ID G1SWG7_RABIT Unreviewed; 1813 AA.
AC G1SWG7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Reelin {ECO:0000256|ARBA:ARBA00023900};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000007831.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000007831.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000007831.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000007831.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000007831.3};
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; AAGW02038495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; G1SWG7; -.
DR STRING; 9986.ENSOCUP00000007831; -.
DR PaxDb; 9986-ENSOCUP00000007831; -.
DR Ensembl; ENSOCUT00000009067.3; ENSOCUP00000007831.3; ENSOCUG00000009050.4.
DR eggNOG; ENOG502QSIP; Eukaryota.
DR GeneTree; ENSGT00580000081623; -.
DR HOGENOM; CLU_000468_0_0_1; -.
DR InParanoid; G1SWG7; -.
DR TreeFam; TF106479; -.
DR Proteomes; UP000001811; Chromosome 7.
DR Bgee; ENSOCUG00000009050; Expressed in prefrontal cortex and 15 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; cd00054; EGF_CA; 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 11.
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; 2.
DR Pfam; PF21471; Reelin_subrepeat-B; 10.
DR SMART; SM00181; EGF; 5.
DR SUPFAM; SSF50939; Sialidases; 2.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 2.
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:UP000001811};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1158..1190
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 1162..1172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1180..1189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1813 AA; 203575 MW; 49F0A241951B7CB7 CRC64;
MPSCQEFTSA SIYHASEFTQ WRRLIALLPQ KTWSSATRFR WSQSYYTAQD EWALDDIYIG
QQCPNMCSGH GSCDHGMCRC DPGYSGTECH PEAALPSTVM SDFENQNGWE SDWQEVIGGE
IVRPEQGCGV ISSGSSLYFS KAGKRQLVSW DLDTSWVDFV QFYIQIGGES AACNQPDSRE
EGVLLQYSNN GGIQWHLLAE MYFSDFSKPR FVYLELPAAA KTPCTRFRWW QPVFSGEDYD
QWAIDDIIIL SEKQKQVIPV VNPTLPQNFY EKPAFDYPMN QMSVWLMLAN EGMVRNETFC
AATPSAMVFG KSDGDRFAVT RDLTLKPGYV LQFKLNIGCA DQFSSTAPVL LQYSHDAGMS
WLLVKEGCYP ASAGKGCEGS SRELSEPTVY HTGDFEEWTR ITIVIPRSLA SSKTRFRWIQ
ESSSQKNVPA FGLDGVYISE PCPSYCSGHG DCISGVCFCD LGYTAAHGTC VSNVPNYSEM
FDRFEGKLSP LWYKITGGQV GTGCGTLNDG KSLYFSGPGK REARTVPLDT RTIRLVQFYI
QIGSKTSGIT CSKPRARNEG LVVQYSNDNG IVWHLLRELD FTSFLEPRII SIDLPREAKT
SATAFRWWQP QHGKHSAQWA LDDVLIGMND SSQTGFQDKF DGSLDLQANW YRIQGGQVDI
DCLSMDTALI FTENIGKPRY AETWDFHVSA STFLQFEMSM GCSKPFSDSH SVRLQYSLNS
GRDWHLVTEE CVPPTIGCLH YTESSTYTSE RFQNWKRITV YLPLSTNSPR TRFRWIQANY
TMGADSWAID NVVLASGCPW MCSGRGICDA GRCVCDRGFG GPYCVPLIPL PSILKDDFNG
NLHPDLWPEV YGAERGDLNG EPIKSGTSLV FKGEGLRMLI SRDLDCTNTM YVQFSLRFIA
KGTPERSHSI LLQFSITGGI TWHLMDEFYF PQTTNILFIN VPLPSTAQTN ATRFRLWQPY
NNGKKEEIWI VDDFIIDGNN LNNPVMLLDT FDFGPREDNW FFYPGGNIGL YCPYSAKGAP
EEDSAMVFVS NEVGEHSITT RDLSVNENTI IQFEINVGCS TDSSSADPVR LEFSRDFGAT
WHLLLPLCYH SSSHVSSLCS TEHHPSSTYY AGTTQGWRRE VVHFGKLHLC GSVRFRWYQG
FYPAGSQPVT WAIDNVYIGP QCEEMCNGHG SCINGTKCIC DPGYSGPTCK ISTKNPDFLK
DDFEGQLESD RFLLLSGGKP SRKCGILSSG NNLFFNEDGL RMLMTRDLDL SHARFVQFFM
RLGCGKGVPD PRSQPVLLQY SRNGGLSWSL LQEFLFSNAS NVGRYIALEM PLKARSASTR
LRWWQPSENG HFYSPWVIDQ ILIGGNISGN TVLEDDFTSL DSRKWLLHPG GTKMPVCGST
GDALVFIEKA STRYVVTTDI AVNEDSFLQI DFAASCSVTD SCYAIELEFS TDLGLSWHPL
VRDCLPTNVE CSRYHLQRVL VSDTFNKWTR ITLPLPPYTR SQATRFRWHQ PAPFDKQQTW
AIDNVYIGDG CVDMCSGHGR CIQGNCVCDE QWGGLYCDEP ETPLPTQLKD NFNRAPSNQN
WLTVNGGKLS TVCGAVASGM ALHFSGGCSR LLVTVDLNLT NAEFIQFYFM YGCLISPNNR
NQGVLLEYSV NGGITWNLLM EIFYDQYSKP GFVNILLPPD AKEIATRFRW WQPRHDGLDQ
NDWAVDNVLI SGSADQRTVM LDTFSAAPVP QHERSPADAG PVGRIAFDML MEDKTAVNEH
WLFHDDCVVE RFCHSPDGVM MCGSHDGREV YAVTHDLTPT EGWIMQFKIS VGCKVSEKLH
RIKFTCSFLQ TLA
//
