INSL5_DROME
ID INSL5_DROME Reviewed; 108 AA.
AC Q7KUD5; Q6ILJ3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable insulin-like peptide 5;
DE Short=dILP5;
DE AltName: Full=Insulin-related peptide 5;
DE Contains:
DE RecName: Full=Probable insulin-like peptide 5 A chain;
DE Contains:
DE RecName: Full=Probable insulin-like peptide 5 B chain;
DE Flags: Precursor;
GN Name=Ilp5 {ECO:0000312|FlyBase:FBgn0044048};
GN Synonyms=HDC09365 {ECO:0000312|EMBL:DAA02868.1}; ORFNames=CG33273;
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] {ECO:0000312|EMBL:AAS65048.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAS65048.1}
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] {ECO:0000305}
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).
RN [4] {ECO:0000305, ECO:0000312|EMBL:DAA02868.1}
RP IDENTIFICATION.
RX PubMed=14709175; DOI=10.1186/gb-2003-5-1-r3;
RA Hild M., Beckmann B., Haas S.A., Koch B., Solovyev V., Busold C.,
RA Fellenberg K., Boutros M., Vingron M., Sauer F., Hoheisel J.D., Paro R.;
RT "An integrated gene annotation and transcriptional profiling approach
RT towards the full gene content of the Drosophila genome.";
RL Genome Biol. 5:R3.1-R3.17(2003).
CC -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC disulfide bonds. {ECO:0000250|UniProtKB:P01308}.
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 Expressed at a moderate level in the larval gut.
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:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS65048.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014296; AAS65048.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK002023; DAA02868.1; -; Genomic_DNA.
DR RefSeq; NP_996037.1; NM_206315.2.
DR PDB; 2WFU; X-ray; 1.85 A; A=87-108, B=24-47.
DR PDB; 2WFV; X-ray; 1.85 A; A=84-108, B=24-46.
DR PDB; 6FEY; X-ray; 3.48 A; E/G/I/K=84-108, F/H/J/L=24-51.
DR PDBsum; 2WFU; -.
DR PDBsum; 2WFV; -.
DR PDBsum; 6FEY; -.
DR AlphaFoldDB; Q7KUD5; -.
DR SMR; Q7KUD5; -.
DR BioGRID; 77841; 8.
DR STRING; 7227.FBpp0076100; -.
DR PaxDb; Q7KUD5; -.
DR DNASU; 2768992; -.
DR EnsemblMetazoa; FBtr0472645; FBpp0422627; FBgn0044048.
DR GeneID; 2768992; -.
DR KEGG; dme:Dmel_CG33273; -.
DR CTD; 2768992; -.
DR FlyBase; FBgn0044048; Ilp5.
DR VEuPathDB; VectorBase:FBgn0044048; -.
DR HOGENOM; CLU_125164_0_1_1; -.
DR InParanoid; Q7KUD5; -.
DR OrthoDB; 1644517at2759; -.
DR Reactome; R-DME-110478; Insulin signaling pathway.
DR SignaLink; Q7KUD5; -.
DR BioGRID-ORCS; 2768992; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; Q7KUD5; -.
DR GenomeRNAi; 2768992; -.
DR PRO; PR:Q7KUD5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0044048; Expressed in brain and 12 other tissues.
DR ExpressionAtlas; Q7KUD5; baseline and differential.
DR Genevisible; Q7KUD5; DM.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0005158; F:insulin receptor binding; IPI:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0033500; P:carbohydrate homeostasis; IDA:FlyBase.
DR GO; GO:0060180; P:female mating behavior; IMP:FlyBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:FlyBase.
DR GO; GO:0061964; P:negative regulation of entry into reproductive diapause; IMP:FlyBase.
DR GO; GO:0030431; P:sleep; 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 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..108
FT /note="Probable insulin-like peptide 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016201"
FT PEPTIDE 23..50
FT /note="Probable insulin-like peptide 5 B chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016202"
FT PROPEP 53..81
FT /note="Connecting peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016203"
FT PEPTIDE 84..108
FT /note="Probable insulin-like peptide 5 A chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016204"
FT DISULFID 29..93
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT DISULFID 41..106
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT DISULFID 92..97
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:2WFU"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6FEY"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2WFU"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:2WFU"
SQ SEQUENCE 108 AA; 11972 MW; 897675835FF76552 CRC64;
MMFRSVIPVL LFLIPLLLSA QAANSLRACG PALMDMLRVA CPNGFNSMFA KRGTLGLFDY
EDHLADLDSS ESHHMNSLSS IRRDFRGVVD SCCRKSCSFS TLRAYCDS
