ID W5NEI9_LEPOC Unreviewed; 3130 AA.
AC W5NEI9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Reelin {ECO:0000256|ARBA:ARBA00023900};
GN Name=RELN {ECO:0000313|Ensembl:ENSLOCP00000019048.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000019048.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000019048.1}
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 EMBL; AHAT01029215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000019080.1; ENSLOCP00000019048.1; ENSLOCG00000015474.1.
DR GeneTree; ENSGT00580000081623; -.
DR Proteomes; UP000018468; Linkage group LG8.
DR Bgee; ENSLOCG00000015474; Expressed in camera-type eye and 8 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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:0007417; P:central nervous system development; IEA:InterPro.
DR GO; GO:0001764; P:neuron migration; IEA:InterPro.
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; 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; cd10052; Reelin_repeat_8_subrepeat_2; 1.
DR CDD; cd10036; Reelin_subrepeat_Nt; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 18.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002861; Reeler_dom.
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; PF21471; Reelin_subrepeat-B; 16.
DR SMART; SM00181; EGF; 7.
DR SUPFAM; SSF50939; Sialidases; 2.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51019; REELIN; 1.
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:UP000018468};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..32
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 1865..1897
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1383..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2930..2949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1869..1879
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1887..1896
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 3130 AA; 345939 MW; DB7D9DE8FBFEF889 CRC64;
ATATHRGQII FKDALAQQLC EQGAPTESPL RPSLAEIHGN HVILRDDFDS NQQGELDLSI
WSECKSCEVG EQCGVLMHGR ALTFCEPFGQ RELTSVPLNT STATVLQFAL GSGSCRFSYS
DPSIVVSYSL NSSDDWIPLE RIRAPSNSST VVHILALPPR SRGEGARVRW AQEPVSGPEG
YESCWSIDNV LLVNTAHRPP LLEDSLDPPD TANWLFFPGA TVKHACQSEG NALYFHGAEG
TGISFASTRD IDLHRQEGQS YWEEEFESLP TGWDIRGAVL GTQCGDVESG SALVFLRDGE
RKVCTPYLDT TAYGNLRFHY TMGGGLCDPG ESHENDVILY GRAEGRRGSH VNGFNPFVVS
VALPPDLQTP TTQFCLEQHS HAGSGRHVWA LDFLQLLPVL PGAQTHVAQF SINLGCGSYQ
PANSVNLEFS TNHGRSWSLL HTECLPELCA GPHLPHSTVY SSDNYSGWSR ITIPLPNAAL
TESTRFRWRQ TGTGPGNMWA VDNVYIGPSC LRFCSGRGQC TRNGCKCDPG FSGPACELAS
QTFPAFLSEG FSSARLSSYH SFQSLRGAEV SFACGVLASG KALVFNRDSR RHLVTTPLDS
SQARYLQFTL RLGSRSTLSS CSAPDQPGEG VLLHYSSDNG ITWTLLEHYP YQGFHEPRIV
