ID A0A6J3HQD7_SAPAP Unreviewed; 3455 AA.
AC A0A6J3HQD7;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Reelin {ECO:0000256|ARBA:ARBA00023900};
GN Name=RELN {ECO:0000313|RefSeq:XP_032132247.1};
OS Sapajus apella (Brown-capped capuchin) (Cebus apella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Sapajus.
OX NCBI_TaxID=9515 {ECO:0000313|Proteomes:UP000504640, ECO:0000313|RefSeq:XP_032132247.1};
RN [1] {ECO:0000313|RefSeq:XP_032132247.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_032132247.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: Extracellular matrix serine protease secreted by pioneer
CC neurons that plays a role in layering of neurons in the cerebral cortex
CC and cerebellum by coordinating cell positioning during
CC neurodevelopment. Regulates microtubule function in neurons and
CC neuronal migration. Binding to the extracellular domains of lipoprotein
CC receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of
CC DAB1 and modulation of TAU phosphorylation. Affects migration of
CC sympathetic preganglionic neurons in the spinal cord, where it seems to
CC act as a barrier to neuronal migration. Enzymatic activity is important
CC for the modulation of cell adhesion. {ECO:0000256|ARBA:ARBA00046064}.
CC -!- SUBUNIT: Oligomer of disulfide-linked homodimers.
CC {ECO:0000256|ARBA:ARBA00044961}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the reelin family.
CC {ECO:0000256|ARBA:ARBA00023773}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_032132247.1; XM_032276356.1.
DR GeneID; 116550355; -.
DR CTD; 5649; -.
DR Proteomes; UP000504640; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0043005; C:neuron projection; IEA:TreeGrafter.
DR GO; GO:0070325; F:lipoprotein particle receptor binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; IEA:InterPro.
DR GO; GO:0001764; P:neuron migration; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd08544; Reeler; 1.
DR CDD; cd10037; Reelin_repeat_1_subrepeat_1; 1.
DR CDD; cd10045; Reelin_repeat_1_subrepeat_2; 1.
DR CDD; cd10038; Reelin_repeat_2_subrepeat_1; 1.
DR CDD; cd10046; Reelin_repeat_2_subrepeat_2; 1.
DR CDD; cd10039; Reelin_repeat_3_subrepeat_1; 1.
DR CDD; cd10047; Reelin_repeat_3_subrepeat_2; 1.
DR CDD; cd10040; Reelin_repeat_4_subrepeat_1; 1.
DR CDD; cd10048; Reelin_repeat_4_subrepeat_2; 1.
DR CDD; cd10041; Reelin_repeat_5_subrepeat_1; 1.
DR CDD; cd10049; Reelin_repeat_5_subrepeat_2; 1.
DR CDD; cd10042; Reelin_repeat_6_subrepeat_1; 1.
DR CDD; cd10050; Reelin_repeat_6_subrepeat_2; 1.
DR CDD; cd10043; Reelin_repeat_7_subrepeat_1; 1.
DR CDD; cd10051; Reelin_repeat_7_subrepeat_2; 1.
DR CDD; cd10044; Reelin_repeat_8_subrepeat_1; 1.
DR CDD; cd10052; Reelin_repeat_8_subrepeat_2; 1.
DR CDD; cd10036; Reelin_subrepeat_Nt; 1.
DR FunFam; 2.60.120.260:FF:000003; Reelin; 4.
DR FunFam; 2.60.120.260:FF:000028; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000030; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000036; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000039; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000040; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000041; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000042; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000044; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000045; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000047; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000052; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000053; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000055; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000056; reelin; 1.
DR FunFam; 2.60.120.260:FF:000057; Reelin; 1.
DR FunFam; 2.60.40.4060:FF:000001; Reelin; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 19.
DR Gene3D; 2.60.40.4060; Reeler domain; 1.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR002861; Reeler_dom.
DR InterPro; IPR042307; Reeler_sf.
DR InterPro; IPR034968; Reelin.
DR InterPro; IPR049419; Reelin_subrepeat-B.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR11841; REELIN; 1.
DR PANTHER; PTHR11841:SF1; REELIN; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF23106; EGF_Teneurin; 2.
