ID   IPP2_RAT                Reviewed;         205 AA.
AC   P50411; Q56A32;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Protein phosphatase inhibitor 2;
DE            Short=IPP-2;
GN   Name=Ppp1r2; Synonyms=Ipp2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7669271; DOI=10.1016/0891-0618(95)00051-8;
RA   Sakagami H., Kondo H.;
RT   "Molecular cloning of the cDNA for rat phosphatase inhibitor-2 and its wide
RT   gene expression in the central nervous system.";
RL   J. Chem. Neuroanat. 8:259-266(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-122 AND SER-130, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Inhibitor of protein-phosphatase 1.
CC   -!- SUBUNIT: Heterodimer with PP1. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Central nervous system.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; S79213; AAB35244.1; -; mRNA.
DR   EMBL; BC092194; AAH92194.1; -; mRNA.
DR   RefSeq; NP_620178.1; NM_138823.2.
DR   AlphaFoldDB; P50411; -.
DR   SMR; P50411; -.
DR   ELM; P50411; -.
DR   STRING; 10116.ENSRNOP00000002361; -.
DR   iPTMnet; P50411; -.
DR   PhosphoSitePlus; P50411; -.
DR   jPOST; P50411; -.
DR   PaxDb; 10116-ENSRNOP00000002361; -.
DR   Ensembl; ENSRNOT00000002361.7; ENSRNOP00000002361.6; ENSRNOG00000001733.8.
DR   Ensembl; ENSRNOT00055028355; ENSRNOP00055022834; ENSRNOG00055016689.
DR   Ensembl; ENSRNOT00060029616; ENSRNOP00060023833; ENSRNOG00060017341.
DR   Ensembl; ENSRNOT00065032652; ENSRNOP00065026077; ENSRNOG00065019393.
DR   GeneID; 192361; -.
DR   KEGG; rno:192361; -.
DR   UCSC; RGD:621099; rat.
DR   AGR; RGD:621099; -.
DR   CTD; 5504; -.
DR   RGD; 621099; Ppp1r2.
DR   eggNOG; KOG4041; Eukaryota.
DR   GeneTree; ENSGT00390000004757; -.
DR   HOGENOM; CLU_084310_2_0_1; -.
DR   InParanoid; P50411; -.
DR   OMA; YRVHEQA; -.
DR   OrthoDB; 5400434at2759; -.
DR   PhylomeDB; P50411; -.
DR   TreeFam; TF105536; -.
DR   PRO; PR:P50411; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR   GO; GO:0030426; C:growth cone; IDA:RGD.
DR   GO; GO:0140678; F:molecular function inhibitor activity; ISO:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
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:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   Gene3D; 6.10.250.1050; -; 2.
DR   InterPro; IPR007062; PPI-2.
DR   PANTHER; PTHR12398; PROTEIN PHOSPHATASE INHIBITOR; 1.
DR   PANTHER; PTHR12398:SF35; PROTEIN PHOSPHATASE INHIBITOR 2-RELATED; 1.
DR   Pfam; PF04979; IPP-2; 1.
DR   Genevisible; P50411; RN.
PE   1: Evidence at protein 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..205
FT                   /note="Protein phosphatase inhibitor 2"
FT                   /id="PRO_0000071484"
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          104..142
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   REGION          163..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..142
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: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         96
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCL8"
FT   MOD_RES         116
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCL8"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   205 AA;  23071 MW;  5D58BC9435A2A5CE CRC64;
     MAASTASHRP IKGILKNKTS TTSSVVASAE QPRRTVEEEL SKKSQKWDEM NILATYHPAD
     KDYGLMKIDE PDTPYHNMIG DDEDVCSDSE GNEVMTPEIL AKKLAAAEGS EPKFRTREQE
     SSGEEDNDLS PEEREKKRQF EMKRKLHYNE GLNIKLARQL ISKDLHDDDE DEEMSETADA
     DSMNIEESNQ GSTAGDHLQH KSQSS
//