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Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)

 PP1A_RABIT              Reviewed;         330 AA.
P62139; P08128; P08129; P20653; P22802;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
21-JUN-2004, sequence version 1.
30-AUG-2017, entry version 116.
RecName: Full=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;
Short=PP-1A;
EC=3.1.3.16;
Name=PPP1CA; Synonyms=PPP1A;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
TISSUE SPECIFICITY.
STRAIN=New Zealand white; TISSUE=Skeletal muscle;
PubMed=2822491; DOI=10.1016/0014-5793(87)80316-2;
Berndt N., Campbell D.G., Caudwell F.B., Cohen P.,
da Cruz e Silva E.F., da Cruz e Silva O.B., Cohen P.T.W.;
"Isolation and sequence analysis of a cDNA clone encoding a type-1
protein phosphatase catalytic subunit: homology with protein
phosphatase 2A.";
FEBS Lett. 223:340-346(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Muscle;
PubMed=2846396;
Bai G., Zhang Z., Amin J., Deans-Zirattu S.A., Lee E.Y.C.;
"Molecular cloning of a cDNA for the catalytic subunit of rabbit
muscle phosphorylase phosphatase.";
FASEB J. 2:3010-3016(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=New Zealand white; TISSUE=Skeletal muscle;
PubMed=2835264; DOI=10.1016/0014-5793(88)80378-8;
Cohen P.T.W.;
"Two isoforms of protein phosphatase 1 may be produced from the same
gene.";
FEBS Lett. 232:17-23(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=New Zealand white; TISSUE=Liver;
PubMed=2541784; DOI=10.1016/0167-4781(89)90181-4;
Cohen P.T.W., Schelling D.L., da Cruz e Silva O.B., Barker H.M.,
Cohen P.;
"The major type-1 protein phosphatase catalytic subunits are the same
gene products in rabbit skeletal muscle and rabbit liver.";
Biochim. Biophys. Acta 1008:125-128(1989).
[5]
INTERACTION WITH PPP1R39.
PubMed=19945436; DOI=10.1016/j.bbrc.2009.11.123;
Chen C.Y., Lai N.S., Yang J.J., Huang H.L., Hung W.C., Li C.,
Lin T.H., Huang H.B.;
"FLJ23654 encodes a heart protein phosphatase 1-binding protein
(Hepp1).";
Biochem. Biophys. Res. Commun. 391:698-702(2010).
[6]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS,
AND COFACTOR.
PubMed=7651533; DOI=10.1038/376745a0;
Goldberg J., Huang H.B., Kwon Y.G., Greengard P., Nairn A.C.,
Kuriyan J.;
"Three-dimensional structure of the catalytic subunit of protein
serine/threonine phosphatase-1.";
Nature 376:745-753(1995).
-!- FUNCTION: Protein phosphatase that associates with over 200
regulatory proteins to form highly specific holoenzymes which
dephosphorylate hundreds of biological targets. Protein
phosphatase 1 (PP1) is essential for cell division, and
participates in the regulation of glycogen metabolism, muscle
contractility and protein synthesis. Involved in regulation of
ionic conductances and long-term synaptic plasticity. May play an
important role in dephosphorylating substrates such as the
postsynaptic density-associated Ca(2+)/calmodulin dependent
protein kinase II. Component of the PTW/PP1 phosphatase complex,
which plays a role in the control of chromatin structure and cell
cycle progression during the transition from mitosis into
interphase. Regulates NEK2 function in terms of kinase activity
and centrosome number and splitting, both in the presence and
absence of radiation-induced DNA damage. Regulator of neural tube
and optic fissure closure, and enteric neural crest cell (ENCCs)
migration during development. In balance with CSNK1D and CSNK1E,
determines the circadian period length, through the regulation of
the speed and rhythmicity of PER1 and PER2 phosphorylation. May
dephosphorylate CSNK1D and CSNK1E (By similarity).
Dephosphorylates CENPA (By similarity). Dephosphorylates the 'Ser-
139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1
complex, thereby inhibiting autophagy (By similarity).
{ECO:0000250|UniProtKB:P62136, ECO:0000250|UniProtKB:P62137}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:7651533};
Note=Binds 2 manganese ions per subunit.
