Tag Content
SG ID
SG00000119 
UniProt Accession
Theoretical PI
5.2  
Molecular Weight
13723 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
chic 
Gene Synonyms/Alias
chi 
Protein Name
Profilin 
Protein Synonyms/Alias
Protein chickadee; 
Organism
Drosophila melanogaster (Fruit fly) 
NCBI Taxonomy ID
7227 
Chromosome Location
chr:2L;5972900-5981025;-1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Temporarily unavailable 
The information of related literatures
1. M. G. Giansanti, S. Bonaccorsi, B. Williams, E. V. Williams, C. Santolamazza, M. L. Goldberg and M. Gatti (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev 12(3): 396-410. 

Abstract
We analyzed male meiosis in mutants of the chickadee (chic) locus, a Drosophila melanogaster gene that encodes profilin, a low molecular weight actin-binding protein that modulates F-actin polymerization. These mutants are severely defective in meiotic cytokinesis. During ana-telophase of both meiotic divisions, they exhibit a central spindle less dense than wild type; certain chic allelic combinations cause almost complete disappearance of the central spindle. Moreover, chic mutant spermatocytes fail to form an actomyosin contractile ring. To further investigate the relationships between the central spindle and the contractile ring, we examined meiosis in the cytokinesis-defective mutants KLP3A and diaphanous and in testes treated with cytochalasin B. In all cases, we found that the central spindle and the contractile ring in meiotic ana-telophases were simultaneously absent. Together, these results suggest a cooperative interaction between elements of the actin-based contractile ring and the central spindle microtubules PMID: [9450933] 

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Figures for illustrating the function of this protein/gene
Ref: M. G. Giansanti, S. Bonaccorsi, B. Williams, E. V. Williams, C. Santolamazza, M. L. Goldberg and M. Gatti (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev 12(3): 396-410. PMID: [9450933]
Ref: M. G. Giansanti, S. Bonaccorsi, B. Williams, E. V. Williams, C. Santolamazza, M. L. Goldberg and M. Gatti (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev 12(3): 396-410. PMID: [9450933]
Ref: M. G. Giansanti, S. Bonaccorsi, B. Williams, E. V. Williams, C. Santolamazza, M. L. Goldberg and M. Gatti (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev 12(3): 396-410. PMID: [9450933]
Ref: M. G. Giansanti, S. Bonaccorsi, B. Williams, E. V. Williams, C. Santolamazza, M. L. Goldberg and M. Gatti (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev 12(3): 396-410. PMID: [9450933]
Ref: M. G. Giansanti, S. Bonaccorsi, B. Williams, E. V. Williams, C. Santolamazza, M. L. Goldberg and M. Gatti (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev 12(3): 396-410. PMID: [9450933]
Ref: M. G. Giansanti, S. Bonaccorsi, B. Williams, E. V. Williams, C. Santolamazza, M. L. Goldberg and M. Gatti (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev 12(3): 396-410. PMID: [9450933]
Ref: M. G. Giansanti, S. Bonaccorsi, B. Williams, E. V. Williams, C. Santolamazza, M. L. Goldberg and M. Gatti (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev 12(3): 396-410. PMID: [9450933]
Ref: M. G. Giansanti, S. Bonaccorsi, B. Williams, E. V. Williams, C. Santolamazza, M. L. Goldberg and M. Gatti (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev 12(3): 396-410. PMID: [9450933]
Ref: M. G. Giansanti, S. Bonaccorsi, B. Williams, E. V. Williams, C. Santolamazza, M. L. Goldberg and M. Gatti (1998) Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis. Genes Dev 12(3): 396-410. PMID: [9450933]
Function
Binds to actin and affects the structure of thecytoskeleton. At high concentrations, profilin prevents thepolymerization of actin, whereas it enhances it at lowconcentrations. By binding to PIP2, it inhibits the formation ofIP3 and DG. This profilin is required for intercellular cytoplasmtransport during Drosophila oogenesis. 
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Subcellular Location
Cytoplasm, cytoskeleton. 
Tissue Specificity
Expressed in ovary and head. 
Gene Ontology
GO IDGO termEvidence
GO:0015629 C:actin cytoskeleton IEA:InterPro.
GO:0005623 C:cell IMP:GOC.
GO:0005737 C:cytoplasm IEA:UniProtKB-KW.
GO:0030041 P:actin filament polymerization TAS:FlyBase.
GO:0007411 P:axon guidance IMP:FlyBase.
GO:0007420 P:brain development IMP:FlyBase.
GO:0000915 P:cytokinesis, actomyosin contractile ring assembly TAS:FlyBase.
GO:0007391 P:dorsal closure TAS:FlyBase.
GO:0007488 P:histoblast morphogenesis IMP:FlyBase.
GO:0030717 P:karyosome formation IMP:FlyBase.
GO:0035193 P:larval central nervous system remodeling IGI:FlyBase.
GO:0032507 P:maintenance of protein location in cell IMP:FlyBase.
GO:0007300 P:ovarian nurse cell to oocyte transport IMP:FlyBase.
GO:0045451 P:pole plasm oskar mRNA localization TAS:FlyBase.
GO:0051491 P:positive regulation of filopodium assembly IMP:FlyBase.
GO:0007283 P:spermatogenesis IMP:FlyBase.
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Interpro
IPR002097;    Profilin.
IPR005455;    Profilin_plant.
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Pfam
PF00235;    Profilin;    1.
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SMART
SM00392;    PROF;    1.
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PROSITE
PS00414;    PROFILIN;    1.
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PRINTS
PR00392;    PROFILIN.;   
PR01640;    PROFILINPLNT.;   
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Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
CHAIN         1    126       Profilin.
                             /FTId=PRO_0000199597.
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Nucleotide Sequence
Length: 1170 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 126 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
Gene Symbol Ref Databases
CG8204BioGRID 
tincBioGRID 
Sec16BioGRID 
Sec16BioGRID 
Act88FIntAct 
Arp66BBioGRID 
capuBioGRID 
capuBioGRID 
capuBioGRID 
capuBioGRID 
capuBioGRID 
CycB-RBBioGRID 
capuBioGRID 
CycBBioGRID 
Cdc42BioGRID 
enaIntAct 
His3IntAct 
His4IntAct 
hepBioGRID 
thIntAct 
JraIntAct 
CG10238IntAct 
Mkk4IntAct 
Ccp84AdBioGRID 
cibBioGRID 
CG8204IntAct 
AblBioGRID 
AblBioGRID 
Arp66BIntAct 
capuBioGRID 
capuBioGRID 
capuBioGRID 
capuBioGRID 
capuBioGRID 
CycB-RBBioGRID 
capuBioGRID 
CycBBioGRID 
Cdc42BioGRID 
enaIntAct 
hepBioGRID 
thIntAct 
Ccp84AdIntAct 
cibBioGRID 
capuBioGRID 
cibBioGRID 
capuBioGRID 
tincIntAct 
ElaIntAct 
WASpIntAct 
capuBioGRID 
CG7945IntAct 
Rac1BioGRID 
Ras85DBioGRID 
WASpBioGRID 
tincBioGRID 
ElaBioGRID 
capuBioGRID 
cibBioGRID 
CG7945BioGRID 
capuBioGRID 
tincBioGRID 
ElaBioGRID 
CG7945BioGRID 
_MINT 
WASpBioGRID 
CG10414IntAct 
capuBioGRID 
CG7945BioGRID 
_MINT 
msnIntAct 
Rac1BioGRID 
Ras85DBioGRID 
Other Protein-Protein interaction resources
String database  
View Microarray data
Temporarily unavailable 
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