| General information | | DisProt: | DP00328 | | Name: | Transcription factor GAGA [Isoform B] | | Synonym(s): | GAGA_DROME
Trithorax-like protein
GAGA factor
GAF
Adh transcription factor 2
Neural conserved at 70F
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | Q08605-2 | | UniGene: | Dm.7610 | | SwissProt: | GAGA_DROME | | TrEMBL: | | | NCBI (GI): | 83287912 | | Source organism: | Drosophila melanogaster (Fruit fly) | | Sequence length: | 519 | | Percent disordered: | 74% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLL - 60
DLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQ - 120
TVTKDDYTTH SIQLQHMIPQ HHDQDQLIAT IATAPQQTVH AQVVEDIHHQ GQILQATTQT - 180
NAAGQQQTIV TTDAAKHDQA VIQAFLPARK RKPRVKKMSP TAPKISKVEG MDTIMGTPTS - 240
SHGSGSVQQV LGENGAEGQL LSSTPIIKSE GQKVETILTM DPNNMIPVTS ANAATGEITP - 300
AQGATGSSGG NTSGVLSTPK AKRAKHPPGT EKPRSRSQSE QPATCPICYA VIRQSRNLRR - 360
HLELRHFAKP GVKKEKKSKS GNDTTLDSSM EMNTTAEGDN TVGSDGAGGA GSAGGQSSGT - 420
TPTRVISNAP QAAGAPAILA QGVLPQQQQQ QQLQQQHQQH LTATLAGGGQ AYIKHEGGGG - 480
GGTGQQQQQQ AAQQQGMQNV IHIVGDQVFI PQQQQPQPQ
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| Functional narrative |
Transcriptional activator that functions by regulating chromatin structure. Overcomes the repressive effects of chromatin by promoting the open chromatin conformation in promoter gene regions, thereby allowing access to other transcription factors. Binds to DNA Polycomb response elements (PREs) at the bithorax complex and to the proximal region of the engrailed promoter, and positively regulates transcription of many genes including homeotic ones. Binds to the DNA sequence (GA)n, with optimal binding to the pentamer 5'-GAGAG-3'. Binds DNA as an oligomer. May also act as a transcriptional repressor, maintaining the repressed state of genes including lolal, and down-regulating its own transcription. Required for dosage compensation in males and may be involved in oogenesis. Also has a role in nuclear division.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | GAF1 | | Location: | 137 - 519 | | Length: | 383 | | Region sequence: |
MIPQHHDQDQLIATIATAPQQTVHAQVVEDIHHQGQILQATTQTNAAGQQQTIVTTDAAK
HDQAVIQAFLPARKRKPRVKKMSPTAPKISKVEGMDTIMGTPTSSHGSGSVQQVLGENGA
EGQLLSSTPIIKSEGQKVETILTMDPNNMIPVTSANAATGEITPAQGATGSSGGNTSGVL
STPKAKRAKHPPGTEKPRSRSQSEQPATCPICYAVIRQSRNLRRHLELRHFAKPGVKKEK
KSKSGNDTTLDSSMEMNTTAEGDNTVGSDGAGGAGSAGGQSSGTTPTRVISNAPQAAGAP
AILAQGVLPQQQQQQQLQQQHQQHLTATLAGGGQAYIKHEGGGGGGTGQQQQQQAAQQQG
MQNVIHIVGDQVFIPQQQQPQPQ | | Modification type: | Fragment
Mutant
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-DNA binding
Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (295 K; )
| References:
- Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. "The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling." J Mol Biol. 1999; 285(2): 527-44. PubMed: 9878427
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | GAF2 | | Location: | 137 - 443 | | Length: | 307 | | Region sequence: |
MIPQHHDQDQLIATIATAPQQTVHAQVVEDIHHQGQILQATTQTNAAGQQQTIVTTDAAK
HDQAVIQAFLPARKRKPRVKKMSPTAPKISKVEGMDTIMGTPTSSHGSGSVQQVLGENGA
EGQLLSSTPIIKSEGQKVETILTMDPNNMIPVTSANAATGEITPAQGATGSSGGNTSGVL
STPKAKRAKHPPGTEKPRSRSQSEQPATCPICYAVIRQSRNLRRHLELRHFAKPGVKKEK
KSKSGNDTTLDSSMEMNTTAEGDNTVGSDGAGGAGSAGGQSSGTTPTRVISNAPQAAGAP
AILAQGV | | Modification type: | Fragment
Mutant
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-DNA binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (295 K; )
| References:
- Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. "The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling." J Mol Biol. 1999; 285(2): 527-44. PubMed: 9878427
| Comments:
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| Region 3 | | Type: | Disordered - Extended | | Name: | DBD | | Location: | 310 - 335 | | Length: | 26 | | Region sequence: |
GNTSGVLSTPKAKRAKHPPGTEKPRS | | Modification type: | Mutant
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-DNA binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (295 K; )
| References:
- Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. "The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling." J Mol Biol. 1999; 285(2): 527-44. PubMed: 9878427
| Comments:
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| References |
- Soeller WC, Oh CE, Kornberg TB. "Isolation of cDNAs encoding the Drosophila GAGA transcription factor." Mol Cell Biol. 1993; 13(12): 7961-70. PubMed: 7504178
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| Comments |
Sequence conflict at residue 278 between sequence from publication and the one from UniProt.
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