PIAA_DICDI
ID PIAA_DICDI Reviewed; 1148 AA.
AC O77203; Q54ZM8; Q76NV6; Q7KPC0;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein pianissimo A;
DE AltName: Full=Developmental gene 1117 protein;
DE AltName: Full=Protein pianissimo;
DE AltName: Full=Target of rapamycin complex 2 subunit piaA;
DE Short=TORC2 subunit piaA;
GN Name=piaA; Synonyms=amiA, DG1117, pia; ORFNames=DDB_G0277399;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=AX3;
RX PubMed=9389653; DOI=10.1101/gad.11.23.3218;
RA Chen M.-Y., Long Y., Devreotes P.N.;
RT "A novel cytosolic regulator, Pianissimo, is required for chemoattractant
RT receptor and G protein-mediated activation of the 12 transmembrane domain
RT adenylyl cyclase in Dictyostelium.";
RL Genes Dev. 11:3218-3231(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-1148.
RC STRAIN=AX4;
RA Iranfar N., Loomis W.F.;
RT "Dictyostelium discoideum developmental gene DG1117.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=9514897; DOI=10.1006/bbrc.1998.8230;
RA Nagasaki A., Sutoh K., Adachi H., Sutoh K.;
RT "A novel Dictyostelium discoideum gene required for cAMP-dependent cell
RT aggregation.";
RL Biochem. Biophys. Res. Commun. 244:505-513(1998).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11973364; DOI=10.1242/jcs.115.10.2241;
RA Nagasaki A., de Hostos E.L., Uyeda T.Q.;
RT "Genetic and morphological evidence for two parallel pathways of cell-
RT cycle-coupled cytokinesis in Dictyostelium.";
RL J. Cell Sci. 115:2241-2251(2002).
RN [7]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-917.
RX PubMed=12413895; DOI=10.1006/dbio.2002.0809;
RA Pergolizzi B., Peracino B., Silverman J., Ceccarelli A., Noegel A.,
RA Devreotes P., Bozzaro S.;
RT "Temperature-sensitive inhibition of development in Dictyostelium due to a
RT point mutation in the piaA gene.";
RL Dev. Biol. 251:18-26(2002).
RN [8]
RP IDENTIFICATION.
RX PubMed=16234315; DOI=10.1093/bioinformatics/bti726;
RA Booth E.O., Van Driessche N., Zhuchenko O., Kuspa A., Shaulsky G.;
RT "Microarray phenotyping in Dictyostelium reveals a regulon of chemotaxis
RT genes.";
RL Bioinformatics 21:4371-4377(2005).
RN [9]
RP DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=16079174; DOI=10.1091/mbc.e05-04-0342;
RA Lee S., Comer F.I., Sasaki A., McLeod I.X., Duong Y., Okumura K.,
RA Yates J.R. III, Parent C.A., Firtel R.A.;
RT "TOR complex 2 integrates cell movement during chemotaxis and signal relay
RT in Dictyostelium.";
RL Mol. Biol. Cell 16:4572-4583(2005).
RN [10]
RP IDENTIFICATION.
RX PubMed=17659086; DOI=10.1186/gb-2007-8-7-r144;
RA Sawai S., Guan X.-J., Kuspa A., Cox E.C.;
RT "High-throughput analysis of spatio-temporal dynamics in Dictyostelium.";
RL Genome Biol. 8:R144.1-R144.15(2007).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18635356; DOI=10.1016/j.cub.2008.06.068;
RA Kamimura Y., Xiong Y., Iglesias P.A., Hoeller O., Bolourani P.,
RA Devreotes P.N.;
RT "PIP3-independent activation of TorC2 and PKB at the cell's leading edge
RT mediates chemotaxis.";
RL Curr. Biol. 18:1034-1043(2008).
CC -!- FUNCTION: Regulates cell growth, chemotaxis, signal relay and the actin
CC cytoskeleton. Required for chemoattractant receptor and G protein-
CC mediated activation of the 12 transmembrane domain adenylyl cyclase.
