ID F1MUS6_BOVIN Unreviewed; 3460 AA.
AC F1MUS6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Reelin {ECO:0000256|ARBA:ARBA00023900};
GN Name=RELN {ECO:0000313|Ensembl:ENSBTAP00000004768.6,
GN ECO:0000313|VGNC:VGNC:53666};
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 {ECO:0000313|Ensembl:ENSBTAP00000004768.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000004768.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000004768.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000004768.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000004768.6};
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}.
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DR RefSeq; NP_001193387.1; NM_001206458.1.
DR SMR; F1MUS6; -.
DR Ensembl; ENSBTAT00000004768.6; ENSBTAP00000004768.6; ENSBTAG00000003658.6.
DR GeneID; 281450; -.
DR KEGG; bta:281450; -.
DR CTD; 5649; -.
DR VEuPathDB; HostDB:ENSBTAG00000003658; -.
DR VGNC; VGNC:53666; RELN.
DR GeneTree; ENSGT00580000081623; -.
DR HOGENOM; CLU_000468_0_0_1; -.
DR InParanoid; F1MUS6; -.
DR OMA; ATIKHAC; -.
DR OrthoDB; 3107368at2759; -.
DR TreeFam; TF106479; -.
DR Reactome; R-BTA-8866376; Reelin signalling pathway.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000003658; Expressed in semen and 85 other cell types or tissues.
DR ExpressionAtlas; F1MUS6; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IBA:GO_Central.
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:UP000009136};
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..3460
FT /note="Reelin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018679299"
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 3460 AA; 388416 MW; F940A4BC2A7D6088 CRC64;
MERSSWAPRT FLLALVLGAT LRARAAVGYY PRFSPFFFLC THHGELEGDG EQGEVLISLH
IAGHPTYYVP GQEYHVTIST STFFDGLLVT GLYTSTSVKA SQSIGGSNAF GFGIMSDHQF
GNQFMCSVVA SHVSHLPTTN LSFVWIAPPA GTGCVNFMAT ATHRGQIIFK DALAQQLCEQ
GAPTEATVHP HLAEIHSDSI ILRDDFDSYH QKELNPNIWV ECNNCETGEQ CGAIMHGNAV
TFCEPYGPRE LITTGLNTTT ASVLQFSIGS GSCRYSYSDP CIIVSYAKNN TADWIQLEKI
RAPSNVSTII HILYLPEDAK GENVQFQWKQ ENLQVGEVYE ACWALDNILI INSAHRQVVL
EDNLDPVDTG NWLFFPGATV KHSCQSDGNS IYFHGNEGSE FNFATTRDVD LSTEDIQEQW
SEEFESQPTG WDIMGAVIGT ECGTIESGLS MVFLKDGERK ICTPYLDTTG YGNLRFYFVM
GGICDPGDSH ENDVALYAKT EGRKEHITLD TLSYSSYKVP SLVSVVINPD LQTPATKFCL
RQKNHQGYNR 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 LDFTNLVEVT QSLGFYLGNV QPYCGHDWTL
CFTGDSKLAS SMRYVETQSM QIGASYMIQF SLVMGCGQKY TPHIDNQVKL EYSTNHGLTW
HLVQEECLPS MPSCQEFTSA SIYHASEFTQ WRRVIVLLPQ KTWSSATRFR WSQSYYTAQD
EWALDSIYIG QQCPNMCSGH GSCDRGMCRC DQGYQGTECH PEAALPSTIM SDFENPSAWE
SDWQEVIGGQ IVKPEEGCGV ISSGSSLYFS 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 FALDGVYISE PCPSYCSGHG DCVSGVCFCD LGYTAAQGTC
VSIVPNHSEM FDRFEGKLSP LWYKITGGQV GTGCGTLNDG KSLYFSGPGK REARTVPLDT
RNIRLVQFYI QIGSKTSGIT CIKPRARNEG LVVQYSNDNG ILWHLLRELD FMSFLEPQII
SIDLPRESKT PATAFRWWQP QHGKHSAQWA LDDVLIGMND SSQTGFQDKF DGSLDLQANW
YRIQGGQVDI DCLSMDTALI FTENIGKPRY AETWDFHVSA STFLQFEMSM GCSKPFSDSH
SVQLQYSLNN GRDWHLVTEE CVPPTIGCLH YTESSIYTSE RFQNWKRITV YLPLSTISPR
TRFRWIQANY TLGADSWAID NVVLASGCPW MCSGRGICDA GRCVCDRGFG GAYCVPVIPL
PSILKDDFNG NLHPDLWPEV YGAERGNLNG ETIKSGTSLI FKGEGLRMLI SRDLDCTNTM
YVQFSLRFIA KSTPERSHSI LLQFSINGGI TWHLMDEFYF PQTTNILFIN VPLPYTAQTN
ATRFRLWQPY NNGKKEEIWI VDDFIIDGNN LNNPVMLLDT FDFGPREDNW FFYPGGNIGL
YCPYSSKGAP EEDSAMVFVS NEVGEHSITT RDLNVNENTI IQFEINVGCS TDSSSADPVR
LEFSRDFGAT WHLLLPLCYH SSGHVSSLCS TEHHPSSTYH 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 CIDMCGGHGR 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
CTTGAVCICD ESFQGDDCSI FSHDLPSYIK DNFESARVTE ANWETIQGGV IGSGCGQLAP
YAHGDSLYFN GCQIRQAATK PLDLTRASKI MFVLQIGSTS QTDSCNSDLS GPHAVDKAVL
LQYSVNNGIT WHVIAQHQPK DFTQAQRVSY NVPLEARMKG VLLRWWQPRH NGTGHDQWAL
DHVEVVLVST RKQNYMMNFS RQHGLRHFYN RRRRSLRRYP
//
