ID A0A183TQ28_SCHSO Unreviewed; 301 AA.
AC A0A183TQ28;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Wnt inhibitory factor 1 {ECO:0000313|WBParaSite:SSLN_0001927301-mRNA-1};
GN ORFNames=SSLN_LOCUS18576 {ECO:0000313|EMBL:VDM04962.1};
OS Schistocephalus solidus (Tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001927301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SSLN_0001927301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM04962.1, ECO:0000313|Proteomes:UP000275846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NST_G2 {ECO:0000313|EMBL:VDM04962.1,
RC ECO:0000313|Proteomes:UP000275846};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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; UYSU01044756; VDM04962.1; -; Genomic_DNA.
DR STRING; 70667.A0A183TQ28; -.
DR WBParaSite; SSLN_0001927301-mRNA-1; SSLN_0001927301-mRNA-1; SSLN_0001927301.
DR Proteomes; UP000050788; Unplaced.
DR Proteomes; UP000275846; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR013111; EGF_extracell.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF198; RE68558P; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000275846};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..301
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041049838"
FT DOMAIN 122..155
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 213..246
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 248..290
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 126..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 145..154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 236..245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 301 AA; 32522 MW; B5DF5800747661A9 CRC64;
MSRQARNHLL DLLLALLLVC TAKCKLPADE AERVARVLEE PVWSGLQNIL VPSPEASETL
AIHNVALTSP VFDGSAQEVP VYGPARSRYN GCFLPVSLRL PPECDCVFPP QALFTPSCAL
PSHLTCPDNC SGKGHCDIAT GKCTCKPGFT GENCATADPC SPESGLTPCQ FKCVAVNATR
VCICPSPFIL QPDGVSCGLA CPTGLTGTDC RTDIDECLTG SHNCQGNCGS NRTCECKKGF
HGISCEKDID KCQETGQNNC HHRCINTFGS FRCECDPGYN LDPRDNRTCV RDKWRMSERT
L
//