ID   PP1GB_XENLA             Reviewed;         323 AA.
AC   Q7SZ10; A4PB28;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1-gamma catalytic subunit B;
DE            Short=PP-1G-B;
DE   AltName: Full=Protein phosphatase 1 zeta {ECO:0000303|PubMed:17448463};
DE            Short=xPP1-zeta {ECO:0000303|PubMed:17448463};
DE            EC=3.1.3.16;
GN   Name=ppp1cc-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:BAF51555.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte {ECO:0000312|EMBL:BAF51555.1};
RX   PubMed=17448463; DOI=10.1016/j.yexcr.2007.03.015;
RA   Ito H., Koyama Y., Takano M., Ishii K., Maeno M., Furukawa K., Horigome T.;
RT   "Nuclear envelope precursor vesicle targeting to chromatin is stimulated by
RT   protein phosphatase 1 in Xenopus egg extracts.";
RL   Exp. Cell Res. 313:1897-1910(2007).
RN   [2] {ECO:0000312|EMBL:AAH54188.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole {ECO:0000312|EMBL:AAH54188.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein phosphatase that associates with over 200 regulatory
CC       proteins to form highly specific holoenzymes which dephosphorylate
CC       hundreds of biological targets. Protein phosphatase 1 (PP1) is
CC       essential for cell division, and participates in the regulation of
CC       glycogen metabolism, muscle contractility and protein synthesis (By
CC       similarity). Promotes nuclear envelope reassembly by targeting nuclear
CC       membrane vesicles to chromatin at the end of mitosis. Acts by
CC       dephosphorylating membrane proteins such as lamin B receptor (lbr) to
CC       regulate the binding of membrane proteins to chromatin (By similarity).
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: 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}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF51555.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAF51555.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB106882; BAF51555.1; ALT_SEQ; mRNA.
DR   EMBL; BC054188; AAH54188.1; -; mRNA.
DR   RefSeq; NP_001080904.1; NM_001087435.1.
DR   AlphaFoldDB; Q7SZ10; -.
DR   SMR; Q7SZ10; -.
DR   DNASU; 380598; -.
DR   GeneID; 380598; -.
DR   KEGG; xla:380598; -.
DR   AGR; Xenbase:XB-GENE-17332984; -.
DR   CTD; 380598; -.
DR   Xenbase; XB-GENE-17332984; ppp1cc.S.
DR   OMA; SDDKMNI; -.
DR   OrthoDB; 19833at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 380598; Expressed in egg cell and 19 other cell types or tissues.
DR   GO; GO:0032154; C:cleavage furrow; 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: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   CDD; cd07414; MPP_PP1_PPKL; 1.
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   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF204; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 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; Glycogen metabolism; Hydrolase; Kinetochore; Manganese;
KW   Metal-binding; Mitochondrion; Mitosis; Nucleus; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..323
FT                   /note="Serine/threonine-protein phosphatase PP1-gamma
FT                   catalytic subunit B"
FT                   /id="PRO_0000365635"
FT   REGION          301..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;  36938 MW;  38D4C5DE036A8C2D 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 TPPRGIITKQ AKK
//