ID   FLP12_SPHAA             Reviewed;          10 AA.
AC   P0DUV1;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   23-FEB-2022, entry version 2.
DE   RecName: Full=FMRFamide-like peptide Sa12b {ECO:0000303|PubMed:31658776};
DE            Short=Sa-12 {ECO:0000303|PubMed:27096870};
DE            Short=Sa12b {ECO:0000303|PubMed:34023397};
DE   AltName: Full=Sa-112 {ECO:0000303|PubMed:27096870};
DE            Short=Sa112 {ECO:0000303|PubMed:34023397};
OS   Sphex argentatus argentatus (Black digger wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Spheciformes; Sphecidae; Sphecinae; Sphecina; Sphex.
OX   NCBI_TaxID=2838366;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, FUNCTION, AND SYNTHESIS.
RC   TISSUE=Venom;
RX   PubMed=31658776; DOI=10.3390/toxins11100585;
RA   Hernandez C., Konno K., Salceda E., Vega R., Zaharenko A.J., Soto E.;
RT   "Sa12b peptide from solitary wasp inhibits ASIC currents in rat dorsal root
RT   ganglion neurons.";
RL   Toxins 11:0-0(2019).
RN   [2]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, FUNCTION, AND PARTIAL AMIDATION AT PHE-10.
RA   Nihei K.-I., Kazuma K., Ando K., Konno K.;
RT   "96. Chemical and biological characterization of a novel neuropeptide in
RT   the venom of solitary digger wasp.";
RL   Toxicon 60:144-144(2012).
RN   [3]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, PARTIAL AMIDATION AT PHE-10, MASS
RP   SPECTROMETRY, SYNTHESIS, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=34023397; DOI=10.1016/j.peptides.2021.170575;
RA   Nihei K.I., Peigneur S., Tytgat J., Lange A.B., Konno K.;
RT   "Isolation and characterization of FMRFamide-like peptides in the venoms of
RT   solitary sphecid wasps.";
RL   Peptides 142:170575-170575(2021).
RN   [4]
RP   REVIEW.
RX   PubMed=27096870; DOI=10.3390/toxins8040114;
RA   Konno K., Kazuma K., Nihei K.;
RT   "Peptide toxins in solitary wasp venoms.";
RL   Toxins 8:114-114(2016).
CC   -!- FUNCTION: May be directly involved in a paralyzing effect, by
CC       inhibiting muscle contraction, or may also act centrally to modulate
CC       prey behaviors (Probable). The non-amidated form (Sa12b) potently
CC       inhibits ASIC current in rat DRG neurons (IC(50)=81 nM) when
CC       preincubated before activation by acidic pH (PubMed:31658776). Has no
CC       consistent action on the time course of desensitization or the
CC       sustained component of the current (PubMed:31658776). Has no activity
CC       when coapplied with acidic pH, suggesting that the peptide needs to
CC       interact with the channel during its closed state (PubMed:31658776).
CC       This effect is concentration-dependent and reversed after washout of
CC       the peptide (PubMed:31658776). Since the inhibition is almost complete
CC       at 1 uM and all ASIC subunits are expressed in dorsal root ganglion
CC       (DRG) neurons, it suggests that it inhibits different ASIC subunits
CC       without an apparent selectivity (PubMed:31658776). It is noteworthy
CC       that it does not show activity on the locust oviduct contraction
CC       (tested at 50 nM), in contrast to the amidated form (Ref.2,
CC       PubMed:34023397). {ECO:0000269|PubMed:31658776,
CC       ECO:0000269|PubMed:34023397, ECO:0000269|Ref.2,
CC       ECO:0000305|PubMed:34023397}.
CC   -!- FUNCTION: The amidated form (Sa112) inhibits both the frequency and
CC       amplitude of spontaneous contractions of the locust oviducts (tested at
CC       50 nM). {ECO:0000269|PubMed:34023397, ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31658776,
CC       ECO:0000269|PubMed:34023397, ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:31658776, ECO:0000305|PubMed:34023397,
CC       ECO:0000305|Ref.2}.
CC   -!- PTM: Is either amidated (Sa112) or non-amidated (Sa12b).
CC       {ECO:0000305|PubMed:27096870, ECO:0000305|PubMed:34023397}.
CC   -!- MASS SPECTROMETRY: Mass=1274.7; Method=MALDI; Note=amidated form
CC       (Sa112), Monoisotopic mass.; Evidence={ECO:0000269|PubMed:34023397};
CC   -!- MASS SPECTROMETRY: Mass=1275.6; Method=MALDI; Note=non-amidated form
CC       (Sa12b), Monoisotopic mass.; Evidence={ECO:0000269|PubMed:34023397};
CC   -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Ion channel impairing toxin;
KW   Neurotoxin; Proton-gated sodium channel impairing toxin; Secreted; Toxin.
FT   PEPTIDE         1..10
FT                   /note="FMRFamide-like peptide Sa12b"
FT                   /evidence="ECO:0000269|PubMed:31658776, ECO:0000269|Ref.2"
FT                   /id="PRO_0000453656"
FT   MOD_RES         10
FT                   /note="Phenylalanine amide; partial"
FT                   /evidence="ECO:0000269|PubMed:31658776, ECO:0000269|Ref.2,
FT                   ECO:0000305|PubMed:27096870"
SQ   SEQUENCE   10 AA;  1276 MW;  D3D51629D2C1EAB2 CRC64;
     EDVDHVFLRF