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Database: UniProt
Entry: IDGF1_DROME
LinkDB: IDGF1_DROME
Original site: IDGF1_DROME 
ID   IDGF1_DROME             Reviewed;         439 AA.
AC   Q8MM24; O96664; Q8MM30; Q8MM31; Q8MM38; Q8MM92; Q8MX42; Q8MX43; Q8MX44;
AC   Q8MX45; Q8MX46; Q8MX47; Q8MX48; Q8MX49; Q8MX50; Q9V3P8;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Chitinase-like protein Idgf1;
DE   AltName: Full=Imaginal disk growth factor protein 1;
DE   Flags: Precursor;
GN   Name=Idgf1; ORFNames=CG4472;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-52, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Imaginal disk;
RX   PubMed=9847235; DOI=10.1242/dev.126.2.211;
RA   Kawamura K., Shibata T., Saget O., Peel D., Bryant P.J.;
RT   "A new family of growth factors produced by the fat body and active on
RT   Drosophila imaginal disc cells.";
RL   Development 126:211-219(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC   STRAIN=MB01a, MB08b, MB13a, MB15b, MB25a, MB29b, MB33a, MB34a, MB36a,
RC   MB37a, MB39b, MB40b, MB45b, MB46b, MB47a, MB48b, MB52b, MB58b, MB63a, and
RC   MB80b;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA   Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA   Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA   Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA   Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA   Celniker S.E., Rubin G.M.;
RT   "An exploration of the sequence of a 2.9-Mb region of the genome of
RT   Drosophila melanogaster: the Adh region.";
RL   Genetics 153:179-219(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-346, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Oregon-R; TISSUE=Head;
RX   PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA   Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA   Panin V.;
RT   "Identification of N-glycosylated proteins from the central nervous system
RT   of Drosophila melanogaster.";
RL   Glycobiology 17:1388-1403(2007).
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. {ECO:0000269|PubMed:9847235}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9847235}.
CC       Note=Secreted in hemolymph. It is probably transported to target
CC       tissues via hemolymph.
CC   -!- TISSUE SPECIFICITY: Primarily expressed in yolk cells and fat body. In
CC       larvae, it is expressed in large salivary gland cells and weakly
CC       expressed in imaginal disks. Less expressed than Idgf2 and Idgf4.
CC       {ECO:0000269|PubMed:9847235}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed throughout development, with a much stronger expression
CC       during larval stages. {ECO:0000269|PubMed:9847235}.
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; AF102236; AAC99417.1; -; mRNA.
DR   EMBL; AF394691; AAM69623.1; -; Genomic_DNA.
DR   EMBL; AF394692; AAM69624.1; -; Genomic_DNA.
DR   EMBL; AF394693; AAM69625.1; -; Genomic_DNA.
DR   EMBL; AF394694; AAM69626.1; -; Genomic_DNA.
DR   EMBL; AF394695; AAM69627.1; -; Genomic_DNA.
DR   EMBL; AF394696; AAM69628.1; -; Genomic_DNA.
DR   EMBL; AF394697; AAM69629.1; -; Genomic_DNA.
DR   EMBL; AF394698; AAM69630.1; -; Genomic_DNA.
DR   EMBL; AF394699; AAM69631.1; -; Genomic_DNA.
DR   EMBL; AF394700; AAM69632.1; -; Genomic_DNA.
DR   EMBL; AF394701; AAM69633.1; -; Genomic_DNA.
DR   EMBL; AF394702; AAM69634.1; -; Genomic_DNA.
DR   EMBL; AF394703; AAM69635.1; -; Genomic_DNA.
DR   EMBL; AF394704; AAM69636.1; -; Genomic_DNA.
DR   EMBL; AF394705; AAM69637.1; -; Genomic_DNA.
DR   EMBL; AF394706; AAM69638.1; -; Genomic_DNA.
DR   EMBL; AF394707; AAM69639.1; -; Genomic_DNA.
DR   EMBL; AF394708; AAM69640.1; -; Genomic_DNA.
DR   EMBL; AF394709; AAM69641.1; -; Genomic_DNA.
DR   EMBL; AF394710; AAM69642.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAF53535.1; -; Genomic_DNA.
DR   EMBL; AY069157; AAL39302.1; -; mRNA.
DR   RefSeq; NP_477258.1; NM_057910.5.
DR   AlphaFoldDB; Q8MM24; -.
DR   SMR; Q8MM24; -.
DR   STRING; 7227.FBpp0080417; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GlyCosmos; Q8MM24; 3 sites, No reported glycans.
DR   GlyGen; Q8MM24; 3 sites.
DR   iPTMnet; Q8MM24; -.
DR   PaxDb; 7227-FBpp0080417; -.
