ID A0A8M1H4K8_URSMA Unreviewed; 3460 AA.
AC A0A8M1H4K8;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=Reelin {ECO:0000256|ARBA:ARBA00023900};
GN Name=RELN {ECO:0000313|RefSeq:XP_040500284.1};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_040500284.1};
RN [1] {ECO:0000313|RefSeq:XP_040500284.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_040500284.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: Extracellular matrix serine protease secreted by pioneer
CC neurons that plays a role in layering of neurons in the cerebral cortex
CC and cerebellum by coordinating cell positioning during
CC neurodevelopment. Regulates microtubule function in neurons and
CC neuronal migration. Binding to the extracellular domains of lipoprotein
CC receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of
CC DAB1 and modulation of TAU phosphorylation. Affects migration of
CC sympathetic preganglionic neurons in the spinal cord, where it seems to
CC act as a barrier to neuronal migration. Enzymatic activity is important
CC for the modulation of cell adhesion. {ECO:0000256|ARBA:ARBA00046064}.
CC -!- SUBUNIT: Oligomer of disulfide-linked homodimers.
CC {ECO:0000256|ARBA:ARBA00044961}.
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; XP_040500284.1; XM_040644350.1.
DR GeneID; 103674717; -.
DR CTD; 5649; -.
DR OrthoDB; 1924787at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0043005; C:neuron projection; IEA:TreeGrafter.
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 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 FunFam; 2.60.120.260:FF:000003; Reelin; 4.
DR FunFam; 2.60.120.260:FF:000028; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000030; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000036; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000039; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000040; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000041; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000042; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000044; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000045; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000047; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000052; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000053; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000055; Reelin; 1.
DR FunFam; 2.60.120.260:FF:000056; reelin; 1.
DR FunFam; 2.60.120.260:FF:000057; Reelin; 1.
DR FunFam; 2.60.40.4060:FF:000001; Reelin; 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.
DR InterPro; IPR013111; EGF_extracell.
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; PF23106; EGF_Teneurin; 2.
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};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; 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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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_5035456656"
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; 387859 MW; FCAEBBA22298D440 CRC64;
MERSCWAPRT FLLALLLGTT LRARAAVGYY PRFSPFFFLC THHGELEGDG EQGEVLISLH
IAGNPTYYVP GQEYHVTIST STFFDGLLVT GLYTSTSAQA SQSIGGSNAF GFGIMSDHQF
GNQFMCSVVA SHVSHLPTTN LSFVWIAPPA GTGCVNFMAT ATHRGQIIFK DALAQQLCEQ
GAPTEATTHP HLAEVHSDSI ILRDDFDSYH QLELNPNIWV ECNNCETGEQ CGAIMHGNAV
TFCEPYGPRE LITTSLNTTT ASVLQFSIGS GSCRFSYSDP SIIVSYAKNN TADWIQLERI
RAPSNVSAII HILYLPQDAK GENVQFQWKQ ESLHVGEVYE ACWALDNILI INSAHRQVIL
