O61643 · INHB_DROME

Function

function

Controls several aspects of neuronal morphogenesis; essential for optic lobe development, EcR-B1 expression in larval brains, mushroom body remodeling, dorsal neuron morphogenesis and motoneuron axon guidance. Ligands Actbeta and daw act redundantly through the Activin receptor Babo and its transcriptional mediator Smad2 (Smox), to regulate neuroblast numbers and proliferation rates in the developing larval brain.

Features

Showing features for site.

1946100200300400500600700800900
TypeIDPosition(s)Description
Site585-586Cleavage; by tok and tld

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 Componentextracellular space
Molecular Functioncytokine activity
Molecular Functiongrowth factor activity
Biological Processactivin receptor signaling pathway
Biological Processglucose homeostasis
Biological Processmushroom body development
Biological Processpositive regulation of glycogen catabolic process
Biological Processpositive regulation of imaginal disc growth
Biological Processpositive regulation of neuroblast proliferation
Biological ProcessR8 cell fate specification
Biological Processregulation of imaginal disc-derived wing size
Biological Processregulation of synapse structure or activity
Biological Processresponse to glucose

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Inhibin beta chain
  • Alternative names
    • Activin beta chain (dAct; dActivin)

Gene names

    • Name
      Actbeta
    • Synonyms
      activin-beta
    • ORF names
      CG11062

Organism names

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

Accessions

  • Primary accession
    O61643
  • Secondary accessions
    • Q8MRB1
    • Q8WR60
    • Q9V497

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Development of larvae with small brains and aberrant photoreceptor axon targeting.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis583-586Abolishes cleavage by tok.

PTM/Processing

Features

Showing features for propeptide, signal, glycosylation, chain, disulfide bond.

TypeIDPosition(s)Description
PropeptidePRO_0000033742?-830
Signal1-?
Glycosylation208N-linked (GlcNAc...) asparagine
Glycosylation217N-linked (GlcNAc...) asparagine
Glycosylation271N-linked (GlcNAc...) asparagine
Glycosylation389N-linked (GlcNAc...) asparagine
Glycosylation471N-linked (GlcNAc...) asparagine
Glycosylation484N-linked (GlcNAc...) asparagine
Glycosylation542N-linked (GlcNAc...) asparagine
Glycosylation561N-linked (GlcNAc...) asparagine
Glycosylation566N-linked (GlcNAc...) asparagine
Glycosylation732N-linked (GlcNAc...) asparagine
Glycosylation804N-linked (GlcNAc...) asparagine
ChainPRO_0000033743834-946Inhibin beta chain
Disulfide bond837↔846
Disulfide bond845↔912
Disulfide bond874↔943
Disulfide bond878↔945
Disulfide bond911Interchain

Post-translational modification

Cleaved in vitro by metalloproteases tok and tld to produce a 30 kDa product.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed in larval brains.

Developmental stage

Expressed in embryonic, larval and adult stages.

Gene expression databases

Interaction

Subunit

Homodimer or heterodimer; disulfide-linked.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region115-142Disordered
Region174-194Disordered
Region436-462Disordered
Compositional bias447-462Basic and acidic residues

Sequence similarities

Belongs to the TGF-beta family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    946
  • Mass (Da)
    108,792
  • Last updated
    2003-01-27 v2
  • Checksum
    7CECD6E73EAA306B
MRFAFDSNHSQSGAPFKGSRCFFNCQCICCRQGCCVVVVKCCCCFNLNCCNSLGSRKSFPQPAAMRKKVADLEVLRVSRFVAVILVLARWVTAVATLLTSCILLDIFSVPGQSGVADRSQASSRTVHVSVPTTPNETPSSTSETKLKLLYGYTSYDINNDQQVKSNNLCRVLCKSRNRKRQRRRRRRRNHRRRRHRYTKRLHHLMQDNMSGFEQRLNFSDAKCQSLETNYGTNYDLVQGGKLFSQSERSLLVSPLREIEAPWPAIHGSMRNCSKIKRNRANLIWLLIGLVWFEVKLINCNGISSSNYYASNLESHKGCTLCHESGKPNIYTDKDNPHTDYNIYNKYHSNNNFNKKTNQPHNNIAPSDEVRLESIKRQILTKLGLSHKPNVSHPLPKQFIWETIYRVDGGRMIPNNAFGSSGKNLDQKTIKLRAFASPGSHLFNGRGGRTDQRSERDPSHHKYRSPFDFTFNISKNNVYGKVLRNRSLERIDKKNSFLNGWTENRQLKINSQIASMPIELKSHHNSSPKELKSGAVRKVNGINGTQMNENALKKSTYPIDINHSIDNKTHTGKNGEMSHNDYEYFNDYSVQTHDKNRYHEGRSSIGYQPAIHNIEYENQKGHHESFADDHENIDHEDFFGNTQEIITFAEEGTQYRQYRILEFSAQNRRVPSQKLSIRSAQIHIRIDKPHSLWIEKAKSLPEKHLLNTKRKWGANKPHHRIKIWVFQLSTSINITEKGIDKAIIFRASFQVDPKNLGWQKFDLTDTIREWYGHTSHEKLRLLIDCTGCGGRYSLHLFQTSKLRGNSSDYLSTNPNRPFLVLHTESSRTRRVRRRAVDCGGALNGQCCKESFYVSFKALGWDDWIIAPRGYFANYCRGDCTGSFRTPDTFQTFHAHFIEEYRKMGLMNGMRPCCAPIKFSSMSLIYYGDDGIIKRDLPKMVVDECGCP

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict275in Ref. 4; AAL51005
Compositional bias447-462Basic and acidic residues
Sequence conflict517in Ref. 4; AAL51005

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014135
EMBL· GenBank· DDBJ
AAF59386.3
EMBL· GenBank· DDBJ
Genomic DNA
AY121686
EMBL· GenBank· DDBJ
AAM52013.1
EMBL· GenBank· DDBJ
mRNA
AF454392
EMBL· GenBank· DDBJ
AAL51005.1
EMBL· GenBank· DDBJ
mRNA
AF054822
EMBL· GenBank· DDBJ
AAC39083.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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