ID A0A0V1LK76_9BILA Unreviewed; 879 AA.
AC A0A0V1LK76;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Spondin-1 {ECO:0000256|ARBA:ARBA00019594};
DE AltName: Full=F-spondin {ECO:0000256|ARBA:ARBA00030964};
GN Name=Spon1 {ECO:0000313|EMBL:KRZ59735.1};
GN ORFNames=T02_4450 {ECO:0000313|EMBL:KRZ59735.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ59735.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ59735.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ59735.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ59735.1}.
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DR EMBL; JYDW01000038; KRZ59735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LK76; -.
DR STRING; 6335.A0A0V1LK76; -.
DR Proteomes; UP000054721; 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; 2.
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:UP000054721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..879
FT /note="Spondin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006881888"
FT DOMAIN 10..199
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 200..415
FT /note="Spondin"
FT /evidence="ECO:0000259|PROSITE:PS51020"
FT DOMAIN 688..738
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 394..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 99260 MW; 8B2F37366C52B5DC CRC64;
MFNLCLTIVV VISITTTAQT KRVDCNRKPI KNDDAIKSPG NNGFHITIQS YPLNQSSQPV
NSYVPGEKYT VSIEGWKTRY TEQTFRGFTL VAVSANDNSQ PLGFFHASTD SRLNGSIYIL
VKEDRDVSWS ADCWHAVTHS SLFPKTNASV VWQAPPSDEG CVHFKAAVLE YPNIWYMDDD
DLTKPFCASA GFTAPGGENS INECCACDEA KYEVTFEGLW SKNTHPKDYP SCKFIYQCCC
QQLQKFTFTV IIISAPVEHL THFSDIIGAS HSPRYTMWTY DGYASDGLKE LAEWGNTQKY
EQEIREQTSE VRTILKARGL WFPDVQGTTR AMFHVDKYHH LVSLASMLGP SPDWVVGVSM
MDLCLKNCSW INEKSLFLYP WDAGVDGGIT YMSPNSPSIP REPIKPITTS DPNDPRSPFY
NANSDVMPPF AKLTFRKEKV YPSECKDPSE YVLAWRSAGA ETETSEDIEN KNTKECTVNS
WTPWSLCSAT CGKGIRMRTR VYKNPIKAHL MGCSRQMNEK QFCNAIISVC DDSENFNDLC
AATTWAQWTP CSVNCGHGVR SRVRNYLNPM AIKQCHIRLT ENENCTGPAG PNCDLKPDPR
CQTTYWSEWS PCSHSCDQGN RIRTRLLYYP ENQKFCEHHQ LLERENCNVQ SCEAFLRMHG
AGETTFHSLF VVFSYANREW TGCFLEICNE PVEPGQCEGT FPRYYFNPAK KACMRFTFTG
CKGNRNNFHS EEQCKNACAD ASDINYNYTE ANNNIVSLLP EMSKVDTGQP VDCVVSGWSD
WSECSQTCGR GRRERVRTVV TPARNGGQPC PVDLVEKARC RLRPCAIVCR IGHWSEWSAC
SANCGTGVQM RQRSAKSSDR RSECPPHQTE KRICVVNNC
//
