O70566 · DIAP2_MOUSE
- ProteinProtein diaphanous homolog 2
- GeneDiaph2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1098 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May be involved in oogenesis.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | actin filament | |
Molecular Function | actin binding | |
Molecular Function | small GTPase binding | |
Biological Process | actin filament polymerization | |
Biological Process | axon midline choice point recognition | |
Biological Process | ephrin receptor signaling pathway | |
Biological Process | multicellular organismal locomotion | |
Biological Process | negative regulation of neuron projection regeneration | |
Biological Process | neuron projection retraction | |
Biological Process | oogenesis | |
Biological Process | protein localization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein diaphanous homolog 2
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO70566
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000194896 | 1-1098 | Protein diaphanous homolog 2 | |||
Sequence: MEELGAAASGAGGGGGGGEEHGGGRSNKRGAGNRAANEEETRNKPKLRDRITSFRKSATKREKPVIQHSIDYQTAVVEIPPALIVHDDRSLILSEKEVLDLFEKMMEDMNLNEEKKAPLRKKDFSIKREMVVQYISATSKSIVGSKVLGGLKNSKHEFTLSSQEYVHELRSGISDEKLLNCLESLRVSLTSHPVSWVNNFGYEGLGVLLDVLEKLLDKKQQENIDKKNQYKVIQCLKAFMNNKFGLQRILGDERSLLLLARAIDPKQQNMMTEIVKILSAICIVGEENILDKLLGGITAAAELNNRERFSPIVEGLENNEALHLQVACMQFINALVTSPYDLDFRIHLRNEFLRCGLKAMLPTLKEIENEGLDIQLRVFEENKEDDLSELSHRLNDIRAEMDDINEVYHLLYNMLKDTAAEPYLLSILQHFLLIRNDYYIRPQYYKIIEECVSQIVLHCSGMDPDFKYRQRIDFDFTHLLDACVNKAKVEENEQKAMEFSKKFDEEFTARQEAQAELQKRDEKIKELETEIQQLRGQGVPSAIPGPPPPPPLPGAGPCPPPPPPPPPPPPLPGVVPPPPPPLPGMPGIPPPPPPPLSGVPPPPPPPGGVFPLLSGPIELPYGMKQKKLYKPDIPMKRINWSKIEPKELSENCVWLKLKEEKYENADLFAKLALTFPSQMKGQRNTEAAEENRSGPPKKKVKELRILDTKTAQNLSIFLGSYRMPYEEIKNIILEVNEEMLSEALIQNLVKYLPDQNALRELAQLKSEYDDLCEPEQFGVVMSTVKMLRPRLTSILFKLTFEEHVNNIKPSIIAVTLACEELKKSESFKRLLELILLVGNYMNSGSRNAQSLGFKINFLCKIKDTKSADQKSTLLHFLAEICDEKYRDILKFPDELEHVESAGKVSAQILKSNLVAMEQSILHLEKNIKNFPPAESHHDKFVEKMMSFTQNAREQYDKLSTMHSNMLKLYESLGEYFIFDPNTVNMEEFFGDLNTFRTLFLEALKENHKRKEMEEKSRRAKLAKEKAEQEKLERQKKKKQLIDINKEGDETGVMDNLLEALQSGAAFRDRRKRIPRNPDNRRPPLERSRSRHNGAMSSK |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed in liver, heart, kidney, ovary and testis, at 16 dpc, P6 and P16.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-62 | Disordered | ||||
Sequence: MEELGAAASGAGGGGGGGEEHGGGRSNKRGAGNRAANEEETRNKPKLRDRITSFRKSATKRE | ||||||
Compositional bias | 22-62 | Basic and acidic residues | ||||
Sequence: GGGRSNKRGAGNRAANEEETRNKPKLRDRITSFRKSATKRE | ||||||
Domain | 90-463 | GBD/FH3 | ||||
Sequence: SLILSEKEVLDLFEKMMEDMNLNEEKKAPLRKKDFSIKREMVVQYISATSKSIVGSKVLGGLKNSKHEFTLSSQEYVHELRSGISDEKLLNCLESLRVSLTSHPVSWVNNFGYEGLGVLLDVLEKLLDKKQQENIDKKNQYKVIQCLKAFMNNKFGLQRILGDERSLLLLARAIDPKQQNMMTEIVKILSAICIVGEENILDKLLGGITAAAELNNRERFSPIVEGLENNEALHLQVACMQFINALVTSPYDLDFRIHLRNEFLRCGLKAMLPTLKEIENEGLDIQLRVFEENKEDDLSELSHRLNDIRAEMDDINEVYHLLYNMLKDTAAEPYLLSILQHFLLIRNDYYIRPQYYKIIEECVSQIVLHCSGMD | ||||||
