Q9V3D4 (IDGF2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chitinase-like protein Idgf2

Alternative name(s):
Imaginal disk growth factor protein 2

Gene names

Name:	Idgf2
ORF Names:	CG4475

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1
Subcellular location	Secreted. Note: Secreted in hemolymph. It is probably transported to target tissues via hemolymph. Ref.1
Tissue specificity	Primarily expressed in yolk cells and fat body. In larvae, it is expressed in the imaginal ring and weakly expressed in imaginal disks. More strongly expressed than Idgf1 and Idgf3. Ref.1
Developmental stage	Expressed both maternally and zygotically. Expressed throughout development, with a much stronger expression during larval stages. Ref.1
Post-translational modification	Glycosylated. Ref.6
Miscellaneous	Lacks the typical Glu active site in position 152 that is replaced by a Gln residue, preventing the hydrolase activity. Its precise function remains unclear.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. IDGF subfamily.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: InterPro imaginal disc development Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	extracellular region Non-traceable author statement Ref.1. Source: UniProtKB
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro chitinase activity Inferred from electronic annotation. Source: InterPro imaginal disc growth factor receptor binding Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Orct	Q9VCA2	1	EBI-187259,EBI-132588

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Chain

21 – 440

420

Chitinase-like protein Idgf2

PRO_0000011983

Amino acid modifications

Glycosylation

220

1

N-linked (GlcNAc...)

Disulfide bond

26 ↔ 53

Ref.6

Disulfide bond

342 ↔ 425

Ref.6

Experimental info

Sequence conflict

137

1

D → E in AAC99418. Ref.1

Sequence conflict

277

1

F → V in AAC99418. Ref.1

Secondary structure

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440

Helix Strand Turn

Details...

Beta strand

23 – 29

7

Helix

30 – 34

5

Helix

43 – 49

7

Helix

50 – 52

3

Beta strand

54 – 63

10

Turn

65 – 67

3

Beta strand

70 – 72

3

Helix

75 – 78

4

Turn

79 – 81

3

Helix

83 – 88

6

Helix

89 – 92

4

Beta strand

98 – 104

7

Helix

116 – 121

6

Helix

125 – 141

17

Beta strand

145 – 150

6

Helix

186 – 204

19

Turn

205 – 208

4

Beta strand

210 – 215

6

Helix

221 – 224

4

Helix

227 – 231

5

Beta strand

235 – 239

5

Turn

247 – 249

3

Helix

275 – 284

10

Helix

289 – 291

3

Beta strand

292 – 304

13

Helix

307 – 309

3

Turn

328 – 330

3

Beta strand

335 – 337

3

Helix

338 – 344

7

Turn

348 – 352

5

Helix

355 – 357

3

Beta strand

360 – 363

4

Beta strand

372 – 376

5

Beta strand

386 – 390

5

Helix

393 – 405

13

Beta strand

409 – 414

6

Helix

416 – 418

3

Turn

424 – 426

3

Helix

431 – 439

9

Sequences

	Sequence		Length	Mass (Da)
	Q9V3D4 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E4FE63E7B673B3EA	FASTA	440	49,159
	10 20 30 40 50 60 MKAWIWFTFV ACLFAASTEA ASNLVCYYDS SSYTREGLGK LLNPDLEIAL QFCSHLVYGY 70 80 90 100 110 120 AGLRGENLQA YSMNENLDIY KHQFSEVTSL KRKYPHLKVL LSVGGDHDID PDHPNKYIDL 130 140 150 160 170 180 LEGEKVRQIG FIRSAYDLVK TYGFDGLDLA YQFPKNKPRK VHGDLGLAWK SIKKLFTGDF 190 200 210 220 230 240 IVDPHAALHK EQFTALVRDV KDSLRADGFL LSLTVLPNVN STWYFDIPAL NGLVDFVNLA 250 260 270 280 290 300 TFDFLTPARN PEEADYSAPI YHPDGSKDRL AHLNADFQVE YWLSQGFPSN KINLGVATYG 310 320 330 340 350 360 NAWKLTKDSG LEGVPVVPET SGPAPEGFQS QKPGLLSYAE ICGKLSNPQN QFLKGNESPL 370 380 390 400 410 420 RRVSDPTKRF GGIAYRPVDG QITEGIWVSY DDPDSASNKA AYARVKNLGG VALFDLSYDD 430 440 FRGQCSGDKY PILRAIKYRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new family of growth factors produced by the fat body and active on Drosophila imaginal disc cells." Kawamura K., Shibata T., Saget O., Peel D., Bryant P.J. Development 126:211-219(1999) [PubMed: 9847235] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Imaginal disk.
[2]	"An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region." 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. Genetics 153:179-219(1999) [PubMed: 10471707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"The genome sequence of Drosophila melanogaster." 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. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"A Drosophila full-length cDNA resource." 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. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[6]	"Crystal structure of imaginal disc growth factor-2. A member of a new family of growth-promoting glycoproteins from Drosophila melanogaster." Varela P.F., Llera A.S., Mariuzza R.A., Tormo J. J. Biol. Chem. 277:13229-13236(2002) [PubMed: 11821393] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), GLYCOSYLATION, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF102237 mRNA. Translation: AAC99418.1.
AE014134 Genomic DNA. Translation: AAF53536.1.
AY060686 mRNA. Translation: AAL28234.1.

RefSeq

NP_477257.2. NM_057909.3.

UniGene

Dm.6611.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JND	X-ray	1.30	A	21-440	[»]
1JNE	X-ray	1.70	A	21-440	[»]

ProteinModelPortal

Q9V3D4.

SMR

Q9V3D4. Positions 22-440.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9V3D4. 1 interaction.

MINT

MINT-1611234.

Protein family/group databases

CAZy

GH18. Glycoside Hydrolase Family 18.

Proteomic databases

PRIDE

Q9V3D4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0080861; FBpp0080418; FBgn0020415.

GeneID

34979.

KEGG

dme:Dmel_CG4475.

NMPDR

fig|7227.3.peg.2626.

Organism-specific databases

CTD

34979.

FlyBase

FBgn0020415. Idgf2.

Phylogenomic databases

eggNOG

inNOG06458.

GeneTree

EMGT00050000005216.

InParanoid

Q9V3D4.

OMA

SYTREGL.

OrthoDB

EOG4C5B0V.

PhylomeDB

Q9V3D4.

Gene expression databases

ArrayExpress

Q9V3D4.

Bgee

Q9V3D4.

GermOnline

CG4475. Drosophila melanogaster.

Family and domain databases

InterPro

IPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR015520. Imaginal_disc_gf.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.

PANTHER

PTHR11177:SF25. Imaginal_disc_gf. 1 hit.

Pfam

PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]

SMART

SM00636. Glyco_18. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Other

NextBio

791197.

Entry information

Entry name

IDGF2_DROME

Accession

Primary (citable) accession number: Q9V3D4
Secondary accession number(s): O96665

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project