DR Pfam; PF21471; Reelin_subrepeat-B; 18.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF50939; Sialidases; 3.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS51019; REELIN; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000504640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..3455
FT /note="Reelin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026939204"
FT DOMAIN 25..190
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 2128..2160
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3227..3259
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 2132..2142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2150..2159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3231..3241
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3249..3258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 3455 AA; 387379 MW; 6640D538F4CE07DB CRC64;
MERSGWAPRT FLLALLLGTT LRARAAAGYY PRFSPFFFLC THHGELEGDG EQGEVLISLH
IAGNPTYYVP GQEYHVTIST STFFDGLLVT GLYTSTSVQA SQTIGGSNAF GFGVMSDHQF
GNQFMCSVVA SHVSHLPTTN LSFVWIAPPA GTGCVNFMAT ATHRGQVIFK DALAQQLCEQ
GAPTEATVHP HLAEIHSDSV ILRDDFDSYH QLQLNPNIWV ECNNCETGEQ CGAIMHGNAV
TFCEPYGPRE LITTGLNTTT ASVLQFSIGS GSCRFSYSDP SIVVLYAKNN SADWIQLEKI
RAPSNVSTII HILYLPEDAK GENVQFQWKQ ESLRVGEVYE ACWALDNILV INSAHRQVIL
EDSLDPVDTG NWLFFPGATV KHSCQSDGNS IYFHGNEGSE FNFATTRDVD LSTEDIQEQW
SEEFESQPTG WEVLGAVIGT ECGTIESGLS MVFLKDGERK LCTPYMDTTG YGNLRFYFVM
GGICDPGNSH ENDIILYAKI EGKKEHIALD TLSYSSYKVP SLVSVVINPE LQTPATKFCL
RQKNHQGHNR NVWAVDFFHV LPVLPSTMSH MIQFSINLGC GTHQPGNSVS LEFSTNHGRS
WSLLHTECLP EICAGPHLPH STVYSSENYS GWNRITIPLP NAALTRNTRI RWRQTGPILG
NMWAIDNVYI GPSCLKFCSG RGQCTRHGCK CDPGFSGPAC EMASQTFPMF ISESFGSSRL
SSYHNFYSIR GAEVSFGCGV LASGKALVFH KDGRRQLITS FLDSSQSRFL QFTLRLGSKS
VLSTCRAPDQ PGEGVLLHYS YDNGITWKLL EHYSYLSYHE PRIISVELPD DARQFGIQFR
WWQPYHSSQG EDVWAIDEII MTSVLFNSIS LDFTNLVEVT QSLGFYLGNV QPYCGHDWTL
CFTGDSKIAS SMRYVETQSM QIGASYMIQF SLVMGCGQKY TPHMDNQVKL EYSTNHGLTW
HLVQEECLPS MPSCQEFTSA SIYHASEFTQ WRRVIVLLPQ KTWSGATRFR WSQSYYTAQD
EWALDSIYIG QQCPNMCSGH GSCDHGMCRC DQGYQGTECH PEAALPSTIM SDFENQNGWE
SDWQEVIGGE IVKPEQGCGV ISSGSSLYFS KAGKRQLVSW DLDTSWVDFV QFYIQIGGES
ASCNKPDSRE EGVLLQYSNN GGIQWHLLAE MYFSDFSKPR FVYLELPAAA KTPCTRFRWW
QPVFSGEDYD QWAVDDIIIL SEKQKQIIPV INPTLPQNFY EKPAFDYPMN QMSVWLMLAN
EGMLKNETFC AATPSAMIFG RSDGDRFAVT RDLTLKPGYV LQFKLNIGCA SQFSNTAPVL
