SIT4_CANAL
ID SIT4_CANAL Reviewed; 314 AA.
AC Q59KY8; A0A1D8PD98;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine/threonine-protein phosphatase SIT4;
DE EC=3.1.3.16;
GN Name=SIT4; OrderedLocusNames=CAALFM_C104380WA;
GN ORFNames=CaO19.12667, CaO19.5200;
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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=14731272; DOI=10.1111/j.1365-2958.2003.03879.x;
RA Lee C.M., Nantel A., Jiang L., Whiteway M., Shen S.H.;
RT "The serine/threonine protein phosphatase SIT4 modulates yeast-to-hypha
RT morphogenesis and virulence in Candida albicans.";
RL Mol. Microbiol. 51:691-709(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH MDS3.
RX PubMed=20457806; DOI=10.1128/mcb.01540-09;
RA Zacchi L.F., Gomez-Raja J., Davis D.A.;
RT "Mds3 regulates morphogenesis in Candida albicans through the TOR
RT pathway.";
RL Mol. Cell. Biol. 30:3695-3710(2010).
CC -!- FUNCTION: Serine/threonine protein phosphatase which is involved in the
CC dephosphorylation of the large subunit of RNA polymerase II. Is
CC required in late G1 for normal G1 cyclin expression, bud initiation and
CC expression of certain genes that are periodically expressed during late
CC G1 (By similarity). Plays a role during hyphal growth through the
CC regulation of cell wall biogenesis, osmosensing and protein
CC translation. Involved in virulence in a mouse systemic infection model.
CC {ECO:0000250, ECO:0000269|PubMed:14731272,
CC ECO:0000269|PubMed:20457806}.
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with MDS3. {ECO:0000269|PubMed:20457806}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Causes growth retardation and leads to
CC significant reduction in virulence. {ECO:0000269|PubMed:14731272}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V)
CC subfamily. {ECO:0000305}.
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DR EMBL; CP017623; AOW26112.1; -; Genomic_DNA.
DR RefSeq; XP_710408.1; XM_705316.2.
DR AlphaFoldDB; Q59KY8; -.
DR SMR; Q59KY8; -.
DR BioGRID; 1231075; 2.
DR STRING; 237561.Q59KY8; -.
DR GeneID; 3647993; -.
DR KEGG; cal:CAALFM_C104380WA; -.
DR CGD; CAL0000187173; SIT4.
DR VEuPathDB; FungiDB:C1_04380W_A; -.
DR eggNOG; KOG0373; Eukaryota.
DR HOGENOM; CLU_004962_0_5_1; -.
DR InParanoid; Q59KY8; -.
DR OMA; CQNKYGN; -.
DR OrthoDB; 808922at2759; -.
DR PHI-base; PHI:378; -.
DR PRO; PR:Q59KY8; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IEA:EnsemblFungi.
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; IGI:CGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IEA:EnsemblFungi.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036171; P:filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:0036168; P:filamentous growth of a population of unicellular organisms in response to heat; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:2001211; P:negative regulation of isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:EnsemblFungi.
DR GO; GO:1900439; P:positive regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:1900442; P:positive regulation of filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0006468; P:protein phosphorylation; IGI:CGD.
DR GO; GO:1903379; P:regulation of mitotic chromosome condensation; IEA:EnsemblFungi.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
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; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Mitosis; Protein phosphatase; Reference proteome; Virulence.
FT CHAIN 1..314
FT /note="Serine/threonine-protein phosphatase SIT4"
FT /id="PRO_0000422107"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 314 AA; 35899 MW; 9D9577F956F7580F CRC64;
MGERGPDQWL EQIKNCISLS ESDMKQLCEL VKELLMEESN IQPVQSPVTV CGDIHGQFHD
LLELFRTAGG LPSDDNQTNF IFLGDYVDRG YFSLETFTLL MVLKVKYPHR ITLVRGNHES
RQITQVYGFY EECLTKYGST TVWKYCCQVF DFLTLAAIID GKILCVHGGL SPEIRMLDQI
RVLSRAQEVP HEGGFCDLVW SDPDNIDTWA VSPRGAGWLF GSKVSREFNH INNLQLIARA
HQLVMEGFRY HFKEKDVVTV WSAPNYCYRC GNVASVMQVD EDLEPNFKIF SAVQDGDLSV
KNNANKQQRS DYFL
