ID   IDGF5_GLOMM             Reviewed;         440 AA.
AC   Q2PQM6;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Chitinase-like protein Idgf5;
DE   AltName: Full=Imaginal disk growth factor protein 5;
DE   Flags: Precursor;
GN   Name=Idgf5;
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 154 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; DQ307197; ABC25097.1; -; mRNA.
DR   AlphaFoldDB; Q2PQM6; -.
DR   SMR; Q2PQM6; -.
DR   STRING; 37546.Q2PQM6; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   VEuPathDB; VectorBase:GMOY009161; -.
DR   PhylomeDB; Q2PQM6; -.
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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..440
FT                   /note="Chitinase-like protein Idgf5"
FT                   /id="PRO_0000291641"
FT   DOMAIN          28..439
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        340..421
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   440 AA;  50108 MW;  D1B547A31A5A2777 CRC64;
     MRNKMIYFNF HLFVIIFANL QIFQVQAANI FCYYDTQRIT DVNAAINYLE PALQFCNFLI
     YGYAGIDGET YQVKSLDYGL NYDIYQAITS LKLKHNRLKV LLSIGGDRDQ TEDLAEDNKY
     LKLLENLSSR NAFINSIQSV IRTYGFDGLD MAWQFPKNPP KHEHSGFRKY LDKLMNLFRR
     SPVIDENSAF HKEQFVSLLT ELRQSLNPMG AIMTMTVLPH VSAELFLDVK PIVNHVDFII
     LATFDYLTPY RDPTIAHYTA PIYAVSEHDP SHNINYDVQY WLNHTTATSK LVLGVPAYGR
     SWTMIKKSGI TGHPPITAGG PGRAGHRTLT AGLLSWPEIC VKIHQNKELE GDAARFRKVS
     DPTKRFGTYA YRSVDENNEY GIWVSYEEPK TAANKAEYAH ARNLSGVALF DLSMDDVTGE
     CGDGTYSILK SIHNAFKKFK