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Database: UniProt
Entry: A0A498SDM4_ACAVI
LinkDB: A0A498SDM4_ACAVI
Original site: A0A498SDM4_ACAVI 
ID   A0A498SDM4_ACAVI        Unreviewed;       849 AA.
AC   A0A498SDM4;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Spondin-1 {ECO:0000256|ARBA:ARBA00019594};
DE   AltName: Full=F-spondin {ECO:0000256|ARBA:ARBA00030964};
GN   ORFNames=NAV_LOCUS3884 {ECO:0000313|EMBL:VBB29075.1};
OS   Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX   NCBI_TaxID=6277 {ECO:0000313|EMBL:VBB29075.1, ECO:0000313|Proteomes:UP000276991};
RN   [1] {ECO:0000313|EMBL:VBB29075.1, ECO:0000313|Proteomes:UP000276991}
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}.
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DR   EMBL; UPTC01000530; VBB29075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498SDM4; -.
DR   STRING; 6277.A0A498SDM4; -.
DR   Proteomes; UP000276991; 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:UP000276991};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          46..215
FT                   /note="Reelin"
FT                   /evidence="ECO:0000259|PROSITE:PS51019"
FT   DOMAIN          216..407
FT                   /note="Spondin"
FT                   /evidence="ECO:0000259|PROSITE:PS51020"
FT   DOMAIN          652..702
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
SQ   SEQUENCE   849 AA;  96649 MW;  C4F8E276F792F11A CRC64;
     MSTRRAEIMK INEFEEKEIG MLAGALSAPH QPPHDQLHSL SSTLPVFILI KQLLLQWKLY
     EAKEEKTPGN SGFMIEISSA TNTSDNNPEG YAPGDSYIVK LRGWRTKFTV QAFRGFGIYA
     QFENGEHAGK FDLQGKKGEA RIAPNCRKAG VSHSNLRPKT SVHVLWHAPE TSEKGCAYFR
     ASVITSRKIW YGDDGPLTKK FCVREGYKKM LTIDEDNLDC CACDEAKYDL EFIGLWSRDT
     HPKDYPSLEH LTHFTDMLGA SHSSNYTMWK FGMIATDGMK EIAEWGNTYK GEQEMKANAK
     EIRTLMKIKG LWYPEVQGRT TSSFVVNKYH HLASLAAMFG PSPDWCVGIS SVNLCLPDCT
     WIPERTFELL PFDAGTDNGP TYMSPNNPAE PRIPIHPITT KLDKRSPFYN PNSDIIAPLA
     RLKLTRKEVM KSVCKTVDEY QTEAYNVTST SEDEEYKDRR ECMVTNWEPW SLCSATCGKG
     IRMRSRVYVF PIKAQMFRCH RQTIERQFCN AEISECHDSD AFNSKCSVSS WSSWTECSVT
     CGHGTRSRSR IFKELDSNNN TCPNVDLVRK DICTGDNGDD CSVTPDPLCR ATSWSEWSPC
     SASCDHGIHV RTRLLFYAEH EERCANVNLL EKENCQLQTC RRLLSVHSKE ICMEDKQEGQ
     CAGTFPRYWY NSKLKRCERF IYTGCKGNRN QFETEDDCKR MCLEYYGSSV GEVVPGHQLV
     NEFGVDQVND GGPPVDCVIS EWTPWGNCSA TCGSGKRKRS RQIEIFPRNG GRSCPEHMVQ
     ELRCELRPCA IQNCHIKPWT MWSPCSVTCG DGKQIRRRRI IRPHRYVDDE EDSPCNAPEK
     ESRPCHVKC
//
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