PP4C_BOVIN
ID PP4C_BOVIN Reviewed; 307 AA.
AC A6H772;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit;
DE Short=PP4C;
DE Short=Pp4;
DE EC=3.1.3.16;
GN Name=PPP4C;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein phosphatase that is involved in many processes such
CC as microtubule organization at centrosomes, maturation of spliceosomal
CC snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha
CC signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of
CC histone acetylation, DNA damage checkpoint signaling, NF-kappa-B
CC activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a
CC role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-
CC PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated
CC on Ser-140 (gamma-H2AX) generated during DNA replication and required
CC for DNA double strand break repair. Dephosphorylates NDEL1 at CDK1
CC phosphorylation sites and negatively regulates CDK1 activity in
CC interphase. In response to DNA damage, catalyzes RPA2
CC dephosphorylation, an essential step for DNA repair since it allows the
CC efficient RPA2-mediated recruitment of RAD51 to chromatin.
CC {ECO:0000250}.
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: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits (By similarity). Component of the PP4 complexes PPP4C-PPP4R1,
CC PPP4C-PPP4R2, PPP4C-PPP4R2-PPP4R3A, PPP4C-PPP4R2-PPP4R3B and PPP4C-
CC PPP4R4 (By similarity). The PPP4C-PPP4R2 complex appears to be a
CC tetramer composed of 2 molecules of PPP4C and 2 molecules of PPP4R2 (By
CC similarity). Interacts with REL, NFKB1/p50 and RELA (By similarity).
CC Interacts with SMN1 AND GEMIN4. Interacts with IRS4 (phosphorylated)
CC (By similarity). Interacts with SMEK1/PPP4R3A; the interaction requires
CC PP4R2 (By similarity). Interacts with HDAC3 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC A6H772; F1MRS1: PPP4R1; NbExp=3; IntAct=EBI-2638542, EBI-2638538;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}.
CC -!- PTM: Methylation at the C-terminal Leu-307 is critical for interactions
CC with regulatory subunits and functions in DNA repair.
CC {ECO:0000250|UniProtKB:P60510}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC subfamily. {ECO:0000305}.
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DR EMBL; BC146137; AAI46138.1; -; mRNA.
DR RefSeq; NP_001092578.1; NM_001099108.2.
DR AlphaFoldDB; A6H772; -.
DR SMR; A6H772; -.
DR ComplexPortal; CPX-1841; PPP4C-PPP4R1 protein phosphatase 4 complex.
DR IntAct; A6H772; 1.
DR STRING; 9913.ENSBTAP00000017178; -.
DR PaxDb; A6H772; -.
DR PRIDE; A6H772; -.
DR Ensembl; ENSBTAT00000017178; ENSBTAP00000017178; ENSBTAG00000012928.
DR GeneID; 540398; -.
DR KEGG; bta:540398; -.
DR CTD; 5531; -.
DR VEuPathDB; HostDB:ENSBTAG00000012928; -.
DR VGNC; VGNC:33268; PPP4C.
DR eggNOG; KOG0372; Eukaryota.
DR GeneTree; ENSGT00930000151040; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; A6H772; -.
DR OMA; HGQFWDM; -.
DR OrthoDB; 808922at2759; -.
DR TreeFam; TF105559; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000012928; Expressed in spermatid and 103 other tissues.
DR ExpressionAtlas; A6H772; baseline and differential.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IDA:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0033128; P:negative regulation of histone phosphorylation; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
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 Acetylation; Cytoplasm; Cytoskeleton; Hydrolase; Manganese; Metal-binding;
KW Methylation; Nucleus; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P60510"
FT CHAIN 2..307
FT /note="Serine/threonine-protein phosphatase 4 catalytic
FT subunit"
FT /id="PRO_0000307863"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P60510"
FT MOD_RES 307
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P60510"
SQ SEQUENCE 307 AA; 35080 MW; D6FE470A5C6CBCAC CRC64;
MAEISDLDRQ IEQLRRCELI KESEVKALCA KAREILVEES NVQRVDSPVT VCGDIHGQFY
DLKELFRVGG DVPETNYLFM GDFVDRGFYS VETFLLLLAL KVRYPDRITL IRGNHESRQI
TQVYGFYDEC LRKYGSVTVW RYCTEIFDYL SLSAIIDGKI FCVHGGLSPS IQTLDQIRTI
DRKQEVPHDG PMCDLLWSDP EDTTGWGVSP RGAGYLFGSD VVAQFNAAND IDMICRAHQL
VMEGYKWHFN ETVLTVWSAP NYCYRCGNVA AILELDEHLQ KDFIIFEAAP QETRGIPSKK
PVADYFL
