ID   IDGF3_DROSI             Reviewed;         441 AA.
AC   Q8MX32;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Chitinase-like protein Idgf3;
DE   AltName: Full=Imaginal disk growth factor protein 3;
DE   Flags: Precursor;
GN   Name=Idgf3;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=5F;
RX   PubMed=12242232; DOI=10.1093/genetics/162.1.177;
RA   Zurovcova M., Ayala F.J.;
RT   "Polymorphism patterns in two tightly linked developmental genes, Idgf1 and
RT   Idgf3, of Drosophila melanogaster.";
RL   Genetics 162:177-188(2002).
CC   -!- FUNCTION: Cooperates with insulin-like peptides to stimulate the
CC       proliferation, polarization and motility of imaginal disk cells. May
CC       act by stabilizing the binding of insulin-like peptides to its receptor
CC       through a simultaneous interaction with both molecules to form a
CC       multiprotein signaling complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted in
CC       hemolymph. It is probably transported to target tissues via hemolymph.
CC       {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Lacks the typical Glu active site in position 153 that
CC       is replaced by a Gln residue, preventing the hydrolase activity. Its
CC       precise function remains unclear.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. IDGF
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF394733; AAM69665.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MX32; -.
DR   SMR; Q8MX32; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   EnsemblMetazoa; FBtr0223968; FBpp0222460; FBgn0044199.
DR   Bgee; FBgn0044199; Expressed in adult organism and 3 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0008084; F:imaginal disc growth factor receptor binding; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0007444; P:imaginal disc development; ISS:UniProtKB.
DR   CDD; cd02873; GH18_IDGF; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR015520; IDGF.
DR   PANTHER; PTHR11177:SF235; PTHR11177:SF235; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF54556; SSF54556; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Developmental protein; Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..441
FT                   /note="Chitinase-like protein Idgf3"
FT                   /id="PRO_0000011985"
FT   DOMAIN          25..441
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          310..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        342..425
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   441 AA;  49080 MW;  702889633CD4D5A0 CRC64;
     MSGSLWLSLA LSLAVLAQFK VSAAPNLVCF YDSQGSQRQG LAQFSITDIE LALQFCTHLV
     YGYAGVNADN FEMQSINKRL DLEQRHLAQV TSMKERYPHI KFLLSVGGDA DTNEGNQYIK
     LLESGQQGHR RFIESARDLV RRYNFDGLDL ALQLPRNKPR KVHGDVGSAW KSFKKFFTGD
     YIVDTESETH KGQVTALIKD LSAALKQNDL LLSLTVLPNV NSSWYYDAPS IAPSLDFINL
     GTFDFLTPQR NPEEADFSAP TYEAVGQNRL GHYNLNFQME HWLLQRVPAN KINIGIATYG
     RTWKMSKDSG DSGMPVVSST QGPAPAGPQS KQEGLLNWAE ICSLMPNPSN SNARGPNAPV
     KRVVDPTKRY GSYAFRAADE NGDHGLWISY DDPDSGSSKA MYARARNLGG VALFDLTQDD
     FRGQCTGDRF PMLRAIKYRL L