ID   INSL3_DROME             Reviewed;         120 AA.
AC   Q9VT52;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   02-SEP-2026, entry version 158.
DE   RecName: Full=Insulin-like peptide 3 {ECO:0000312|FlyBase:FBgn0044050};
DE            Short=dILP3;
DE   AltName: Full=Insulin-related peptide 3;
DE   Contains:
DE     RecName: Full=Insulin-like peptide 3 A chain;
DE   Contains:
DE     RecName: Full=Insulin-like peptide 3 B chain;
DE   Flags: Precursor;
GN   Name=Ilp3 {ECO:0000312|FlyBase:FBgn0044050};
GN   ORFNames=CG14167 {ECO:0000312|FlyBase:FBgn0044050};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   IDENTIFICATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11250149; DOI=10.1016/s0960-9822(01)00068-9;
RA   Brogiolo W., Stocker H., Ikeya T., Rintelen F., Fernandez R., Hafen E.;
RT   "An evolutionarily conserved function of the Drosophila insulin receptor
RT   and insulin-like peptides in growth control.";
RL   Curr. Biol. 11:213-221(2001).
CC   -!- FUNCTION: Possible ligand of InR/insulin-like receptor. {ECO:0000305}.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed at a high level in seven cells of each
CC       larval brain hemisphere that may correspond to neurosecretory cells.
CC       {ECO:0000269|PubMed:11250149}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the larva, but not in the embryo.
CC       {ECO:0000269|PubMed:11250149}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AE014296; AAF50203.2; -; Genomic_DNA.
DR   RefSeq; NP_648360.2; NM_140103.3.
DR   AlphaFoldDB; Q9VT52; -.
DR   BioGRID; 64539; 2.
DR   FunCoup; Q9VT52; 263.
DR   STRING; 7227.FBpp0076102; -.
DR   PaxDb; 7227-FBpp0076102; -.
DR   PeptideAtlas; Q9VT52; -.
DR   DNASU; 39151; -.
DR   EnsemblMetazoa; FBtr0076373; FBpp0076102; FBgn0044050.
DR   GeneID; 39151; -.
DR   KEGG; dme:Dmel_CG14167; -.
DR   AGR; FB:FBgn0044050; -.
DR   CTD; 39151; -.
DR   FlyBase; FBgn0044050; Ilp3.
DR   VEuPathDB; VectorBase:FBgn0044050; -.
DR   eggNOG; ENOG502S3FQ; Eukaryota.
DR   HOGENOM; CLU_125164_0_1_1; -.
DR   InParanoid; Q9VT52; -.
DR   OMA; VYGFNAM; -.
DR   OrthoDB; 10019596at2759; -.
DR   PhylomeDB; Q9VT52; -.
DR   Reactome; R-DME-110478; Insulin signaling pathway.
DR   SignaLink; Q9VT52; -.
DR   BioGRID-ORCS; 39151; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 39151; -.
DR   PRO; PR:Q9VT52; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0044050; Expressed in central nervous system and 17 other cell types or tissues.
DR   ExpressionAtlas; Q9VT52; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0005158; F:insulin receptor binding; ISS:UniProtKB.
DR   GO; GO:0060180; P:female mating behavior; IMP:FlyBase.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IMP:FlyBase.
DR   GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR   GO; GO:0061964; P:negative regulation of entry into reproductive diapause; IMP:FlyBase.
DR   GO; GO:0009743; P:response to carbohydrate; IEP:FlyBase.
DR   GO; GO:0030431; P:sleep; IMP:FlyBase.
DR   CDD; cd04366; IlGF_insulin_bombyxin_like; 1.
DR   FunFam; 1.10.100.10:FF:000010; GM24840; 1.
DR   Gene3D; 1.10.100.10; Insulin-like; 1.
DR   InterPro; IPR022352; Ins/IGF/rlx.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   PANTHER; PTHR13647:SF4; INSULIN-LIKE PEPTIDE 1-RELATED; 1.
DR   PANTHER; PTHR13647; INSULIN-LIKE PEPTIDE 2-RELATED; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; Insulin-like; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..120
FT                   /note="Insulin-like peptide 3"
FT                   /id="PRO_0000016193"
FT   PEPTIDE         30..48
FT                   /note="Insulin-like peptide 3 B chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016194"
FT   PROPEP          51..89
FT                   /note="Connecting peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016195"
FT   PEPTIDE         92..120
FT                   /note="Insulin-like peptide 3 A chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016196"
FT   DISULFID        34..101
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..114
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        100..105
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   120 AA;  13708 MW;  FA834C8BAE1CE31B CRC64;
     MGIEMRCQDR RILLPSLLLL ILMIGGVQAT MKLCGRKLPE TLSKLCVYGF NAMTKRTLDP
     VNFNQIDGFE DRSLLERLLS DSSVQMLKTR RLRDGVFDEC CLKSCTMDEV LRYCAAKPRT
//