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Q9VT51 (INSL2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable insulin-like peptide 2

Short name=dILP2
Alternative name(s):
Insulin-related peptide 2
Gene names
Name:Ilp2
Synonyms:IRP
ORF Names:CG8167
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a role in regulating body size by increasing cell size and cell number of individual organs. Probably mediates its growth effects by acting as a ligand for the insulin receptor and transducing a signal via the Chico/PI3K/Akt(PKB) pathway. Ref.5

Subunit structure

Heterodimer of a B chain and an A chain linked by two disulfide bonds By similarity.

Subcellular location

Secreted Potential.

Tissue specificity

Broadly expressed at a low level in the embryonic mesoderm, beginning at stage 12. Expressed at a high level in the embryonic anterior midgut, with expression diminishing at late stage 16. Expressed at a low level in larval imaginal disks. Expressed at a high level in larval salivary glands and in seven cells of each larval brain hemisphere that may correspond to neurosecretory cells. Ref.5

Developmental stage

Expressed in the embryo and larva. Ref.5

Miscellaneous

Of the insulin-like peptides, Ilp2 is the closest homolog of human insulin.

Sequence similarities

Belongs to the insulin family.

Ontologies

Keywords
   Biological processGrowth regulation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGrowth factor
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcarbohydrate utilization

Inferred from mutant phenotype. Source: FlyBase

determination of adult lifespan

Inferred from mutant phenotype. Source: FlyBase

female mating behavior

Inferred from mutant phenotype. Source: FlyBase

germ-line stem-cell niche homeostasis

Inferred from mutant phenotype. Source: FlyBase

growth

Traceable author statement. Source: FlyBase

insulin receptor signaling pathway

Inferred from genetic interaction Ref.5. Source: UniProtKB

larval feeding behavior

Inferred from mutant phenotype. Source: FlyBase

positive regulation of cell growth

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of multicellular organism growth

Inferred from mutant phenotype. Source: FlyBase

regulation of cell size

Inferred from mutant phenotype Ref.5. Source: FlyBase

regulation of growth rate

Inferred from mutant phenotype. Source: FlyBase

regulation of organ growth

Inferred from mutant phenotype Ref.5. Source: UniProtKB

triglyceride homeostasis

Inferred from mutant phenotype. Source: FlyBase

   Cellular componentextracellular region

Non-traceable author statement Ref.5. Source: UniProtKB

   Molecular functiongrowth factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

hormone activity

Inferred from electronic annotation. Source: InterPro

insulin receptor binding

Inferred from genetic interaction Ref.5. Source: UniProtKB

transmembrane receptor protein tyrosine kinase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 137111Probable insulin-like peptide 2
PRO_0000016189
Peptide27 – 5024Probable insulin-like peptide 2 B chain Potential
PRO_0000016190
Propeptide53 – 10452Connecting peptide Potential
PRO_0000016191
Peptide108 – 13730Probable insulin-like peptide 2 A chain Potential
PRO_0000016192

Amino acid modifications

Disulfide bond29 ↔ 119Interchain (between B and A chains) By similarity
Disulfide bond41 ↔ 132Interchain (between B and A chains) By similarity
Disulfide bond118 ↔ 123 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9VT51 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F5B2A357D7B653D6

FASTA13715,255
        10         20         30         40         50         60 
MSKPLSFISM VAVILLASST VKLAQGTLCS EKLNEVLSMV CEEYNPVIPH KRAMPGADSD 

        70         80         90        100        110        120 
LDALNPLQFV QEFEEEDNSI SEPLRSALFP GSYLGGVLNS LAEVRRRTRQ RQGIVERCCK 

       130 
KSCDMKALRE YCSVVRN 

« Hide

References

« Hide 'large scale' references
[1]"Neuropeptides and their precursors in the fruitfly, Drosophila melanogaster."
Vanden Broeck J.J.M.
Peptides 22:241-254(2001) [PubMed: 11179818] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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.
[3]"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. expand/collapse author list , 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.
[4]"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.
[5]"An evolutionarily conserved function of the Drosophila insulin receptor and insulin-like peptides in growth control."
Brogiolo W., Stocker H., Ikeya T., Rintelen F., Fernandez R., Hafen E.
Curr. Biol. 11:213-221(2001) [PubMed: 11250149] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ291726 mRNA. Translation: CAC17605.1.
AE014296 Genomic DNA. Translation: AAF50204.1.
AY069095 mRNA. Translation: AAL39240.1.
RefSeqNP_524012.1. NM_079288.2.
UniGeneDm.2285.

3D structure databases

ProteinModelPortalQ9VT51.
SMRQ9VT51. Positions 24-133.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9VT51.

Proteomic databases

PRIDEQ9VT51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076329; FBpp0076058; FBgn0036046.
GeneID39150.
KEGGdme:Dmel_CG8167.
NMPDRfig|7227.3.peg.9154.

Organism-specific databases

CTD39150.
FlyBaseFBgn0036046. Ilp2.

Phylogenomic databases

GeneTreeEMGT00050000016173.
InParanoidQ9VT51.
OMARRTRQGI.
OrthoDBEOG48W9JM.
PhylomeDBQ9VT51.

Enzyme and pathway databases

ReactomeREACT_115106. Signal Transduction.
REACT_6313. Insulin receptor mediated signaling.

Gene expression databases

BgeeQ9VT51.
GermOnlineCG8167. Drosophila melanogaster.

Family and domain databases

InterProIPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
Gene3DG3DSA:1.10.100.10. Ins/IGF/relaxin. 2 hits.
PfamPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSPR00276. INSULINFAMLY.
SMARTSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMSSF56994. Insulin-like. 1 hit.
PROSITEPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio812196.

Entry information

Entry nameINSL2_DROME
AccessionPrimary (citable) accession number: Q9VT51
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families