ID G1N471_MELGA Unreviewed; 1979 AA.
AC G1N471;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Reelin {ECO:0000256|ARBA:ARBA00023900};
GN Name=RELN {ECO:0000313|Ensembl:ENSMGAP00000006594.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000006594.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000006594.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000006594.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSMGAT00000007348.3; ENSMGAP00000006594.3; ENSMGAG00000006446.3.
DR GeneTree; ENSGT00580000081623; -.
DR HOGENOM; CLU_000468_0_0_1; -.
DR InParanoid; G1N471; -.
DR TreeFam; TF106479; -.
DR Proteomes; UP000001645; Chromosome 1.
DR Bgee; ENSMGAG00000006446; Expressed in spleen and 12 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: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; 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 11.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
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; 2.
DR Pfam; PF21471; Reelin_subrepeat-B; 11.
DR SMART; SM00181; EGF; 5.
DR SUPFAM; SSF50939; Sialidases; 3.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 649..681
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1748..1780
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 653..663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 671..680
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1752..1762
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1770..1779
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1979 AA; 223853 MW; C926214BD542F84F CRC64;
IFRRILENGF GKIQGHGGSF MQMKMLVQFY VQIGSKATGN SCNRPRSRNE GLVVQYTNDN
GITWHLLREL DFMSYLEPQV VSIDLPREAK TSATAFRWWQ PQHGKHSAQW ALDDVLIGMN
DSSQTGFQDK FDGTVDLQAS WYRIQGGQVD IDCLSMDTAL MFSENIEKPR YAETWDFHVS
ASTFLQFELS MGCSKPYSNS HSIHLQYSLN NGRDWHLVTE ECVPPTIGCQ HYTESSIYTS
ERFQNWKRIT VYLPPITNSP RTRFRWIQYN YASGVDSWAI DNVVLATGCP WMCSGHGICD
AGHCVCDRGF GGPYCVPVIP LPSVLKDDFN GNLHPDLWPE VYGAERGNLN GDTIKSGTAL
IFKGEGLRML VSRDLDCTNT VYIQFSFKFI AKGTPERSHS ILLQYSVNGG ITWHLIDEFY
FTQTTDVLFI NVPLPYTAQS NATRFRLWQP YNNGKKEEIW IIDDFIIDGN NLKNPIILLD
TFDFGPKEDN WFFYPGGNIG LYCPYSSKGA PEEDSAMVFV SNEVGEHSIT TRDLSVNENT
IIQFEINIGC TTDSSSADPV KLEFSRDLGA TWHLLLPLCY SSSSHLSSLC STEHHPSSTY
YTGTTQGWRR EVIHFGKLHL CGLARFRWYQ GFYPAGSQPV TWAIDNVYIG PQCEEMCNGH
GSCINGTKCI CDPGYSGPTC KISTKNSDFL KDDFEGQLES DRFLLVSGGK PSRKCGIMSG
GNNLFFNEEG LRMLMTRDLD LSQARFVQFF MRLGCGKGVP DPRSQPVLLQ YSLNGGLTWS
LLQEFLFSNS SNVGRYIALE IPMKARSSST RLRWWQPSEN GHFYSPWVID QILIGGNISG
NTVLEDDFTT LDSRKWLLHP GGTKMPVCGS TGDALVFIEK ASTRYVVTTD IVVNEDSFLQ
IDFAASCSVT DSCYAIELEY SVDLGITWHP ILRDCLPTNV ECNKYHLQRI LISDTFNKWT
RITLPLPPYT RSQATRFRWH QPAPFDKQQT WAIDNVYIGD GCIDMCSGHG KCTQDNCVCD
EHWGGLYCDE PETPLPTQLK DNFNRSPSNQ NWLTVNGGKL STVCGAVASG MALHFSGGCS
RMLVTVDLNL TSAEFIQFYF MYGCLITPNN RNQGVLLEYS VNGGITWSLL MEIFYDQFSK
PGFVNILLPY DAKAIGTRFR WWQPKHDGLD QNDWAIDNVL ISGSADQRTV MLDTFSSAPL
PQHERSPADA GPTGRIAFDM FMEDKTTVNE HWLFHDDCSI ERFCDSPDGV MICGSHDGRE
VYAVTHDLTP TEGWIMQFKV SVGCKTSEKL AQNQVHVQYS TDFGVSWSYL VPQCLPADPK
CSGSVSQPSV FFPTKGWKRV TYSLPENLVG NPVRFRFYQK YSDMQWAIDN FYLGPGCLEN
CRGHGDCLKE QCICDPGYSG PNCYLTQTLK TFLKERFDNE EIKPDLWMSL EGGNTCTECG
ILAEDTTLYF GGQTVRQAVT QDLDLRGAKF LQYWGRIGSE NNMTTCHRPT CRKEGVLLDY
SIDGGITWTL LHEMDYQKYI SVRHDYILLP EHALTNTTRL RWWQPFTISN GIVVSGPDRA
QWALDNILIG GAEINPSQLV DTFDDEGTSH EENWSFYPNA VRTAGFCGNP SFHLYWPNKK
KDKTHNILSS RELIIQPGYM MQFKIVVGCE ASSCGDLHSV MLEYTKDART DSWQLVQTHC
LPSSSNSIGC SPFQFHEATI YNSVNSSMWK RITIQLPDHV SSSATQFRWI QKGEELEKQS
WAIDHVYIGE ACPKLCSGRG YCTTGAICIC DEGYQGDDCS VFSHDLPSYI KDNFESERVT
EINWETIQGG VIGNGCGQLA PYAHGDSLYF NGCQVRQAVT KPLDLTRASK IMFVLQIGSI
SQTDSCNTNL SDPNTVDKAV LLQYSVNNGI TWQVIAQHQP KDFIQAQRVS YNVPLEARMK
GVLLRWWQPR HNGTGHDQWA LDHVEVVLTR KQNYMMNFSR QHGLRHFYNR RRRSLRRYP
//