DR   DNASU; 34978; -.
DR   EnsemblMetazoa; FBtr0080860; FBpp0080417; FBgn0020416.
DR   GeneID; 34978; -.
DR   KEGG; dme:Dmel_CG4472; -.
DR   AGR; FB:FBgn0020416; -.
DR   CTD; 34978; -.
DR   FlyBase; FBgn0020416; Idgf1.
DR   VEuPathDB; VectorBase:FBgn0020416; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   GeneTree; ENSGT00940000167840; -.
DR   HOGENOM; CLU_002833_3_2_1; -.
DR   InParanoid; Q8MM24; -.
DR   OMA; VEFQVNY; -.
DR   OrthoDB; 2663738at2759; -.
DR   PhylomeDB; Q8MM24; -.
DR   Reactome; R-DME-189085; Digestion of dietary carbohydrate.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 34978; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 34978; -.
DR   PRO; PR:Q8MM24; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0020416; Expressed in spermathecum and 28 other cell types or tissues.
DR   Genevisible; Q8MM24; DM.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0008084; F:imaginal disc growth factor receptor binding; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
DR   GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase.
DR   GO; GO:0018990; P:ecdysis, chitin-based cuticle; IMP:FlyBase.
DR   GO; GO:1990399; P:epithelium regeneration; IMP:FlyBase.
DR   GO; GO:0007444; P:imaginal disc development; IDA:UniProtKB.
DR   GO; GO:2000035; P:regulation of stem cell division; IMP:FlyBase.
DR   GO; GO:0042060; P:wound healing; IMP:FlyBase.
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   1: Evidence at protein level;
KW   Developmental protein; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:9847235"
FT   CHAIN           21..439
FT                   /note="Chitinase-like protein Idgf1"
FT                   /id="PRO_0000011980"
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:0000269|PubMed:17893096"
FT   DISULFID        26..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        340..423
FT                   /evidence="ECO:0000250"
FT   VARIANT         8
FT                   /note="I -> L (in strain: MB15b and MB25a)"
FT   VARIANT         44
FT                   /note="N -> S (in strain: MB13a, MB15b, MB25a, MB34a, MB37a
FT                   and MB63a)"
FT   VARIANT         100
FT                   /note="S -> G (in strain: MB01a and MB33a)"
FT   VARIANT         116
FT                   /note="V -> I (in strain: MB08b, MB29b, MB36a, MB40b,
FT                   MB47a, MB48b, MB52b and MB58b)"
FT   VARIANT         186
FT                   /note="E -> Q (in strain: MB08b, MB29b, MB40b, MB45b,
FT                   MB47a, MB48b, MB52b and MB80b)"
FT   VARIANT         305
FT                   /note="G -> E (in strain: MB01a, MB08b, MB29b, MB36a,
FT                   MB45b, MB47a, MB48b and MB52b and MB80b)"
FT   VARIANT         313
FT                   /note="I -> V (in strain: MB48b and MB52b)"
FT   VARIANT         399
FT                   /note="V -> E (in strain: MB34a and MB39b)"
FT   VARIANT         403
FT                   /note="G -> S (in strain: MB08b, MB15b, MB25a, MB29b,
FT                   MB33a, MB34a, MB36a, MB39b, MB45b, MB46b, MB47a, MB48b,
FT                   MB52b, MB58b, MB63a and MB80b)"
FT   CONFLICT        264
FT                   /note="Q -> E (in Ref. 1; AAC99417)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        396
FT                   /note="I -> L (in Ref. 1; AAC99417)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   439 AA;  49376 MW;  8CBE7CA0A1D59179 CRC64;
     MRFQLFYILG LLSVTSLTHA ASNLICYYDS NSYLRQGLAK MHTNELDLAL QFCTHLVYGY
     AGLKSGTLEL FSLNVDLDMF YYKDITALRQ KFPQLKILLS VGGDRDVDEA HPNKYVELLE
     ANRTAQQNFI DSSMILLKRN GFDGLDLAFQ LPRNKPRKVH GSLGSYWKSF KKLFTGDFVV
     DPQAEEHKSQ FTDLVGNIKN AFRSANLMLS LTVLPNVNST WYFDVPKLHP QFDYINLAAF
     DFLTPLRNPE EADFTAPIFF QDEQNRLPHL NVEFQINYWL QNHCPGQKLN LGIASYGRAW
     KLSKGSGLSG APIVHETCGV APGGIQIQSA EGLLSWPEIC SKLSQNASAQ YRGELAPLRK
     VTDLTQKYGN YALRPADDNG DFGVWLSFDD PDFAGIKAVY AKGKGLGGIA LFDLSYDDFR
     GLCTGQKYPI LRSIKYFMG
//
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