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 14-DEC-2022, entry version 138. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyGen; Q8MM24; 3 sites. DR iPTMnet; Q8MM24; -. DR PaxDb; Q8MM24; -. 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; 482694at2759; -. 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 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 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; 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 //