RELN_CHICK
ID RELN_CHICK Reviewed; 3209 AA.
AC O93574;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Reelin;
DE EC=3.4.21.-;
DE Flags: Fragment;
GN Name=RELN;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10861519;
RX DOI=10.1002/1096-9861(20000703)422:3<448::aid-cne10>3.0.co;2-4;
RA Bernier B., Bar I., D'Arcangelo G., Curran T., Goffinet A.M.;
RT "Reelin mRNA expression during embryonic brain development in the chick.";
RL J. Comp. Neurol. 422:448-463(2000).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomer of disulfide-linked homodimers. Binds to the
CC ectodomains of VLDLR and LRP8/APOER2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- DOMAIN: The basic C-terminal region is essential for secretion.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the reelin family. {ECO:0000305}.
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DR EMBL; AF090441; AAC35559.1; -; mRNA.
DR STRING; 9031.ENSGALP00000013329; -.
DR PaxDb; O93574; -.
DR PRIDE; O93574; -.
DR VEuPathDB; HostDB:geneid_427850; -.
DR eggNOG; ENOG502QSIP; Eukaryota.
DR InParanoid; O93574; -.
DR OrthoDB; 9177at2759; -.
DR PhylomeDB; O93574; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0070325; F:lipoprotein particle receptor binding; IBA:GO_Central.
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:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0021800; P:cerebral cortex tangential migration; ISS:UniProtKB.
DR GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0048265; P:response to pain; ISS:UniProtKB.
DR GO; GO:0021511; P:spinal cord patterning; ISS:UniProtKB.
DR GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR041161; EGF_Tenascin.
DR InterPro; IPR034968; Reelin.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR11841; PTHR11841; 12.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18720; EGF_Tenascin; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF50939; SSF50939; 6.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 3.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Developmental protein; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Hydrolase;
KW Metal-binding; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Zinc.
FT CHAIN <1..3209
FT /note="Reelin"
FT /id="PRO_0000168144"
FT REPEAT 340..351
FT /note="BNR 1"
FT DOMAIN 418..449
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 546..557
FT /note="BNR 2"
FT REPEAT 699..710
FT /note="BNR 3"
FT DOMAIN 777..808
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 904..915
FT /note="BNR 4"
FT REPEAT 1070..1081
FT /note="BNR 5"
FT DOMAIN 1157..1190
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1283..1294
FT /note="BNR 6"
FT REPEAT 1434..1445
FT /note="BNR 7"
FT DOMAIN 1513..1544
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1632..1643
FT /note="BNR 8"
FT REPEAT 1791..1802
FT /note="BNR 9"
FT DOMAIN 1877..1909
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1998..2009
FT /note="BNR 10"
