PP1GB_XENLA
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 03-AUG-2022, entry version 93.
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 CTD; 380598; -.
DR Xenbase; XB-GENE-17332984; ppp1cc.S.
DR OMA; GDHECAR; -.
DR OrthoDB; 766640at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 380598; Expressed in egg cell and 19 other 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: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; 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
