ID A0A2Y9LKV1_DELLE Unreviewed; 3458 AA.
AC A0A2Y9LKV1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Reelin {ECO:0000256|ARBA:ARBA00023900};
GN Name=RELN {ECO:0000313|RefSeq:XP_022410100.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022410100.1};
RN [1] {ECO:0000313|RefSeq:XP_022410100.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022410100.1};
RG RefSeq;
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; XP_022410100.1; XM_022554392.2.
DR Ensembl; ENSDLET00000006995; ENSDLEP00000006307; ENSDLEG00000004664.
DR Proteomes; UP000248483; Unplaced.
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: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 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; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 1.
DR SUPFAM; SSF50939; Sialidases; 3.
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:UP000248483};
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..3458
FT /note="Reelin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015986900"
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 3458 AA; 388158 MW; 97D2BBC39FE9BEF0 CRC64;
MERSGWAPRT FLLALMLGAT LRVRAAVGYY PRFSPFFFLC THHGELEGDG EQGEVLISLH
IAGHPTYYVP GQEYHVTIST STFFDGLLVT GLYTSTSVQA SQSIRGSSAF GFGIMSDHQF
GNQFMCSVVA SHVSHLPTTN LSFVWIAPPA GTGCVNFMAT ATHKGQIIFK DALAQQLCEQ
GAPTEASMHP HLAEIHSDSI ILRDDFDSSH QKELNPNIWV ECNNCETGEQ CGAIMHGNAV
TFCEPYGPRE LITTGLNTTT ASVLQFSIGS GSCRFSYSDP CIIVSYAKNN TVDWIQLEKI
RAPSNVSTIV HILYLPEDAK GENVQFQWKQ ENLRVGEVYE ACWALDNVLV INSAHRQVVL
EDNLDPIDTG NWLFFPGATV KHSCQSDGNS IYFHGNEGSE FNFATTRDVD LSTEDIQEQW
SEEFESQPTG WDILGAVIGT ECGTIESGLS MVFLKDGERK ICTPYLDTTG YGNLRFYFVM
GGICDPGESH ENDIILYAKT EGRKEHITLD TLSYSSYKVP SLVSVVINPE LQTPATRFCL
RQKNHQGHNR NVWAIDFFHV LPVLPSTMSH MIQFSINLGC GTQQPGNSVS LEFSTNHGRS
WSLLHTECLP EICAGPHLPH STIYSSENYS GWNRITIPLP NAALTRDTRI CWRQTGPILG
NMWAIDNVYV GPSCLRFCSG 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 TPHMDNQVKL EYSTNHGLTW
HLVQEECLPS MPSCQEFTSA SIYHASEFTQ WKRVIVLLPQ KTWSSATRFR WSQSYYTAQD
EWALDSIYIG QQCPNMCSGH GSCDHGVCRC DQGYQGTECH PEAALPSTIM SDFEDPNAWE
SDWQEVIGGE IVKPEEGCGV ISSGSSLYFS KAGKRRLVSW DLDTSWVDFV QFYIQIGGES
AACNKPDSRE EGILLQYSNN GGIQWHLLAE MYFSDFSKPR FVYLELPAAA KTPCTSFRWW
