INSL2_DROME
ID INSL2_DROME Reviewed; 137 AA.
AC Q9VT51;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Probable insulin-like peptide 2;
DE Short=dILP2;
DE AltName: Full=Insulin-related peptide 2;
DE Contains:
DE RecName: Full=Probable insulin-like peptide 2 A chain;
DE Contains:
DE RecName: Full=Probable insulin-like peptide 2 B chain;
DE Flags: Precursor;
GN Name=Ilp2; Synonyms=IRP; ORFNames=CG8167;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11179818; DOI=10.1016/s0196-9781(00)00376-4;
RA Vanden Broeck J.J.M.;
RT "Neuropeptides and their precursors in the fruitfly, Drosophila
RT melanogaster.";
RL Peptides 22:241-254(2001).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, 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: Plays a role in regulating body size by increasing cell size
CC and cell number of individual organs. Probably mediates its growth
CC effects by acting as a ligand for the insulin receptor and transducing
CC a signal via the Chico/PI3K/Akt(PKB) pathway.
CC {ECO:0000269|PubMed:11250149}.
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: Broadly expressed at a low level in the embryonic
CC mesoderm, beginning at stage 12. Expressed at a high level in the
CC embryonic anterior midgut, with expression diminishing at late stage
CC 16. Expressed at a low level in larval imaginal disks. Expressed at a
CC high level in larval salivary glands and in seven cells of each larval
CC brain hemisphere that may correspond to neurosecretory cells.
CC {ECO:0000269|PubMed:11250149}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo and larva.
CC {ECO:0000269|PubMed:11250149}.
CC -!- MISCELLANEOUS: Of the insulin-like peptides, Ilp2 is the closest
CC homolog of human insulin.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR EMBL; AJ291726; CAC17605.1; -; mRNA.
DR EMBL; AE014296; AAF50204.1; -; Genomic_DNA.
DR EMBL; AY069095; AAL39240.1; -; mRNA.
DR RefSeq; NP_524012.1; NM_079288.3.
DR AlphaFoldDB; Q9VT51; -.
DR BioGRID; 64538; 13.
DR STRING; 7227.FBpp0076058; -.
DR PaxDb; Q9VT51; -.
DR DNASU; 39150; -.
DR EnsemblMetazoa; FBtr0076329; FBpp0076058; FBgn0036046.
DR GeneID; 39150; -.
DR KEGG; dme:Dmel_CG8167; -.
DR CTD; 39150; -.
DR FlyBase; FBgn0036046; Ilp2.
DR VEuPathDB; VectorBase:FBgn0036046; -.
DR eggNOG; ENOG502T6SN; Eukaryota.
DR HOGENOM; CLU_125164_0_1_1; -.
DR InParanoid; Q9VT51; -.
DR OMA; CKEFNSV; -.
DR OrthoDB; 1644517at2759; -.
DR PhylomeDB; Q9VT51; -.
DR Reactome; R-DME-110478; Insulin signaling pathway.
DR SignaLink; Q9VT51; -.
DR BioGRID-ORCS; 39150; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39150; -.
DR PRO; PR:Q9VT51; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036046; Expressed in brain and 11 other tissues.
DR ExpressionAtlas; Q9VT51; baseline and differential.
DR Genevisible; Q9VT51; DM.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0005158; F:insulin receptor binding; IGI:UniProtKB.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0033500; P:carbohydrate homeostasis; IMP:FlyBase.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0060180; P:female mating behavior; IMP:FlyBase.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR GO; GO:0042593; P:glucose homeostasis; IGI:FlyBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0030536; P:larval feeding behavior; 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:2000252; P:negative regulation of feeding behavior; IMP:FlyBase.
DR GO; GO:0045818; P:negative regulation of glycogen catabolic process; IDA:FlyBase.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:FlyBase.
DR GO; GO:0008361; P:regulation of cell size; IMP:FlyBase.
DR GO; GO:0040009; P:regulation of growth rate; IMP:FlyBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0046620; P:regulation of organ growth; IMP:UniProtKB.
DR GO; GO:1990928; P:response to amino acid starvation; IEP:FlyBase.
DR GO; GO:0032094; P:response to food; IEP:FlyBase.
DR GO; GO:0030431; P:sleep; IMP:FlyBase.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:FlyBase.
DR InterPro; IPR016179; Insulin-like.
DR InterPro; IPR036438; Insulin-like_sf.
DR InterPro; IPR040228; Insulin-relat-peptide_inver.
DR InterPro; IPR022353; Insulin_CS.
DR InterPro; IPR022352; Insulin_family.
DR PANTHER; PTHR13647; PTHR13647; 1.
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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Growth factor;
KW Growth regulation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..137
FT /note="Probable insulin-like peptide 2"
FT /id="PRO_0000016189"
FT PEPTIDE 27..50
FT /note="Probable insulin-like peptide 2 B chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016190"
FT PROPEP 53..104
FT /note="Connecting peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016191"
FT PEPTIDE 108..137
FT /note="Probable insulin-like peptide 2 A chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016192"
FT DISULFID 29..119
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 41..132
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 118..123
FT /evidence="ECO:0000250"
SQ SEQUENCE 137 AA; 15255 MW; F5B2A357D7B653D6 CRC64;
MSKPLSFISM VAVILLASST VKLAQGTLCS EKLNEVLSMV CEEYNPVIPH KRAMPGADSD
LDALNPLQFV QEFEEEDNSI SEPLRSALFP GSYLGGVLNS LAEVRRRTRQ RQGIVERCCK
KSCDMKALRE YCSVVRN