Coiled coil | 375-416 | |||||
Sequence: QLRVFEENKEDDLSELSHRLNDIRAEMDDINEVYHLLYNMLK | ||||||
Coiled coil | 490-539 | |||||
Sequence: EENEQKAMEFSKKFDEEFTARQEAQAELQKRDEKIKELETEIQQLRGQGV | ||||||
Region | 537-565 | Disordered | ||||
Sequence: QGVPSAIPGPPPPPPLPGAGPCPPPPPPP | ||||||
Compositional bias | 541-565 | Pro residues | ||||
Sequence: SAIPGPPPPPPLPGAGPCPPPPPPP | ||||||
Domain | 544-620 | FH1 | ||||
Sequence: PGPPPPPPLPGAGPCPPPPPPPPPPPPLPGVVPPPPPPLPGMPGIPPPPPPPLSGVPPPPPPPGGVFPLLSGPIELP | ||||||
Region | 578-611 | Disordered | ||||
Sequence: PPPPLPGMPGIPPPPPPPLSGVPPPPPPPGGVFP | ||||||
Domain | 625-1025 | FH2 | ||||
Sequence: QKKLYKPDIPMKRINWSKIEPKELSENCVWLKLKEEKYENADLFAKLALTFPSQMKGQRNTEAAEENRSGPPKKKVKELRILDTKTAQNLSIFLGSYRMPYEEIKNIILEVNEEMLSEALIQNLVKYLPDQNALRELAQLKSEYDDLCEPEQFGVVMSTVKMLRPRLTSILFKLTFEEHVNNIKPSIIAVTLACEELKKSESFKRLLELILLVGNYMNSGSRNAQSLGFKINFLCKIKDTKSADQKSTLLHFLAEICDEKYRDILKFPDELEHVESAGKVSAQILKSNLVAMEQSILHLEKNIKNFPPAESHHDKFVEKMMSFTQNAREQYDKLSTMHSNMLKLYESLGEYFIFDPNTVNMEEFFGDLNTFRTLFLEALKENHKRKEMEEKSRRAKLAKEK | ||||||
Region | 679-699 | Disordered | ||||
Sequence: MKGQRNTEAAEENRSGPPKKK | ||||||
Compositional bias | 685-699 | Basic and acidic residues | ||||
Sequence: TEAAEENRSGPPKKK | ||||||
Coiled coil | 999-1050 | |||||
Sequence: FLEALKENHKRKEMEEKSRRAKLAKEKAEQEKLERQKKKKQLIDINKEGDET | ||||||
Region | 1007-1047 | Disordered | ||||
Sequence: HKRKEMEEKSRRAKLAKEKAEQEKLERQKKKKQLIDINKEG | ||||||
Domain | 1048-1078 | DAD | ||||
Sequence: DETGVMDNLLEALQSGAAFRDRRKRIPRNPD | ||||||
Region | 1063-1098 | Disordered | ||||
Sequence: GAAFRDRRKRIPRNPDNRRPPLERSRSRHNGAMSSK | ||||||
Compositional bias | 1064-1092 | Basic and acidic residues | ||||
Sequence: AAFRDRRKRIPRNPDNRRPPLERSRSRHN |
Domain
The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).
Sequence similarities
Belongs to the formin homology family. Diaphanous subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,098
- Mass (Da)124,871
- Last updated2004-02-16 v2
- ChecksumBB19D49E049EA8CA
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q6W4W7 | Q6W4W7_MOUSE | Diaph2 | 1102 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 22-62 | Basic and acidic residues | ||||
Sequence: GGGRSNKRGAGNRAANEEETRNKPKLRDRITSFRKSATKRE | ||||||
Compositional bias | 541-565 | Pro residues | ||||
Sequence: SAIPGPPPPPPLPGAGPCPPPPPPP | ||||||
Compositional bias | 685-699 | Basic and acidic residues | ||||
Sequence: TEAAEENRSGPPKKK | ||||||
Sequence conflict | 750-751 | in Ref. 2; CAA75871 | ||||
Sequence: KY → RD | ||||||
Compositional bias | 1064-1092 | Basic and acidic residues | ||||
Sequence: AAFRDRRKRIPRNPDNRRPPLERSRSRHN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK088648 EMBL· GenBank· DDBJ | BAC40476.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
Y15910 EMBL· GenBank· DDBJ | CAA75871.1 EMBL· GenBank· DDBJ | mRNA |