C9A_GEMSP
ID C9A_GEMSP Reviewed; 35 AA.
AC P0C844;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Turripeptide gsp9a;
OS Gemmula speciosa (Splendid gem-turris) (Pleurotoma speciosa).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Turridae; Gemmula.
OX NCBI_TaxID=439592;
RN [1]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, HYDROXYLATION AT PRO-3 AND PRO-4,
RP GAMMA-CARBOXYGLUTAMATION AT GLU-14 AND GLU-17, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=18272193; DOI=10.1016/j.toxicon.2007.12.022;
RA Heralde F.M. III, Imperial J., Bandyopadhyay P.K., Olivera B.M.,
RA Concepcion G.P., Santos A.D.;
RT "A rapidly diverging superfamily of peptide toxins in venomous Gemmula
RT species.";
RL Toxicon 51:890-897(2008).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18272193}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:18272193}.
CC -!- DOMAIN: The cysteine framework is IX (C-C-C-C-C-C). {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=4071.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18272193};
CC -!- SIMILARITY: Belongs to the Pg turripeptide superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C844; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR026210; Toxin_Pg.
DR PRINTS; PR02080; TOXINPGFAMLY.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW Hydroxylation; Secreted; Toxin.
FT PEPTIDE 1..35
FT /note="Turripeptide gsp9a"
FT /evidence="ECO:0000269|PubMed:18272193"
FT /id="PRO_0000346141"
FT MOD_RES 3
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18272193"
FT MOD_RES 4
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:18272193"
FT MOD_RES 14
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18272193"
FT MOD_RES 17
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:18272193"
FT DISULFID 7..22
FT /evidence="ECO:0000250"
FT DISULFID 12..26
FT /evidence="ECO:0000250"
FT DISULFID 18..33
FT /evidence="ECO:0000250"
SQ SEQUENCE 35 AA; 3957 MW; 8EDA2D0F6F5013DC CRC64;
IDPPRYCNHI ICYEDSECSQ WCTAGCNSIT SKCDT