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 01-MAY-2013, entry version 53.
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; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
OC Conus.
OX NCBI_TaxID=6494;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-40 AND 70-80, AND
RP MASS 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
RT to 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
CC their propeptide precursors. The target propeptide requires
CC minimum four residues including a leucine N-terminal of the
CC cleavage site for efficient substrate processing (example: Xaa-
CC Xaa-Xaa-Leu-Asn-Lys-Arg-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; Range=25-300;
CC Source=PubMed:12759345;
CC -!- SIMILARITY: Belongs to the CRISP family.
CC -!- SIMILARITY: Contains 1 SCP domain.
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DR EMBL; AJ491318; CAD36507.1; -; mRNA.
DR ProteinModelPortal; 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; IPR001283; Allrgn_V5/Tpx1.
DR InterPro; IPR014044; CAP_domain.
DR InterPro; IPR004153; CXCXC_repeat.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 1.
DR Pfam; PF03128; CXCXC; 1.
DR PRINTS; PR00837; V5TPXLIKE.
DR SMART; SM00198; SCP; 1.
DR SUPFAM; SSF55797; SCP-like_extracellular; 1.
DR PROSITE; PS01009; CRISP_1; FALSE_NEG.
DR PROSITE; PS01010; CRISP_2; FALSE_NEG.
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 /FTId=PRO_0000006291.
FT CHAIN 25 300 Cysteine-rich venom protein.
FT /FTId=PRO_0000006292.
FT DOMAIN 62 183 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
//
