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Chitinase-like protein Idgf1 (Imaginal disk growth factor protein 1)

 IDGF1_DROME             Reviewed;         439 AA.
Q8MM24; O96664; Q8MM30; Q8MM31; Q8MM38; Q8MM92; Q8MX42; Q8MX43;
Q8MX44; Q8MX45; Q8MX46; Q8MX47; Q8MX48; Q8MX49; Q8MX50; Q9V3P8;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
15-MAR-2004, sequence version 2.
05-DEC-2018, entry version 123.
RecName: Full=Chitinase-like protein Idgf1;
AltName: Full=Imaginal disk growth factor protein 1;
Flags: Precursor;
Name=Idgf1; ORFNames=CG4472;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-52, FUNCTION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Imaginal disk;
PubMed=9847235;
Kawamura K., Shibata T., Saget O., Peel D., Bryant P.J.;
"A new family of growth factors produced by the fat body and active on
Drosophila imaginal disc cells.";
Development 126:211-219(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
STRAIN=MB01a, MB08b, MB13a, MB15b, MB25a, MB29b, MB33a, MB34a, MB36a,
MB37a, MB39b, MB40b, MB45b, MB46b, MB47a, MB48b, MB52b, MB58b, MB63a,
and MB80b;
PubMed=12242232;
Zurovcova M., Ayala F.J.;
"Polymorphism patterns in two tightly linked developmental genes,
Idgf1 and Idgf3, of Drosophila melanogaster.";
Genetics 162:177-188(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10471707;
Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G.,
Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G.,
Martin C., Moshrefi A.R., Palazzolo M., Reese M.G., Spradling A.C.,
Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.;
"An exploration of the sequence of a 2.9-Mb region of the genome of
Drosophila melanogaster: the Adh region.";
Genetics 153:179-219(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-346, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Oregon-R; TISSUE=Head;
PubMed=17893096; DOI=10.1093/glycob/cwm097;
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
Panin V.;
"Identification of N-glycosylated proteins from the central nervous
system of Drosophila melanogaster.";
Glycobiology 17:1388-1403(2007).
-!- FUNCTION: Cooperates with insulin-like peptides to stimulate the
proliferation, polarization and motility of imaginal disk cells.
May act by stabilizing the binding of insulin-like peptides to its
receptor through a simultaneous interaction with both molecules to
form a multiprotein signaling complex.
{ECO:0000269|PubMed:9847235}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9847235}.
Note=Secreted in hemolymph. It is probably transported to target
tissues via hemolymph.
-!- TISSUE SPECIFICITY: Primarily expressed in yolk cells and fat
body. In larvae, it is expressed in large salivary gland cells and
weakly expressed in imaginal disks. Less expressed than Idgf2 and
Idgf4. {ECO:0000269|PubMed:9847235}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Expressed throughout development, with a much stronger expression
during larval stages. {ECO:0000269|PubMed:9847235}.
-!- MISCELLANEOUS: Lacks the typical Glu active site in position 150
that is replaced by a Gln residue, preventing the hydrolase
activity. Its precise function remains unclear.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. IDGF
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF102236; AAC99417.1; -; mRNA.
EMBL; AF394691; AAM69623.1; -; Genomic_DNA.
EMBL; AF394692; AAM69624.1; -; Genomic_DNA.
EMBL; AF394693; AAM69625.1; -; Genomic_DNA.
EMBL; AF394694; AAM69626.1; -; Genomic_DNA.
EMBL; AF394695; AAM69627.1; -; Genomic_DNA.
EMBL; AF394696; AAM69628.1; -; Genomic_DNA.
EMBL; AF394697; AAM69629.1; -; Genomic_DNA.
EMBL; AF394698; AAM69630.1; -; Genomic_DNA.
EMBL; AF394699; AAM69631.1; -; Genomic_DNA.
EMBL; AF394700; AAM69632.1; -; Genomic_DNA.
EMBL; AF394701; AAM69633.1; -; Genomic_DNA.
EMBL; AF394702; AAM69634.1; -; Genomic_DNA.
EMBL; AF394703; AAM69635.1; -; Genomic_DNA.
EMBL; AF394704; AAM69636.1; -; Genomic_DNA.
EMBL; AF394705; AAM69637.1; -; Genomic_DNA.
EMBL; AF394706; AAM69638.1; -; Genomic_DNA.
EMBL; AF394707; AAM69639.1; -; Genomic_DNA.
EMBL; AF394708; AAM69640.1; -; Genomic_DNA.
EMBL; AF394709; AAM69641.1; -; Genomic_DNA.
EMBL; AF394710; AAM69642.1; -; Genomic_DNA.
EMBL; AE014134; AAF53535.1; -; Genomic_DNA.
EMBL; AY069157; AAL39302.1; -; mRNA.
RefSeq; NP_477258.1; NM_057910.5.
UniGene; Dm.2253; -.
ProteinModelPortal; Q8MM24; -.
SMR; Q8MM24; -.
STRING; 7227.FBpp0080417; -.
