ID   VKT1A_CONCL             Reviewed;          78 AA.
AC   D2Y488;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Kunitz-type serine protease inhibitor conotoxin Cal9.1a {ECO:0000303|PubMed:21172372};
DE   Flags: Precursor;
OS   Californiconus californicus (California cone) (Conus californicus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Californiconus.
OX   NCBI_TaxID=1736779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=21172372; DOI=10.1016/j.toxicon.2010.12.008;
RA   Elliger C.A., Richmond T.A., Lebaric Z.N., Pierce N.T., Sweedler J.V.,
RA   Gilly W.F.;
RT   "Diversity of conotoxin types from Conus californicus reflects a diversity
RT   of prey types and a novel evolutionary history.";
RL   Toxicon 57:311-322(2011).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21172372}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:21172372}.
CC   -!- DOMAIN: The cysteine framework is IX (C-C-C-C-C-C).
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; GU306152; ADB04231.1; -; mRNA.
DR   AlphaFoldDB; D2Y488; -.
DR   SMR; D2Y488; -.
DR   ConoServer; 3962; Conkunitzin-Cal9.1a precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00109; KU; 1.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW   Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..20
FT                   /evidence="ECO:0000305|PubMed:21172372"
FT                   /id="PRO_0000414945"
FT   PEPTIDE         23..78
FT                   /note="Kunitz-type serine protease inhibitor conotoxin
FT                   Cal9.1a"
FT                   /evidence="ECO:0000305|PubMed:21172372"
FT                   /id="PRO_0000414946"
FT   DOMAIN          25..75
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            35..36
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        34..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        50..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   78 AA;  8649 MW;  F81BE48A81636A27 CRC64;
     MTFLLLLVSV CMMATGEERT KRDVCELPFE EGPCFAAIRV YAYNAETGDC EQLTYGGCEG
     NGNRFATLED CDNACARY