ID   AKH1B_AGRIP             Reviewed;          68 AA.
AC   C0HL92; C0HKR0;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Adipokinetic prohormone type 1 {ECO:0000250|UniProtKB:P55319};
DE   Contains:
DE     RecName: Full=Adipokinetic hormone 1 {ECO:0000303|PubMed:29466015};
DE              Short=AKH-1 {ECO:0000303|PubMed:29466015};
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 21-30, TISSUE SPECIFICITY,
RP   MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AMIDATION AT
RP   GLY-30, AND PYROGLUTAMATE FORMATION AT GLN-21.
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: This hormone, released from cells in the corpora cardiaca,
CC       causes release of diglycerides from the fat body and stimulation of
CC       muscles to use these diglycerides as an energy source during energy-
CC       demanding processes. {ECO:0000250|UniProtKB:P55319}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in antennal lobe (AL), corpora cardiaca
CC       (CC), corpora allata (CA) and gnathal ganglion (GNG) (at protein
CC       level). Expression in CC and CA detected in all animals, expression in
CC       GNG in some animals and in AL in few animals (at protein level).
CC       {ECO:0000269|PubMed:29466015}.
CC   -!- MASS SPECTROMETRY: Mass=1087.49; Mass_error=0.01; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29466015};
CC   -!- SIMILARITY: Belongs to the AKH/HRTH/RPCH family. {ECO:0000305}.
CC   -!- CAUTION: The mature peptide AKH-1 is also encoded by another precursor
CC       (AC C0HL91). {ECO:0000305}.
CC   -!- CAUTION: Further mature peptides might exist. {ECO:0000305}.
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DR   AlphaFoldDB; C0HL92; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR002047; Adipokinetic_hormone_CS.
DR   InterPro; IPR010475; AKH/RPCH_hormone.
DR   Pfam; PF06377; Adipokin_hormo; 1.
DR   PROSITE; PS00256; AKH; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Hormone; Neuropeptide; Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         21..30
FT                   /note="Adipokinetic hormone 1"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444167"
FT   PROPEP          34..68
FT                   /evidence="ECO:0000305|PubMed:29466015"
FT                   /id="PRO_0000444168"
FT   MOD_RES         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT   MOD_RES         30
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
SQ   SEQUENCE   68 AA;  7602 MW;  355B263A042793BD CRC64;
     MNKIYFVIVF VACFCLFAEA QLTFTSSWGG GKRSGVAPMS CKNEEAVATI FKLIQNEAER
     FIICQQKS