ID   IPP2_BOVIN              Reviewed;         207 AA.
AC   Q3SZX2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Protein phosphatase inhibitor 2;
DE            Short=IPP-2;
GN   Name=PPP1R2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibitor of protein-phosphatase 1. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with PP1. {ECO:0000250}.
CC   -!- PTM: Phosphorylation on Ser-44 by ATM activates PP1 by dissociating the
CC       PP1-PPP1R2 complex. Phosphorylation on Thr-73 by GSK3 activates PP1 by
CC       dissociating the PP1-PPP1R2 complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 2 family.
CC       {ECO:0000305}.
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DR   EMBL; BC102669; AAI02670.1; -; mRNA.
DR   RefSeq; NP_001030469.1; NM_001035392.2.
DR   AlphaFoldDB; Q3SZX2; -.
DR   STRING; 9913.ENSBTAP00000001128; -.
DR   PaxDb; Q3SZX2; -.
DR   PeptideAtlas; Q3SZX2; -.
DR   PRIDE; Q3SZX2; -.
DR   GeneID; 532726; -.
DR   KEGG; bta:532726; -.
DR   CTD; 5504; -.
DR   eggNOG; KOG4041; Eukaryota.
DR   InParanoid; Q3SZX2; -.
DR   OrthoDB; 1321970at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW   Protein phosphatase inhibitor; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P11845"
FT   CHAIN           2..207
FT                   /note="Protein phosphatase inhibitor 2"
FT                   /id="PRO_0000286136"
FT   REGION          1..44
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          65..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..152
FT                   /note="Required for binding PPP1CC catalytic center,
FT                   displacing metal ions and inhibition of PPP1CC catalytic
FT                   activity"
FT                   /evidence="ECO:0000250"
FT   REGION          165..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P11845"
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:0000250|UniProtKB:P11845"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41236"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCL8"
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         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41236"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41236"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41236"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCL8"
SQ   SEQUENCE   207 AA;  22982 MW;  DBC48D9989823B26 CRC64;
     MAASTASHRP IKGILKNKSS TTSSVVSTAE QPGKSVDEEL SKKSQKWDEM SILATYHPAD
     KDYGLMKIDE PSTPYHSMVA DDEDALSDSE TTEALTPDIL ARKLTAAAAE SLEPKYRVRE
     QESSGDEDSD LSPEEREKKR QFEMKRKLHY NEGLNIKLAR QLISKDLNDE EEDEEMSETA
     AGESMNMEES SQGSATSDQL QNKSQSS