ID   IDGF3_DROYA             Reviewed;         441 AA.
AC   Q8MX31;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Chitinase-like protein Idgf3;
DE   AltName: Full=Imaginal disk growth factor protein 3;
DE   Flags: Precursor;
GN   Name=Idgf3;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=#14021-0261.0;
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; AF394734; AAM69666.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MX31; -.
DR   SMR; Q8MX31; -.
DR   STRING; 7245.FBpp0258119; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   eggNOG; KOG2806; Eukaryota.
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_0000011986"
FT   DOMAIN          25..441
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          309..331
FT                   /note="Disordered"
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;  49193 MW;  1FF36DAE58B81680 CRC64;
     MTGSLWLSLA LSLAVLAQFK VSAAPNLVCF YDSQGFQRQG LAQFSMTDME LALQFCTHLV
     YGYAGVNADN YEMQSINKRL DLEQRHLAQV SSLKERYPHI KFLLSVGGDA DTNEGNQYIK
     LLESGQQGHR RFIESARDLV RRYNFDGLDL ALQLPRNKPR KVHGDVGSAW KSFKKFFTGD
     FIVDTDSETH KGQVTALIKD LSAALKQNDL LLSLTVLPNV NSSWYYDAPS IAPSLDFINL
     GTFDFLTPQR NPEEADFSAP TYEAVGQNRL GHYNLNFQTE HWLLQRVPAN KINIGIATYG
     RTWKMTKDSG DSGMPVVPST QGPAPAGPQS KKEGLLNWAE ICSLMPNPGN TNARGPSAPV
     KRVLDPTKRY GSYAFRAADE NGDHGLWISY DDPDSASSKA MFARVRNLGG VALFDLTQDD
     FRGQCTNDRF PMLRAIKYRL L