ID A0A016UM54_9BILA Unreviewed; 811 AA.
AC A0A016UM54;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Spondin-1 {ECO:0000256|ARBA:ARBA00019594};
DE AltName: Full=F-spondin {ECO:0000256|ARBA:ARBA00030964};
GN Name=Acey_s0036.g3216 {ECO:0000313|EMBL:EYC15568.1};
GN Synonyms=Acey-spon-1 {ECO:0000313|EMBL:EYC15568.1};
GN ORFNames=Y032_0036g3216 {ECO:0000313|EMBL:EYC15568.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC15568.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC15568.1}.
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DR EMBL; JARK01001372; EYC15568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016UM54; -.
DR STRING; 53326.A0A016UM54; -.
DR Proteomes; UP000024635; 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; 5.
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:UP000024635};
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..811
FT /note="Spondin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013198188"
FT DOMAIN 3..178
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 178..369
FT /note="Spondin"
FT /evidence="ECO:0000259|PROSITE:PS51020"
FT DOMAIN 613..663
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 811 AA; 91992 MW; 9D2729A29C488C9B CRC64;
MRLLIILINT LLTLADKCTI RPYEAKGPKR SGNNGYAIEV DAATTRSDNG STGFIPGETY
KISIRGWRTK FTVQTFRGFV LSALFEDGKP AGKFEVVRGR GDARTSPGCR KGGVSHSNLR
PKTSVHTIWK APDVSTGCVI LRASVIESKY VWYSEEGDLT KKFCIQDGYQ KVVPVDDPNM
ECCACDQAKY ELEFIGLWSK ETHPKDFPTL EHLTHFTDML GASHSRNYSL WEIGGISTDG
MKEIAEWGNT FKAEAEAKEK AAEVRTLMKV KGLWYPEVQG RTKSSFVVNK YHHLASLATM
FGPSPDWCVG ISSVNLCLPD CSWVAERTFD LLPFDAGTDS GPTYMSPNSP QEPRVPIRWI
TTKDDPLSPF YSTETDVIPP LAKLILKRTE VIPMRCLADD EYQREAFNST NTSEDEEYKD
RRECLMSNWG SWSLCSATCG KGIRMRSRVF VFPIKAQMFN CHRQTTERQF CNAKINECED
SEAFNSKCAV GSWEPWSECS VTCGHGTRTR TRAFLNPKQQ ESECNVDLIR KDICVGESGD
DCSVTPDPLC KTTSWSEWSP CSASCDDGVR VRTRLFFFAE HEQRCSHITL QEKDSCILQS
CRRFIEQNSE EICQEPKEEG QCGGTFPRYW YNHEKQKCER FVYTGCKGNR NQFETEDECK
RVCVPGYEIE KSSVPNHQLI DEFGAGEVND GGDPVPCEMN EWTPWGQCSV TCGRGKKTRT
RQIKTFPRNG GTPCPEHLIQ ELRCELRPCP STKCRAGSWS RWSRCSVTCG EGVQTRRRRV
QKGRNGDWEE EECKEKETEE RICRIPCPRF P
//