QPVFSGEGYD QWAVDDIIIL SEKQKQIIPV VNPTLPQNFY EKPAFDYPMN QMSVWLMLAN
EGMVKNETFC SATPSAMVFG KSDGDRFAVT RDLTLKPGYV LQFKLNIGCA NQFSSAAPVL
LQYSHDAGMS WFLVKEGCYP ASAGKGCEGN SRELSEPTLY HTGDFEEWTR ITIVIPRSLA
SSKTRFRWIQ ESSSQKNVPP FGLDGVYISE PCPSYCSGHG DCVSGVCFCD LGYTATQGTC
VSVVPNHSEM FDRFEGKLSP LWYKITGGQI GTGCGTLNDG KSLYFSGPGK REARTIPLDT
RNIRLVQFYI QIGSKTSGIT CIKPRARNEG LVVQYSNDNG ILWHLLRELD FMSFLEPQII
SIDLPREAKT PATAFRWWQP QHGKHSAQWA LDDVLIGMND SSQTGFQDKF DGSLDLQANW
YRIQGGQVNT DCLSMDTALI FTENIGKPRY AETWDFHVSA STFLQFEMSM GCSKPFSDSH
GIQLQYSLNN GRDWHLVTEE CVPPTIGCLH YTESSVYTSE RFQNWKRITV YLPLSTISPR
TRFRWIQANY TMGADSWAID NVVLASGCPW MCSGRGICDA GRCVCDRGFG GTYCVPVVPL
PSILKDDFNG NLHPDLWPEV YGAERGNLNG ETIKSGTSLI FKGEGLRMLI SRDLDCTNTM
YVQFSLRFIA KGTPERSHSI LLQFSANGGI TWHLMDEFYF PQMTNILFIN VPLPYTAQTN
ATRFRLWQPY NNGKKEEIWI VDDFIIDGNN LNNPVMLLDT FDFGPREDNW FFYPGGNIGL
YCPYSSKGAP EEDSAMVFVS NEVGEHSITA RDLNVNENTI IQFEINVGCS TDSSSADPVR
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
GTKMPVCGST GDALVFIEKA STRYVVTTDI AVNEDSFLQI DFAASCSVTD SCYAIELEYS
VDLGLSWHPL VRDCLPTNVE CNRYHLQRIL VSDTFNKWTR ITLPLPPYTR SQATRFRWHQ
PAPFDKQQTW AIDNVYIGDG CTDMCSGHGR CIQGNCVCDE QWGGLYCDEP QTSLPTQLKD
NFNRAPSNQN WLTVNGGKLS TVCGAVASGM ALHFSGGCSR LLVTVDLNLT NSEFIQFYFM
YGCLITPNNR NQGVLLEYSV NGGITWNLLM EIFYDQYSKP GFVNILLPSD AKEIATRFRW
WQPRHDGLDQ NDWAIDNVLI SGSADQRTVM LDTFSSAPVP QHERSPSDAG PVGRIAFDMF
MEDKTAVNEH WLFHDDCTVE RFCDSPDGVM ICGSHDGREV YAVTHDLTPT EGWIMQFKIS
VGCKVSEKVT QNQIHVQYST DFGVSWSYLV PQCLPADPKC SGSVSQPSVF FPTKGWKRIT
YPLPESLVGN PVRFRFYQKH SDTQWAIDNF YLGPECLDNC RGHGDCLKEQ CICDPGYSGP
NCYLTHTLKT FLKERFDSEE IKPDLWMSLE GGSTCTECGI LAEDTALYFG GSTVRQAITQ
DLDLRGAKFL QYWGRIGSEN NMTSCHRPIC RKEGVLLDYS TDGGITWTLL HEMDYQKYIS
VRHDYILLPE DALTNTTRLR WWQPFVISNG LVVSGVERAQ WALDNILIGG AEINPSQLVD
TFDDEGTSHE ENWSFYPNAV RTAGFCGNPS FHLYWPNKKK DKTHNALSSR ELIIQPGYMM
QFKIVVGCEA TSCGDLHSVM LEYTKDARSD SWQLVQTQCL PSSSNSIGCS PFQFHEATIY
NAVNSSSWKR ITIQLPDHVS SSATQFRWIQ KGEETEKQSW AIDHVYIGEA CPKLCSGHGY
CTTGAICICD ESFQGDDCSV FSHDLPSYIK DNFESARVTE ANWETIQGGV IGSGCGQLAP
YAHGDSLYFN GCQIRQAATK PLDLTRASKI MFVLQIGSTS QTDSCNSDLS GPHSVDKAVL
LQYSVNNGIT WHVIAQHQPK DFTQAQRVSY NVPLEARMKG VLLRWWQPRH NGTGHDQWAL
DHVEVVLTRK QNYMMNFSRQ HGLRHFYNRR RRSLRRYP
//