LQYSHDAGMS WFLVKEGCFP ASTGKGCEGN SRELSEPTMY HTGDFEEWTR ITIVIPRSLA
SSKTRFRWIQ ESSSQKNVPP FGLDGVYISE PCPSYCSGHG DCISGVCFCD LGYTAAQGTC
VSNVPNHNEM FDRFEGKLSP LWYKITGGQV GTGCGTLNDG KSLYFNGPGK REARTVPLDT
RNIRLVQFYI QIGSKTSGIT CIKPRARNEG LIVQYSNDNG ILWHLLRELD FMSFLDPQII
SIDLPQEAKT PATAFRWWQP QHGKHSAQWA LDDVLIGMND SSQTGFQDKF DGSLDLQANW
YRIQGGQVDI DCLSMDTALI FTENIGKPRY AETWDFHVSA STFLQFEMSM GCSKPFSNSH
SVQLQYSLNN GKDWHLVTEE CVPPTIGCLH YTESSIYTSE RFQNWKRITV YLPLSTISPR
TRFRWIQANY TVGADSWAID NVILASGCPW MCSGRGICDA GRCVCDRGFG GPYCVPVVPL
PSILKDDFNG NLHPDLWPEV YGAERGNLNG ETIKSGTSLI FKGEGLRMLI SRDLDCTNTM
YVQFSLRFIA KGTPERSHSI LLQFSINGGI TWHLMDEFYF PQTTNILFIN VPLPYTAQTN
ATRFRLWQPY NNGKKEEIWI VDDFIIDGNN LNNPVMLLDT FDFGPKEDNW FFYPGGNIGL
YCPYSSKGAP EEDSAMVFVS NEVGEHSIIT RDLNVNENTI IQFEINVGCS TDSSSADPVR
LEFSRDFGAT WHLLLPLCYH SSSHVSSLCS TEHHPSSTYY AGTMQGWRRE VVHFGKLHLC
GSVRFRWYQG FYPAGSQPVT WAIDNVYIGP QCEEMCNGQG SCVNGTKCIC DPGYSGPTCK
ISTKNPDFLK DDFEGQLESD RFLLMSGGKP SRKCGILSSG NNLFFNEDGL RMLMTRDLDL
SHARFVQFFM RLGCGKGVPD PRSQPVLLQY SLNGGLSWSL LQEFLFSNSS NVGRYIALEI
PLKARSGSTR LRWWQPSENG HFYSPWVIDQ ILIGGNISGN TVLEDDFTTL DSRKWLLHPG
GTKMPVCGST GDALVFIEKA STRYVVSTDI AVNEDSFLQI DFAASCSVTD SCYAIELEYS
VDLGLSWHPL VRDCLPTNVE CSRYHLQRIL VSDTFNKWTR ITLPLPPYTR SQATRFRWHQ
PAPFDKQQTW AIDNVYIGDG CIDMCSGHGR CIQGNCVCDE QWGGLYCDDP ETSLPTQLKD
NFNRSPSNQN WLTVNGGKLS TVCGAVASGM ALHFSGGCSR LLVTVDLNLT NAEFIQFYFM
YGCLITPNNR NQGVLLEYSV NGGITWNLLM EIFYDQYSKP GFVNILLPPD AKEIATRFRW
WQPRHDGLDQ NDWAIDNVLI SGSADQRTVM LDTFSSAPVP QHERSPADAG PVGRIAFDMF
MEDKTSVNEH WLFHDDCTVE RFCDSPDGVM LCGSHDGREV YAVTHDLTPT EGWIMQFKIS
VGCKVSEKIA QNQIHVQYST DFGVSWNYLV PQCLPADPKC SGSVSQPSVF FPTKGWKRIT
YPLPESLVGN PVRFRFYQKY SDMQWAIDNF YLGPGCLDNC RGHGDCLREQ CICDPGYSGP
NCYLTHTLKT FLKERFDSEE IKPDLWMSLE GGSTCTECGI LAENTALYFG GSTVRQAITQ
DLDLRGAKFL QYWGRIGSEN NMTSCHRPIC RKEGVLLDYS TDGGITWTLL HEMDYQKYIS
VRHDYILLPE DALTNTTRLR WWQPFVISNG IVVSGVERAQ WALDNILIGG AEINPSQLVD
TFDDEGTSHE ENWSFYPNAV RTAGFCGNPS FHLYWPNKKK DKTHNALSSR ELIIQPGYMM
QFKIVVGCEA TSCGDLHSVM LEYTKDARSD SWQLVQTQCL PSSSNSIGCS PFQFHEATIY
NSVNSSSWKR ITIQLPDHVS SSATQFRWIQ KGEETEKQSW AIDHVYIGEA CPKLCSGHGY
CTTGAICICD ESFQGDDCSV FSHDLPTYIK DNFESARVTE ANWETIQGGV IGSGCGQLAP
YAHGDSLYFN GCQIRQAATK PLDLTRASKI MFVLQIGSMS QTDSCNSDLS GPHAVDKAVL
LQYSVNNGIT WHVIAQHQPK DFTQAQRVSY NVPLEARMKG VLLRWWQPRH NGTGHDQWAL
DHVEVVLSCR TGMLMSRRVR TDGSKWLARR GESSR
//
