Q24212 · STNB_DROME
- ProteinProtein stoned-B
- GenestnB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1262 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Adapter protein involved in endocytic recycling of synaptic vesicles membranes. May act by mediating the retrieval of synaptotagmin protein Syt from the plasma membrane, thereby facilitating the internalization of multiple synaptic vesicles from the plasma membrane.
Miscellaneous
StnA, which is involved in the same pathway, is derived from the same bicistronic transcript that encodes these two different proteins.
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 | AP-2 adaptor complex | |
Cellular Component | endocytic vesicle | |
Cellular Component | presynaptic active zone | |
Cellular Component | synaptic vesicle | |
Molecular Function | clathrin adaptor activity | |
Molecular Function | scaffold protein binding | |
Biological Process | chemical synaptic transmission | |
Biological Process | clathrin-dependent endocytosis | |
Biological Process | regulation of endocytosis | |
Biological Process | regulation of synaptic vesicle endocytosis | |
Biological Process | synaptic vesicle cycle | |
Biological Process | synaptic vesicle endocytosis | |
Biological Process | synaptic vesicle transport |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein stoned-B
- Short namesStn-B; StonedB
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ24212
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 1186 | in RNA edited version | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000185735 | 1-1262 | Protein stoned-B | |||
Sequence: MANPFLMDEDLDGCDAAANPFLMQSEPEPSSDNPFMAATVASNPFAFGADDLELGAEPEAEATHDNDLDPAMSFFGTTIEAEDDTLSLKSGAEEEDEGKKPPQSQPQLQSHAHPHPPPPRPLVPPQSTQDLISTVSSQLDETSSELLGRIPATRSPSPVSMRDLHSPSPTPDSGLADLLDVSVDSGSSAHTQGIEADLISGVAGGVRLDNPFAVPTAVPNIQAAVPLPATPIKQPPRPPPPRPAPPRPAPPGQAAPQRPPPPLAAVNPPPAAPEADDLLDMFGTTACKPAKPPPPKSKEDILSLFEQPHVPLSQPASKPDLLHDDLDETIGEGEPPEQEEPDTEQSNEISSRDEPVFTSLLIRPDESTHDITSQPQAATGLERQVNNMAAPSGTASTQRATTPDIEITTVEDLPRSDDEDEPEAMQEPETETKPQIEPDTEPEIVSEHSPPTERLVTQAALVDGELIAAEPEPEEMDTGLDFPLASSGQLSANPFASPDEEEPNFAPMPAAVANIFAVNDPDSQMETPKAPSHTANIFASDPDEFDAFSAKFDSVKKDNISIMDGFGGSGAITPTGGDAWGGSAFGSTTISANACGDTNSADDGFGNDDDDFYAMQAPARADSVESVDKDFSVVIRPMAEETSGVAPQLAPPPPPARGVNQAQTTSLPGLTVNPFEDVSGFPAPGLPPTDGTAIKRTDSQDTPQTPLYDEDVSQPLEEFPRLHYIGPGWEMQLRQPNKKKITGQRFWKKIVVRLVVQNDVPVVQLLNQAGDKQPFQELPLQPSYSVSEIGAQQYDQFGKIFTMKLQYIFYKERPGVRPGQVTKAERITNKLTKFAQYAIAGDYEGVKEFGSDLKKLGLPVEHAPQSSQLFKIGSMNYEDMKQFSVCIEEALFKIPALRERALTYKMEEVQVTAVDEITVEQDFEGKILKQIARVRLFFLAFLTGMPTIELGVNDMWRQGKEVVGRHDIIPVATEEWIRLEAVEFHSVVNQKEYERTRTIKFQPPDANYIELLRFRVRPPKNRELPLQLKATWCVSGNKVELRADILVPGFTSRKLGQIPCEDVSVRFPIPECWIYLFRVEKHFRYGSVKSAHRRTGKIKGIERILGAVDTLQESLIEVTSGQAKYEHHHRAIVWRCPRLPKEGQGAYTTHQLVCRMALTSYDQIPSELAPYAFVEFTMPATQVSHTTVRSVSVQDSDGDEPPEKYVRYLARHEYKVGIETTHGESTNAYLAATRPIREEPPTTATKPTASPVAPSDSDTDSN | ||||||
Modified residue | 623 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 626 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Present at synaptic connections both in the CNS and in neuromuscular junctions in the mature embryo (20-22h) and throughout larval development. In the third instar larva, it is expressed in all synaptic bouton types, including I, II and III boutons.