FT REPEAT 2147..2158
FT /note="BNR 11"
FT DOMAIN 2226..2257
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 2346..2357
FT /note="BNR 12"
FT REPEAT 2526..2537
FT /note="BNR 13"
FT DOMAIN 2601..2632
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 2727..2738
FT /note="BNR 14"
FT REPEAT 2891..2903
FT /note="BNR 15"
FT DOMAIN 2976..3008
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 3111..3122
FT /note="BNR 16"
FT BINDING 1822
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1927
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2012
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1014
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2065
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 287..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 356..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 422..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 439..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 642..684
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 715..722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1018..1057
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1086..1096
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1381..1421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1450..1457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1849
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1881..1891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1885..1897
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1899..1908
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1943..1983
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2096..2135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2141..2307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2292..2332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2542..2549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2667..2714
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2908..2918
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2980..2990
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2984..2996
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2998..3007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3044..3094
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT NON_TER 1
SQ SEQUENCE 3209 AA; 361294 MW; 81A7B6676BCAA3D1 CRC64;
TNGLNTTTAS VLQFSLGSGS CRFSYSDPSI TVSYSKNSSA DWTQLEKISA PSNVSTIIHI
LYLPEDAKGE NVHFQWKQDY LHAGEVYEAC WALDNILIIN AAHRKVVLED NLDPVDTGNW
LFFPGATVKH SCQSDGNSIY FHGTEGSEFN FATTRDVDLS TEDAQEQWAE EFESQPKGWD
ILGAVIGTEC GTLESGSSMV FLRDGERKIC TPYMDTTGYG NLRFYFSMGG NCDSGESHEN
DVILYAKIEG RREHIALDTL TYAAYKVPSL VSVVISPDLQ TPATKFCLKQ KSHQGHNRNV
WAVDYFHVLP VLPSTVTHMI QFSINLGCGT YQPGNSVSLE FSTNHGRSWS LLHTECLPEI
CAGPHLPHST VYASENYSGW NRITTPVPNA ALTSDTRIRW RQTGPIHGNM WAIDNIYIGP
SCLKFCSGRG QCTRNGCKCD PGFSGPACET ASQTFPMFIS ESFASSRLSS YHNFYSIRGA
EVSFGCGVLA SGKALVFNKD GRRQLITAFL DSSQSRFLQF TLRLGSKSVL STCKAPDQPG
