IDGF5_DROME
ID IDGF5_DROME Reviewed; 444 AA.
AC Q8T0R7; Q9V8G4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Chitinase-like protein Idgf5;
DE AltName: Full=Imaginal disk growth factor protein 5;
DE Flags: Precursor;
GN Name=Idgf5; ORFNames=CG5154;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably required to stimulate the proliferation,
CC polarization and motility of imaginal disk cells. May act by
CC 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted in
CC hemolymph. It is probably transported to target tissues via hemolymph.
CC {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Lacks the typical Glu active site in position 161 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 -!- SEQUENCE CAUTION:
CC Sequence=AAL39252.1; Type=Frameshift; Evidence={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; AE013599; AAF57703.2; -; Genomic_DNA.
DR EMBL; AY069107; AAL39252.1; ALT_FRAME; mRNA.
DR EMBL; BT012501; AAS93772.1; -; mRNA.
DR RefSeq; NP_611321.3; NM_137477.4.
DR AlphaFoldDB; Q8T0R7; -.
DR SMR; Q8T0R7; -.
DR BioGRID; 62783; 2.
DR STRING; 7227.FBpp0085849; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyGen; Q8T0R7; 2 sites.
DR PaxDb; Q8T0R7; -.
DR DNASU; 37104; -.
DR EnsemblMetazoa; FBtr0086668; FBpp0085849; FBgn0064237.
DR GeneID; 37104; -.
DR KEGG; dme:Dmel_CG5154; -.
DR CTD; 37104; -.
DR FlyBase; FBgn0064237; Idgf5.
DR VEuPathDB; VectorBase:FBgn0064237; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000167840; -.
DR HOGENOM; CLU_002833_3_2_1; -.
DR InParanoid; Q8T0R7; -.
DR OMA; QCAGEKF; -.
DR OrthoDB; 482694at2759; -.
DR PhylomeDB; Q8T0R7; -.
DR Reactome; R-DME-189085; Digestion of dietary carbohydrate.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 37104; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37104; -.
DR PRO; PR:Q8T0R7; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0064237; Expressed in capitellum (Drosophila) and 13 other tissues.
DR ExpressionAtlas; Q8T0R7; baseline and differential.
DR Genevisible; Q8T0R7; 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: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..26
FT /evidence="ECO:0000250"
FT CHAIN 27..444
FT /note="Chitinase-like protein Idgf5"
FT /id="PRO_0000011988"
FT DOMAIN 29..444
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 349..429
FT /evidence="ECO:0000250"
SQ SEQUENCE 444 AA; 50108 MW; D4D9C5A1E9CAD52D CRC64;
MMWIQKNPFL GLLLCSFLAF FQSTYAEVGK LVCFYDAQSF VREGPAQMSL AELEPALQFC
NFLVYGYAGI DAVTYKIKSL DPSLTNDRQH YRHITALRKK YPHVRFLLSV GGDRDVNSEG
VADSDKYLRL LEQSEHRKSF QASVLAELNN NGFDGIDLAW QFPKNRPKLQ QGVFKRVWGS
LRGWFSSSSV DEKSEEHREQ FATLLEELQS DLRRGGQLLT VSMLPHVSAE LFIDVPKVLS
NVDFVNLGTY DFQTPERDPK VADLPTPLYA MYDRDPSHNV QYQVQYWMNQ TSEISVHKLH
VGVTSYGRAW NMTRNSGITG YPPIPAANGA APPGRQTVTP GLLSWPEICD LLQQQPQDRE
VPHLRKVGDP TKRFGIYAYR AADDQGENGL WVGYEDPLTA AIKAGFVHAQ GLGGVAFHDL
SMDDFRGQCA GEKFPILRSI KFKL