Gene expression databases
Interaction
Subunit
Interacts with the second C2 domain of Syt.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q24212 | Syt1 P21521 | 5 | EBI-604879, EBI-484504 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 3-5 | NPF 1 | ||||
Sequence: NPF | ||||||
Region | 17-36 | Disordered | ||||
Sequence: AANPFLMQSEPEPSSDNPFM | ||||||
Motif | 19-21 | NPF 2 | ||||
Sequence: NPF | ||||||
Motif | 33-35 | NPF 3 | ||||
Sequence: NPF | ||||||
Motif | 43-45 | NPF 4 | ||||
Sequence: NPF | ||||||
Region | 49-189 | Disordered | ||||
Sequence: ADDLELGAEPEAEATHDNDLDPAMSFFGTTIEAEDDTLSLKSGAEEEDEGKKPPQSQPQLQSHAHPHPPPPRPLVPPQSTQDLISTVSSQLDETSSELLGRIPATRSPSPVSMRDLHSPSPTPDSGLADLLDVSVDSGSSA | ||||||
Compositional bias | 86-101 | Basic and acidic residues | ||||
Sequence: LSLKSGAEEEDEGKKP | ||||||
Compositional bias | 111-125 | Pro residues | ||||
Sequence: HAHPHPPPPRPLVPP | ||||||
Compositional bias | 126-150 | Polar residues | ||||
Sequence: QSTQDLISTVSSQLDETSSELLGRI | ||||||
Motif | 210-212 | NPF 5 | ||||
Sequence: NPF | ||||||
Region | 225-452 | Disordered | ||||
Sequence: VPLPATPIKQPPRPPPPRPAPPRPAPPGQAAPQRPPPPLAAVNPPPAAPEADDLLDMFGTTACKPAKPPPPKSKEDILSLFEQPHVPLSQPASKPDLLHDDLDETIGEGEPPEQEEPDTEQSNEISSRDEPVFTSLLIRPDESTHDITSQPQAATGLERQVNNMAAPSGTASTQRATTPDIEITTVEDLPRSDDEDEPEAMQEPETETKPQIEPDTEPEIVSEHSPPT | ||||||
Compositional bias | 229-269 | Pro residues | ||||
Sequence: ATPIKQPPRPPPPRPAPPRPAPPGQAAPQRPPPPLAAVNPP | ||||||
Compositional bias | 330-344 | Acidic residues | ||||
Sequence: IGEGEPPEQEEPDTE | ||||||
Compositional bias | 365-405 | Polar residues | ||||
Sequence: DESTHDITSQPQAATGLERQVNNMAAPSGTASTQRATTPDI | ||||||
Compositional bias | 427-448 | Basic and acidic residues | ||||
Sequence: EPETETKPQIEPDTEPEIVSEH | ||||||
Region | 474-507 | Disordered | ||||
Sequence: EEMDTGLDFPLASSGQLSANPFASPDEEEPNFAP | ||||||
Motif | 493-495 | NPF 6 | ||||
Sequence: NPF | ||||||
Region | 643-709 | Disordered | ||||
Sequence: SGVAPQLAPPPPPARGVNQAQTTSLPGLTVNPFEDVSGFPAPGLPPTDGTAIKRTDSQDTPQTPLYD | ||||||
Motif | 673-675 | NPF 7 | ||||
Sequence: NPF | ||||||
Compositional bias | 693-709 | Polar residues | ||||
Sequence: AIKRTDSQDTPQTPLYD | ||||||
Domain | 728-902 | SHD | ||||
Sequence: GWEMQLRQPNKKKITGQRFWKKIVVRLVVQNDVPVVQLLNQAGDKQPFQELPLQPSYSVSEIGAQQYDQFGKIFTMKLQYIFYKERPGVRPGQVTKAERITNKLTKFAQYAIAGDYEGVKEFGSDLKKLGLPVEHAPQSSQLFKIGSMNYEDMKQFSVCIEEALFKIPALRERAL | ||||||
Region | 847-1108 | Interaction with Syt | ||||
