ID   IDGF1_GLOMM             Reviewed;         444 AA.
AC   Q2PQN0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   22-FEB-2023, entry version 65.
DE   RecName: Full=Chitinase-like protein Idgf1;
DE   AltName: Full=Imaginal disk growth factor protein 1;
DE   Flags: Precursor;
GN   Name=Idgf1;
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 157 that
CC       is replaced by a Lys 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; DQ307193; ABC25093.1; -; mRNA.
DR   AlphaFoldDB; Q2PQN0; -.
DR   SMR; Q2PQN0; -.
DR   STRING; 37546.Q2PQN0; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GlyCosmos; Q2PQN0; 3 sites, No reported glycans.
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   Gene3D; 3.20.20.80; Glycosidases; 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; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF235; CHITINASE-LIKE PROTEIN IDGF1-RELATED; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..444
FT                   /note="Chitinase-like protein Idgf1"
FT                   /id="PRO_0000291639"
FT   DOMAIN          29..444
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        346..429
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   444 AA;  50582 MW;  9420CE24FE4510DB CRC64;
     MTSLLFVILN IILTLHLCAG QTPAADNNKR LICYYDAQSY LRPGFAEMKL SFLKTAAEFC
     THLIYGYADL NDDLYEISSL NVDLDMFHYK EITSLKAEFP HLRIYLSIGG DHDNGHYDAG
     KYMRFLESGK DRQNTFIESA IHLLKMNDFD GLDLAFKLPT NKPRKVHSEF GLLWKKFKKL
     FTGDFIVDPD AALHKQQYTE FVGNLARTFR NANLSLTMTV LPNVNSTWYF DVSEIYNNFE
     YINLFSFDFL TPLRNPEEAD YTAPIYLRDE ENRLAHYNID YQMNYWVNHG CPAHKLNLGI
     ATYGRAWKLS AKSGISCKPV VRETLGPAEP GLQSNISGLL SWPEICSKLA ITNGAGYKGA
     DAPVRKVQDL ERLYGNYAFR PADDNDEHGI WISFDDPDFA GIKTNFVKTK FIGGVALYDL
     SYDDFRGLCT GVKFPILRSV RGHL
//