ID   PP2AB_DICDI             Reviewed;         312 AA.
AC   Q54RD6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Protein phosphatase 2A catalytic subunit B {ECO:0000303|PubMed:20493808};
DE            EC=3.1.3.16 {ECO:0000305|PubMed:20493808};
DE   AltName: Full=PP2A-C2 {ECO:0000303|PubMed:20493808};
GN   Name=pho2B {ECO:0000303|PubMed:20493808}; ORFNames=DDB_G0283187;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
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   [2]
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: Component of the Sca1 complex, a regulator of cell motility,
CC       chemotaxis and signal relay (PubMed:20493808). 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 where it regulates F-actin dynamics and signal relay by
CC       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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000305|PubMed:20493808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000305|PubMed:20493808};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P36873};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000250|UniProtKB:P36873};
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: Cell membrane {ECO:0000269|PubMed:20493808}.
CC       Note=The Sca1 complex is recruited to the plasma membrane in a
CC       chemoattractant- and F-actin-dependent manner and is enriched at the
CC       leading edge of chemotaxing cells (PubMed:20493808). Membrane
CC       localization of the Sca1 complex is regulated by scaA phosphorylation
CC       by PKB and PKB-related PKBR1 (PubMed:20493808).
CC       {ECO:0000269|PubMed:20493808}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000051; EAL65832.1; -; Genomic_DNA.
DR   RefSeq; XP_639209.1; XM_634117.1.
DR   AlphaFoldDB; Q54RD6; -.
DR   SMR; Q54RD6; -.
DR   STRING; 44689.Q54RD6; -.
DR   PaxDb; 44689-DDB0234188; -.
DR   EnsemblProtists; EAL65832; EAL65832; DDB_G0283187.
DR   GeneID; 8623982; -.
DR   KEGG; ddi:DDB_G0283187; -.
DR   dictyBase; DDB_G0283187; pho2b.
DR   eggNOG; KOG0372; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; Q54RD6; -.
DR   OMA; HQLCMDG; -.
DR   PhylomeDB; Q54RD6; -.
DR   PRO; PR:Q54RD6; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1905742; C:Ras guanyl-nucleotide exchange factor complex; IDA:dictyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0061509; P:asymmetric protein localization to old mitotic spindle pole body; IBA:GO_Central.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   PANTHER; PTHR45619:SF6; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A-LIKE PPG1; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Manganese; Membrane; Metal-binding; Methylation;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..312
FT                   /note="Protein phosphatase 2A catalytic subunit B"
FT                   /id="PRO_0000368207"
FT   ACT_SITE        116
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P36873"
FT   BINDING         55
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P36873"
FT   BINDING         57
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P36873"
FT   BINDING         83
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P36873"
FT   BINDING         83
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P36873"
FT   BINDING         115
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P36873"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P36873"
FT   BINDING         240
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P36873"
SQ   SEQUENCE   312 AA;  35694 MW;  11DA221AB338021F CRC64;
     MNTSTFNLDH CIEKLQKCEI LPESTIKEIT DKMKELLISE SNVQEIRSPV TVVGDVHGQF
     YDVLEIFKIG GQCPDTNYLF LGDYVDRGYH SVETISLLTC LKLRYPSRIT LLRGNHESRQ
     ITQVYGFYGE CMRKYGNPTV WKYFTEMFDY LSVAAIIDEA IYCVHGGLSP SALSIDQIKV
     LDRFQEVPNE GALSDILWSD PDPDREGFVE SQRGAGYSYG KDVTLRFLQN NKMQHIIRAH
     QLCMDGYQTL FDNKLSTVWS APNYCNRCGN MASIVEVNEK LERYFNTYAA APQSLSNKPT
     LDTNKELPDY FL
//