ID   AKH2_AGRIP              Reviewed;          73 AA.
AC   C0HKR1;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Adipokinetic prohormone type 2 {ECO:0000305|PubMed:29466015};
DE   Contains:
DE     RecName: Full=Adipokinetic hormone 2 {ECO:0000303|PubMed:29466015};
DE              Short=AKH-2 {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   ASN-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 corpora cardiaca (CC), corpora allata
CC       (CA) and gnathal ganglion (GNG) (at protein level). Expression in CC
CC       and CA detected in all animals, expression in GNG detected in few
CC       animals (at protein level). Not expressed in antennal lobe (AL) (at
CC       protein level). {ECO:0000269|PubMed:29466015}.
CC   -!- MASS SPECTROMETRY: Mass=1100.47; 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: Further mature peptides might exist. {ECO:0000305}.
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DR   AlphaFoldDB; C0HKR1; -.
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:0000269|PubMed:29466015"
FT   PEPTIDE         21..30
FT                   /note="Adipokinetic hormone 2"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444513"
FT   PROPEP          34..73
FT                   /evidence="ECO:0000305|PubMed:29466015"
FT                   /id="PRO_0000444514"
FT   MOD_RES         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT   MOD_RES         30
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
SQ   SEQUENCE   73 AA;  8146 MW;  D892708E9C723940 CRC64;
     MCRIFIVLLV VAALAIIIEG QLTFSSGWGN GKRSISSEQI NDDCNPEEAI FQIYKLIVSE
     GERIRACQRD GKM