PPIG_XENTR
ID PPIG_XENTR Reviewed; 323 AA.
AC Q6NVU2;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-gamma catalytic subunit {ECO:0000250|UniProtKB:P36873};
DE Short=PP-1G {ECO:0000250|UniProtKB:P36873};
DE EC=3.1.3.16;
GN Name=ppp1cc {ECO:0000312|EMBL:AAH67911.1}; ORFNames=TEgg061c20.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAJ81429.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg {ECO:0000312|EMBL:CAJ81429.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAJ81429.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH67911.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein phosphatase 1 (PP1) is essential for cell division,
CC and participates in the regulation of glycogen metabolism, muscle
CC contractility and protein synthesis. Promotes nuclear envelope
CC reassembly by targeting nuclear membrane vesicles to chromatin at the
CC end of mitosis. Acts by dephosphorylating membrane proteins such as
CC lamin B receptor (lbr) to regulate the binding of membrane proteins to
CC chromatin (By similarity). {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: PP1 comprises a catalytic subunit, ppp1c1, ppp1cb or ppp1cc,
CC which is folded into its native form by inhibitor 2 and glycogen
CC synthetase kinase 3, and then is complexed to one or several targeting
CC or regulatory subunits. {ECO:0000250|UniProtKB:P63088}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36874}. Nucleus
CC {ECO:0000250}. Cleavage furrow {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome,
CC centromere, kinetochore {ECO:0000250}. Nucleus speckle {ECO:0000250}.
CC Midbody {ECO:0000250}. Mitochondrion {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center
CC {ECO:0000250|UniProtKB:P36873}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000255}.
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DR EMBL; CR761289; CAJ81429.1; -; mRNA.
DR EMBL; BC067911; AAH67911.1; -; mRNA.
DR RefSeq; NP_998835.1; NM_213670.2.
DR AlphaFoldDB; Q6NVU2; -.
DR SMR; Q6NVU2; -.
DR STRING; 8364.ENSXETP00000052896; -.
DR PaxDb; Q6NVU2; -.
DR DNASU; 407879; -.
DR Ensembl; ENSXETT00000052896; ENSXETP00000052896; ENSXETG00000024480.
DR GeneID; 407879; -.
DR KEGG; xtr:407879; -.
DR CTD; 5501; -.
DR Xenbase; XB-GENE-967934; ppp1cc.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; Q6NVU2; -.
DR OMA; GDHECAR; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; Q6NVU2; -.
DR TreeFam; TF354243; -.
DR Reactome; R-XTR-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-XTR-180024; DARPP-32 events.
DR Reactome; R-XTR-2467813; Separation of Sister Chromatids.
DR Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000024480; Expressed in egg cell and 16 other tissues.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; 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; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; 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; IPR037981; PPP1CC.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668:SF204; PTHR11668:SF204; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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 Carbohydrate metabolism; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Glycogen metabolism; Hydrolase; Kinetochore;
KW Manganese; Metal-binding; Mitochondrion; Mitosis; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..323
FT /note="Serine/threonine-protein phosphatase PP1-gamma
FT catalytic subunit"
FT /id="PRO_0000365636"
FT REGION 300..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 36956 MW; 8CD4C5DE036A8C2B CRC64;
MADVDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL
QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
KKKPNASRPV TPPRGMITKQ AKK