{ECO:0000269|PubMed:7651533};
-!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
PPP1CC, which is folded into its native form by inhibitor 2 and
glycogen synthetase kinase 3, and then complexed to one or several
targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C
mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B
(in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate
binding to glycogen. Interacts with PPP1R15A and PPP1R15B; the
interactions mediate binding to EIF2S1. Part of a complex
containing PPP1R15B, PP1 and NCK1/2. Component of the MLL5-L
complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB,
PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R9A, PPP1R9B and
PPP1R7. Interacts with YLPM1. Forms a complex with ILF2, ILF3,
YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8.
Interacts with PPP1R16B. Interacts with RPSA only in the presence
of PPP1R16B. Component of the PTW/PP1 phosphatase complex,
composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or
PPP1CC. Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with
WDR82 in the presence of PPP1R10/PNUTS. Interacts with TRIM28; the
interaction dephosphorylates TRIM28 on 'Ser-824' and forms a
complex at the p21 promoter site (By similarity). Interacts with
PPP1R39. Interacts with NEK2. Interacts with PHACTR4; which acts
as an activator of PP1 activity. Interacts with FER; this promotes
phosphorylation at Thr-320 (By similarity). Interacts with BTBD10
(By similarity). Interacts with KCTD20 (By similarity). Interacts
with FOXP3 (By similarity). Interacts with CENPA (By similarity).
Interacts with ATG16L1 (By similarity).
{ECO:0000250|UniProtKB:P62136, ECO:0000250|UniProtKB:P62137,
ECO:0000269|PubMed:19945436}.
-!- INTERACTION:
Q13224:GRIN2B (xeno); NbExp=2; IntAct=EBI-2008988, EBI-2256942;
O60927:PPP1R11 (xeno); NbExp=2; IntAct=EBI-2008988, EBI-1048104;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus,
nucleolus {ECO:0000250}. Note=Primarily nuclear and largely
excluded from the nucleolus. Highly mobile in cells and can be
relocalized through interaction with targeting subunits. NOM1
plays a role in targeting this protein to the nucleolus. In the
presence of PPP1R8 relocalizes from the nucleus to nuclear
speckles (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=1-alpha-2;
IsoId=P62139-1, P08129-1;
Sequence=Displayed;
Name=1; Synonyms=1-alpha-1;
IsoId=P62139-2, P08128-1;
Sequence=VSP_010642;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein
level). Detected in skeletal muscle. {ECO:0000269|PubMed:2822491}.
-!- PTM: Phosphorylated. Dephosphorylated at Thr-320 in the presence
of ionizing radiation (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget
- Issue 32 of March 2003;
URL="http://web.expasy.org/spotlight/back_issues/032";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; Y00701; CAA68693.1; -; mRNA.
EMBL; X07798; CAA30645.1; -; mRNA.
EMBL; X14832; CAA32941.1; -; mRNA.
PIR; S04335; PARB11.
RefSeq; NP_001095176.1; NM_001101706.1.
UniGene; Ocu.2075; -.
PDB; 1FJM; X-ray; 2.10 A; A/B=1-330.
PDBsum; 1FJM; -.
ProteinModelPortal; P62139; -.
SMR; P62139; -.
BioGrid; 1172319; 80.
ELM; P62139; -.
IntAct; P62139; 5.
MINT; MINT-106725; -.
STRING; 9986.ENSOCUP00000024093; -.
ChEMBL; CHEMBL5458; -.
iPTMnet; P62139; -.
PRIDE; P62139; -.
GeneID; 100009298; -.
KEGG; ocu:100009298; -.
CTD; 5499; -.
HOVERGEN; HBG000216; -.
InParanoid; P62139; -.
KO; K06269; -.
EvolutionaryTrace; P62139; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:CAFA.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
GO; GO:1901567; F:fatty acid derivative binding; IDA:CAFA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0072542; F:protein phosphatase activator activity; IDA:CAFA.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:ParkinsonsUK-UCL.
GO; GO:1904886; P:beta-catenin destruction complex disassembly; IDA:ParkinsonsUK-UCL.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
GO; GO:0032091; P:negative regulation of protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0070262; P:peptidyl-serine dephosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; NAS:ParkinsonsUK-UCL.
