FLP5_ISOHA
ID FLP5_ISOHA Reviewed; 10 AA.
AC P0DUV2;
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 Sh5a {ECO:0000303|PubMed:34023397};
DE AltName: Full=FMRFamide-like peptide Sa-112 {ECO:0000303|PubMed:27096870};
DE Short=Sa112 {ECO:0000303|PubMed:34023397};
DE Contains:
DE RecName: Full=FMRFamide-like peptide Sh5b {ECO:0000303|PubMed:31658776};
OS Isodontia harmandi (Grass-carrying wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Spheciformes; Sphecidae; Sphecinae; Sphecina; Isodontia.
OX NCBI_TaxID=2838365;
RN [1]
RP PROTEIN SEQUENCE OF 2-10, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, FUNCTION, SYNTHESIS, AND AMIDATION AT PHE-10.
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 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, AND PARTIAL AMIDATION AT PHE-10.
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: [FMRFamide-like peptide Sh5a]: May be directly involved in a
CC paralyzing effect, by inhibiting muscle contraction, or may also act
CC centrally to modulate prey behaviors (Probable). Inhibits both the
CC frequency and amplitude of spontaneous contractions of the locust
CC oviducts (tested at 50 nM) (Ref.2). {ECO:0000269|Ref.2,
CC ECO:0000305|PubMed:34023397}.
CC -!- FUNCTION: [FMRFamide-like peptide Sh5b]: Does not produce consistent
CC and reproducible effects on ASIC currents (PubMed:31658776). Inhibits
CC spontaneous oviduct contractions to the same extent as that of
CC SchistoFLRFamide (Probable). {ECO:0000269|PubMed:31658776,
CC ECO:0000305|PubMed:34023397}.
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: Both the long peptide (Sh5a) and the short peptide (Sh5b) (residue
CC 2-10) are amidated. {ECO:0000269|PubMed:31658776}.
CC -!- MASS SPECTROMETRY: Mass=1274.6; Method=MALDI; Note=Sh5a, Monoisotopic
CC mass.; Evidence={ECO:0000269|PubMed:34023397};
CC -!- MASS SPECTROMETRY: Mass=1145.6; Method=MALDI; Note=Sh5b, Monoisotopic
CC 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:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Neurotoxin; Secreted; Toxin.
FT PEPTIDE 1..10
FT /note="FMRFamide-like peptide Sh5a"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000453657"
FT PEPTIDE 2..10
FT /note="FMRFamide-like peptide Sh5b"
FT /evidence="ECO:0000269|PubMed:31658776"
FT /id="PRO_0000453658"
FT MOD_RES 10
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:31658776"
SQ SEQUENCE 10 AA; 1276 MW; D3D51629D2C1EAB2 CRC64;
EDVDHVFLRF