IDGF2_DROME
ID IDGF2_DROME Reviewed; 440 AA.
AC Q9V3D4; O96665;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Chitinase-like protein Idgf2;
DE AltName: Full=Imaginal disk growth factor protein 2;
DE Flags: Precursor;
GN Name=Idgf2; ORFNames=CG4475;
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=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 [LARGE SCALE GENOMIC DNA].
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 [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=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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), GLYCOSYLATION, AND DISULFIDE BONDS.
RX PubMed=11821393; DOI=10.1074/jbc.m110502200;
RA Varela P.F., Llera A.S., Mariuzza R.A., Tormo J.;
RT "Crystal structure of imaginal disc growth factor-2. A member of a new
RT family of growth-promoting glycoproteins from Drosophila melanogaster.";
RL J. Biol. Chem. 277:13229-13236(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 the imaginal ring and weakly expressed in
CC imaginal disks. More strongly expressed than Idgf1 and Idgf3.
CC {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:0000269|PubMed:11821393}.
CC -!- MISCELLANEOUS: Lacks the typical Glu active site in position 152 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; AF102237; AAC99418.1; -; mRNA.
DR EMBL; AE014134; AAF53536.1; -; Genomic_DNA.
DR EMBL; AY060686; AAL28234.1; -; mRNA.
DR RefSeq; NP_477257.2; NM_057909.5.
DR PDB; 1JND; X-ray; 1.30 A; A=21-440.
DR PDB; 1JNE; X-ray; 1.70 A; A=21-440.
DR PDBsum; 1JND; -.
DR PDBsum; 1JNE; -.
DR AlphaFoldDB; Q9V3D4; -.
DR SMR; Q9V3D4; -.
DR BioGRID; 60988; 2.
DR IntAct; Q9V3D4; 1.
DR STRING; 7227.FBpp0080418; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyGen; Q9V3D4; 1 site.
DR iPTMnet; Q9V3D4; -.
DR PaxDb; Q9V3D4; -.
DR PRIDE; Q9V3D4; -.
DR DNASU; 34979; -.
DR EnsemblMetazoa; FBtr0080861; FBpp0080418; FBgn0020415.
DR GeneID; 34979; -.
DR KEGG; dme:Dmel_CG4475; -.
DR CTD; 34979; -.
DR FlyBase; FBgn0020415; Idgf2.
DR VEuPathDB; VectorBase:FBgn0020415; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000167840; -.
DR InParanoid; Q9V3D4; -.
DR OMA; NDRYPIL; -.
DR PhylomeDB; Q9V3D4; -.
DR Reactome; R-DME-189085; Digestion of dietary carbohydrate.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 34979; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; Q9V3D4; -.
DR GenomeRNAi; 34979; -.
DR PRO; PR:Q9V3D4; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0020415; Expressed in spermathecum and 33 other tissues.
DR ExpressionAtlas; Q9V3D4; baseline and differential.
DR Genevisible; Q9V3D4; DM.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA: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:0007444; P:imaginal disc development; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; 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 3D-structure; Developmental protein; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT CHAIN 21..440
FT /note="Chitinase-like protein Idgf2"
FT /id="PRO_0000011983"
FT DOMAIN 22..440
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11821393"
FT DISULFID 26..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258,
FT ECO:0000269|PubMed:11821393"
FT DISULFID 342..425
FT /evidence="ECO:0000269|PubMed:11821393"
FT CONFLICT 137
FT /note="D -> E (in Ref. 1; AAC99418)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="F -> V (in Ref. 1; AAC99418)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1JNE"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:1JND"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1JND"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 125..141
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 186..204
FT /evidence="ECO:0007829|PDB:1JND"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1JND"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 292..304
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:1JNE"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:1JND"
FT TURN 348..352
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1JNE"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 393..405
FT /evidence="ECO:0007829|PDB:1JND"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:1JND"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:1JND"
FT HELIX 431..439
FT /evidence="ECO:0007829|PDB:1JND"
SQ SEQUENCE 440 AA; 49159 MW; E4FE63E7B673B3EA CRC64;
MKAWIWFTFV ACLFAASTEA ASNLVCYYDS SSYTREGLGK LLNPDLEIAL QFCSHLVYGY
AGLRGENLQA YSMNENLDIY KHQFSEVTSL KRKYPHLKVL LSVGGDHDID PDHPNKYIDL
LEGEKVRQIG FIRSAYDLVK TYGFDGLDLA YQFPKNKPRK VHGDLGLAWK SIKKLFTGDF
IVDPHAALHK EQFTALVRDV KDSLRADGFL LSLTVLPNVN STWYFDIPAL NGLVDFVNLA
TFDFLTPARN PEEADYSAPI YHPDGSKDRL AHLNADFQVE YWLSQGFPSN KINLGVATYG
NAWKLTKDSG LEGVPVVPET SGPAPEGFQS QKPGLLSYAE ICGKLSNPQN QFLKGNESPL
RRVSDPTKRF GGIAYRPVDG QITEGIWVSY DDPDSASNKA AYARVKNLGG VALFDLSYDD
FRGQCSGDKY PILRAIKYRL
