VPI1_SCOJE
ID VPI1_SCOJE Reviewed; 94 AA.
AC P0DM55;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Venom peptide SjAPI {ECO:0000303|PubMed:23533574};
DE AltName: Full=Ascaris-type protease inhibitor {ECO:0000305};
DE Flags: Precursor;
OS Scorpiops jendeki (Scorpion) (Scorpiops hardwickii jendeki).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Chactoidea; Euscorpiidae; Scorpiopinae; Scorpiopini;
OC Scorpiops.
OX NCBI_TaxID=587368;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF 63-ALA--VAL-65,
RP CIRCULAR DICHROISM, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom gland;
RX PubMed=23533574; DOI=10.1371/journal.pone.0057529;
RA Chen Z., Wang B., Hu J., Yang W., Cao Z., Zhuo R., Li W., Wu Y.;
RT "SjAPI, the first functionally characterized Ascaris-type protease
RT inhibitor from animal venoms.";
RL PLoS ONE 8:E57529-E57529(2013).
CC -!- FUNCTION: Recombinant protein inhibits both alpha-chymotrypsin (Ki=97.1
CC nM) and elastase (Ki=3700 nM). {ECO:0000269|PubMed:23533574}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23533574}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23533574}.
CC -!- MISCELLANEOUS: Does not inhibit trypsin. {ECO:0000305|PubMed:23533574}.
CC -!- SIMILARITY: Belongs to the serine protease inhibitor-like (TIL domain-
CC containing) family. {ECO:0000305}.
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DR AlphaFoldDB; P0DM55; -.
DR SMR; P0DM55; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR Pfam; PF01826; TIL; 1.
DR SUPFAM; SSF57567; SSF57567; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..30
FT /evidence="ECO:0000250"
FT /id="PRO_0000423041"
FT CHAIN 31..94
FT /note="Venom peptide SjAPI"
FT /id="PRO_0000423042"
FT DOMAIN 33..92
FT /note="TIL"
FT REGION 63..65
FT /note="Protease binding loop"
FT DISULFID 33..70
FT /evidence="ECO:0000250"
FT DISULFID 43..66
FT /evidence="ECO:0000250"
FT DISULFID 47..62
FT /evidence="ECO:0000250"
FT DISULFID 51..92
FT /evidence="ECO:0000250"
FT DISULFID 72..86
FT /evidence="ECO:0000250"
FT MUTAGEN 63..65
FT /note="AAV->PLM: Inhibits both chymotrypsin and elastase,
FT but not trypsin."
FT /evidence="ECO:0000269|PubMed:23533574"
FT MUTAGEN 63..65
FT /note="AAV->TKD: Inhibits both chymotrypsin and elastase,
FT but not trypsin."
FT /evidence="ECO:0000269|PubMed:23533574"
FT MUTAGEN 63..65
FT /note="AAV->TLE: Inhibits both trypsin and chymotrypsin,
FT but not elastase."
FT /evidence="ECO:0000269|PubMed:23533574"
FT MUTAGEN 63..65
FT /note="AAV->TME: Inhibits both chymotrypsin and elastase,
FT but not trypsin."
FT /evidence="ECO:0000269|PubMed:23533574"
FT MUTAGEN 63..65
FT /note="AAV->TMQ: Inhibits both chymotrypsin and elastase,
FT but not trypsin."
FT /evidence="ECO:0000269|PubMed:23533574"
FT MUTAGEN 63..65
FT /note="AAV->TRE: Inhibits both trypsin and chymotrypsin,
FT but not elastase."
FT /evidence="ECO:0000269|PubMed:23533574"
SQ SEQUENCE 94 AA; 10312 MW; 72BD4FE165B0761F CRC64;
MKWGALLCIF GFLAFCSVLD RGLGWIPDIW QKCSSKNEEF QQCGSSCPET CANHKNPEPK
SCAAVCFVGC VCKPGFIRDD LKGSICVKPE DCSK