pfam
 PF12661; hEGF
 PF02014; Reeler 
SMART
 SM00181; EGF 
PROSITE
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS51019; REELIN 
PRINTS