IDGF4_DROME
ID IDGF4_DROME Reviewed; 442 AA.
AC Q9W303; A4V476; O96667;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Chitinase-like protein Idgf4;
DE AltName: Full=Imaginal disk growth factor protein 4;
DE Flags: Precursor;
GN Name=Idgf4; ORFNames=CG1780;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Larva;
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 [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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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 the imaginal ring, the salivary duct, large
CC salivary gland cells and weakly expressed in imaginal disks. More
CC strongly expressed than Idgf1 and Idgf3. {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 156 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; AF102239; AAC99420.1; -; mRNA.
DR EMBL; AE014298; AAF46534.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09618.1; -; Genomic_DNA.
DR EMBL; AY070943; AAL48565.1; -; mRNA.
DR EMBL; BT003236; AAO24992.1; -; mRNA.
DR RefSeq; NP_001285068.1; NM_001298139.1.
DR RefSeq; NP_511101.2; NM_078546.4.
DR RefSeq; NP_727374.1; NM_167207.3.
DR AlphaFoldDB; Q9W303; -.
DR SMR; Q9W303; -.
DR BioGRID; 58363; 10.
DR IntAct; Q9W303; 2.
DR STRING; 7227.FBpp0071328; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyGen; Q9W303; 1 site.
DR PaxDb; Q9W303; -.
DR PRIDE; Q9W303; -.
DR DNASU; 31926; -.
DR EnsemblMetazoa; FBtr0071393; FBpp0071328; FBgn0026415.
DR EnsemblMetazoa; FBtr0071394; FBpp0071329; FBgn0026415.
DR EnsemblMetazoa; FBtr0343030; FBpp0309782; FBgn0026415.
DR GeneID; 31926; -.
DR KEGG; dme:Dmel_CG1780; -.
DR CTD; 31926; -.
DR FlyBase; FBgn0026415; Idgf4.
DR VEuPathDB; VectorBase:FBgn0026415; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_3_2_1; -.
DR InParanoid; Q9W303; -.
DR OMA; HHLLCYY; -.
DR OrthoDB; 482694at2759; -.
DR PhylomeDB; Q9W303; -.
DR Reactome; R-DME-189085; Digestion of dietary carbohydrate.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 31926; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Idgf4; fly.
DR GenomeRNAi; 31926; -.
DR PRO; PR:Q9W303; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0026415; Expressed in seminal fluid secreting gland and 44 other tissues.
DR ExpressionAtlas; Q9W303; baseline and differential.
DR Genevisible; Q9W303; 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 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; PTHR11177:SF235; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..442
FT /note="Chitinase-like protein Idgf4"
FT /id="PRO_0000011987"
FT DOMAIN 25..442
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 29..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 343..426
FT /evidence="ECO:0000250"
FT CONFLICT 80
FT /note="L -> P (in Ref. 1; AAC99420)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="V -> L (in Ref. 1; AAC99420)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="R -> P (in Ref. 1; AAC99420)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 48604 MW; 99EF61E9E3D66694 CRC64;
MKLYALFSLL VGSLAIGQIS AAGSHHLLCY YDGNSFVREG LSKLILTDLE PALQYCTHLV
YGYAGINPSS NKLVSNNEKL DLDLGSSLFR QVTGLKRKYP ALKVLLSVGG DKDTVDPENN
KYLTLLESSN ARIPFINSAH SLVKTYGFDG LDLGWQFPKN KPKKVHGSIG KFWKGFKKIF
SGDHVVDEKA EEHKEAFTAL VRELKNAFRP DGYILGLSVL PNVNSSLFFD VPAIINNLDY
VNLHTYDFQT PERNNEVADF PAPIYELNER NPEFNVNYQV KYWTGNRAPA AKINVGIATY
GRAWKLTKDS GLTGLPPVAE ADGVAPAGTQ TQIPGLLSWP EVCAKLPNPA NQHLKGADGP
LRKVGDPTKR FGSYAYRSAD DSGENGVWVG YEDPDTAAIK AEYVKREGLG GIAVVDLSFD
DFRGGCTGHD KFPILRQVKS KL
