ID A0A452EUK3_CAPHI Unreviewed; 3469 AA.
AC A0A452EUK3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Reelin {ECO:0000256|ARBA:ARBA00023900};
GN Name=RELN {ECO:0000313|Ensembl:ENSCHIP00000015693.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000015693.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000015693.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000015693.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Extracellular matrix serine protease that plays a role in
CC layering of neurons in the cerebral cortex and cerebellum. Regulates
CC microtubule function in neurons and neuronal migration. Affects
CC migration of sympathetic preganglionic neurons in the spinal cord,
CC where it seems to act as a barrier to neuronal migration. Enzymatic
CC activity is important for the modulation of cell adhesion. Binding to
CC the extracellular domains of lipoprotein receptors VLDLR and
CC LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of
CC TAU phosphorylation. {ECO:0000256|ARBA:ARBA00024808}.
CC -!- SUBUNIT: Oligomer of disulfide-linked homodimers. Binds to the
CC ectodomains of VLDLR and LRP8/APOER2. {ECO:0000256|ARBA:ARBA00025845}.
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 EMBL; LWLT01000003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9925.ENSCHIP00000015693; -.
DR Ensembl; ENSCHIT00000023496.1; ENSCHIP00000015693.1; ENSCHIG00000016204.1.
DR GeneTree; ENSGT00580000081623; -.
DR Proteomes; UP000291000; Chromosome 4.
DR Bgee; ENSCHIG00000016204; Expressed in cerebellum and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0110157; C:reelin complex; IEA:Ensembl.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; IEA:Ensembl.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0021800; P:cerebral cortex tangential migration; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0010001; P:glial cell differentiation; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:1904936; P:interneuron migration; IEA:Ensembl.
DR GO; GO:0097477; P:lateral motor column neuron migration; IEA:Ensembl.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; IEA:Ensembl.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:1902078; P:positive regulation of lateral motor column neuron migration; IEA:Ensembl.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0090129; P:positive regulation of synapse maturation; IEA:Ensembl.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IEA:Ensembl.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; IEA:Ensembl.
DR GO; GO:0035418; P:protein localization to synapse; IEA:Ensembl.
DR GO; GO:0097120; P:receptor localization to synapse; IEA:Ensembl.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0050795; P:regulation of behavior; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0048265; P:response to pain; IEA:Ensembl.
DR GO; GO:0021511; P:spinal cord patterning; IEA:Ensembl.
DR GO; GO:0021517; P:ventral spinal cord development; IEA:Ensembl.
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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 19.
DR Gene3D; 2.60.40.4060; Reeler domain; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR041161; EGF_Tenascin.
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; PF18720; EGF_Tenascin; 1.
DR Pfam; PF21471; Reelin_subrepeat-B; 18.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF50939; Sialidases; 4.
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}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW 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 Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..3469
FT /note="Reelin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019467083"
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 3469 AA; 388876 MW; 8A314D812A02DEC9 CRC64;
