VKT1B_CONCL
ID VKT1B_CONCL Reviewed; 60 AA.
AC D2Y489;
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 Cal9.1b {ECO:0000303|PubMed:21172372};
DE Flags: Precursor; Fragment;
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}.
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; GU306153; ADB04232.1; -; mRNA.
DR AlphaFoldDB; D2Y489; -.
DR SMR; D2Y489; -.
DR ConoServer; 3963; Conkunitzin-Cal9.1b 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 2: Evidence at transcript level;
KW Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW Toxin.
FT PROPEP <1..2
FT /evidence="ECO:0000305|PubMed:21172372"
FT /id="PRO_5000566306"
FT PEPTIDE 5..60
FT /note="Kunitz-type serine protease inhibitor conotoxin
FT Cal9.1b"
FT /evidence="ECO:0000305|PubMed:21172372"
FT /id="PRO_5000566307"
FT DOMAIN 7..57
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 17..18
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000250"
FT DISULFID 7..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 16..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 32..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT NON_TER 1
SQ SEQUENCE 60 AA; 6708 MW; 901FD1842BE17DA5 CRC64;
RTKRDVCELP FEEGPCFAAI RVYAYNAETG DCEQLTYGGC EGNGNRFATL EDCDNTCARY