ID A0A3P6TDV4_LITSI Unreviewed; 812 AA.
AC A0A3P6TDV4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Spondin-1 {ECO:0000256|ARBA:ARBA00019594};
DE AltName: Full=F-spondin {ECO:0000256|ARBA:ARBA00030964};
GN ORFNames=NLS_LOCUS7566 {ECO:0000313|EMBL:VDK86342.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK86342.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK86342.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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; UYRX01000802; VDK86342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P6TDV4; -.
DR STRING; 42156.A0A3P6TDV4; -.
DR Proteomes; UP000277928; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 1.
DR CDD; cd08544; Reeler; 1.
DR Gene3D; 2.60.40.2130; F-spondin domain; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR Gene3D; 2.60.40.4060; Reeler domain; 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
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 NCBIfam; NF038123; NF038123_dom; 1.
DR PANTHER; PTHR11311; SPONDIN; 1.
DR PANTHER; PTHR11311:SF16; SPONDIN-1; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF02014; Reeler; 1.
DR Pfam; PF06468; Spond_N; 1.
DR Pfam; PF19028; TSP1_spondin; 1.
DR Pfam; PF00090; TSP_1; 4.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS51019; REELIN; 1.
DR PROSITE; PS51020; SPONDIN; 1.
DR PROSITE; PS50092; TSP1; 4.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000277928};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..812
FT /note="Spondin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018183938"
FT DOMAIN 4..179
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 180..352
FT /note="Spondin"
FT /evidence="ECO:0000259|PROSITE:PS51020"
FT DOMAIN 603..653
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 812 AA; 92378 MW; 61236C1682CB1C96 CRC64;
MCLILLLPVI STITGEENCL RKLYEAKEER TPGNSGFVIE ISSATNTSDI NPDGYTPGDS
YIVKLRGWRT KFTVQAFRGF GIYAQFENDD HAGKFDLQGR KGEARIAPNC RKAGVSHSNL
RPKTSVHVLW YAPDTSEKGC VYFRASVITS RKVWYGDDGS LTKKFCIKEG YKKTLAIDES
NLDCCACDEA KYDLEFIGLW SRDTHPKDYP SLEHLTHFTD MLGASHSGNY TMWKFGMIAT
DGMKEIAEWG NTYKGEQEMK ANVTRILITK IIRYHHFASL AAMFGPSPDW CVGISSVNLC
LPDCTWISER TFELLPFDAG TDNGPTYMSP NNPAEPRIPI HPITTKLDKR SPFYSESSDV
IAPLARLKLT RKEVVKSTCK TIDEYQTEAY NVTNTSEDEE YKDRRECMVT NWEPWSLCSA
TCGKGIRMRS RVYVFPIKAQ MFRCLRQTIE RQFCNAEISE CYDSDAFNSK CSVSGWSPWT
ECSVTCGHGV RSRSRIFKES NSNSSTCPNV ELIRKDICTG DIRVSGDNGE DCSVTPDPLC
RATSWSEWSP CSASCDDGVH VRTRLLFYAE HEERCSNINL LEKENCQLQT CRRLLSAHSK
EICMEDKQEG QCAGTFPRYW YNSKRKRCER FIYTGCKGNR NQFETEEECK RMCAEHYENP
IGEVVPGHQL VNEFGVDQVN DGGPPVDCVI SEWTPWGNCS ATCGTGKRLR SRQIEVCIIL
ISKDGMIIFP RNGGRSCPER MIQELRCELR PCAIQNCHIK PWTTWSPCSV TCGDGKQIRR
RRIIRPHRYI DEEEDSVCNA PEKEYRPCYV KC
//
