ID A9V5K8_MONBE Unreviewed; 1281 AA.
AC A9V5K8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Reelin {ECO:0000256|ARBA:ARBA00023900};
DE Flags: Fragment;
GN ORFNames=MONBRDRAFT_10226 {ECO:0000313|EMBL:EDQ87057.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ87057.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ87057.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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; CH991561; EDQ87057.1; -; Genomic_DNA.
DR RefSeq; XP_001748000.1; XM_001747948.1.
DR EnsemblProtists; EDQ87057; EDQ87057; MONBRDRAFT_10226.
DR GeneID; 5893258; -.
DR KEGG; mbr:MONBRDRAFT_10226; -.
DR InParanoid; A9V5K8; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
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 InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR034968; Reelin.
DR PANTHER; PTHR11841; REELIN; 1.
DR PANTHER; PTHR11841:SF1; REELIN; 1.
DR Pfam; PF07974; EGF_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1281
FT /note="Reelin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002744686"
FT DOMAIN 1058..1092
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1095..1149
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DISULFID 1082..1091
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1281
FT /evidence="ECO:0000313|EMBL:EDQ87057.1"
SQ SEQUENCE 1281 AA; 132599 MW; 31F8F0E44B1FB7CB CRC64;
MGTLALLCIA LLQLPVPCQG VVSTLQLSGP LTGTLNIPAF SIVSVDATFS VPAGAALIVN
QGTVFFVAPE AAMNLAGSIT LAGRINDPIF ILPKGTHNDD PTAVRHAYGA HGAGAFSNLA
TAFDTFTVTS TANINLKHVV IAGASGGVSY QACSNLTGLK IVGVASASIT TPTGCNLPLL
HAGLYVGHMP TALQVLTAGN NANVLIRTSR FEAMPAGALS IARNPRSDVT IAFSTFVQCA
RTSGAALLAF LDFSKGNVPI HQRGATTVRA CAFTDGGVAV VSEDSEVSVI GATFTNNSVP
SGHAVLEAID EDSTFAFSVQ DSTFTRNQGQ LVLASQAGDA VVRDCVFQHN SHTSPGDTMI
KVTGVVRESR IIGATYGTLI SAATVADITL FRVNGSAAII SGITGATNLT CLHCSADAFI
DSDALLTLNL TRVALSGEVQ VNYFAKAAAA IIGSDIFYIG GAVASITSSL LSVLIDETTE
EPCFMIPELA IIGGTCHRIM TMADDSIWNI ESNLVIGSQG SLVVSEGAQL LLSAGMGVQV
LGSVVMAGTE SKPVVLTCRP EDNAAALGTL LGCRDTLAGL PTEDVQFSAA TKDDCVDKCA
QAGAAKALYL ANQCICPSAP KLSFQSATSC APGAWAVSAA AACHSWGTFT IGANAATTSL
SHVTLRRGGF SPSALAGAPG VALQVNGPAD LDFVTVSGSV GMGMILNDGP ANAADTIQAA
NVTIEASKSH GLALQAGSCQ NFCFFTGARI RQNQGYAVYY NGSTDEQRIY LQNSFITANA
LSGTLDSQIF VQGVEGSPHP GIALVSTVVT GNTGSSLLHL NHAASALMDA TLSSTRVSVT
GLFATAGDHV MINSRFSRLR GGISLSNPMV VNLTDVTFSG LTDVAVKVAL TSSSSDAIAR
VLLLDRIRVV ESTGPTMISV VDSVESLPPV HTAAQLRNIY LHDNNVSRAA VEILPHEKLS
IDLLNARIED NYANSATTPG DSGPMPVAAL LISGAGAVNG TFLDNVILDN PRLSVEVLVV
NDWRINATDL YVPDAASNIV CLADNAVAPV AFSAKPDATF DCSSINDCSG HGTCILPQIC
LCNAGHEGDD CSLTSCAPGT ARPSAGVACT AICEATGAWP QAFVGETVTM PCLTGQEGSA
RRTCLQTGYG TVDRSDCRSP ELVNLKARFA SNGFNDATIL QDWASEVTRY RGRMGAQDVA
VCLESIHLAC ETMGEDDEND IDVSNALLQV ARVVDVLVNT DRAMLMEGER VSTDDTSYAA
TLEEFAFRLR SRLVESTSYS H
//