Sequence: KEFGSDLKKLGLPVEHAPQSSQLFKIGSMNYEDMKQFSVCIEEALFKIPALRERALTYKMEEVQVTAVDEITVEQDFEGKILKQIARVRLFFLAFLTGMPTIELGVNDMWRQGKEVVGRHDIIPVATEEWIRLEAVEFHSVVNQKEYERTRTIKFQPPDANYIELLRFRVRPPKNRELPLQLKATWCVSGNKVELRADILVPGFTSRKLGQIPCEDVSVRFPIPECWIYLFRVEKHFRYGSVKSAHRRTGKIKGIERILGAV | ||||||
Domain | 906-1219 | MHD | ||||
Sequence: MEEVQVTAVDEITVEQDFEGKILKQIARVRLFFLAFLTGMPTIELGVNDMWRQGKEVVGRHDIIPVATEEWIRLEAVEFHSVVNQKEYERTRTIKFQPPDANYIELLRFRVRPPKNRELPLQLKATWCVSGNKVELRADILVPGFTSRKLGQIPCEDVSVRFPIPECWIYLFRVEKHFRYGSVKSAHRRTGKIKGIERILGAVDTLQESLIEVTSGQAKYEHHHRAIVWRCPRLPKEGQGAYTTHQLVCRMALTSYDQIPSELAPYAFVEFTMPATQVSHTTVRSVSVQDSDGDEPPEKYVRYLARHEYKVGIE | ||||||
Region | 1226-1262 | Disordered | ||||
Sequence: TNAYLAATRPIREEPPTTATKPTASPVAPSDSDTDSN | ||||||
Compositional bias | 1243-1262 | Polar residues | ||||
Sequence: TATKPTASPVAPSDSDTDSN |
Domain
The Asn-Pro-Phe (NPF) motifs, which are found in proteins involved in the endocytic pathway, are known to interact with the EH domain.
Sequence similarities
Belongs to the Stoned B family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,262
- Mass (Da)137,781
- Last updated2011-10-19 v4
- Checksum877E3EE6B964C23A
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 86-101 | Basic and acidic residues | ||||
Sequence: LSLKSGAEEEDEGKKP | ||||||
Compositional bias | 111-125 | Pro residues | ||||
Sequence: HAHPHPPPPRPLVPP | ||||||
Compositional bias | 126-150 | Polar residues | ||||
Sequence: QSTQDLISTVSSQLDETSSELLGRI | ||||||
Compositional bias | 229-269 | Pro residues | ||||
Sequence: ATPIKQPPRPPPPRPAPPRPAPPGQAAPQRPPPPLAAVNPP | ||||||
Compositional bias | 330-344 | Acidic residues | ||||
Sequence: IGEGEPPEQEEPDTE | ||||||
Compositional bias | 365-405 | Polar residues | ||||
Sequence: DESTHDITSQPQAATGLERQVNNMAAPSGTASTQRATTPDI | ||||||
Compositional bias | 427-448 | Basic and acidic residues | ||||
Sequence: EPETETKPQIEPDTEPEIVSEH | ||||||
Sequence conflict | 657-658 | in Ref. 1; AAC16666 | ||||
Sequence: RG → VE | ||||||
Compositional bias | 693-709 | Polar residues | ||||
Sequence: AIKRTDSQDTPQTPLYD | ||||||
Sequence conflict | 1012 | in Ref. 1; AAC16666 | ||||
Sequence: L → V | ||||||
Compositional bias | 1243-1262 | Polar residues | ||||
Sequence: TATKPTASPVAPSDSDTDSN |
RNA Editing
Edited at position 1186
Partially edited
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U54982 EMBL· GenBank· DDBJ | AAC16666.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014298 EMBL· GenBank· DDBJ | ABI31012.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | EAA46059.3 EMBL· GenBank· DDBJ | Genomic DNA |