C5210_DROME
ID C5210_DROME Reviewed; 452 AA.
AC Q23997; A2RVC8; E1UIC7; E1UIC9; E1UID0; E1UID3; E1UID4; Q9V7S9;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Imaginal disk growth factor 6 {ECO:0000312|FlyBase:FBgn0013763};
DE Flags: Precursor;
GN Name=Idgf6 {ECO:0000312|FlyBase:FBgn0013763};
GN ORFNames=CG5210 {ECO:0000312|FlyBase:FBgn0013763};
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 19-41; 269-279; 380-386 AND
RP 415-432, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND VARIANT ILE-266.
RC TISSUE=Embryo;
RX PubMed=7875581; DOI=10.1016/0378-1119(94)00756-i;
RA Kirkpatrick R.B., Matico R.E., McNulty D.E., Strickler J.E.,
RA Rosenberg M.M.;
RT "An abundantly secreted glycoprotein from Drosophila melanogaster is
RT related to mammalian secretory proteins produced in rheumatoid tissues and
RT by activated macrophages.";
RL Gene 153:147-154(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-228; ILE-266 AND
RP SER-296.
RC STRAIN=ZBMEL131, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377,
RC ZBMEL384, ZBMEL398, ZBMEL82, and ZBMEL84;
RX PubMed=20150340; DOI=10.1093/molbev/msq046;
RA Parsch J., Novozhilov S., Saminadin-Peter S.S., Wong K.M., Andolfatto P.;
RT "On the utility of short intron sequences as a reference for the detection
RT of positive and negative selection in Drosophila.";
RL Mol. Biol. Evol. 27:1226-1234(2010).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CHITIN-BINDING, LACK OF ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=18342251; DOI=10.1016/j.ibmb.2007.06.011;
RA Zhu Q., Arakane Y., Beeman R.W., Kramer K.J., Muthukrishnan S.;
RT "Characterization of recombinant chitinase-like proteins of Drosophila
RT melanogaster and Tribolium castaneum.";
RL Insect Biochem. Mol. Biol. 38:467-477(2008).
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:0000269|PubMed:18342251,
CC ECO:0000269|PubMed:7875581}. Note=It is transported to target tissues
CC via hemolymph.
CC -!- TISSUE SPECIFICITY: In larvae, it is expressed in the fat body and by
CC hemocytes. {ECO:0000269|PubMed:7875581}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and in adults.
CC {ECO:0000269|PubMed:7875581}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:7875581}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. IDGF
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks the typical Glu active site in position 165 that is
CC replaced by a Gln residue, exhibits no chitinolytic activity towards
CC either polymeric and oligomeric substrates. Its precise function
CC remains unclear. {ECO:0000305}.
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DR EMBL; U13825; AAC48306.1; -; mRNA.
DR EMBL; FN544129; CBA35210.1; -; Genomic_DNA.
DR EMBL; FN544130; CBA35211.1; -; Genomic_DNA.
DR EMBL; FN544131; CBA35212.1; -; Genomic_DNA.
DR EMBL; FN544132; CBA35213.1; -; Genomic_DNA.
DR EMBL; FN544133; CBA35214.1; -; Genomic_DNA.
DR EMBL; FN544134; CBA35215.1; -; Genomic_DNA.
DR EMBL; FN544135; CBA35216.1; -; Genomic_DNA.
DR EMBL; FN544136; CBA35217.1; -; Genomic_DNA.
DR EMBL; FN544137; CBA35218.1; -; Genomic_DNA.
DR EMBL; FN544138; CBA35219.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57965.1; -; Genomic_DNA.
DR EMBL; AY058510; AAL13739.1; -; mRNA.
DR EMBL; BT029919; ABM92793.1; -; mRNA.
DR PIR; JC4038; JC4038.
DR RefSeq; NP_001286499.1; NM_001299570.1.
DR RefSeq; NP_477081.1; NM_057733.4.
