ID   NBRKB_SCODV             Reviewed;          14 AA.
AC   P0DV01;
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=Beta-scoliidine {ECO:0000303|PubMed:34194483};
DE   Contains:
DE     RecName: Full=Alpha-scoliidine {ECO:0000303|PubMed:34194483};
OS   Scolia decorata ventralis (Solitary wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Scolioidea;
OC   Scoliidae; Scolia; Scolia decorata.
OX   NCBI_TaxID=2856346;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SYNTHESIS, MASS SPECTROMETRY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom;
RX   PubMed=34194483; DOI=10.1590/1678-9199-jvatitd-2020-0171;
RA   Alberto-Silva C., Portaro F.C.V., Kodama R.T., Pantaleao H.Q., Rangel M.,
RA   Nihei K.I., Konno K.;
RT   "Novel neuroprotective peptides in the venom of the solitary scoliid wasp
RT   Scolia decorata ventralis.";
RL   J. Venom. Anim. Toxins Incl. Trop. Dis. 27:e20200171-e20200171(2021).
CC   -!- FUNCTION: [Beta-scoliidine]: Shows general neuroprotective effects
CC       against oxidative stress-induced neurotoxicity in PC12 cells. In fact,
CC       it shows cytotoxic effect after 3 hours of treatment, but it increases
CC       the cell number after 24 to 48 hours, suggesting it increases the cell
CC       rate proliferation. Is similar to bradykinin, but does not behave as
CC       ACE substrate or inhibitor. {ECO:0000269|PubMed:34194483}.
CC   -!- FUNCTION: [Alpha-scoliidine]: In contrast to beta-scoliidine, it does
CC       not show neuroprotective effects against oxidative stress-induced
CC       neurotoxicity in PC12 cells. Is similar to bradykinin, but does not
CC       behave as ACE substrate or inhibitor. {ECO:0000269|PubMed:34194483}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34194483}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:34194483}.
CC   -!- MASS SPECTROMETRY: [Beta-scoliidine]: Mass=1580.88; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:34194483};
CC   -!- MASS SPECTROMETRY: [Alpha-scoliidine]: Mass=1381.75; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:34194483};
CC   -!- MISCELLANEOUS: Both alpha- and beta-scoliidines are the two major
CC       peptide components of the venom. Cleavage products of these peptides
CC       have also been found in the venom but are not shown here.
CC       {ECO:0000269|PubMed:34194483}.
CC   -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..14
FT                   /note="Beta-scoliidine"
FT                   /evidence="ECO:0000269|PubMed:34194483"
FT                   /id="PRO_0000454098"
FT   PEPTIDE         1..12
FT                   /note="Alpha-scoliidine"
FT                   /evidence="ECO:0000269|PubMed:34194483"
FT                   /id="PRO_0000454099"
SQ   SEQUENCE   14 AA;  1581 MW;  2E36EA41F75CEDC8 CRC64;
     DYVTVKGFSP LRKA