PP4CA_DANRE
ID PP4CA_DANRE Reviewed; 311 AA.
AC A8WGP3; Q7ZWF9;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit A;
DE Short=PP4C-A;
DE EC=3.1.3.16;
GN Name=ppp4ca; Synonyms=pp4c; ORFNames=zgc:56413;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein phosphatase that regulates many processes such as
CC microtubule organization at centrosomes. {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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC subfamily. {ECO:0000305}.
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DR EMBL; BC049430; AAH49430.1; -; mRNA.
DR EMBL; BC154790; AAI54791.1; -; mRNA.
DR RefSeq; NP_001103884.1; NM_001110414.1.
DR AlphaFoldDB; A8WGP3; -.
DR SMR; A8WGP3; -.
DR STRING; 7955.ENSDARP00000094516; -.
DR PaxDb; A8WGP3; -.
DR PeptideAtlas; A8WGP3; -.
DR PRIDE; A8WGP3; -.
DR Ensembl; ENSDART00000103741; ENSDARP00000094516; ENSDARG00000070570.
DR GeneID; 100003080; -.
DR KEGG; dre:100003080; -.
DR CTD; 100003080; -.
DR ZFIN; ZDB-GENE-030131-4433; ppp4ca.
DR eggNOG; KOG0372; Eukaryota.
DR GeneTree; ENSGT00930000151040; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; A8WGP3; -.
DR OMA; CELITEQ; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; A8WGP3; -.
DR TreeFam; TF105559; -.
DR PRO; PR:A8WGP3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000070570; Expressed in cleaving embryo and 29 other tissues.
DR ExpressionAtlas; A8WGP3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:ZFIN.
DR GO; GO:0048264; P:determination of ventral identity; IMP:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Hydrolase; Manganese; Metal-binding; Methylation;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..311
FT /note="Serine/threonine-protein phosphatase 4 catalytic
FT subunit A"
FT /id="PRO_0000353206"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 311
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250"
FT CONFLICT 128
FT /note="Y -> H (in Ref. 1; AAH49430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 35456 MW; C9D785FD393887F5 CRC64;
MCVIMGDFTD LDRQIEQLRR CELIKENEVK ALCAKAREIL VEESNVQSVD SPVTVCGDIH
GQFYDLKELF RVGGEVPETN YLFMGDFVDR GFYSVETFLL LLALKVRYPD RITLIRGNHE
SRQITQVYGF FDECHRKYGS ATVWRYCTEI FDYLSLSAIV DGKIFCVHGG LSPSIQTLDQ
IRTIDRKQEV PHDGPMCDLL WSDPEDTTGW GVSPRGAGYL FGSDVVAQFN AANDISMICR
AHQLVMEGYK WHFNDTVLTV WSAPNYCYRC GNVAAILELD EHLQKEFIIF EAAPQETRGL
PSKKPVADYF L
