ID   IRP4_AGRIP              Reviewed;          88 AA.
AC   C0HKS5;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Insulin-related peptide 4 {ECO:0000303|PubMed:29466015};
DE            Short=IRP-4 {ECO:0000303|PubMed:29466015};
DE   Contains:
DE     RecName: Full=DAGWWLTRGAARSLGGVR-amide {ECO:0000305|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 48-65, TISSUE SPECIFICITY,
RP   MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT
RP   ARG-65.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: DAGWWLTRGAARSLGGVR-amide: Expressed in corpora
CC       cardiaca (CC), corpora allata (CA), antennal lobe (AL) and gnathal
CC       ganglion (GNG) (at protein level). Expression in CC and CA detected in
CC       most animals, in AL and GNG in few animals (at protein level).
CC       {ECO:0000269|PubMed:29466015}.
CC   -!- MASS SPECTROMETRY: Mass=1928.03; Mass_error=0.01; Method=MALDI;
CC       Note=DAGWWLTRGAARSLGGVR-amide.; Evidence={ECO:0000269|PubMed:29466015};
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- CAUTION: Further mature peptides might exist. {ECO:0000305}.
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DR   AlphaFoldDB; C0HKS5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Neuropeptide; Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..45
FT                   /evidence="ECO:0000305|PubMed:29466015"
FT                   /id="PRO_0000444523"
FT   PEPTIDE         48..65
FT                   /note="DAGWWLTRGAARSLGGVR-amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444524"
FT   PROPEP          69..88
FT                   /evidence="ECO:0000305|PubMed:29466015"
FT                   /id="PRO_0000444525"
FT   MOD_RES         65
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
SQ   SEQUENCE   88 AA;  9682 MW;  085811083EDD7B6E CRC64;
     MKLTLIILLV VAYSWCSEAQ NEARVFCGRV LSERLAALCW GPNSVKRDAG WWLTRGAARS
     LGGVRGKRGL ATECCDKACT VEELLSYC