PPG1_CANAL
ID PPG1_CANAL Reviewed; 416 AA.
AC Q5A6B6; A0A1D8PM78; Q5A6J5;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A-like PPG1 {ECO:0000303|PubMed:25326520};
DE EC=3.1.3.16 {ECO:0000269|PubMed:25326520};
GN Name=PPG1 {ECO:0000303|PubMed:25326520};
GN OrderedLocusNames=CAALFM_C405050CA; ORFNames=CaO19.11256, CaO19.3774;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION.
RX PubMed=18708562; DOI=10.1128/ec.00129-08;
RA Hanaoka N., Takano Y., Shibuya K., Fugo H., Uehara Y., Niimi M.;
RT "Identification of the putative protein phosphatase gene PTC1 as a
RT virulence-related gene using a silkworm model of Candida albicans
RT infection.";
RL Eukaryot. Cell 7:1640-1648(2008).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=20543849; DOI=10.1038/ng.605;
RA Noble S.M., French S., Kohn L.A., Chen V., Johnson A.D.;
RT "Systematic screens of a Candida albicans homozygous deletion library
RT decouple morphogenetic switching and pathogenicity.";
RL Nat. Genet. 42:590-598(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-90; HIS-173 AND HIS-248,
RP AND ACTIVITY REGULATION.
RX PubMed=25326520; DOI=10.1128/ec.00199-14;
RA Albataineh M.T., Lazzell A., Lopez-Ribot J.L., Kadosh D.;
RT "Ppg1, a PP2A-type protein phosphatase, controls filament extension and
RT virulence in Candida albicans.";
RL Eukaryot. Cell 13:1538-1547(2014).
CC -!- FUNCTION: Serine/threonine-protein phosphatase that plays an important
CC role in controlling colony morphology, filament extension and agar
CC invasion. Down-regulates expression of NRG1 and affects the expression
CC of multiple filament-specific transcripts in response to serum and 37
CC degrees Celsius. Plays a crucial role in virulence in a mouse model of
CC systemic candidiasis. {ECO:0000269|PubMed:25326520}.
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:0000269|PubMed:25326520};
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:0000269|PubMed:25326520};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P67775};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P67775};
CC -!- ACTIVITY REGULATION: Inhibited by okadaic acid, a specific inhibitor of
CC serine/threonine phosphatases of types 1, 2A and 2B.
CC {ECO:0000269|PubMed:25326520}.
CC -!- DISRUPTION PHENOTYPE: Leads to defect in morphogenesis and reduced
CC virulence. {ECO:0000269|PubMed:20543849}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC {ECO:0000305}.
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DR EMBL; CP017626; AOW29246.1; -; Genomic_DNA.
DR RefSeq; XP_717179.1; XM_712086.2.
DR AlphaFoldDB; Q5A6B6; -.
DR SMR; Q5A6B6; -.
DR STRING; 237561.Q5A6B6; -.
DR GeneID; 3641143; -.
DR KEGG; cal:CAALFM_C405050CA; -.
DR CGD; CAL0000190355; PPG1.
DR VEuPathDB; FungiDB:C4_05050C_A; -.
DR eggNOG; KOG0372; Eukaryota.
DR HOGENOM; CLU_004962_0_2_1; -.
DR OrthoDB; 808922at2759; -.
DR PHI-base; PHI:4878; -.
DR PRO; PR:Q5A6B6; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IBA:GO_Central.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; IDA:CGD.
DR GO; GO:0061509; P:asymmetric protein localization to old mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:CGD.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..416
FT /note="Serine/threonine-protein phosphatase PP2A-like PPG1"
FT /id="PRO_0000431445"
FT REGION 363..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 90
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 90
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT VARIANT 305
FT /note="S -> STKHGKVDDSS (in allele: CaO19.11256)"
FT MUTAGEN 90
FT /note="D->L: Abolishes catalytic activity; when associated
FT with A-173 and A-248."
FT /evidence="ECO:0000269|PubMed:25326520"
FT MUTAGEN 173
FT /note="H->A: Abolishes catalytic activity; when associated
FT with L-90 and A-248."
FT /evidence="ECO:0000269|PubMed:25326520"
FT MUTAGEN 248
FT /note="H->A: Abolishes catalytic activity; when associated
FT with L-90 and A-173."
FT /evidence="ECO:0000269|PubMed:25326520"
SQ SEQUENCE 416 AA; 47040 MW; 1E48676379B30EEC CRC64;
MTVPFKIPIS DLDYCLEQLL DHKPPKILPP ETIQQLCHTL KTELLQTPNI ISLQSPISVV
GDIHGQYHDL LEIFQIGGSP PQTNYLFLGD YVDRGYYSVE TISLLLVLKL RYPERVFLIR
GNHESRTITT NYGFYTEVLN KYQGSADVWT FITDLFDYLP LGATIDGKIF ACHGGLSPSC
QQLDQIRAVD RFREIPHDGI MADLVWSDPD VAISDFKLSP RGAGYLFGND VIDKFCQDNN
LVQMIRAHQL CNEGYTSYWK GKCLTVWSAP NYCYRCGNKA SVLEILHSNY DSKDPTNGSD
GEISSINGEF IGVNTSFESF GDDDDDYNDY RNRFNNSSRL HKQQGVLPGQ FFNVFEASKE
NDEDTLQGKS VNGINFDDEL STSDDTSGSG GNNNKGDFFA AFFQERPKRQ QVEYFL