SVELPQGART FGVQFRWWQP YHSGRGQDVW ALDEITMTSV LFNSISLDFS NVLEVTQSLG
FYLGHVQPYC QHDWTLSFTG ESSPGSSIRY VETQSMQIGA SYMLQFALVL GCGREASPHI
DTQVSLEFST NHGLTWHLVQ EACLPGMPSC VEFTAPSVYH PSEFSQWRRV TLPLPQKTWS
SATRFRWIQS YYGAPDEWAL DDIYIGQQCP SMCQGHGWCN HGTCRCDEGF SGPDCQPSTH
LPSSVMSDFE SQSSLHSAWK EVIGGQVVTP EQGCGVVSAG SSLYFSKAGR RQLVSWDLDT
EWVEFVQFYL RVGGDWAECN HADSREEGVL LQYSNNGGIS WGLIAEMYFT DFTKPRFVHY
EIPSSAKTPC TRFRWWQPLH SGEGYDQWAI DDIIILSERE KHIIPIANPT LPQNFYEKPA
FDYPLNQLSV WLMLGNEGME KNESFCAPTP SAMVFGRSEG DRMAVTRDLA LRPGYTLQFK
LNIGCESQFS ASAPVLLQFS QDAGRSWALV REGCYPASPG GGTCQGSRRE LREPTVYSAG
DYEHWTRVTV VIPRTVAASK TRFRWFQESS VHRDAPPFAL DGVYISEPCP NHCGGHGDCI
SGVCFCDMGY TVEEGTCVPT QPSPTEMWEG FEGKLSPLWQ GQTGGQVGMG CGTISEGKAL
YFNGPGRREA RTVPLDTTHT RLLQFFIRIG SKALGSSCSR PRSRDEGRHT LAHLCMGNHR
ARHTNPWSDT GTDTHTTTQT CHGHGHATDR HENMNSYSLP VQLTLNLIEQ IHLTVHSWNV
VLFLELVLIP FLPSCGSWWE AVNERVPSVS VNHYPQNAVL LTRRVNPSCC PGESGWALDN
VLLSPGCPWL CSGHGFCDNG HCVCDRGFGG PHCVPVTPMP SVLREDFNEN LRPERWPEVY
GAERGTLNGE TLKSGTALIF KGEGLRMLVS RDLDCSGTLY IQFSFKFITK GVPERSHSVL
LQYSVNGGIS WLLLDEFYFP QSTDTLFLHL PLPASAQSNA TRFRFWQPYS NGKKEEVWVI
DDLIIDGGAL RTLQLLSDSF EGGPREDSWL FYPGGNIGLY CPYLKGALED ESAMVFVSSE
AGEHSITTQE IDVNENTIVQ FEINVGCTSD SSAAHPARLE FSRDFGATWH LLVPLCQGGP
QLSSLCSTEM HPASVYYPGT TQGWRREVIH FGKLRLCGSV RFRWYQGFYS SGTPPPTWAL
DNVYIGPQCL DMCNGHGACV GGTHCVCDPG YSGPACGTRD NPNPDFLKED FEGGSIDPKR
FLLVSGGKPS RKCSILSSGN NLFFSEEGFR MLVTTDLDLS NARFVQFFLR LGCGKSPPDP
RSQPVLLQFS VDGGLSWTLL QEFLFSNSSN QGRLVALELP LRARTPATRL RWWQPSDNGH
FYSPWVMDQV VVGGSASGWG PLEDDFSTLD GRSWLLHPGG THMPVCGSDG DAFAFIEKAS
TRYAVSTDIS LGQSSFMQFD FSASCSVTNS CYAIELEFSL DLGMSWQPLL RDCLPTSLDC
SSYSLQRVLV SDTYNKWGRV TLPIPPYARS PATRFRWYQP APFDKQQTWA LDNLYIGDGC
PDMCSGHGRC QQDSCLCDPD WGGEDCDEPQ VTLPSQLKDS FGRPPSPANW LLLTGGKLST
VCGAVASGAA LHFSGGCSRQ LVTVDLNLTS AEFIQFYFMY GCMIPPSSRN QGVLLDFSVN
GGISWILLTE IFYDQYSKPG FVNVLLPPAA RAEGVRVRWW QPQHEGAEQS DWALDNVLIG
GSDPHSSILD TFGGSLLPNH ERAPADGVPT GRIALEPHPE DIGTVSEHWM FHEDCAVQRF
CRAPDGVMVC GGADGREVYA VTHDIVPARG WIMQFKIAVG CGAPEKQTAR QVHVQYSVDF
GVSWRYLVPQ CLPAEPRCAG QVSQPSVFFP AAGWKRVVFP LPDALTDTPV RFRFYQQHSD
AQWAIDNFYI GPPCPDHCGG HGDCLQQRCL CDPGFSGPNC YLSASLRVRP GPRVRSLSTS
SGQLSHSAVE KDRSLDGKWG SFVPLLVCGR FVEYWARIGS EDNLTTCHRP SCRREGVLLD
YSTDGGVSWT LLHEMDYLKY ISVRRDYIVL PLGALTNATR LRWWQPFAME TGLATPSLER
AQWAIDNILI GGSDINPSSL LDTFDDEGAS HEESWSFYPN AVRTAGFCGN PSFHLYWPNK
KQDGTRNILA TRELIVQPGY IVQFKTIQKC NSAHCTDRHP VLLCLTLDCL TPCATVSLDC
LTLLFDSLRL LEFQNCRVIS FSFLASADLA RAVWILLPFF LSSGHCHGHD RSTSRPPGSE
AGGVQTEGEL LQFPPPPGDD CSLSSADLPS YIKDNFESEA VTAQNWQLIQ GGGTGSGCGQ
LAPHAHGNSL YFNGCKMRQA VTKILDLTRA SKIMFVLQIG SVSQTESCNT ALTQPNTVDR
AVLLQYSINS GITWHVIAQH QPKDFIQAQR VSYNIPLEAR VKGVELRWWQ PRHDGAGHDQ
WALDHVEVVL
//