CC Functions as a part of protein complex TORC2. TORC2, is presumed to be
CC indirectly negatively modulated by rapamycin and regulates actin
CC polarization. TORC2, but not TORC1, negatively regulates phagocytosis.
CC This protein and dagA protein CRAC, a cytosolic regulator, are both
CC essential for activation of the enzyme adenylyl cyclase. This protein
CC and CRAC do not function redundantly. Both proteins are integral
CC components of the adenylyl cyclase activation pathway.
CC {ECO:0000269|PubMed:11973364, ECO:0000269|PubMed:18635356,
CC ECO:0000269|PubMed:9389653}.
CC -!- SUBUNIT: Part of a complex, TORC2, consisting of tor, lst8, piaA and
CC ripA. Additional proteins, such as 14-3-3 and heat-shock proteins, may
CC also belong to the TORC2 complex. {ECO:0000269|PubMed:16079174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Expression peaks between 2.5 and 5 hours of
CC development. {ECO:0000269|PubMed:9389653}.
CC -!- DISRUPTION PHENOTYPE: Cells are unable to aggregate on bacterial lawns
CC and show impaired chemotaxis, rounded morphology and lack polarity.
CC Phosphorylations of endogenous pkbA/PKB substrates greatly reduced
CC including loss of phosphorylation at 'Thr-470' in endogenous pkgB. In
CC null cells neither chemoattractant stimulation of intact cells nor
CC guanosine gamma thio-phosphate treatment of lysates activates the
CC enzyme adenylyl cyclase. Constitutive expression of piaA reverses these
CC defects. dagA and piaA double mutants require both proteins for
CC reconstitution and activation of adenylyl cyclase. Null cells can
CC respond to exogenous signals by expression of developmental genes
CC necessary for spore formation, although the efficiency of the process
CC is reduced. Null cells possess the machinery to respond to cAMP
CC signals. However, they are unable to aggregate in pure populations
CC suggesting that the defect may be in the production of the cAMP
CC signals. {ECO:0000269|PubMed:11973364, ECO:0000269|PubMed:12413895,
CC ECO:0000269|PubMed:16079174, ECO:0000269|PubMed:18635356,
CC ECO:0000269|PubMed:9389653, ECO:0000269|PubMed:9514897}.
CC -!- SIMILARITY: Belongs to the RICTOR family. {ECO:0000305}.
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DR EMBL; AF085194; AAC35553.1; -; mRNA.
DR EMBL; AAFI02000020; EAL68662.1; -; Genomic_DNA.
DR EMBL; AF080675; AAC31824.1; -; Genomic_DNA.
DR PIR; JC5984; JC5984.
DR RefSeq; XP_642614.1; XM_637522.1.
DR AlphaFoldDB; O77203; -.
DR SMR; O77203; -.
DR BioGRID; 1246034; 1.
DR STRING; 44689.DDB0185055; -.
DR PaxDb; O77203; -.
DR PRIDE; O77203; -.
DR EnsemblProtists; EAL68662; EAL68662; DDB_G0277399.
DR GeneID; 8621031; -.
DR KEGG; ddi:DDB_G0277399; -.
DR dictyBase; DDB_G0277399; piaA.
DR eggNOG; KOG3694; Eukaryota.
DR HOGENOM; CLU_001013_0_0_1; -.
DR InParanoid; O77203; -.
DR OMA; RYVRAGC; -.
DR PhylomeDB; O77203; -.
DR Reactome; R-DDI-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DDI-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-DDI-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DDI-6804757; Regulation of TP53 Degradation.
DR PRO; PR:O77203; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0031932; C:TORC2 complex; IDA:dictyBase.
DR GO; GO:0008047; F:enzyme activator activity; IMP:dictyBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IMP:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IGI:dictyBase.
DR GO; GO:0030010; P:establishment of cell polarity; IGI:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:dictyBase.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:dictyBase.
DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IGI:dictyBase.
DR GO; GO:0043520; P:regulation of myosin II filament assembly; IMP:dictyBase.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IGI:dictyBase.
DR GO; GO:0051602; P:response to electrical stimulus; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR GO; GO:0038203; P:TORC2 signaling; IDA:dictyBase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028268; Pianissimo_fam.
