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PP1B_XENLA
ID   PP1B_XENLA              Reviewed;         327 AA.
AC   Q6GQL2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit;
DE            Short=PP-1B;
DE            EC=3.1.3.16;
GN   Name=ppp1cb;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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 (PP1) is essential
CC       for cell division, it participates in the regulation of glycogen
CC       metabolism, muscle contractility and protein synthesis. Involved in
CC       regulation of ionic conductances and long-term synaptic plasticity (By
CC       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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC072730; AAH72730.1; -; mRNA.
DR   RefSeq; NP_001085426.1; NM_001091957.1.
DR   RefSeq; XP_018120397.1; XM_018264908.1.
DR   AlphaFoldDB; Q6GQL2; -.
DR   SMR; Q6GQL2; -.
DR   BioGRID; 102015; 1.
DR   IntAct; Q6GQL2; 2.
DR   MaxQB; Q6GQL2; -.
DR   GeneID; 108717671; -.
DR   GeneID; 443852; -.
DR   KEGG; xla:108717671; -.
DR   KEGG; xla:443852; -.
DR   CTD; 108717671; -.
DR   CTD; 443852; -.
DR   Xenbase; XB-GENE-961676; ppp1cb.L.
DR   Xenbase; XB-GENE-17344746; ppp1cb.S.
DR   OMA; TVQMSEN; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 108717671; Expressed in camera-type eye and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS: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:0050115; F:myosin-light-chain-phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030155; P:regulation of cell adhesion; 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   InterPro; IPR031675; STPPase_N.
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   Acetylation; Carbohydrate metabolism; Cell cycle; Cell division; Cytoplasm;
KW   Glycogen metabolism; Hydrolase; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..327
FT                   /note="Serine/threonine-protein phosphatase PP1-beta
FT                   catalytic subunit"
FT                   /id="PRO_0000293481"
FT   REGION          305..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        124
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
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"
SQ   SEQUENCE   327 AA;  37173 MW;  F337A83332B89705 CRC64;
     MADGELNVDS LISRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI
     CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL
     RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ
     SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL
     DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK
     KAKYQYGGLN SGRPVTPPRT ANPPKKR
 
 
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