ANNU_CAMAN
ID ANNU_CAMAN Reviewed; 11 AA.
AC P0DW51;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 1.
DT 03-AUG-2022, entry version 1.
DE RecName: Full=Annulatin {ECO:0000303|PubMed:34941722};
DE AltName: Full=Linear alpha-helical peptide {ECO:0000303|PubMed:34941722};
OS Campsomeriella annulata (Wasp) (Campsomeris annulata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Scolioidea;
OC Scoliidae; Campsomeriella.
OX NCBI_TaxID=1574124;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP AMIDATION AT GLY-11, AND SYNTHESIS.
RC TISSUE=Venom;
RX PubMed=34941722; DOI=10.3390/toxins13120885;
RA Alberto-Silva C., Vieira Portaro F.C., Kodama R.T., Pantaleao H.Q.,
RA Inagaki H., Nihei K.I., Konno K.;
RT "Comprehensive analysis and biological characterization of venom components
RT from solitary scoliid wasp a annulata annulata.";
RL Toxins 13:0-0(2021).
CC -!- FUNCTION: Amphiphilic linear alpha-helical peptide that shows histamine
CC releasing activity from mast cells. Also shows low hemolytic activity,
CC but no antimicrobial activities against all bacteria tested (E.coli,
CC S.aureus, and S.cerevisiae). {ECO:0000269|PubMed:34941722}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34941722}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:34941722}.
CC -!- MASS SPECTROMETRY: Mass=1128.69; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:34941722};
CC -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC {ECO:0000305}.
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PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Secreted.
FT PEPTIDE 1..11
FT /note="Annulatin"
FT /evidence="ECO:0000269|PubMed:34941722"
FT /id="PRO_0000456300"
FT MOD_RES 11
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:34941722"
SQ SEQUENCE 11 AA; 1129 MW; C835457D45B3372D CRC64;
ISEALKSIIV G