P40797 · PNUT_DROME
- ProteinProtein peanut
- Genepnut
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids539 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in cytokinesis and possibly cellularization (PubMed:8181057).
Also acts as an enhancer of the sina gene, thus having a role in photoreceptor development (PubMed:8181057).
May be involved in p53-dependent apoptosis (PubMed:17456438).
Also acts as an enhancer of the sina gene, thus having a role in photoreceptor development (PubMed:8181057).
May be involved in p53-dependent apoptosis (PubMed:17456438).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 149-156 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GASGLGKS | ||||||
Binding site | 183 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 209 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 288-296 | GTP (UniProtKB | ChEBI) | ||||
Sequence: KADTMTPDE | ||||||
Binding site | 345 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 360 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameProtein peanut
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP40797
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Apical cell membrane ; Peripheral membrane protein
Note: Localized to the cleavage furrow of dividing cells during cytokinesis and to the intercellular bridge connecting postmitotic daughter cells. Equally found on the cell surfaces of the embryonic central nervous system and on the apical membranes of developing photoreceptor cells in the eye imaginal disk (PubMed:8181057).
Colocalizes with hil at the cell cortex (PubMed:15818553).
Colocalizes with hil at the cell cortex (PubMed:15818553).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000173510 | 1-539 | Protein peanut | |||
Sequence: MNSPRSNAVNGGSGGAISALPSTLAQLALRDKQQAASASASSATNGSSGSESLVGVGGRPPNQPPSVPVAASGKLDTSGGGASNGDSNKLTHDLQEKEHQQAQKPQKPPLPVRQKPMEIAGYVGFANLPNQVYRKAVKRGFEFTLMVVGASGLGKSTLINSMFLSDIYNAEQYPGPSLRKKKTVAVEATKVMLKENGVNLTLTVVDTPGFGDAVDNSNCWVPILEYVDSKYEEYLTAESRVYRKTISDSRVHCCLYFIAPSGHGLLPLDIACMQSLSDKVNLVPVIAKADTMTPDEVHLFKKQILNEIAQHKIKIYDFPATLEDAAEEAKTTQNLRSRVPFAVVGANTIIEQDGKKVRGRRYPWGLVEVENLTHCDFIALRNMVIRTHLQDLKDVTNNVHYENYRCRKLSELGLVDGKARLSNKNPLTQMEEEKREHEQKMKKMEAEMEQVFDMKVKEKMQKLRDSELELARRHEERKKALELQIRELEEKRREFEREKKEWEDVNHVTLEELKRRSLGANSSTDNVDGKKEKKKKGLF | ||||||
Modified residue | 6 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 13 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 517 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated by park, leading to its degradation by the proteasome.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Accumulates at the leading edge of the cleavage furrow in dividing cells and cellularizing embryos (at protein level).
Developmental stage
Maternal gene products found in the early embryo prior to zygotic transcription.
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 29-52 | Polar residues | ||||
Sequence: LRDKQQAASASASSATNGSSGSES | ||||||
Region | 29-90 | Disordered | ||||
Sequence: LRDKQQAASASASSATNGSSGSESLVGVGGRPPNQPPSVPVAASGKLDTSGGGASNGDSNKL | ||||||
Domain | 139-411 | Septin-type G | ||||
Sequence: RGFEFTLMVVGASGLGKSTLINSMFLSDIYNAEQYPGPSLRKKKTVAVEATKVMLKENGVNLTLTVVDTPGFGDAVDNSNCWVPILEYVDSKYEEYLTAESRVYRKTISDSRVHCCLYFIAPSGHGLLPLDIACMQSLSDKVNLVPVIAKADTMTPDEVHLFKKQILNEIAQHKIKIYDFPATLEDAAEEAKTTQNLRSRVPFAVVGANTIIEQDGKKVRGRRYPWGLVEVENLTHCDFIALRNMVIRTHLQDLKDVTNNVHYENYRCRKLSE | ||||||
Region | 149-156 | G1 motif | ||||
Sequence: GASGLGKS | ||||||
Region | 206-209 | G3 motif | ||||
Sequence: DTPG | ||||||
Region | 287-290 | G4 motif | ||||
Sequence: AKAD | ||||||
Coiled coil | 420-516 | |||||
Sequence: RLSNKNPLTQMEEEKREHEQKMKKMEAEMEQVFDMKVKEKMQKLRDSELELARRHEERKKALELQIRELEEKRREFEREKKEWEDVNHVTLEELKRR | ||||||
Region | 513-539 | Disordered | ||||
Sequence: LKRRSLGANSSTDNVDGKKEKKKKGLF |
Sequence similarities
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length539
- Mass (Da)60,143
- Last updated2005-11-08 v2
- ChecksumA8009F7E6F331A32
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 29-52 | Polar residues | ||||
Sequence: LRDKQQAASASASSATNGSSGSES | ||||||
Sequence conflict | 79 | in Ref. 1; AAA19603 | ||||
Sequence: G → S | ||||||
Sequence conflict | 249 | in Ref. 1; AAA19603 | ||||
Sequence: S → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U08103 EMBL· GenBank· DDBJ | AAA19603.1 EMBL· GenBank· DDBJ | mRNA | ||
AE013599 EMBL· GenBank· DDBJ | AAM68857.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY058663 EMBL· GenBank· DDBJ | AAL13892.1 EMBL· GenBank· DDBJ | mRNA |