ID IDGF3_DROME Reviewed; 441 AA.
AC Q8MLZ7; A4V0S4; O96666; Q8MM23; Q8MX33; Q8MX34; Q8MX35; Q8MX36; Q8MX37;
AC Q8MX38; Q8MX39; Q9V3B9;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 24-JAN-2024, entry version 143.
DE RecName: Full=Chitinase-like protein Idgf3;
DE AltName: Full=Imaginal disk growth factor protein 3;
DE Flags: Precursor;
GN Name=Idgf3; ORFNames=CG4559;
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 24-55, VARIANT THR-351,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP 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 VAL-14; ILE-46; ASN-47;
RP PHE-139; MET-183; HIS-250; THR-349; THR-351 AND CYS-434.
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], AND VARIANT TYR-113.
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], AND VARIANT TYR-113.
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], AND VARIANT TYR-113.
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).
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 small and large salivary gland cells, and
CC weakly expressed in imaginal disks. Less expressed than Idgf2 and
CC Idgf4. {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 -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Lacks the typical Glu active site in position 153 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; AF102238; AAC99419.1; -; mRNA.
DR EMBL; AF394713; AAM69645.1; -; Genomic_DNA.
DR EMBL; AF394714; AAM69646.1; -; Genomic_DNA.
DR EMBL; AF394715; AAM69647.1; -; Genomic_DNA.
DR EMBL; AF394716; AAM69648.1; -; Genomic_DNA.
DR EMBL; AF394717; AAM69649.1; -; Genomic_DNA.
DR EMBL; AF394718; AAM69650.1; -; Genomic_DNA.
DR EMBL; AF394719; AAM69651.1; -; Genomic_DNA.
DR EMBL; AF394720; AAM69652.1; -; Genomic_DNA.
DR EMBL; AF394721; AAM69653.1; -; Genomic_DNA.
DR EMBL; AF394722; AAM69654.1; -; Genomic_DNA.
DR EMBL; AF394723; AAM69655.1; -; Genomic_DNA.
DR EMBL; AF394724; AAM69656.1; -; Genomic_DNA.
DR EMBL; AF394725; AAM69657.1; -; Genomic_DNA.
DR EMBL; AF394726; AAM69658.1; -; Genomic_DNA.
DR EMBL; AF394727; AAM69659.1; -; Genomic_DNA.
DR EMBL; AF394728; AAM69660.1; -; Genomic_DNA.
DR EMBL; AF394729; AAM69661.1; -; Genomic_DNA.
DR EMBL; AF394730; AAM69662.1; -; Genomic_DNA.
DR EMBL; AF394731; AAM69663.1; -; Genomic_DNA.
DR EMBL; AF394732; AAM69664.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53537.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10940.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10941.1; -; Genomic_DNA.
DR EMBL; AY047561; AAK77293.1; -; mRNA.
DR RefSeq; NP_001285982.1; NM_001299053.1.
DR RefSeq; NP_477256.1; NM_057908.4.
DR RefSeq; NP_723966.1; NM_165157.2.
DR RefSeq; NP_723967.1; NM_165158.1.
DR AlphaFoldDB; Q8MLZ7; -.
DR SMR; Q8MLZ7; -.
DR IntAct; Q8MLZ7; 1.
DR STRING; 7227.FBpp0309719; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyCosmos; Q8MLZ7; 1 site, No reported glycans.
DR GlyGen; Q8MLZ7; 1 site.
DR PaxDb; 7227-FBpp0080419; -.
DR DNASU; 34981; -.
DR GeneID; 34981; -.
DR KEGG; dme:Dmel_CG4559; -.
DR UCSC; CG4559-RB; d. melanogaster.
DR AGR; FB:FBgn0020414; -.
DR CTD; 34981; -.
DR FlyBase; FBgn0020414; Idgf3.
DR VEuPathDB; VectorBase:FBgn0020414; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_3_2_1; -.
DR InParanoid; Q8MLZ7; -.
DR OrthoDB; 2663738at2759; -.
DR PhylomeDB; Q8MLZ7; -.
DR Reactome; R-DME-189085; Digestion of dietary carbohydrate.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 34981; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34981; -.
DR PRO; PR:Q8MLZ7; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR ExpressionAtlas; Q8MLZ7; baseline and differential.
DR Genevisible; Q8MLZ7; DM.
DR GO; GO:0005576; C:extracellular region; HDA:FlyBase.
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:0007444; P:imaginal disc development; IDA:UniProtKB.
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..23
FT /evidence="ECO:0000269|PubMed:9847235"
FT CHAIN 24..441
FT /note="Chitinase-like protein Idgf3"
FT /id="PRO_0000011984"
FT DOMAIN 25..441
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 307..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 29..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 342..425
FT /evidence="ECO:0000250"
FT VARIANT 14
FT /note="A -> V (in strain: MB01a, MB13a, MB15b and MB46b)"
FT /evidence="ECO:0000269|PubMed:12242232"
FT VARIANT 46
FT /note="M -> I (in strain: MB25a)"
FT /evidence="ECO:0000269|PubMed:12242232"
FT VARIANT 47
FT /note="I -> N (in strain: MB25a)"
FT /evidence="ECO:0000269|PubMed:12242232"
FT VARIANT 113
FT /note="N -> Y (in strain: Berkeley)"
FT /evidence="ECO:0000269|PubMed:10471707,
FT ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:12537569"
FT VARIANT 139
FT /note="L -> F (in strain: MB29b)"
FT /evidence="ECO:0000269|PubMed:12242232"
FT VARIANT 183
FT /note="V -> M (in strain: MB47a)"
FT /evidence="ECO:0000269|PubMed:12242232"
FT VARIANT 250
FT /note="R -> H (in strain: MB33a and MB36a)"
FT /evidence="ECO:0000269|PubMed:12242232"
FT VARIANT 349
FT /note="S -> T (in strain: MB36a)"
FT /evidence="ECO:0000269|PubMed:12242232"
FT VARIANT 351
FT /note="S -> T (in strain: MB34a, MB36a, MB45b, MB46b, MB47a
FT and MB58b)"
FT /evidence="ECO:0000269|PubMed:12242232,
FT ECO:0000269|PubMed:9847235"
FT VARIANT 434
FT /note="R -> C (in strain: MB37a)"
FT /evidence="ECO:0000269|PubMed:12242232"
SQ SEQUENCE 441 AA; 49206 MW; DD9C2E0A0EBA7C0F CRC64;
MTGSLWLSLA LSLAVLAQFK VSAAPNLVCF YDSQGSQRQG LAQFSMIDIE LALQFCTHLV
YGYAGVNADN YEMQSINKRL DLEQRHLAQI TSMKERYPHI KFLLSVGGDA DTNEGNQYIK
LLESGQQGHR RFIESARDLV RRYNFDGLDL ALQLPRNKPR KVHGDVGSAW KSFKKFFTGD
FIVDTESETH KGQVTALIKD LSAALKQNDL LLSLTVLPNV NSSWYYDAPS IAPSLDFINL
GTFDFLTPQR NPEEADFSAP TYEAVGQNRL GHYNLNFQME HWLLQRVPAN KINIGIATYG
RSWKMSKDSG DSGMPVVPST QGPAPAGPQS KQEGLLNWAE ICSLMPNPSN SNARGPNAPV
KRVVDPTKRY GSYAFRAADE NGDHGLWISY DDPDSASSKA MYARARNLGG VALFDLTQDD
FRGQCTNDRF PMLRAIKYRL L
//
