O77203 · PIAA_DICDI

Function

function

Regulates cell growth, chemotaxis, signal relay and the actin cytoskeleton. Required for chemoattractant receptor and G protein-mediated activation of the 12 transmembrane domain adenylyl cyclase. Functions as a part of protein complex TORC2. TORC2, is presumed to be indirectly negatively modulated by rapamycin and regulates actin polarization. TORC2, but not TORC1, negatively regulates phagocytosis. This protein and dagA protein CRAC, a cytosolic regulator, are both essential for activation of the enzyme adenylyl cyclase. This protein and CRAC do not function redundantly. Both proteins are integral components of the adenylyl cyclase activation pathway.

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 Componentcytoplasm
Cellular Componentcytosol
Cellular ComponentTORC2 complex
Molecular Functionadenylate cyclase activator activity
Molecular Functionguanyl-nucleotide exchange factor activity
Biological Processaggregation involved in sorocarp development
Biological Processchemotaxis
Biological Processchemotaxis to cAMP
Biological Processestablishment of cell polarity
Biological ProcessG protein-coupled chemorepellent receptor signaling pathway
Biological Processmitotic cytokinesis
Biological Processnegative regulation of asexual reproduction
Biological Processnegative regulation of phagocytosis
Biological Processnegative regulation of Ras protein signal transduction
Biological Processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Processregulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway
Biological Processregulation of myosin II filament assembly
Biological Processregulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Processresponse to electrical stimulus
Biological Processsorocarp development
Biological ProcessTORC2 signaling

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein pianissimo A
  • Alternative names
    • Developmental gene 1117 protein
    • Protein pianissimo
    • Target of rapamycin complex 2 subunit piaA (TORC2 subunit piaA)

Gene names

    • Name
      piaA
    • Synonyms
      amiA, DG1117, pia
    • ORF names
      DDB_G0277399

Organism names

Accessions

  • Primary accession
    O77203
  • Secondary accessions
    • Q54ZM8
    • Q76NV6
    • Q7KPC0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Cells are unable to aggregate on bacterial lawns and show impaired chemotaxis, rounded morphology and lack polarity. Phosphorylations of endogenous pkbA/PKB substrates greatly reduced including loss of phosphorylation at 'Thr-470' in endogenous pkgB. In null cells neither chemoattractant stimulation of intact cells nor guanosine gamma thio-phosphate treatment of lysates activates the enzyme adenylyl cyclase. Constitutive expression of piaA reverses these defects. dagA and piaA double mutants require both proteins for reconstitution and activation of adenylyl cyclase. Null cells can respond to exogenous signals by expression of developmental genes necessary for spore formation, although the efficiency of the process is reduced. Null cells possess the machinery to respond to cAMP signals. However, they are unable to aggregate in pure populations suggesting that the defect may be in the production of the cAMP signals.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis917Temperature-sensitive phenotype and defective G protein-linked adenylyl cyclase activation.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003774801-1148Protein pianissimo A

Proteomic databases

Expression

Developmental stage

Expression peaks between 2.5 and 5 hours of development.

Interaction

Subunit

Part of a complex, TORC2, consisting of tor, lst8, piaA and ripA. Additional proteins, such as 14-3-3 and heat-shock proteins, may also belong to the TORC2 complex.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-41Disordered
Domain803-914N-terminal Ras-GEF

Sequence similarities

Belongs to the RICTOR family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,148
  • Mass (Da)
    129,529
  • Last updated
    1998-11-01 v1
  • Checksum
    A417189FA3B3DBAE
MTSSDSSVNTTSSSFGNISISSPNHSSSTPPLNNGNGNNVSASETELKKHVLYSLQCLDEKTLTLKVKLDHLNKLVELKKSIPDLNKLGISPTQLYKSVRPFIALPPKTIRTAGLRVMRYYLSNSNNVKELLDLKVQYFITRSLERDKHSEPERIQALKIIRTIMEIDCSLMPHCFVKGLVSIAENQEDNFCRVCLECLTEISIRNPQISSHCGGIRTVFDAVLDPFYQGIQESLLICILYLLSDKDTRIYIRPKSDLEIILAPLTNSFNIGVKLKGASKEKEKEKEKEDEVAMKKWTASSKAVLTLIKSWIGIISLNSDDQGLKSVVDTLRMPQIELQEKALDSIFEIFRVQLPKSIQETFGPQKATQTFNFGSETLQDLPSRTRSLRHNLLNNYLSVLLIAFIDNGLIEGLVYLGNYVANRDGMSEQEKECSKNISLKSTVLLAELLHMSNALLPPSQCAKLQTLPSLVNSAISFRLDPRLRSSSNTMVTNLHSYSHNKSSTTLMDSTLAIGLTGANKWRRIKGQDRRLDKVDDVKMKMEWHMDDNQFQQKIKDTQVLVTKDYQKWSWELMFELLEGPLNNPQHLSNTLKTKFIKRILSFLRPNKKLFSTMAWTTENLKYVRTACVALEVLISHEIGFDFLKDNKTIIQIADMLKVELDYNIKPPPSSSSSSENKKDNVRLLNPEKVLKTMSREYFTMLGTLSSNLLGLEILARNNIFDYIKPLAELPGRDDLSHLIMTSLDYNVNGASRTILQKILTSSSRVVRYLATKYLRFLLRSGVQDFSNWGVELLVQQLNDVDAKVSALSLNVLDEACDDPSCLEVLIDLKPNLLKLGKPGKSLLLRFLSSPKGLENLLQNNGFVEQEEQLWITSENATYVNAIESAVSESLSPSVWRFKEAPDGSSTSGVYLPPHFFGELAKTEKGCQLIRKSNNYQRFLKIIQDPTAKQLDKRASLIAIGHIGSSVDGYSFVKESDTIKLLIGIAEKSQCLALRSTCFYALGMISCIEEAQPIFNSFGWESPSDLNSRILLPKDLKNSTFLSVPQYQYQGSWADHSFETLPSNHFSDPIKNEIISFVGNLSSHITAEGASKNLKRLKIKYPDHFATSEILNAVFILLNTFKYRLGARRFIYDLFDVAIFSSDPYHDLN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF085194
EMBL· GenBank· DDBJ
AAC35553.1
EMBL· GenBank· DDBJ
mRNA
AAFI02000020
EMBL· GenBank· DDBJ
EAL68662.1
EMBL· GenBank· DDBJ
Genomic DNA
AF080675
EMBL· GenBank· DDBJ
AAC31824.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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