ID   DIUX_AGRIP              Reviewed;         112 AA.
AC   C0HKT3;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Diuretic hormone class 2 {ECO:0000250|UniProtKB:P85826};
DE   AltName: Full=DH(31) {ECO:0000303|PubMed:29466015};
DE   AltName: Full=Diuretic peptide {ECO:0000250|UniProtKB:P82372};
DE            Short=DP {ECO:0000250|UniProtKB:P82372};
DE   Flags: Precursor;
OS   Agrotis ipsilon (Black cutworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Noctuinae; Noctuini; Agrotis.
OX   NCBI_TaxID=56364;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 74-104, TISSUE SPECIFICITY,
RP   MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT
RP   PRO-104.
RX   PubMed=29466015; DOI=10.1021/acs.jproteome.7b00779;
RA   Diesner M., Gallot A., Binz H., Gaertner C., Vitecek S., Kahnt J.,
RA   Schachtner J., Jacquin-Joly E., Gadenne C.;
RT   "Mating-induced differential peptidomics of neuropeptides and protein
RT   hormones in Agrotis ipsilon moths.";
RL   J. Proteome Res. 17:1397-1414(2018).
CC   -!- FUNCTION: Regulation of fluid secretion. Stimulates Malpighian tubule
CC       fluid secretion. {ECO:0000250|UniProtKB:P85826}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in corpora cardiaca (CC), corpora allata
CC       (CA), antennal lobe (AL) and gnathal ganglion (GNG) (at protein level).
CC       Expression in CC, CA and AL detected in most animals, expression in GNG
CC       in few animals (at protein level). {ECO:0000269|PubMed:29466015}.
CC   -!- MASS SPECTROMETRY: Mass=3042.65; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29466015};
CC   -!- SIMILARITY: Belongs to the diuretic hormone class 2 family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HKT3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008613; F:diuretic hormone activity; IEA:InterPro.
DR   GO; GO:0007589; P:body fluid secretion; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR034439; DH2-like.
DR   PANTHER; PTHR41146; PTHR41146; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Hormone; Neuropeptide; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..71
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444226"
FT   PEPTIDE         74..104
FT                   /note="Diuretic hormone class 2"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444227"
FT   PROPEP          108..112
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444228"
FT   MOD_RES         104
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
SQ   SEQUENCE   112 AA;  12626 MW;  C69BB6E9FF56D6F3 CRC64;
     MVRATCLLAS CVLFALLLIV PASAYPRYPS NYFREEGQYE PEEIMDMLNR LGNLIQMERK
     MENYKEDITS EKRALDLGLS RGYSGALQAK HLMGLAAANY AGGPGRRRRD AH