ID A0A158PLT3_ANGCS Unreviewed; 590 AA.
AC A0A158PLT3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Kunitz/Bovine pancreatic trypsin inhibitor domain protein {ECO:0000313|WBParaSite:ACOC_0001175301-mRNA-1};
GN ORFNames=ACOC_LOCUS11754 {ECO:0000313|EMBL:VDM63339.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0001175301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0001175301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM63339.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM63339.1,
RC ECO:0000313|Proteomes:UP000267027};
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:PRU00500}.
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DR EMBL; UYYA01004783; VDM63339.1; -; Genomic_DNA.
DR WBParaSite; ACOC_0001175301-mRNA-1; ACOC_0001175301-mRNA-1; ACOC_0001175301.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 3.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 3.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF217; PROTEIN CBG23496; 1.
DR Pfam; PF00014; Kunitz_BPTI; 3.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 3.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF57362; BPTI-like; 3.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 3.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..590
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040569040"
FT DOMAIN 114..178
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 271..321
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 466..516
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 528..569
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DISULFID 148..155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 590 AA; 64871 MW; 469E7D42625B511D CRC64;
MRYLALLAAA CAILAAVDAV DPCKRQPFRG RCPSKNGESP KRSQFVLRYY MRSGECVSYP
YGHCANDESE PQLYRYKEEC EDACINPPPG SQLNLRPRLQ EFVRKSDRSL IISTSECERR
RAHAAVTSIR GGFVPVCTAQ GDFEKVQCEP DGRQCFCVDA RGLEIANSRT RNGRKPDCNS
IQSASTPRTK DCVGGAVRGP CSGSLDRWYY DEDEAECKGE PLKTKLGVAV NCAKSDCPSG
YKCSVVQQSS VCCPENNKII GLQMSGSDDV CSLPKDRGPC DKYELRFYFN AELKECKYFF
WGGCEGNGNN FEKVEECEST CGIIKVKQSM PITTRTTPTV TIGRQPSFSF KTTQGIRITP
SNRPKVEELT TLGKLVDQQS TIALSRTSVA TSISTGATAA TATTATVPVG VLSTGSSTLQ
LANKLSTEAK VVAPVVHVTY TRAPPIPEMS LLEGSEDNTA DGVNRCLHPR DPGNCRGQFV
RWYWDNENKV CDVFTYTGCQ GNGNNYASRE ECLAICHKEV ALSPGNLCEH DIEVGECSGV
FVRFGYDKLT NDCRQFTYGG CGGKQWQQFC DSTRMSECVR EEIVQSKSTV
//