MERSSWAPRT FLLALLLGAT LRARAAVGYY PRFSPFFFLC THHGELEGDG EQGEVLISLH
IAGHPTYYVP GQEYHVTIST STFFDGLLVT GLYTSTSVQA SQSIGGSNAF GFGIMSDHQF
GNQFMCSVVA SHVSHLPTTN LSFVWIAPPA GTGCVNFMAT ATHRGQIIFK DALAQQLCEQ
GAPTEATVHP HLAEIHSNSI ILRDDFDSYH QKELNPNIWV ECNNCETGEQ CGAIMHGNAV
TFCEPYGPRE LITTGLNTTT ASVLQFSIGS GSCRYSYSDP CIIVSYAKNN TADWIQLEKI
RAPSNVSTII HILYLPEDAK GENVQFQWKQ ENLRVGEVYE ACWALDNILI INSAHRQVVL
EDNLDPVDTG NWLFFPGATV KHSCQSDGNS IYFHGNEGSE FNFATTRDVD LSTEDIQEQW
SEEFESQPTG WDIVGAVIGT ECGTIESGLS MVFLKDGERK ICTPYLDTTG YGNLRFYFVM
GGICDPGASH ENDVALYAKT EGRKEHITLD TLSYSSYKVP SLVSVVINPD LQTPATKFCL
RQKNHQGRNR NVWAVDFFHV LPVLPSTMSH MIQFSINLGC GTQQPGNSIS LEFSTNHGRS
WSLLHTECLP EICAGPHLPH STIYSSENYS GWNRITIPLP NAALTRDTRI RWRQTGPILG
NMWAIDNVYI GPSCLKFCSG RGQCTRHGCK CDPGFSGPAC EMASQTFPMF ISESFGSSRL
SSYHNFYSIR GAEVSFGCGV LASGKALVFN KDGRRQLITS FLDSSQSRFL QFTLRLGSKS
VLSTCKAPDQ PGEGVLLHYS YDNGITWKLL EHYSYLNYHE PRIISVELPD DARQFGIQFR
WWQPYHSSQG EDVWAIDEII MTSVLFNSIS LDFSNLVEVT QSLGFYLGNV QPYCGHDWTL
CFTGDSKLAS SMRYVETQSM QIGASYMIQF SLVMGCGQKY TPHMDNQVKL EYSTNHGLTW
HLVQEECLPS MPSCQEFTSA SIYHASEFTQ WRRVIVLLPQ KTWSSATRFR WSQSYYTAQD
EWALDSIYIG QQCPNMCSGH GSCSRGMCRC DQGYQGTECH PEAALPSTIM SDFENPSAWE
SDWQEVIGGQ IVKPEEGCGV VSSGSSLYFS KAGKRQLVSW DLDTSWVDFV QFYIQIGGES
SACNKPDSRE EGVLLQYSNN GGIQWHLLAE MYFSDFSKPR FVYLELPAAA KTPCTRFRWW
QPVFSGEDYD QWAVDDIIIL SEKQKQIIPV VNPTLPQNFY EKPAFDYPMN QMSVWLMLAN
EGMVKNETFC SATPSAMVFG KSDGDRFAVT RDLTLKPGYV LQFKLNIGCA NQFSSAAPVL
LQYSHDAGMS WFLVKEGCYP ASAGKGCEGN SRELSEPTMY HTGDFEEWTR ITIVIPRSLA
SSKTRFRWIQ ESSSQKNVPP FGLDGVYISE PCPSYCSGHG DCVSGVCFCD LGYTAAQGTC
VSIVPNHSEM FDRFEGKLSP LWYKITGGQV GTGCGTLNDG KSLYFSGPGK REARTVPLDT
RNIRLVQFYI QIGSKTSGIT CIKPRARNEG LVVQYSNDNG ILWHLLRELD FMSFLEPQII
SIDLPREAKT PATAFRWWQP QHGKHSAQWA LDDVLIGMND SSQTGFQDKF DGSLDLQANW
YRIQGGQVDI DCLSMDTALI FAENIGKPRY AETWDFHVSA STFLQFEMSM GCSKPFSDSH
SVQLQYSLNN GRDWHLVTEE CVPPTIGCLH YTESSIYTSE RFQNWKRITV YLPLSTISPR
TRFRWIQANY TVGADSWAID NVVLASGCPW MCSGRGICGA GRCVCDRGFG GAYCVPVIPL
PSILKDDFNG NLHPDLWPEV YGAERGNLNG ETIKSGTSLI FKGEGLRMLI SRDLDCTNTM
YVQFSLRFIA KSTPERSHSI LLQFSINGGI TWHLMDEFYF PQTTNILFIN VPLPYTAQTN
ATRFRLWQPY NNGKKEEIWI VDDFIIDGNN LNNPVMLLDT FDFGPREDNW FFYPGGNIGL
YCPYSSKGAP EEDSAMVFVS NEVGEHSITT RDLNVNENTI IQFEINIGCS TDSSSADPVR
LEFSRDFGAT WHLLLPLCYH SSGHVSSLCS TEHHPSSTYY AGTTQGWRRE VVHFGKLHLC
GSVRFRWYQG FYSAGSQPVT WAIDNVYIGP QCEEMCNGHG SCINGTKCIC DPGYSGPTCK
ISTKNPDFLK DDFEGQLESD RFLLMSGGKP SRKCGILSSG NNLFFNEDGL RMLMTRDLDL
SHARFVQFFM RLGCGKGVPD PRSQPVLLQY SLNGGLSWSL LQEFLFSNSS NVGRYIALEI
PLKARSASTR LRWWQPSENG HFYSPWVIDQ ILIGGNISGN TVLEDDFTTL DSRKWLLHPG
GTKMPVCGST GDALVFIEKA STRYVVTTDI AVNEDSFLQI DFAASCSVTD SCYAIELEYS
IDLGLSWHPL IRDCLPTNVE CSRYHLQRIL VSDTFNKWTR ITVPLPPYTR SQATRFRWHQ
PAPFDKQQTW AIDNVYIGDG CIDMCSGHGR CIQGNCVCDE QWGGLYCDEP ETSLPTQLKD
NFNRAPSNQN WLTVNGGKLS TVCGAVASGM ALHFSGGCSR LLVTVDLNLT NAEFIQFYFM
YGCLITPNNR NQGVLLEYSV NGGITWNLLM EIFYDQYSKP GFVNILLPPD AKEIATRFRW
WQPRHDGLDQ NDWAIDNVLI SGSADQRTVM LDTFSSAPVP QHERSPADAG PVGRIAFDMF
MEDKTAVNEH WLFHDDCTVE RFCDSPDGVM ICGSHDGREV YAVTHDLTPT EGWIMQFKIS
VGCKVSEKVT QNQIHVQYST DFGVSWNYLV PQCLPADAKC SGSVSQPSVF FPTKGWKRIT
YPLPESLVGN PVRFRFYQKH SDMQWAIDNF YLGPECLDNC RGHGDCLKEQ CICDPGYSGP
NCYLTHTLKT FLKERFDSEE IKPDLWMSLE GGSTCTECGI LAEDTALYFG GSTVRQAITQ
DLDLRGAKFL QYWGRIGSEN NMTSCHRPIC RKEGVLLDYS TDGGITWTLL HEMDYQKYIS
VRHDYILLPE EALTNTTRLR WWQPFVISNG LVVSGVERAQ WALDNILIGG AEINPSQLVD
TFDDEGTSHE ENWSFYPNAV RTAGFCGNPS FHLYWPNKKK DKTHNALSSR ELIIQPGYMM
QFKIVVGCEA TSCGDLHSVM LEYTKDARSD SWQLVQTQCL PSSSNSIGCS PFQFHEATIY
NAVNSSSWKR ITIQLPDHVS SSATQFRWIQ KGEETEKQSW AIDHVYIGEA CPKLCSGHGY
CTTGAICICD ESFQGDDCSI FSHDLPSYIK DNFESARVTE ANWETIQGGV IGSGCGQLAP
YAHGDSLYFN GCQIRQAATK PLDLTRASKI MFVLQIGSTS QTDSCNSDLS GPHAVDKAVL
LQYSVNNGIT WHVIAQHQPK DFTQAQRVSY NVPLEARMKG VLLRWWQPRH NGTGHDQWAL
DHVEVVLDEK SYIASKPDQT FMTNHSAACV ERHFLTCVIF HYLLSLVFH
//