ID   TX31_CONTE              Reviewed;         300 AA.
AC   Q7YT83;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Cysteine-rich venom protein;
DE            Short=CRVP;
DE            EC=3.4.-.-;
DE   AltName: Full=Substrate-specific endoprotease Tex31;
DE   Flags: Precursor;
OS   Conus textile (Cloth-of-gold cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=6494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-40 AND 70-80, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom duct;
RX   PubMed=12759345; DOI=10.1074/jbc.m304843200;
RA   Milne T.J., Abbenante G., Tyndall J.D.A., Halliday J., Lewis R.J.;
RT   "Isolation and characterization of a cone snail protease with homology to
RT   CRISP proteins of the pathogenesis-related protein superfamily.";
RL   J. Biol. Chem. 278:31105-31110(2003).
CC   -!- FUNCTION: Protease responsible for cleaving the conotoxins from their
CC       propeptide precursors. The target propeptide requires minimum four
CC       residues including a leucine N-terminal of the cleavage site for
CC       efficient substrate processing (example: Xaa-Xaa-Xaa-Leu-Asn-Lys-Arg-
CC       toxin).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- PTM: Contains 11 disulfide bonds.
CC   -!- MASS SPECTROMETRY: Mass=30853; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12759345};
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; AJ491318; CAD36507.1; -; mRNA.
DR   AlphaFoldDB; Q7YT83; -.
DR   SMR; Q7YT83; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hydrolase; Protease; Secreted; Signal.
FT   SIGNAL          1..21
FT   PROPEP          22..24
FT                   /evidence="ECO:0000269|PubMed:12759345"
FT                   /id="PRO_0000006291"
FT   CHAIN           25..300
FT                   /note="Cysteine-rich venom protein"
FT                   /id="PRO_0000006292"
FT   DOMAIN          62..183
FT                   /note="SCP"
SQ   SEQUENCE   300 AA;  33373 MW;  1254D5864EE34327 CRC64;
     MLSTMQTVGA VLMLSIVLVA GRKRHHCDSK YYELTPAHTM CLTDKPNAVA VPLTQETEHE
     ILEMHNKIRA DVTDAANMLK MEWDERLATV AQKWAMQCIL GHDSGRRGEP DLPGSVGQNV
     AWSSGDLTFL GAVQMWADEI VDFQYGVWTD GTGHYIQQVF AGASRIGCGQ SACGNNKYFV
     CNYYKGTMGD EPYQLGRPCS QCRSSCQHIR GSQGRWGSLC DCTNGPDACF NGGIFNINTC
     QCECSGIWGG ADCQEKHCPN EDFDDMCRYP DALRRPQHWC QYDNFQSDCP ILCGYCPNPN