GO; GO:0006470; P:protein dephosphorylation; IDA:CAFA.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0036496; P:regulation of translational initiation by eIF2 alpha dephosphorylation; IDA:ParkinsonsUK-UCL.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
InterPro; IPR031675; STPPase_N.
Pfam; PF00149; Metallophos; 1.
Pfam; PF16891; STPPase_N; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
SUPFAM; SSF56300; SSF56300; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Biological rhythms;
Carbohydrate metabolism; Cell cycle; Cell division; Complete proteome;
Cytoplasm; Direct protein sequencing; Glycogen metabolism; Hydrolase;
Manganese; Metal-binding; Nucleus; Phosphoprotein;
Protein phosphatase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P62136}.
CHAIN 2 330 Serine/threonine-protein phosphatase PP1-
alpha catalytic subunit.
/FTId=PRO_0000058776.
ACT_SITE 125 125 Proton donor. {ECO:0000250}.
METAL 64 64 Manganese 1.
METAL 66 66 Manganese 1.
METAL 92 92 Manganese 1.
METAL 92 92 Manganese 2.
METAL 124 124 Manganese 2.
METAL 173 173 Manganese 2.
METAL 248 248 Manganese 2.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P62136}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P62136}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000250|UniProtKB:P62136}.
MOD_RES 305 305 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62137}.
MOD_RES 306 306 Phosphotyrosine.
{ECO:0000250|UniProtKB:P62137}.
MOD_RES 320 320 Phosphothreonine.
{ECO:0000250|UniProtKB:P62136}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000250|UniProtKB:P62136}.
VAR_SEQ 1 33 MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTEN -> MVTI
MTTSEYLSGY (in isoform 1).
{ECO:0000303|PubMed:2822491}.
/FTId=VSP_010642.
CONFLICT 309 309 F -> L (in Ref. 1; CAA68693 and 3;
CAA30645). {ECO:0000305}.
HELIX 9 18 {ECO:0000244|PDB:1FJM}.
TURN 19 22 {ECO:0000244|PDB:1FJM}.
HELIX 32 48 {ECO:0000244|PDB:1FJM}.
STRAND 51 55 {ECO:0000244|PDB:1FJM}.
STRAND 57 62 {ECO:0000244|PDB:1FJM}.
HELIX 69 79 {ECO:0000244|PDB:1FJM}.
STRAND 87 89 {ECO:0000244|PDB:1FJM}.
STRAND 94 98 {ECO:0000244|PDB:1FJM}.
HELIX 100 113 {ECO:0000244|PDB:1FJM}.
TURN 115 117 {ECO:0000244|PDB:1FJM}.
STRAND 118 120 {ECO:0000244|PDB:1FJM}.
HELIX 128 134 {ECO:0000244|PDB:1FJM}.
HELIX 136 143 {ECO:0000244|PDB:1FJM}.
HELIX 146 156 {ECO:0000244|PDB:1FJM}.
STRAND 162 165 {ECO:0000244|PDB:1FJM}.
TURN 166 168 {ECO:0000244|PDB:1FJM}.
STRAND 169 174 {ECO:0000244|PDB:1FJM}.
HELIX 183 188 {ECO:0000244|PDB:1FJM}.
STRAND 197 199 {ECO:0000244|PDB:1FJM}.
HELIX 200 206 {ECO:0000244|PDB:1FJM}.
STRAND 214 218 {ECO:0000244|PDB:1FJM}.
STRAND 222 227 {ECO:0000244|PDB:1FJM}.
HELIX 229 239 {ECO:0000244|PDB:1FJM}.
STRAND 242 246 {ECO:0000244|PDB:1FJM}.
STRAND 254 258 {ECO:0000244|PDB:1FJM}.
TURN 259 262 {ECO:0000244|PDB:1FJM}.
STRAND 263 267 {ECO:0000244|PDB:1FJM}.
STRAND 274 276 {ECO:0000244|PDB:1FJM}.
STRAND 280 285 {ECO:0000244|PDB:1FJM}.
STRAND 291 296 {ECO:0000244|PDB:1FJM}.
SEQUENCE 330 AA; 37512 MW; 60C37E1AD9831DAC CRC64;
MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL
QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK


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