SPON1_XENLA
ID SPON1_XENLA Reviewed; 803 AA.
AC P35447;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Spondin-1;
DE AltName: Full=F-spondin;
DE Flags: Precursor;
GN Name=spon1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8367492; DOI=10.1073/pnas.90.17.8268;
RA Ruiz i Altaba A., Cox C., Jessell T.M., Klar A.;
RT "Ectopic neural expression of a floor plate marker in frog embryos injected
RT with the midline transcription factor Pintallavis.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8268-8272(1993).
CC -!- FUNCTION: Promotes the attachment of spinal cord and sensory neuron
CC cells and the outgrowth of neurites in vitro. May contribute to the
CC growth and guidance of axons in both the spinal cord and the PNS.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the floor plate.
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DR EMBL; L09123; AAA19105.1; -; mRNA.
DR PIR; A47723; A47723.
DR AlphaFoldDB; P35447; -.
DR SMR; P35447; -.
DR Proteomes; UP000186698; Genome assembly.
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; IEA:UniProtKB-KW.
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:0000255"
FT CHAIN 24..803
FT /note="Spondin-1"
FT /id="PRO_0000035869"
FT DOMAIN 24..190
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT DOMAIN 191..383
FT /note="Spondin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00364"
FT DOMAIN 436..489
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 495..549
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 552..605
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 608..662
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 664..717
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 750..802
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 353..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 152..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 195..331
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT DISULFID 196..335
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT DISULFID 198..409
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT DISULFID 437..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 448..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 453..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 496..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 507..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 542..548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 553..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 564..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 599..604
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 803 AA; 90703 MW; D3A54E329548AED9 CRC64;
MGLIFQPLFW QYVATSYALM VLGFLDETVE KAIKSEGYCS RILRAQGGTR KEGYNEFSMR
VEGDPEFYKP GNTYRVTILA VSPAYFRGFT LIALKEGKEG EKEEDHAGSF QIIDEEDTQF
MSNCPVAVTE STPRRRTRIQ VFWTAPSIGT GCVILKASIV QKKIIYFQDE GSLTKRMCEL
DLTLEGGNEK TIPDCCACGT AKYRLTFYGN WSEKAHPKDY PRRANHWSAI IGGSHSGEYV
LWEYGQASDG VKQVAELGSP VKMEEEIRQK GDEVLTVIKA KAQWPAWQPL NVRAAPSAEF
SVDRSRHLMS FLAMMGPSPD WNVGLTSEDL CTKECGWVQK VVQDLIPWDA GTDSGVTYES
PNKPTIPQDK IRPLTSLDHP QSPSMTRGGP IIPIARVVIE RIARKGEQCN IIPDNVDDIV
ADLVTEEKDE DDTPETCIYS NWSPWSACSS ATCDKGKRMR QRMLKAQLDL SVPCPDTQDF
EPCMGPGCSD DEASTCMMSE WITWSPCSAS CGMGIEVRER YVKQFPEDGS LCKVPTEETE
KCIVNEECEP SSCIVTEWAE WEECSATCRM GMKKRHRMIK MTPADGSMCK ADTTEVEKCM
MPECHTIPCV LSPWSEWSDC SVTCGKGTRT RQRMLKSPSE LGDCNEELEL KQVEKCMLPE
CPISCELTEW SYWSECNKSC GKGHMIRTRM ITMEPQFGGA VCPETVQRKK CRLRKCQKSS
GNERRHLKDA REKRRSEKIK EDSDGEQYPV CKMKPWTAWT ECTKFCGGGI QERFMTVKKR
FKSSQFTSCK DKKEIRACNV HPC
