ID   IDGF1_DROSI             Reviewed;         439 AA.
AC   Q8MX41;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Chitinase-like protein Idgf1;
DE   AltName: Full=Imaginal disk growth factor protein 1;
DE   Flags: Precursor;
GN   Name=Idgf1;
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 150 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; AF394711; AAM69643.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MX41; -.
DR   SMR; Q8MX41; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PRIDE; Q8MX41; -.
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:0040003; P:chitin-based cuticle development; IEA:EnsemblMetazoa.
DR   GO; GO:0018990; P:ecdysis, chitin-based cuticle; IEA:EnsemblMetazoa.
DR   GO; GO:1990399; P:epithelium regeneration; IEA:EnsemblMetazoa.
DR   GO; GO:0007444; P:imaginal disc development; ISS:UniProtKB.
DR   GO; GO:2000035; P:regulation of stem cell division; IEA:EnsemblMetazoa.
DR   GO; GO:0042060; P:wound healing; IEA:EnsemblMetazoa.
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..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..439
FT                   /note="Chitinase-like protein Idgf1"
FT                   /id="PRO_0000011981"
FT   DOMAIN          22..439
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        340..423
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  49441 MW;  22A2671F0B375044 CRC64;
     MRFQLFYILG LLSVTSLTQA ANNLVCYYDS TSYLRQGLAK MHTNELDLAL QFCTHLVYGY
     AGLKSGTLEL FSLNVDLDMF YYKDITALRQ KFPQLKILLS VGGDRDVDEA HPNKYVELLE
     ANRTAQQNFI DSSMILLKRN GFDGLDLAFQ LPRNKPRKVH GSLGTYWKSF KKLFTGDFVV
     DPLAEQHKSQ FTDLVGNIKN AFRSANLMLS LTVLPNVNST WYFDVPKLHP QFDYINLAAF
     DFLTPLRNPE EADYTAPIFF QDEQNRLPHL NVEFQVNYWL QNHCPGQKLN LGIASYGRAW
     KLSKESGLSG APIVHETCGA APGGIQIQSA EGLLSWPEIC SKLSQNASAQ YRGELAPLRK
     VTDLTQKYGN YALRPADENG DFGVWLSFDD PDFAGIKAVY AKSKGLGGIA LFDLSYDDFR
     GLCTGQKYPI VRSIKYFMG