IPP2_RABIT
ID IPP2_RABIT Reviewed; 205 AA.
AC P11845;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein phosphatase inhibitor 2;
DE Short=IPP-2;
GN Name=PPP1R2; Synonyms=IPP2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RX PubMed=8288648; DOI=10.1016/s0021-9258(17)42203-4;
RA Park I.-K., Roach P., Bondor J., Fox S.P., Depaoli-Roach A.A.;
RT "Molecular mechanism of the synergistic phosphorylation of phosphatase
RT inhibitor-2. Cloning, expression, and site-directed mutagenesis of
RT inhibitor-2.";
RL J. Biol. Chem. 269:944-954(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=1323285; DOI=10.1016/0006-291x(92)90869-m;
RA Zhang Z., Bai G., Lee E.Y.C.;
RT "PCR cloning of the cDNA of rabbit skeletal muscle protein phosphatase
RT inhibitor-2.";
RL Biochem. Biophys. Res. Commun. 186:1168-1170(1992).
RN [3]
RP PROTEIN SEQUENCE OF 2-204, AND ACETYLATION AT ALA-2.
RC TISSUE=Skeletal muscle;
RX PubMed=3512270; DOI=10.1111/j.1432-1033.1986.tb09473.x;
RA Holmes C.F.B., Campbell D.G., Caudwell F.B., Aitken A., Cohen P.;
RT "The protein phosphatases involved in cellular regulation. Primary
RT structure of inhibitor-2 from rabbit skeletal muscle.";
RL Eur. J. Biochem. 155:173-182(1986).
RN [4]
RP PROTEIN SEQUENCE OF 67-77, AND PHOSPHORYLATION AT THR-73.
RX PubMed=6091765; DOI=10.1016/0167-4838(84)90034-7;
RA Aitken A., Holmes C.F., Campbell D.G., Resink T.J., Cohen P., Leung C.T.,
RA Williams D.H.;
RT "Amino acid sequence at the site on protein phosphatase inhibitor-2,
RT phosphorylated by glycogen synthase kinase-3.";
RL Biochim. Biophys. Acta 790:288-291(1984).
RN [5]
RP SUBUNIT, AND PHOSPHORYLATION.
RX PubMed=6297978; DOI=10.1016/0014-5793(82)80760-6;
RA Hemmings B.A., Resink T.J., Cohen P.;
RT "Reconstitution of a Mg-ATP-dependent protein phosphatase and its
RT activation through a phosphorylation mechanism.";
RL FEBS Lett. 150:319-324(1982).
RN [6]
RP ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-87; SER-121 AND SER-122, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=3036252; DOI=10.1016/0167-4889(87)90178-9;
RA Holmes C.F.B., Tonks N.K., Major H., Cohen P.;
RT "Analysis of the in vivo phosphorylation state of protein phosphatase
RT inhibitor-2 from rabbit skeletal muscle by fast-atom bombardment mass
RT spectrometry.";
RL Biochim. Biophys. Acta 929:208-219(1987).
CC -!- FUNCTION: Inhibitor of protein-phosphatase 1.
CC -!- SUBUNIT: Heterodimer with PP1. {ECO:0000269|PubMed:6297978}.
CC -!- PTM: Phosphorylation on Ser-44 by ATM activates PP1 by dissociating the
CC PP1-PPP1R2 complex (By similarity). Phosphorylation on Thr-73 by GSK3
CC activates PP1 by dissociating the PP1-PPP1R2 complex. {ECO:0000250,
CC ECO:0000269|PubMed:3036252, ECO:0000269|PubMed:6091765,
CC ECO:0000269|PubMed:6297978}.
CC -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 2 family.
CC {ECO:0000305}.
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DR EMBL; L20858; AAA17541.1; -; mRNA.
DR EMBL; M95581; AAA31405.1; -; mRNA.
DR PIR; I46876; I46876.
DR RefSeq; NP_001076213.1; NM_001082744.2.
DR AlphaFoldDB; P11845; -.
DR DIP; DIP-439N; -.
DR ELM; P11845; -.
DR STRING; 9986.ENSOCUP00000012136; -.
DR iPTMnet; P11845; -.
DR Ensembl; ENSOCUT00000014121; ENSOCUP00000012136; ENSOCUG00000014123.
DR GeneID; 100009520; -.
DR KEGG; ocu:100009520; -.
DR CTD; 5504; -.
DR eggNOG; KOG4041; Eukaryota.
DR GeneTree; ENSGT00390000004757; -.
DR InParanoid; P11845; -.
DR OrthoDB; 1321970at2759; -.
DR TreeFam; TF105536; -.
DR Proteomes; UP000001811; Chromosome 14.
DR Bgee; ENSOCUG00000014123; Expressed in testis and 17 other tissues.
DR ExpressionAtlas; P11845; baseline.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IMP:CAFA.
DR GO; GO:0098723; C:skeletal muscle myofibril; IDA:CAFA.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IPI:CAFA.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:CAFA.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:CAFA.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR InterPro; IPR007062; PPI-2.
DR PANTHER; PTHR12398; PTHR12398; 1.
DR Pfam; PF04979; IPP-2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Direct protein sequencing;
KW Glycogen metabolism; Phosphoprotein; Protein phosphatase inhibitor;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3036252,
FT ECO:0000269|PubMed:3512270"
FT CHAIN 2..205
FT /note="Protein phosphatase inhibitor 2"
FT /id="PRO_0000071483"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 12..17
FT /note="Required for binding PPP1CC"
FT /evidence="ECO:0000250"
FT REGION 43..55
FT /note="Required for binding PPP1CC"
FT /evidence="ECO:0000250"
FT REGION 64..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..150
FT /note="Required for binding PPP1CC catalytic center,
FT displacing metal ions and inhibition of PPP1CC catalytic
FT activity"
FT /evidence="ECO:0000250"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:3036252,
FT ECO:0000269|PubMed:3512270"
FT MOD_RES 44
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:P41236"
FT MOD_RES 73
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0000269|PubMed:6091765"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:3036252"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P41236"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P41236"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCL8"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:3036252"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:3036252"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41236"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCL8"
SQ SEQUENCE 205 AA; 23011 MW; B82E80AAD2A0A7D5 CRC64;
MAASTASHRP IKGILKNKTS STSSRVASAE QPRGSVDEEL SKKSQKWDEM NILATYHPAD
KDYGLMKIDE PSTPYHSMIG DDDDAYSDTE TTEAMTPDTL AKKLAAAEGS EPKYRIREQE
SSGEEDSDLS PEEREKKRQF EMKRKLHYNE GLNIKLARQL ISKDLHDDEE DEEMSETADG
ESMNTEESNQ GSTPSDQRQN KSQSS
