ID   AMPU2_AMPCP             Reviewed;          50 AA.
AC   A0A1W6EVN2;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Ampulexin 2 {ECO:0000303|PubMed:29350905};
DE            Short=Axn2 {ECO:0000303|PubMed:29350905};
DE   Flags: Precursor;
OS   Ampulex compressa (Emerald cockroach wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Spheciformes; Ampulicidae; Ampulicini; Ampulex.
OX   NCBI_TaxID=860918 {ECO:0000312|EMBL:ARK19788.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-50, FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:29350905}, and
RC   Venom gland {ECO:0000303|PubMed:29350905};
RX   PubMed=29350905; DOI=10.1021/acs.biochem.7b00916;
RA   Moore E.L., Arvidson R., Banks C., Urenda J.P., Duong E., Mohammed H.,
RA   Adams M.E.;
RT   "Ampulexins: A New Family of Peptides in Venom of the Emerald Jewel Wasp,
RT   Ampulex compressa.";
RL   Biochemistry 57:1907-1916(2018).
RN   [2] {ECO:0000312|EMBL:AUX80732.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Amphipathic peptide which probably adopts an alpha-helical
CC       structure. Has no antimicrobial activity against E.coli DH5alpha or
CC       B.thuringiensis. Is not cytotoxic in vitro.
CC       {ECO:0000269|PubMed:29350905}.
CC   -!- SUBUNIT: Dimer; disulfide-linked. {ECO:0000269|PubMed:29350905}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29350905}.
CC   -!- TISSUE SPECIFICITY: Expressed in venom sac and, to a lesser extent, in
CC       venom gland. Not expressed in brain. {ECO:0000269|PubMed:29350905}.
CC   -!- MASS SPECTROMETRY: Mass=5613; Method=MALDI; Note=Dimer.;
CC       Evidence={ECO:0000269|PubMed:29350905};
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DR   EMBL; MF804415; AUX80732.1; -; mRNA.
DR   EMBL; KY563379; ARK19788.1; -; mRNA.
DR   AlphaFoldDB; A0A1W6EVN2; -.
DR   SMR; A0A1W6EVN2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:29350905"
FT   PEPTIDE         27..50
FT                   /note="Ampulexin 2"
FT                   /evidence="ECO:0000269|PubMed:29350905"
FT                   /id="PRO_0000444896"
FT   DISULFID        40
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305|PubMed:29350905"
SQ   SEQUENCE   50 AA;  5614 MW;  1249BF64295D509F CRC64;
     MKAIMVLFYV MTLTIIGSFS MVSGSPGQND YVNPKLQFAC DLLQKAKERQ