ID   IDGF4_GLOMM             Reviewed;         444 AA.
AC   Q2PQM7;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Chitinase-like protein Idgf4;
DE   AltName: Full=Imaginal disk growth factor protein 4;
DE   Flags: Precursor;
GN   Name=Idgf4;
OS   Glossina morsitans morsitans (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fat body;
RX   PubMed=16907828; DOI=10.1111/j.1365-2583.2006.00649.x;
RA   Attardo G.M., Strickler-Dinglasan P., Perkin S.A.H., Caler E.,
RA   Bonaldo M.F., Soares M.B., El-Sayeed N.M.A., Aksoy S.;
RT   "Analysis of fat body transcriptome from the adult tsetse fly, Glossina
RT   morsitans morsitans.";
RL   Insect Mol. Biol. 15:411-424(2006).
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}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Lacks the typical Glu active site in position 158 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; DQ307196; ABC25096.1; -; mRNA.
DR   AlphaFoldDB; Q2PQM7; -.
DR   SMR; Q2PQM7; -.
DR   STRING; 37546.Q2PQM7; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   Proteomes; UP000092444; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Developmental protein; Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..444
FT                   /note="Chitinase-like protein Idgf4"
FT                   /id="PRO_0000291640"
FT   DOMAIN          27..444
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        345..428
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   444 AA;  49075 MW;  B38A67FB15104175 CRC64;
     MKLLLILLGA LLAVLTIKRT SAVQGSNHLI CYYDGTSYTR EGLAKLTLND LEPALQFCTH
     LVYGHAAINP SSNKLVSNNE KLDLDVGTGL YRTITGMKKK YPHLKVLLSV GGDKDEVDAD
     NNKYLTLLES SNARIPFINS AHSMVKTYGF DGLELGWQFP KNKPKKVHGS IGKLWKGFKK
     IFTGDFIVDE KAEEHKEEFT ALVRELKNAL RPDGYILGLA VLPNVNSSLF YDVPAIVNNL
     DYVNLMAYDF QTPQRNPEMA DFPAPIYELN ERNPESNVNY QVQYWLQNHC PASKINVGIP
     SYGRAWKMTT DSGLTGLPPV SDADGPAAGG LQTQTEGLLS WPEVCAKLPN PANQHLKGAD
     SPLRKVGDPT KRFGNYAYRS TDDKGENGIW VSYEDPDTAA NKAAYVKTKG LGGVALVDLS
     FDDFRGACTG DKYPILRAIK FKFQ