ID G3UDE2_LOXAF Unreviewed; 2536 AA.
AC G3UDE2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Reelin {ECO:0000256|ARBA:ARBA00023900};
GN Name=RELN {ECO:0000313|Ensembl:ENSLAFP00000025850.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000025850.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000025850.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000025850.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000025850.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000025850.1};
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 Ensembl; ENSLAFT00000030128.1; ENSLAFP00000025850.1; ENSLAFG00000003384.4.
DR GeneTree; ENSGT00580000081623; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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; cd00054; EGF_CA; 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; cd10036; Reelin_subrepeat_Nt; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 15.
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; 1.
DR Pfam; PF21471; Reelin_subrepeat-B; 14.
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; 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:UP000007646};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1953..1985
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 1957..1967
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1975..1984
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2536 AA; 285070 MW; 56C582374D47BDAB CRC64;
APTEATMHPH LAEVHSDSII LRDDFDSYHQ LRLNPNICHT PWVECNNCET GEQCGAIMHG
NAVTFCEPYG PRELITTSLN TTTASVLQFS IGSGSCRFSY SDPSITVSYT KNNSADWIQL
EKIRAPSNVS TIIHILYLPE DAKGENVQFQ WKQESLRGGE VYEACWALDN ILIINSAHRQ
VVLEDNLDPV DTGNWLFFPG ATVKHSCQSD GNSIYFHGNE GSEFNFATTR DVDLSTEDIQ
EQWSEEFESQ PTGWDILGAV IGTECGTIES GLSMVFLKDG ERKLCTPYMD TTGFGNLRFY
FVIGGICDPG DSHENDIILY AKIEGKKEHI ALDSLSFSSY KVPTLVSVVI NPELQTPATK
FCLRQKNHQG HNRNVWAVDF FHILPVLPTT MSHMIQFSIN LGCGTHQPGN SVSLEFSTNH
GRSWSLIHTE CLPEICAGPH LPHSTVYSSE NYSGWNRITI PLPNAALTRD TRIRWRQTGP
ILGNMWAIDN VYIGPSCLKF CSGRGQCTRH GCKCDPGFSG PACEMASQTF PMFISESFGS
SRLSSYHNFY SIRGAEVSFG CGVLASGKAL VFNKDGRRQL ITSFLDSSQS RFLQFTLRLG
SKSVLSTCRA PDQPGEGVLL HYSYDNGITW KLLEHYSYLN YHEPRIISVE LPDDARQFGI
QFRWWQPYYS SQGEDVWAID EIIMTSVLFN SISLDFTNLV EVTQSLGFYL GNVQPYCGHD
WTLCFTGDSK LASSMRYVET QSMQIGASYM IQFSLVMGCG QKYTPHMDNQ VKLEYSTNHG
LTWHLVQEEC LPSVPSCQEF TSASVYHASE FIQWRRVTLL LPQKTWSSAT RFRWSQSYYT
IQDEWALDSI YIGQQCPNMC SGHGWCDHGV CRCDQGYQGT ECHPEATLPS TIMSDFENQN
GWESDWQEVI GGEIVKPEQG CGVISSGSSL YFSKAGKRQL VSWDLDTSWV DFVQFYIQIG
GESAACNKPD SREEGVLLQY SNNGGIQWYL LAEMYFSDFS KPRFVYLELP AAAKTPCTRF
RWWQPVFSGE DYDQWAVDDI IILSEKQKQI IPVVNPTLPQ NFYEKPAFDY PMNQMSVWLM
LANEGMVKNE TFCSVTPSAM VFGKSDGDRF AVTRDLTLKP GYVLQFKLNI GCANQFSSTA
PVLLQYSHDA GMSWFLVKEG CYPASAGKGC EGNSRELSEP TMYHTGDFEE WTRITIVIPR
SLAASKTRFR WIQESSSQKN VPPFGLDGVY ISEPCPSYCS GHGDCVSGVC FCDLGYTEAA
QGTCVSNIPN HSEMFDRFEG KLSPLWYKIT GGQVGTGCGT LNDGKSLYFN GPGKREARTV
PLDTRNIRLV QFYIQIGSKT SGITCIKPRA RNEGLVVQYS NDNGILWHLL RELDFMSFLE
PQIISIDLPR EAKTPATAFR WWQPQHGKHS AQWALDDVLI GMNDSSQTGF QDKFDGSLDL
QANWYRIQGG QVDIDCLSMD TALIFSENIV GKPRYAETWD FHVSASTFLQ FEMSMGCSKP
FSNSHSVQLQ YSLNNGRDWH LVTDECVPPT IGCLHYTESS IYTSERFQNW KRITVYLPPS
TISPRTRFRW IQANYTVGAD SWAIDNVILA SGCPWMCSGR GICDAGRCMC DRGFGGPYCV
PVLPLPSILK DDFNGNLHPD LWPEVYGAER GNLNGETIKS GTSLIFKGEG LRMLISRDLD
CTNTMYVQFS LRFIAKGTPE RSHSILLQFS INGGITWHLM DEFYFPQTTN ILFINVPLPY
TAQTNATRFR LWQPYNNGKK EEIWIVDDFI IDGNNLNNPV LLLDTFDFGP REDNWFFYPG
GNIGLYCPYS SKGAPEEDSA MVFVSNEVGE HSITTRDLNV NENTIIQFEI NIGCSTDSSS
ADPVRLEFSR DFGATWHLLL PLCYHSSSHV SSLCSTEHHP SSTYYAGTTQ GWRREVVHFG
KLHLCGSVRF RWYQGFYPAG SQPVTWAIDN VYVGPQCEEM CNGHGSCING TKCICDPGYS
GPTCKISTKN PDFLKDDFEG QLESDRFLLM SGGKPSRKCG ILSSGNNLFF NEDGLRMLMT
RDLDLSQARF VQFFMRLGCG KGVPDPRSQP VLLQYSLNGA LSWSLLQEFL FSNSSNVGRY
IALEIPLKAR SGSTRLRWWQ PSENGHFYSP WVIDQILIGG NISGNTVLED DFTTLDSRKW
LLHPGGTKMP VCGSTGDALV FIEKASTRYV VTTDIAVNED SFLQIDFAAS CSVTDSCYAI
ELEYSVDLGL SWHPLVRDCL PTNVECSRYH LQRILVSDTF NKWTRITLPL PPYTRSQATR
FRWHQPAPFD KQQTWAIDNV YIGDGCIDMC SGHGRCIQGS CVCDERWGGL YCDEPEATLP
TQLKDNFNRA PSNQNWLTVN GGKLSTVCGA VASGMALHFS GGCSRLLVTV DLNLTNAEFI
QFYFMYGCLI TPNNRNQGVL LEYSVNGGIT WNLLMEIFYD QYSKPGFVNI LLPPDAKEIA
TRFRWWQPRH DGLDQNDWAI DNVLISGSAD QRTVMLDTFS SAPVPQHERS PADAGPVGRI
AFDMFMEDKT AEHENW
//