ID   IRP2_AGRIP              Reviewed;          86 AA.
AC   C0HKS4;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Insulin-related peptide 2 {ECO:0000303|PubMed:29466015};
DE            Short=IRP-2 {ECO:0000303|PubMed:29466015};
DE   Contains:
DE     RecName: Full=DAGWWVPPQSARALGGGR-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 46-63, TISSUE SPECIFICITY,
RP   MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT
RP   ARG-63.
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: DAGWWVPPQSARALGGGR-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 in some animals and in GNG in few animals (at
CC       protein level). {ECO:0000269|PubMed:29466015}.
CC   -!- MASS SPECTROMETRY: Mass=1879.94; Mass_error=0.01; Method=MALDI;
CC       Note=DAGWWVPPQSARALGGGR-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; C0HKS4; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR017097; Bombyxin.
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; PR02003; BOMBYXIN.
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..43
FT                   /evidence="ECO:0000305|PubMed:29466015"
FT                   /id="PRO_0000444520"
FT   PEPTIDE         46..63
FT                   /note="DAGWWVPPQSARALGGGR-amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444521"
FT   PROPEP          67..86
FT                   /evidence="ECO:0000305|PubMed:29466015"
FT                   /id="PRO_0000444522"
FT   MOD_RES         63
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
SQ   SEQUENCE   86 AA;  9440 MW;  214C3330F4801E62 CRC64;
     MKFYIVFALI LACAACVSSQ EGTNFYCGRQ LSRTLALVCW GAEKRDAGWW VPPQSARALG
     GGRGKRGPVD ECCLKPCSIE EMLTYC