2AAA_DICDI
ID 2AAA_DICDI Reviewed; 584 AA.
AC Q54QR9; Q23922;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein phosphatase 2A scaffold subunit {ECO:0000305};
DE AltName: Full=Protein phosphatase 2A 65 kDa regulatory subunit {ECO:0000305};
DE AltName: Full=Protein phosphatase 2A A subunit {ECO:0000305};
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit pppA {ECO:0000305};
GN Name=pppA; Synonyms=rcdB, veg124; ORFNames=DDB_G0283601;
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].
RC STRAIN=AX4;
RA Loomis W.F.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=18673380; DOI=10.1111/j.1432-0436.2008.00301.x;
RA Lee N.-S., Veeranki S., Kim B., Kim L.;
RT "The function of PP2A/B56 in non-metazoan multicellular development.";
RL Differentiation 76:1104-1110(2008).
RN [4]
RP IDENTIFICATION IN THE SCA1 COMPLEX, AND FUNCTION.
RX PubMed=20493808; DOI=10.1016/j.devcel.2010.03.017;
RA Charest P.G., Shen Z., Lakoduk A., Sasaki A.T., Briggs S.P., Firtel R.A.;
RT "A Ras signaling complex controls the RasC-TORC2 pathway and directed cell
RT migration.";
RL Dev. Cell 18:737-749(2010).
CC -!- FUNCTION: Scaffolding molecule which may coordinate the assembly of the
CC catalytic subunit and a variable regulatory B subunit
CC (PubMed:20493808). Component of the Sca1 complex, a regulator of cell
CC motility, chemotaxis and signal relay (PubMed:20493808). The Sca1
CC complex is recruited to the plasma membrane in a chemoattractant- and
CC F-actin-dependent manner and is enriched at the leading edge of
CC chemotaxing cells where it regulates F-actin dynamics and signal relay
CC by controlling the activation of rasC and the downstream target of
CC rapamycin complex 2 (TORC2)-Akt/protein kinase B (PKB) pathway
CC (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
CC -!- SUBUNIT: Component of the Sca1 complex composed of at least gefA, gefH,
CC scaA, phr, and the protein phosphatase 2A subunits pppA and pho2B
CC (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18673380}.
CC Cell membrane {ECO:0000269|PubMed:20493808}. Note=The Sca1 complex is
CC recruited to the plasma membrane in a chemoattractant- and F-actin-
CC dependent manner and is enriched at the leading edge of chemotaxing
CC cells (PubMed:20493808). Membrane localization of the Sca1 complex is
CC regulated by scaA phosphorylation by PKB and PKB-related PKBR1
CC (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
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DR EMBL; U61987; AAB03670.1; -; mRNA.
DR EMBL; AAFI02000056; EAL65567.1; -; Genomic_DNA.
DR RefSeq; XP_638954.1; XM_633862.1.
DR AlphaFoldDB; Q54QR9; -.
DR SMR; Q54QR9; -.
DR STRING; 44689.DDB0191258; -.
DR PaxDb; Q54QR9; -.
DR EnsemblProtists; EAL65567; EAL65567; DDB_G0283601.
DR GeneID; 8624194; -.
DR KEGG; ddi:DDB_G0283601; -.
DR dictyBase; DDB_G0283601; pppA.
DR eggNOG; KOG0211; Eukaryota.
DR HOGENOM; CLU_015533_2_1_1; -.
DR InParanoid; Q54QR9; -.
DR OMA; SSLCMSW; -.
DR PhylomeDB; Q54QR9; -.
DR Reactome; R-DDI-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-DDI-198753; ERK/MAPK targets.
DR Reactome; R-DDI-202670; ERKs are inactivated.
DR Reactome; R-DDI-389513; CTLA4 inhibitory signaling.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DDI-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-DDI-69231; Cyclin D associated events in G1.
DR Reactome; R-DDI-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR PRO; PR:Q54QR9; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:dictyBase.
DR GO; GO:1905742; C:Ras guanyl-nucleotide exchange factor complex; IDA:dictyBase.
DR GO; GO:0017018; F:myosin phosphatase activity; IDA:dictyBase.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IDA:dictyBase.
DR GO; GO:0031034; P:myosin filament assembly; IDA:dictyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR Pfam; PF02985; HEAT; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 11.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Reference proteome; Repeat.
FT CHAIN 1..584
FT /note="Protein phosphatase 2A scaffold subunit"
FT /id="PRO_0000367475"
FT REPEAT 7..45
FT /note="HEAT 1"
FT REPEAT 46..84
FT /note="HEAT 2"
FT REPEAT 86..123
FT /note="HEAT 3"
FT REPEAT 168..206
FT /note="HEAT 4"
FT REPEAT 207..239
FT /note="HEAT 5"
FT REPEAT 240..278
FT /note="HEAT 6"
FT REPEAT 279..317
FT /note="HEAT 7"
FT REPEAT 318..356
FT /note="HEAT 8"
FT REPEAT 358..395
FT /note="HEAT 9"
FT REPEAT 397..434
FT /note="HEAT 10"
FT REPEAT 441..479
FT /note="HEAT 11"
FT REPEAT 480..512
FT /note="HEAT 12"
FT REPEAT 513..551
FT /note="HEAT 13"
FT REPEAT 553..584
FT /note="HEAT 14"
FT CONFLICT 494
FT /note="L -> F (in Ref. 1; AAB03670)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="S -> F (in Ref. 1; AAB03670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 584 AA; 65076 MW; 74A4AB12F62A359F CRC64;
MASINTESDD YHPIVILIDE LKNEDIQLRL NSIKKLQSIA KALGPERTRT ELIPYLQDSV
LEDEDEVLVV LSEELGNLIE FVGGAEHAVC LLPPLQILAG AEELVVREKA VESLCKIAKE
IPTSSFEESF LPLLFSLSKA DWFTSRTSAC GLFTVSYPRA NAEMKKSLRK TFGGLCHDDT
PMVKRAAATN LGSFAKQIEK ESVKSEILPL FQSLSTDEQD SVRLLGVENC ALLGSMLTNE
ENIQFILPTI KASSLDKSWR VRYMVARLLK ELCESMGTEI TKTELIGAFV KLLKDTEAEV
RTEASLRIAD VCSLLTKEMN IKTILPCVKD LVSDSSQHVR AALAQVIMSL APIYGKEDTL
THLLELFLHL LKDDFPDVRL NIISKLDQVS KVIGIEMLSQ SLLPAIVELA EDHQWRVRLA
IIDYIPLLAS QLGVEFFDEK LGNLCMTWLG DPVFSIREAA TNNLKKLTEV FGVDWAKNNI
IPKVLSLHSH PNYLYRMTTL FSISTLSTVV GGDVISSSMV PLLAKMVSDK VPNIRFNVAK
TFQTIIPLLD STIVQSRVKP LLVKLHEDTD KDVKFYASQA LQLC