DR InterPro; IPR028267; Pianissimo_N.
DR InterPro; IPR029453; Rictor_IV.
DR InterPro; IPR029451; RICTOR_M.
DR InterPro; IPR029452; RICTOR_V.
DR PANTHER; PTHR13298; PTHR13298; 1.
DR Pfam; PF14663; RasGEF_N_2; 1.
DR Pfam; PF14666; RICTOR_M; 1.
DR Pfam; PF14664; RICTOR_N; 1.
DR Pfam; PF14668; RICTOR_V; 1.
DR SMART; SM01307; RICTOR_M; 1.
DR SMART; SM01308; RICTOR_N; 1.
DR SMART; SM01310; RICTOR_V; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Guanine-nucleotide releasing factor;
KW Reference proteome.
FT CHAIN 1..1148
FT /note="Protein pianissimo A"
FT /id="PRO_0000377480"
FT DOMAIN 803..914
FT /note="N-terminal Ras-GEF"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 917
FT /note="G->D: Temperature-sensitive phenotype and defective
FT G protein-linked adenylyl cyclase activation."
FT /evidence="ECO:0000269|PubMed:12413895"
SQ SEQUENCE 1148 AA; 129529 MW; A417189FA3B3DBAE CRC64;
MTSSDSSVNT TSSSFGNISI SSPNHSSSTP PLNNGNGNNV SASETELKKH VLYSLQCLDE
KTLTLKVKLD HLNKLVELKK SIPDLNKLGI SPTQLYKSVR PFIALPPKTI RTAGLRVMRY
YLSNSNNVKE LLDLKVQYFI TRSLERDKHS EPERIQALKI IRTIMEIDCS LMPHCFVKGL
VSIAENQEDN FCRVCLECLT EISIRNPQIS SHCGGIRTVF DAVLDPFYQG IQESLLICIL
YLLSDKDTRI YIRPKSDLEI ILAPLTNSFN IGVKLKGASK EKEKEKEKED EVAMKKWTAS
SKAVLTLIKS WIGIISLNSD DQGLKSVVDT LRMPQIELQE KALDSIFEIF RVQLPKSIQE
TFGPQKATQT FNFGSETLQD LPSRTRSLRH NLLNNYLSVL LIAFIDNGLI EGLVYLGNYV
ANRDGMSEQE KECSKNISLK STVLLAELLH MSNALLPPSQ CAKLQTLPSL VNSAISFRLD
PRLRSSSNTM VTNLHSYSHN KSSTTLMDST LAIGLTGANK WRRIKGQDRR LDKVDDVKMK
MEWHMDDNQF QQKIKDTQVL VTKDYQKWSW ELMFELLEGP LNNPQHLSNT LKTKFIKRIL
SFLRPNKKLF STMAWTTENL KYVRTACVAL EVLISHEIGF DFLKDNKTII QIADMLKVEL
DYNIKPPPSS SSSSENKKDN VRLLNPEKVL KTMSREYFTM LGTLSSNLLG LEILARNNIF
DYIKPLAELP GRDDLSHLIM TSLDYNVNGA SRTILQKILT SSSRVVRYLA TKYLRFLLRS
GVQDFSNWGV ELLVQQLNDV DAKVSALSLN VLDEACDDPS CLEVLIDLKP NLLKLGKPGK
SLLLRFLSSP KGLENLLQNN GFVEQEEQLW ITSENATYVN AIESAVSESL SPSVWRFKEA
PDGSSTSGVY LPPHFFGELA KTEKGCQLIR KSNNYQRFLK IIQDPTAKQL DKRASLIAIG
HIGSSVDGYS FVKESDTIKL LIGIAEKSQC LALRSTCFYA LGMISCIEEA QPIFNSFGWE
SPSDLNSRIL LPKDLKNSTF LSVPQYQYQG SWADHSFETL PSNHFSDPIK NEIISFVGNL
SSHITAEGAS KNLKRLKIKY PDHFATSEIL NAVFILLNTF KYRLGARRFI YDLFDVAIFS
SDPYHDLN
