CONOI_CONVL
ID CONOI_CONVL Reviewed; 7 AA.
AC P85015;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 22-APR-2020, entry version 28.
DE RecName: Full=Conophan vil-I'/vil-I'(O2P) {ECO:0000303|PubMed:17153339};
OS Conus villepinii (Villepin's cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Dauciconus.
OX NCBI_TaxID=257347;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, HYDROXYLATION
RP AT PRO-2, AND D-AMINO ACID AT ILE-5.
RC TISSUE=Venom;
RX PubMed=17153339; DOI=10.1007/978-3-540-30880-5_4;
RA Franco A., Pisarewicz K., Moller C., Mora D., Fields G.B., Mari F.;
RT "Hyperhydroxylation: a new strategy for neuronal targeting by venomous
RT marine molluscs.";
RL Prog. Mol. Subcell. Biol. 43:83-103(2006).
CC -!- FUNCTION: May act as a neurotoxin.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17153339}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000269|PubMed:17153339}.
CC -!- PTM: Occurs in 2 forms, vil-I' contains 4-hydroxyproline at Pro-2, vil-
CC I'(O2P) contains unmodified proline at Pro-2.
CC {ECO:0000269|PubMed:17153339}.
CC -!- MISCELLANEOUS: The mature peptide does not contain cysteine residue.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conophan family. {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW D-amino acid; Direct protein sequencing; Hydroxylation; Neurotoxin;
KW Secreted; Toxin.
FT PEPTIDE 1..7
FT /note="Conophan vil-I'/vil-I'(O2P)"
FT /evidence="ECO:0000269|PubMed:17153339"
FT /id="PRO_0000259383"
FT MOD_RES 2
FT /note="4-hydroxyproline; in form vil-I'"
FT /evidence="ECO:0000269|PubMed:17153339"
FT MOD_RES 5
FT /note="D-allo-isoleucine"
FT /evidence="ECO:0000269|PubMed:17153339"
SQ SEQUENCE 7 AA; 832 MW; 75A37045B4576B70 CRC64;
EPNSIWS