CAZy; GH18; Glycoside Hydrolase Family 18.
iPTMnet; Q8MM24; -.
PaxDb; Q8MM24; -.
PRIDE; Q8MM24; -.
EnsemblMetazoa; FBtr0080860; FBpp0080417; FBgn0020416.
GeneID; 34978; -.
KEGG; dme:Dmel_CG4472; -.
CTD; 34978; -.
FlyBase; FBgn0020416; Idgf1.
eggNOG; KOG2806; Eukaryota.
eggNOG; COG3325; LUCA.
GeneTree; ENSGT00940000167840; -.
InParanoid; Q8MM24; -.
OMA; NVEFQVN; -.
OrthoDB; EOG091G06UD; -.
PhylomeDB; Q8MM24; -.
GenomeRNAi; 34978; -.
PRO; PR:Q8MM24; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0020416; Expressed in 32 organ(s), highest expression level in arthropod fat body.
Genevisible; Q8MM24; DM.
GO; GO:0005576; C:extracellular region; IBA:GO_Central.
GO; GO:0008061; F:chitin binding; IBA:GO_Central.
GO; GO:0008084; F:imaginal disc growth factor receptor binding; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase.
GO; GO:0018990; P:ecdysis, chitin-based cuticle; IMP:FlyBase.
GO; GO:1990399; P:epithelium regeneration; IMP:FlyBase.
GO; GO:0007444; P:imaginal disc development; IDA:UniProtKB.
GO; GO:2000035; P:regulation of stem cell division; IMP:FlyBase.
GO; GO:0042060; P:wound healing; IMP:FlyBase.
CDD; cd02873; GH18_IDGF; 1.
Gene3D; 3.10.50.10; -; 1.
InterPro; IPR011583; Chitinase_II.
InterPro; IPR029070; Chitinase_insertion_sf.
InterPro; IPR001223; Glyco_hydro18_cat.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR015520; IDGF.
PANTHER; PTHR11177:SF235; PTHR11177:SF235; 1.
Pfam; PF00704; Glyco_hydro_18; 1.
SMART; SM00636; Glyco_18; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF54556; SSF54556; 1.
1: Evidence at protein level;
Complete proteome; Developmental protein; Direct protein sequencing;
Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000269|PubMed:9847235}.
CHAIN 21 439 Chitinase-like protein Idgf1.
/FTId=PRO_0000011980.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 218 218 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096}.
DISULFID 26 53 {ECO:0000250}.
DISULFID 340 423 {ECO:0000250}.
VARIANT 8 8 I -> L (in strain: MB15b and MB25a).
VARIANT 44 44 N -> S (in strain: MB13a, MB15b, MB25a,
MB34a, MB37a and MB63a).
VARIANT 100 100 S -> G (in strain: MB01a and MB33a).
VARIANT 116 116 V -> I (in strain: MB08b, MB29b, MB36a,
MB40b, MB47a, MB48b, MB52b and MB58b).
VARIANT 186 186 E -> Q (in strain: MB08b, MB29b, MB40b,
MB45b, MB47a, MB48b, MB52b and MB80b).
VARIANT 305 305 G -> E (in strain: MB01a, MB08b, MB29b,
MB36a, MB45b, MB47a, MB48b and MB52b and
MB80b).
VARIANT 313 313 I -> V (in strain: MB48b and MB52b).
VARIANT 399 399 V -> E (in strain: MB34a and MB39b).
VARIANT 403 403 G -> S (in strain: MB08b, MB15b, MB25a,
MB29b, MB33a, MB34a, MB36a, MB39b, MB45b,
MB46b, MB47a, MB48b, MB52b, MB58b, MB63a
and MB80b).
CONFLICT 264 264 Q -> E (in Ref. 1; AAC99417).
{ECO:0000305}.
CONFLICT 396 396 I -> L (in Ref. 1; AAC99417).
{ECO:0000305}.
SEQUENCE 439 AA; 49376 MW; 8CBE7CA0A1D59179 CRC64;
MRFQLFYILG LLSVTSLTHA ASNLICYYDS NSYLRQGLAK MHTNELDLAL QFCTHLVYGY
AGLKSGTLEL FSLNVDLDMF YYKDITALRQ KFPQLKILLS VGGDRDVDEA HPNKYVELLE
ANRTAQQNFI DSSMILLKRN GFDGLDLAFQ LPRNKPRKVH GSLGSYWKSF KKLFTGDFVV
DPQAEEHKSQ FTDLVGNIKN AFRSANLMLS LTVLPNVNST WYFDVPKLHP QFDYINLAAF
DFLTPLRNPE EADFTAPIFF QDEQNRLPHL NVEFQINYWL QNHCPGQKLN LGIASYGRAW
KLSKGSGLSG APIVHETCGV APGGIQIQSA EGLLSWPEIC SKLSQNASAQ YRGELAPLRK
VTDLTQKYGN YALRPADDNG DFGVWLSFDD PDFAGIKAVY AKGKGLGGIA LFDLSYDDFR
GLCTGQKYPI LRSIKYFMG


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