SPON1_CHICK
ID SPON1_CHICK Reviewed; 802 AA.
AC Q9W770;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Spondin-1;
DE AltName: Full=F-spondin;
DE Flags: Precursor;
GN Name=SPON1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10197528; DOI=10.1016/s0896-6273(00)80703-5;
RA Debby-Brafman A., Burstyn-Cohen T., Klar A., Kalcheim C.;
RT "F-spondin, expressed in somite regions avoided by neural crest cells,
RT mediates inhibition of distinct somite domains to neural crest migration.";
RL Neuron 22:475-488(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10399931; DOI=10.1016/s0896-6273(00)80776-x;
RA Burstyn-Cohen T., Tzarfaty V., Frumkin A., Feinstein Y., Stoeckli E.,
RA Klar A.;
RT "F-spondin is required for accurate pathfinding of commissural axons at the
RT floor plate.";
RL Neuron 23:233-246(1999).
CC -!- FUNCTION: Cell adhesion protein that promotes the attachment of spinal
CC cord and sensory neuron cells and the outgrowth of neurites in vitro.
CC May contribute to the growth and guidance of axons in both the spinal
CC cord and the PNS (By similarity). Somite-derived spondin 1 is an
CC inhibitory signal involved in patterning the segmental migration of
CC neural crest cells and their topographical segregation within the
CC rostral somites in vitro. May be required to prevent the lateral
CC drifting of the commissural axons after having crossed the floor plate.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
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; AF149302; AAD41495.1; -; mRNA.
DR RefSeq; NP_990182.1; NM_204851.1.
DR AlphaFoldDB; Q9W770; -.
DR SMR; Q9W770; -.
DR STRING; 9031.ENSGALP00000039229; -.
DR PaxDb; Q9W770; -.
DR GeneID; 395657; -.
DR KEGG; gga:395657; -.
DR CTD; 10418; -.
DR VEuPathDB; HostDB:geneid_395657; -.
DR eggNOG; KOG3539; Eukaryota.
DR InParanoid; Q9W770; -.
DR OrthoDB; 517669at2759; -.
DR PhylomeDB; Q9W770; -.
DR PRO; PR:Q9W770; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR CDD; cd08544; Reeler; 1.
DR Gene3D; 2.20.100.10; -; 6.
DR Gene3D; 2.60.40.2130; -; 1.
DR Gene3D; 2.60.40.4060; -; 1.
DR InterPro; IPR002861; Reeler_dom.
DR InterPro; IPR042307; Reeler_sf.
DR InterPro; IPR009465; Spondin_N.
DR InterPro; IPR038678; Spondin_N_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR044004; TSP1_spondin_dom.
DR Pfam; PF02014; Reeler; 1.
DR Pfam; PF06468; Spond_N; 1.
DR Pfam; PF19028; TSP1_spondin; 1.
DR Pfam; PF00090; TSP_1; 5.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF82895; SSF82895; 6.
DR PROSITE; PS51019; REELIN; 1.
DR PROSITE; PS51020; SPONDIN; 1.
DR PROSITE; PS50092; TSP1; 6.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..802
FT /note="Spondin-1"
FT /id="PRO_0000035868"
FT DOMAIN 24..189
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT DOMAIN 190..383
FT /note="Spondin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00364"
FT DOMAIN 437..490
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 496..550
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 553..606
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 609..661
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 663..716
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 749..801
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 151..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 194..331
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT DISULFID 195..335
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT DISULFID 197..410
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT DISULFID 438..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 449..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 454..489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 497..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 508..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 543..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 554..590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 565..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 600..605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 610..645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 621..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 655..660
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 802 AA; 90510 MW; 0644D2BDD0A0FE12 CRC64;
MAARLRPLAL RLLARTFPLV ARGFSDETLE KAAKSEGYCS RILRAQGTRR EGYNEFSLRV
EGDPEFYKPG NSYRVTLSAA TPAYFRGFTL IALKEGKEGD KEEDHAGTFQ IIDEEETQFM
SNCPVAVTES TPRRRTRIQV FWTAPPTGTG CVILKASIVQ KRIIYFQDEG SLTKRICEQD
SASEGVTDKP TLDCCACGTA KYRLTFYGNW SEKTHPKDFP RRTNHWSAII GSSHSKNYIL
WEYGGYASEG VKQVAELGSP VKMEEEIRQQ SDEVLTVIKA KAQWPAWQPL NVRAAPSAEF
SVDRHRHLMS FLTMLGPSPD WNVGLSAEDL CTKDCGWVQK VVQDLIPWDA GTDSGVTYES
PNKPTVPQEK IRPLTSLDHP QSPFYDPEGG SIKLVARVVL ERIARKGEQC NFVPDNIDDI
VADLAPEEKE EDDTPETCIY SNWSPWSACS SSTCEKGKRM RQRMLKAQLD LSVPCPDTQD
FQPCMGPGCS DEDGSTCMMS DWITWSPCSV SCGMGTRSRE RYVKQFPEDG SMCKVPTEET
EKCIVNEECS PSSCLVTEWG EWDECSASCG TGMKRRHRMI KMTPADGSMC KAETTEAEKC
MMPECHTIPC LLSPWSEWSD CSVTCGKGMR TRQRMLKSAA ELGDCNEELE QAEKCMLPEC
PIDCELTEWS QWSECNTSCG KGHMIRTRMI KIEPQFGGTA CPETVQRTKC RVRKCLRGPG
MEKRRWKEAR EKRRSEQAKK NIDNEQYPVC RLKPWTAWTE CSTLCGGGIQ ERYMMVKKRS
KSTQFTSCKD KKELRACNVH PC