EDSLDPVDTG NWLFFPGATV KHSCQSDGNS IYFHGNEGSE FNFATTRDVD LSTEDIQEQW
SEEFESQPTG WDILGAVIGT ECGTVESGLS MVFLKDGERK LCTPYMDTTG YGNLRFYFVM
GGVCDPGDSP ENDITLYAKI EGRKEHITLD SLSYSSYKVP SLVSVVINPE LQTPATRFCL
RQKNHQGHNR NVWAVDFFHV LPVLPSTMSH MIQFSINLGC GTHQPGNSVG LEFSTNHGRS
WSLLHTECLP EICAGPHLPH STIYSSENYS GWNRITIPLP NAALTRDTRI RWRQMGPILG
NMWAIDNVYI GPSCLKFCSG RGQCTRHGCK CDPGFSGPAC EMASQTFPMF ISESFGSSRL
SSYHNFYSIR GAEVSFGCGV LASGKALVFN KDGRRQLITS FLDSSQSRFL QFTLRLGSKS
VLSTCRAPDQ PGEGVLLHYS YDNGITWKLL EHYSYLNYHE PRIISVELPD DARQFGIQFR
WWQPYHSSQG EDVWAIDEII MTSVLFNSIS LDFTNLVEVT QSLGFYLGNV QPYCGHDWTL
CFTGDSKLAS SMRYVETQSM QIGASYMIQF SLVMGCGQKY TPHMDNQVKL EYSTNHGLTW
HLVQEECLPS MPSCQEFTSA SIYHASEFTQ WRRVIVLLPQ KTWSSATRFR WSQSYYTAQD
EWALDSIYIG QQCPNMCSGH GSCDHGVCRC DQGYQGTECH PEAALPSTIM SDFENQNGWE
SDWQEVIGGE VVKPEQGCGV ISSGSSLYFS KAGKRQLVSW DLDTSWVDFV QFYIQIGGES
AACNKPDSRE EGVLLQYSNN GGIQWHLLAE MYFSDFSKPR FVYLELPAAA KTPCTRFRWW
QPVFSGEGYD QWAVDDIIIL SEKQKQVIPI VNPTLPQNFY EKPAFDYPIN QMSVWLMLAN
EGMAKNETFC SATPSAMVFG KSDGDRFAVT RDLTLKPGYV LQFKLNIGCA NQFSSAAPVL
LQYSHDAGMS WFLVKEGCYP ASAGKGCEGN SRELSEPTMY HTGDFEEWTR ITIVIPRSLA
SSKTRFRWIQ ESSSQKNVPP FGLDGVYISE PCPSYCSGHG DCVSGVCFCD LGYTAAQGTC
VSNVPNHSEM FDRFEGKLSP LWYKITGGQV GTGCGTLNDG KSLYFNGPGK REARTVPLDT
RNIRLVQFYI QIGSKTSGIT CIKPRARNEG LVVQYSNDNG ILWHLLRELD FMSFLEPQII
SIDLPREAKT PATAFRWWQA QHGKHSAQWA LDDVLIGMND SSQTGFQDKF DGSIDLQASW
YRIQGGQVGT DCLSMDTALI FTESIGKPRY AETWDFHVSA STFLQFEMSM GCSKPFSDTH
GVQLQYSLNN GRDWHLVTEE CVPPTIGCLH YTESSVYTSE RFQNWKRITV YLPLSTISPR
TRFRWIQSNY TAGADAWAID NVVLASGCPW LCSGRGICDA GRCVCDRGFG GAYCVPIVPL
PSILKDDFNG NLHPDLWPEV YGAERGNLNG ETIKSGTSLI FKGEGLRMLI SRDLDCTNTM
YVQFSLRFIA KGTPERSHSI LLQFSINGGI TWHLMDEFYF PQTTNILFIN VPLPYTAQTN
ATRFRLWQPY NNGKKEEIWI VDDFIIDGNN LNNPLMLLDT FDFGPREDNW FFYPGGNIGL
YCPYSSKGAP EEDSAMVFVS NEVGEHSITT RDLDVNENTI IQFEINVGCS TDSSSTDPVR
LEFSRDFGAT WHLLLPLCYH SSSHVSSLCS TEHHPSSTYY AGTTQGWRRE VVHFGKLHLC
GSVRFRWYQG FYPAGSQPVT WAIDNVYIGP QCEEMCNGHG SCINGTKCIC DPGYSGPTCK
ISTKNPDFLK DDFEGQLESD RFLLMSGGKP SRKCGILSSG NNLFFNEDGL RMLMTRDLDL
SHARFVQFFM RLGCGKGVPD PRSQPVLLQY SLNGGLSWSL LQEFLFSNSS NVGRYIALEI
PLKARSASTR LRWWQPSENG HFYSPWVIDQ ILIGGNISGN TVLEDDFTTL DSRKWLLHPG
GTKMPVCGSS GDALVFIEKA STRYVVTTDI AVNEDSFLQI DFAASCSVTD SCYAIELEYS
VDLGLSWHPL VRDCLPTNVE CSRYHLQRIL VSDTFNKWTR ITLPLPPYTR SQATRFRWHQ
PAPFDKQQTW AIDNVYIGDG CIDMCGGHGR CIQGSCICDE QWGGLYCDEP EISLPTQLKD
NFNRAPSSQN WLTVNGGKLS TVCGAVASGM ALHFSGGCSR LLVTVDLNLT NAEFIQFYFM
YGCLITPNNR NQGVLLEYSV NGGITWNLLM EIFYDQYSKP GFVNILLPPD AKEIATRFRW
WQPRHDGLDQ NDWAIDNVLI SGSADQRTVM LDTFSSAPVP QHERSPADAG PVGRIAFDMF
MEDKTAVNEH WLFHDDCTVE RFCDSPDGVM ICGSHDGREV YAVTHDLTPT EGWIMQFKIS
VGCKVSEKVA QNQVHVQYST DFGVSWNYLV PQCLPADPKC SGSVSQPSVF FPTKGWKRIT
YPLPESLVGN PVRLRFYQKY SDMQWAIDNF YLGPGCLDNC RGHGDCLKEQ CICDPGYSGP
NCYLTLTLKT FLKERFDSEE IKPDLWMSLE GGSTCTECGI LAEDTALYFG GSTVRQAITQ
DLDLRGAKFL QYWGRIGSEN NMTSCHRPIC RKEGVLLDYS TDGGITWTLL HEMDYQKYIS
VRHDYILLPE DALTNTTRLR WWQPFVTSNG LVVSGVERAQ WALDNILIGG AEINPSQLVD
TFDDEGTSHE ENWSFYPNAV RTAGFCGNPS FHLYWPNKKK DKTHNALSSR ELIIQPGYMM
QFKIVVGCEA TSCGDLHSVM LEYTKDARSD SWQLVQTQCL PSSSNSIGCS PFQFHEATIY
NAVNSSSWKR ITIQLPDHVS SSATQFRWIQ KGEETEKQSW AIDHVYIGEA CPKLCSGHGY
CTTGAVCICD ESFQGDDCSV FSHDLPSYIK DNFESARVTE ANWETIQGGV IGSGCGQLAP
YAHGDSLYFN GCQIRQAATK PLDLTRASKI MFVLQIGSTS QTDSCNSDVS GPHAVDKAVL
LQYSVNNGIT WHVIAQHQPK DFTQAQRVSY NVPLEARMKG VLLRWWQPRH NGTGHDQWAL
DHVEVVLVST RKQNYMMNFS RQHGLRHFYN RRRRSLRRYP
//
