ID IDG1_DROME STANDARD; PRT; 439 AA. AC Q8MM24; O96664; Q8MM30; Q8MM31; Q8MM38; Q8MM92; Q8MX42; Q8MX43; AC Q8MX44; Q8MX45; Q8MX46; Q8MX47; Q8MX48; Q8MX49; Q8MX50; Q9V3P8; DT 29-MAR-2004 (Rel. 43, Created) DT 29-MAR-2004 (Rel. 43, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) DE Chitinase-like protein Idgf1 precursor (Imaginal disk growth factor DE protein 1). GN Name=Idgf1; ORFNames=CG4472; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., SEQUENCE OF 21-52, FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Imaginal disks; RX PubMed=9847235; 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 SEQUENCE FROM N.A., AND VARIANTS. RC STRAIN=MB01a, MB08b, MB13a, MB15b, MB25a, MB29b, MB33a, MB34a, MB36a, RC MB37a, MB39b, MB40b, MB45b, MB46b, MB47a, MB48b, MB52b, MB58b, MB63a, RC and MB80b; RX MEDLINE=22226651; PubMed=12242232; RA Zurovcova M., Ayala F.J.; RT "Polymorphism patterns in two tightly linked developmental genes, RT Idgf1 and Idgf3, of Drosophila melanogaster."; RL Genetics 162:177-188(2002). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=99403001; PubMed=10471707; 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., RA Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., RA Martin C., Moshrefi A.R., Palazzolo M., Reese M.G., Spradling A.C., RA Tsang G., Wan K.H., Whitelaw K., 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 SEQUENCE FROM N.A. RC STRAIN=Berkeley; RX MEDLINE=20196006; 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: Cooperates with insulin-like peptides to stimulate the CC proliferation, polarization and motility of imaginal disk cells. CC May act by stabilizing the binding of insulin-like peptides to its CC receptor through a simultaneous interaction with both molecules to CC form a multiprotein signaling complex. CC -!- SUBCELLULAR LOCATION: Secreted. It is probably transported to CC target tissues via hemolymph. CC -!- TISSUE SPECIFICITY: Primarily expressed in yolk cells and fat CC body. In larvae, it is expressed in large salivary gland cells and CC weakly expressed in imaginal disks. Less expressed than Idgf2 and CC Idgf4. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. CC Expressed throughout development, with a much stronger expression CC during larval stages. CC -!- PTM: Glycosylated (By similarity). CC -!- MISCELLANEOUS: Lacks the typical Glu active site in position 150 CC that is replaced by a Gln residue, preventing the hydrolase CC activity. Its precise function remains unclear. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. IDGF CC subfamily. 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; -. DR EMBL; AF394691; AAM69623.1; -. DR EMBL; AF394692; AAM69624.1; -. DR EMBL; AF394693; AAM69625.1; -. DR EMBL; AF394694; AAM69626.1; -. DR EMBL; AF394695; AAM69627.1; -. DR EMBL; AF394696; AAM69628.1; -. DR EMBL; AF394697; AAM69629.1; -. DR EMBL; AF394698; AAM69630.1; -. DR EMBL; AF394699; AAM69631.1; -. DR EMBL; AF394700; AAM69632.1; -. DR EMBL; AF394701; AAM69633.1; -. DR EMBL; AF394702; AAM69634.1; -. DR EMBL; AF394703; AAM69635.1; -. DR EMBL; AF394704; AAM69636.1; -. DR EMBL; AF394705; AAM69637.1; -. DR EMBL; AF394706; AAM69638.1; -. DR EMBL; AF394707; AAM69639.1; -. DR EMBL; AF394708; AAM69640.1; -. DR EMBL; AF394709; AAM69641.1; -. DR EMBL; AF394710; AAM69642.1; -. DR EMBL; AE003416; AAF45016.1; -. DR EMBL; AE003651; AAF53535.1; -. DR EMBL; AY069157; AAL39302.1; -. DR HSSP; O96665; 1JND. DR FlyBase; FBgn0020416; Idgf1. DR GO; GO:0005576; C:extracellular; IDA. DR InterPro; IPR001223; Glyco_hydro_18. DR Pfam; PF00704; Glyco_hydro_18; 1. DR ProDom; PD000471; Chitinase_II; 1. DR SMART; SM00636; Glyco_18; 1. KW Developmental protein; Direct protein sequencing; Glycoprotein; KW Signal. FT SIGNAL 1 20 FT CHAIN 21 439 Chitinase-like protein Idgf1. FT DISULFID 26 53 By similarity. FT DISULFID 340 423 By similarity. FT CARBOHYD 122 122 N-linked (GlcNAc...) (Potential). FT CARBOHYD 218 218 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 346 346 N-linked (GlcNAc...) (Potential). FT VARIANT 8 8 I -> L (in strains MB15b and MB25a). FT VARIANT 44 44 N -> S (in strains MB13a, MB15b, MB25a, FT MB34a, MB37a and MB63a). FT VARIANT 100 100 S -> G (in strains MB01a and MB33a). FT VARIANT 116 116 V -> I (in strains MB08b, MB29b, MB36a, FT MB40b, MB47a, MB48b, MB52b and MB58b). FT VARIANT 186 186 E -> Q (in strains MB08b, MB29b, MB40b, FT MB45b, MB47a, MB48b, MB52b and MB80b). FT VARIANT 305 305 G -> E (in strains MB01a, MB08b, MB29b, FT MB36a, MB45b, MB47a, MB48b and MB52b and FT MB80b). FT VARIANT 313 313 I -> V (in strains MB48b and MB52b). FT VARIANT 399 399 V -> E (in strains MB34a and MB39b). FT VARIANT 403 403 G -> S (in strains MB08b, MB15b, MB25a, FT MB29b, MB33a, MB34a, MB36a, MB39b, MB45b, FT MB46b, MB47a, MB48b, MB52b, MB58b, MB63a FT and MB80b). FT CONFLICT 264 264 Q -> E (in Ref. 1). FT CONFLICT 396 396 I -> L (in Ref. 1). 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 //