ID A0A287DAA4_ICTTR Unreviewed; 298 AA.
AC A0A287DAA4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit {ECO:0000256|ARBA:ARBA00040741};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.53 {ECO:0000256|ARBA:ARBA00038961};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000030497.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000030497.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[myosin light chain] = L-seryl-[myosin
CC light chain] + phosphate; Xref=Rhea:RHEA:12849, Rhea:RHEA-COMP:13684,
CC Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.53;
CC Evidence={ECO:0000256|ARBA:ARBA00036592};
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 Evidence={ECO:0000256|ARBA:ARBA00001512};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[myosin light chain] = L-threonyl-
CC [myosin light chain] + phosphate; Xref=Rhea:RHEA:53988, Rhea:RHEA-
CC COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.53;
CC Evidence={ECO:0000256|ARBA:ARBA00035866};
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 Evidence={ECO:0000256|ARBA:ARBA00001482};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000256|ARBA:ARBA00005333}.
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DR EMBL; AGTP01104710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A287DAA4; -.
DR STRING; 43179.ENSSTOP00000030497; -.
DR Ensembl; ENSSTOT00000037365.1; ENSSTOP00000030497.1; ENSSTOG00000034695.1.
DR GeneTree; ENSGT00940000154644; -.
DR InParanoid; A0A287DAA4; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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:SF472; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-BETA 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.
PE 3: Inferred from homology;
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell cycle {ECO:0000256|ARBA:ARBA00022618};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 30..269
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|SMART:SM00156"
SQ SEQUENCE 298 AA; 33470 MW; EE409420BF7806CD CRC64;
LSSGEALSLV STSTHLLVVP GCRPGKIVQM TQAEVQGLCI KSHAIFLSQP ILLELEAPLK
ICGDIHGQYT DLLRLFEYGG FPPEANYLFL GDYVERGTQS LETICFIDRI YGFYDECKRR
FNIRLWKTFT DCFDCLPIAA IVDEKIFCRH GGLSPDLQSM EQIQRIMRPT NVPDAGLLYK
DVQGWGENDR GVSFTFGAEV VSEFLNHHDL DLICRAHQVV GDGYEFFAKR QLVTLFSAPN
YCGEFDNAGG MMSVDETLMC SFQILKPSEK KKLNPNSKLS IKVTSSCITI FKVEKHPS
//
