ID   CU61_CONBY              Reviewed;          79 AA.
AC   P0DTJ8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
DE   RecName: Full=Conotoxin ba-2281 {ECO:0000303|PubMed:33916793};
DE   AltName: Full=Conotoxin ba6.1 {ECO:0000305};
DE   Flags: Precursor;
OS   Conus bayani (Bayan's cone) (Stellaconus bayani).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Splinoconus.
OX   NCBI_TaxID=2070216;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-79, MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, AND HYDROXYLATION AT PRO-59; PRO-67; PRO-68 AND
RP   PRO-73.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=33916793; DOI=10.3390/md19040202;
RA   Rajaian Pushpabai R., Wilson Alphonse C.R., Mani R., Arun Apte D.,
RA   Franklin J.B.;
RT   "Diversity of Conopeptides and Conoenzymes from the Venom Duct of the
RT   Marine Cone Snail Conus bayani as Determined from Transcriptomic and
RT   Proteomic Analyses.";
RL   Mar. Drugs 19:0-0(2021).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33916793}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:33916793}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=2881.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:33916793};
CC   -!- SIMILARITY: Belongs to the conotoxin U superfamily. {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   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   Direct protein sequencing; Disulfide bond; Hydroxylation; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..52
FT                   /evidence="ECO:0000305|PubMed:33916793"
FT                   /id="PRO_0000454994"
FT   PEPTIDE         53..79
FT                   /note="Conotoxin ba-2281"
FT                   /evidence="ECO:0000269|PubMed:33916793"
FT                   /id="PRO_0000454995"
FT   MOD_RES         59
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:33916793"
FT   MOD_RES         67
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:33916793"
FT   MOD_RES         68
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:33916793"
FT   MOD_RES         73
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:33916793"
FT   DISULFID        58..66
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        61..71
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        65..76
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   79 AA;  8799 MW;  01E1E727A89C5B76 CRC64;
     MNRMGFFLML TAAVLLTSLV CTEATPADES KVKRARWSRI EGSRLFRHRL PKSSQSTCPY
     CQISCCPPAY CQPSGCRGP