GenomeNet

Database: UniProt
Entry: TX31_CONTE
LinkDB: TX31_CONTE
Original site: TX31_CONTE 
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   14-MAY-2014, entry version 56.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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; 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                                /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
//
DBGET integrated database retrieval system