ID   RELN_BOVIN              Reviewed;          52 AA.
AC   Q9N117;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Reelin;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
GN   Name=RELN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Brown Swiss;
RA   Speidel S.E., Oberg E.A., Ben-Abdallah M., DeNise S.K.;
RT   "Genetic analysis of candidate gene (RELN) for Weaver Syndrome in Brown
RT   Swiss cattle.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
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   -!- TISSUE SPECIFICITY: Abundantly produced during brain ontogenesis by the
CC       Cajal-Retzius cells and other pioneer neurons located in the
CC       telencephalic marginal zone and by granule cells of the external
CC       granular layer of the cerebellum.
CC   -!- SIMILARITY: Belongs to the reelin family. {ECO:0000305}.
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DR   EMBL; AF232904; AAF64286.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9N117; -.
DR   SMR; Q9N117; -.
DR   STRING; 9913.ENSBTAP00000004768; -.
DR   PaxDb; Q9N117; -.
DR   PRIDE; Q9N117; -.
DR   eggNOG; ENOG502QSIP; Eukaryota.
DR   HOGENOM; CLU_000468_0_0_1; -.
DR   OrthoDB; 9177at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   InterPro; IPR034968; Reelin.
DR   PANTHER; PTHR11841; PTHR11841; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Developmental protein; Extracellular matrix;
KW   Hydrolase; Metal-binding; Protease; Reference proteome; Secreted;
KW   Serine protease; Zinc.
FT   CHAIN           <1..>52
FT                   /note="Reelin"
FT                   /id="PRO_0000168143"
FT   NON_TER         1
FT   NON_TER         52
SQ   SEQUENCE   52 AA;  6069 MW;  B4699D90CDC998F7 CRC64;
     ENVQFQWKQE NLQVGEVYEA CWALDNILII NSAHRQVVLE DNLDPVDTGN WL