DR AlphaFoldDB; Q23997; -.
DR SMR; Q23997; -.
DR BioGRID; 62579; 1.
DR IntAct; Q23997; 1.
DR STRING; 7227.FBpp0086257; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyGen; Q23997; 1 site.
DR PaxDb; Q23997; -.
DR PRIDE; Q23997; -.
DR DNASU; 36868; -.
DR EnsemblMetazoa; FBtr0087111; FBpp0086257; FBgn0013763.
DR EnsemblMetazoa; FBtr0340066; FBpp0309072; FBgn0013763.
DR GeneID; 36868; -.
DR KEGG; dme:Dmel_CG5210; -.
DR UCSC; CG5210-RA; d. melanogaster.
DR CTD; 36868; -.
DR FlyBase; FBgn0013763; Idgf6.
DR VEuPathDB; VectorBase:FBgn0013763; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000167840; -.
DR HOGENOM; CLU_002833_3_2_1; -.
DR InParanoid; Q23997; -.
DR OMA; IWVSFED; -.
DR OrthoDB; 482694at2759; -.
DR PhylomeDB; Q23997; -.
DR Reactome; R-DME-189085; Digestion of dietary carbohydrate.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 36868; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36868; -.
DR PRO; PR:Q23997; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0013763; Expressed in embryonic/larval hemocyte (Drosophila) and 42 other tissues.
DR ExpressionAtlas; Q23997; baseline and differential.
DR Genevisible; Q23997; DM.
DR GO; GO:0005576; C:extracellular region; HDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0008061; F:chitin binding; IDA:FlyBase.
DR GO; GO:0008084; F:imaginal disc growth factor receptor binding; ISS:FlyBase.
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; ISS: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; 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 1: Evidence at protein level;
KW Chitin-binding; Developmental protein; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:7875581"
FT CHAIN 19..452
FT /note="Imaginal disk growth factor 6"
FT /id="PRO_0000011979"
FT DOMAIN 29..452
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 33..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 352..435
FT /evidence="ECO:0000250"
FT VARIANT 228
FT /note="V -> L (in strain: ZBMEL229)"
FT /evidence="ECO:0000269|PubMed:20150340"
FT VARIANT 266
FT /note="V -> I (in strain: ZBMEL131, ZBMEL157, ZBMEL186 and
FT ZBMEL191)"
FT /evidence="ECO:0000269|PubMed:20150340,
FT ECO:0000269|PubMed:7875581"
FT VARIANT 296
FT /note="N -> S (in strain: ZBMEL131, ZBMEL186, ZBMEL229,
FT ZBMEL377 and ZBMEL398)"
FT /evidence="ECO:0000269|PubMed:20150340"
FT CONFLICT 180
FT /note="S -> N (in Ref. 1; AAC48306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 50354 MW; EA18949BCA445258 CRC64;
MIIKALAIVS LCLASIQASK VGAPQLPKKH LVCYYDSASF VKEGLGKLVI DELEPALQFC
DYLVYGYAGI ERDSHKAVSL NQQLDLDLGK GLYRTVTRLK RKYPNVKILL SVGGDKDIEL
DKDAKELPNK YLELLESPTG RTRFVNTVYS LVKTYGFDGL DVAWQFPKNK PKKVHSGIGS
LWKGFKKVFS GDSIVDEKSE EHKEQFTALL RDVKNAFRPD NLLLSTTVLP NVNSSLFYDI
PAVVNYLDFV NLGTFDFFTP QRNPEVADYA APIYELSERN PEFNVAAQVK YWLRNNCPAS
KINVGVATYG RPWKLTDDSG DTGVPPVKDV KDEAPVGGNT QVPGIYSWPE VCALLPNQNN
AYLKGANAPL IKVQDPAKRF GSYAYRAADK KGDNGIWVSF EDPDTAADKA GYVRTENLGG
VALFDLSYDD FRGLCTNEKY PILRAIKYRL TN