EGVLLHYSYD NGITWKLLEH YSYLNYHEPR IISVELPEDA RQIGIQFRWW QPYHSSQGED
VWAIDEIVMT SVLFNSISLD FTNLVEVTQS LGFYLGNVQP YCGHDWTLCF TGDSKLTSSM
RYVETQSMQI GASYMIQFNL VMGCGQKFTP HMDNQVKLEY STNHGLTWHL VQEECLPSMP
SCQEFTSASI YHSNEFTQWR RITVLLPQKT WSSATRFRWS QCYYTAPDEW ALDNIYIGQQ
CPNMCSGHGW CDHGVCRCDS GFRGTECQPE NPLPSTVMSD FENPDVLKTE WQEIIGGEIV
KPEEGCGVIS SGSSLYFNKA GKRQLVSWDL DTTWVDFVQF YIQIGGESSS CNRPDSREEG
VLLQYSNNGG INWQLLAEMY FSDFSKPRFV YLELPAAAKT PCTRFRWWQP VFSGEGYDQW
AIDDIIILSE KQKHIIPVVN PTLPQNFYEK PAFDYPMNQL SVWLILANEG MTKNESFCSA
TPSAMLFGKS DGDRFAVTRD LTLKPGYVLQ FKLNIGCTNQ YSSSAPVLLQ YSHDAGLFWS
LVKEGCYPAS PGTKGCEGSS RELSEPTVYH TGDFEDWTRI TIVIPRSLAA SKTRFRWIQE
SSSHKSVPPF GLDGVYISEP CPNYCNGHGD CVSGVCFCDL GYTASHGTCV SNVPNHSEMF
DRFERKLSPL WYKITGGQVG TGCGVLSDGK SLYFNGPGKR EARTVPLDTT NIRLVQFYVQ
IGSKATGNSC NRPRSRNEGL IVQYTNDNGI TWHLLRELDF MSYLEPQVVS IDLPREAKTS
ATAFRWWQPQ HGKHSAQWAL DDVLIGMNDS SQTGFQDKFD GTVDLQASWY RIQGGQVDID
CLSMDTALMF SENIEKPRYA ETWDFHVSAS TFLQFELSMG CSKPYSNSHS IHLQYSLNNG
RDWHLVTEEC VPPTIGCQHY TESSIYTSER FQNWKRITAY LPPITNSPRT RFRWIQYNYA
SGVDSWAIDN VVLATGCPWM CSGHGICDAG HCVCDRGFGG PYCVHVNPLP SVLKDDFNGN
LHPDLWPEVY GAERGNLNGD TIKSGTALIF KGEGLRMLVS RDLDCTNTVY IQFSFKFIAK
GTPERSHSIL LQYSVNGGIT WHLIDEFYFT QTTDVLFINV PLPYTAQSNA TRFRLWQPYN
SGKKEEIWII DDFIIDGNNL KNPIILLDTF DFGPKEDNWF FYPGGNIGLY CPYSSKGAPE
EDSAMVFVSN EVGEHSITTR DLSVNENTII QFEINIGCTT DSSSADPVKL EFSRDLGATW
HLLLPLCYSS SSHLSSLCST EHHPSSTYYT GTTQGWRREV IHFGKLHLCG LTRFRWYQGF
YPAGSQPVTW AIDNVYIGPQ CEEMCNGHGS CINGTKCICD PGYSGPTCKI STKNSDSLKD
DFEGQLESDR FLLVSGGKPS RKCGIMSGGN NLFFNEEGLR MLMTRDLDLS QARFVQFFMR
LGCGKGVPDP RSQLSXLQYS LNGGLTWSLL QEFLFSNSSN VGRYIALEIP MKARSSSTRL
RWWQPSENGH FYSPWVIDQI LIGGNISGST VLEDDFTTLD SRKWLLHPGG TKMPVCGSTG
DALVFIEKAS TRYVVTTDIV VNEDSFLQID FAASCSVTGS CYAIELEYSV DLGITWHPIL
RDCLPTNVEC NRYHLQRILI SDTFNKWTRI TLPLPPYTRS QATRFRWHQP APFDKQQTWA
IDNVYIGDGC IDMCSGHGKC TQDNCVCDEH WGGLYCDEPE TPLPTQLKDN FNRSPSNQNW
LTVNGGKLST VCGAVASGMA LHFSGGCSRM LVTVDLNLTN AEFIQFYFMY GCLITPNNRN
QGVLLEYSVN GGITWSPLME IFYDQFSKPG FVNILLPYDA KTIGTRFRWW QPKHDGLDQN
DWAIDNVLIS GSTDQRTVML DTFSSAPLPQ HERSPADAGP TGRIAFDMFM EDKTTVNEHW
LFHDDCSIER FCDSPDGVMI CGSHDGREVY AVTHDLTPTE GWIMQFKVSV GCKTSEKLAQ
NQVHVQYSTD FGVSWSYLVP QCLPADPKCS GSVSQPSVFF PTKGWKRVTY SLPENLVGNP
VRFRFYQKYS DVQWAIDNFY LGPGCLENCR GHGDCLKEQC ICDPGYSGPN CYLTQTLKTF
LKERFDNEEI KPDLWMSLEG GNTCTECGIL AEDTTLYFGG QTVRQAVTQD LDLRGAKFLQ
YWGRIGSENN MTTCHRPTCR KEGVLLDYSI DGGITWTLLH EMDYQKYISV RHDYILLPEH
ALTNTTRLRW WQPFTISNGI VVSGPDRAQW ALDNILIGGA EINPSQLVDT FDDEGTSHEE
NWSSYPNAVR TAGFCGNPSF HLYWPNKKKD KTHNILSSRE LIIQPGYMMQ FKIVVGCEAS
SCGDLHSVML EYTKDARTDS WQLVQTHCLP SSSNSIGCSP FQFHEATIYN SVNSSMWRRI
TIQLPDHVSS SATQFRWIQK GEELEKQSWA IDHVYIGEAC PKLCSGRGYC STGAICICDE
GYQGDDCSVF SHDLPSYIKD NFESERVTEI NWETIQGGVI GNGCGQLAPY AHGDSLYFNG
CQVRQAVTKP LDLTRASKIM FVLQIGSISQ TDSCNTNLID PNTVDKAVLL QYSVNNGITW
QVIAQHQPKD FIQAQRVSYN VPLEARMKGV LLRWWQPRHN GTGHDQWALD HVEVVLISTR
KQNYMMNFSR QHGLRHFYNR RRRSLRRYP
