Q24212 · STNB_DROME

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentAP-2 adaptor complex
Cellular Componentendocytic vesicle
Cellular Componentpresynaptic active zone
Cellular Componentsynaptic vesicle
Molecular Functionclathrin adaptor activity
Molecular Functionscaffold protein binding
Biological Processchemical synaptic transmission
Biological Processclathrin-dependent endocytosis
Biological Processregulation of endocytosis
Biological Processregulation of synaptic vesicle endocytosis
Biological Processsynaptic vesicle cycle
Biological Processsynaptic vesicle endocytosis
Biological Processsynaptic vesicle transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein stoned-B
  • Short names
    Stn-B; StonedB

Gene names

    • Name
      stnB
    • ORF names
      CG12473

Organism names

  • Taxonomic identifier
  • Strains
    • Oregon-R
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q24212
  • Secondary accessions
    • A4V4V9
    • Q7PLF4
    • Q9W5J3

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Synapse
Note: Colocalizes with synaptic vesicle pools. Colocalizes with the endocytic network within synaptic boutons.

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant1186in RNA edited version

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001857351-1262Protein stoned-B
Modified residue623Phosphoserine
Modified residue626Phosphoserine

Keywords

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

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q24212Syt1 P215215EBI-604879, EBI-484504

Protein-protein interaction databases

Family & Domains

Features

Showing features for motif, region, compositional bias, domain.

TypeIDPosition(s)Description
Motif3-5NPF 1
Region17-36Disordered
Motif19-21NPF 2
Motif33-35NPF 3
Motif43-45NPF 4
Region49-189Disordered
Compositional bias86-101Basic and acidic residues
Compositional bias111-125Pro residues
Compositional bias126-150Polar residues
Motif210-212NPF 5
Region225-452Disordered
Compositional bias229-269Pro residues
Compositional bias330-344Acidic residues
Compositional bias365-405Polar residues
Compositional bias427-448Basic and acidic residues
Region474-507Disordered
Motif493-495NPF 6
Region643-709Disordered
Motif673-675NPF 7
Compositional bias693-709Polar residues
Domain728-902SHD
Region847-1108Interaction with Syt
Domain906-1219MHD
Region1226-1262Disordered
Compositional bias1243-1262Polar residues

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,262
  • Mass (Da)
    137,781
  • Last updated
    2011-10-19 v4
  • Checksum
    877E3EE6B964C23A
MANPFLMDEDLDGCDAAANPFLMQSEPEPSSDNPFMAATVASNPFAFGADDLELGAEPEAEATHDNDLDPAMSFFGTTIEAEDDTLSLKSGAEEEDEGKKPPQSQPQLQSHAHPHPPPPRPLVPPQSTQDLISTVSSQLDETSSELLGRIPATRSPSPVSMRDLHSPSPTPDSGLADLLDVSVDSGSSAHTQGIEADLISGVAGGVRLDNPFAVPTAVPNIQAAVPLPATPIKQPPRPPPPRPAPPRPAPPGQAAPQRPPPPLAAVNPPPAAPEADDLLDMFGTTACKPAKPPPPKSKEDILSLFEQPHVPLSQPASKPDLLHDDLDETIGEGEPPEQEEPDTEQSNEISSRDEPVFTSLLIRPDESTHDITSQPQAATGLERQVNNMAAPSGTASTQRATTPDIEITTVEDLPRSDDEDEPEAMQEPETETKPQIEPDTEPEIVSEHSPPTERLVTQAALVDGELIAAEPEPEEMDTGLDFPLASSGQLSANPFASPDEEEPNFAPMPAAVANIFAVNDPDSQMETPKAPSHTANIFASDPDEFDAFSAKFDSVKKDNISIMDGFGGSGAITPTGGDAWGGSAFGSTTISANACGDTNSADDGFGNDDDDFYAMQAPARADSVESVDKDFSVVIRPMAEETSGVAPQLAPPPPPARGVNQAQTTSLPGLTVNPFEDVSGFPAPGLPPTDGTAIKRTDSQDTPQTPLYDEDVSQPLEEFPRLHYIGPGWEMQLRQPNKKKITGQRFWKKIVVRLVVQNDVPVVQLLNQAGDKQPFQELPLQPSYSVSEIGAQQYDQFGKIFTMKLQYIFYKERPGVRPGQVTKAERITNKLTKFAQYAIAGDYEGVKEFGSDLKKLGLPVEHAPQSSQLFKIGSMNYEDMKQFSVCIEEALFKIPALRERALTYKMEEVQVTAVDEITVEQDFEGKILKQIARVRLFFLAFLTGMPTIELGVNDMWRQGKEVVGRHDIIPVATEEWIRLEAVEFHSVVNQKEYERTRTIKFQPPDANYIELLRFRVRPPKNRELPLQLKATWCVSGNKVELRADILVPGFTSRKLGQIPCEDVSVRFPIPECWIYLFRVEKHFRYGSVKSAHRRTGKIKGIERILGAVDTLQESLIEVTSGQAKYEHHHRAIVWRCPRLPKEGQGAYTTHQLVCRMALTSYDQIPSELAPYAFVEFTMPATQVSHTTVRSVSVQDSDGDEPPEKYVRYLARHEYKVGIETTHGESTNAYLAATRPIREEPPTTATKPTASPVAPSDSDTDSN

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
X2JGF5X2JGF5_DROMEstnB1262
X2JCY4X2JCY4_DROMEstnB1241

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias86-101Basic and acidic residues
Compositional bias111-125Pro residues
Compositional bias126-150Polar residues
Compositional bias229-269Pro residues
Compositional bias330-344Acidic residues
Compositional bias365-405Polar residues
Compositional bias427-448Basic and acidic residues
Sequence conflict657-658in Ref. 1; AAC16666
Compositional bias693-709Polar residues
Sequence conflict1012in Ref. 1; AAC16666
Compositional bias1243-1262Polar residues

RNA Editing

Edited at position 1186
Partially edited

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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