ID   IRP1_AGRIP              Reviewed;          87 AA.
AC   C0HKS3;
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 1 {ECO:0000303|PubMed:29466015};
DE            Short=IRP-1 {ECO:0000303|PubMed:29466015};
DE   Contains:
DE     RecName: Full=DAGWWIPQHGHHALAGVR-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 47-64, TISSUE SPECIFICITY,
RP   MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT
RP   ARG-64.
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: DAGWWIPQHGHHALAGVR-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=2007.02; Mass_error=0.01; Method=MALDI;
CC       Note=DAGWWIPQHGHHALAGVR-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; C0HKS3; -.
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..44
FT                   /evidence="ECO:0000305|PubMed:29466015"
FT                   /id="PRO_0000444517"
FT   PEPTIDE         47..64
FT                   /note="DAGWWIPQHGHHALAGVR-amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444518"
FT   PROPEP          68..87
FT                   /evidence="ECO:0000305|PubMed:29466015"
FT                   /id="PRO_0000444519"
FT   MOD_RES         64
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
SQ   SEQUENCE   87 AA;  9813 MW;  865AD5936C0D8DBF CRC64;
     MKSFMVFVLI FACFSCYYAQ ESTNFYCGRT LSRALAVLCY GAESKRDAGW WIPQHGHHAL
     AGVRGKRGPV DECCEKACSI QELMTYC