PPR1A_RAT
ID PPR1A_RAT Reviewed; 171 AA.
AC P19103; Q6DSU5;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 1A;
DE AltName: Full=Protein phosphatase inhibitor 1;
DE Short=I-1;
DE Short=IPP-1;
GN Name=Ppp1r1a; Synonyms=Ipp1;
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 STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=1696252; DOI=10.1016/s0021-9258(18)77359-6;
RA Elbrecht A., Direnzo J., Smith R.G., Shenolikar S.;
RT "Molecular cloning of protein phosphatase inhibitor-1 and its expression in
RT rat and rabbit tissues.";
RL J. Biol. Chem. 265:13415-13418(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=11269652; DOI=10.1023/a:1007141514750;
RA Aleem E.A., Flohr T., Hunziker A., Mayer D., Bannasch P., Thielmann H.W.;
RT "Detection and quantification of protein phosphatase inhibitor-1 gene
RT expression in total rat liver and isolated hepatocytes.";
RL Mol. Cell. Biochem. 217:1-12(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Liu Q.-R., Uhl G.R.;
RT "Drug altered brain phosphorylation by two families of PP1 inhibitory
RT proteins activated by PKA or PKC.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-47 AND SER-67, 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. This protein may be
CC important in hormonal control of glycogen metabolism. Hormones that
CC elevate intracellular cAMP increase I-1 activity in many tissues. I-1
CC activation may impose cAMP control over proteins that are not directly
CC phosphorylated by PKA. Following a rise in intracellular calcium, I-1
CC is inactivated by calcineurin (or PP2B). Does not inhibit type-2
CC phosphatases.
CC -!- SUBUNIT: Interacts with PPP1R15A. {ECO:0000250}.
CC -!- PTM: Phosphorylation of Thr-35 is required for activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family.
CC {ECO:0000305}.
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DR EMBL; J05592; AAA41933.1; -; mRNA.
DR EMBL; AJ276593; CAB77674.1; -; mRNA.
DR EMBL; AY648296; AAT66740.1; -; mRNA.
DR EMBL; BC078820; AAH78820.1; -; mRNA.
DR PIR; A37110; A37110.
DR RefSeq; NP_073167.1; NM_022676.3.
DR AlphaFoldDB; P19103; -.
DR ELM; P19103; -.
DR STRING; 10116.ENSRNOP00000052146; -.
DR iPTMnet; P19103; -.
DR PhosphoSitePlus; P19103; -.
DR PaxDb; P19103; -.
DR PRIDE; P19103; -.
DR Ensembl; ENSRNOT00000055271; ENSRNOP00000052146; ENSRNOG00000036827.
DR GeneID; 58977; -.
DR KEGG; rno:58977; -.
DR CTD; 5502; -.
DR RGD; 62018; Ppp1r1a.
DR eggNOG; ENOG502S1WG; Eukaryota.
DR GeneTree; ENSGT00940000161232; -.
DR HOGENOM; CLU_092269_1_0_1; -.
DR InParanoid; P19103; -.
DR OMA; PKTQERC; -.
DR OrthoDB; 1571652at2759; -.
DR PhylomeDB; P19103; -.
DR TreeFam; TF332576; -.
DR PRO; PR:P19103; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000036827; Expressed in skeletal muscle tissue and 16 other tissues.
DR Genevisible; P19103; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR InterPro; IPR008466; PPP1R1A/B/C.
DR PANTHER; PTHR15417; PTHR15417; 1.
DR Pfam; PF05395; DARPP-32; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..171
FT /note="Protein phosphatase 1 regulatory subunit 1A"
FT /id="PRO_0000071480"
FT REGION 9..12
FT /note="Essential for activity"
FT REGION 17..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..54
FT /note="Essential for activity"
FT /evidence="ECO:0000305"
FT REGION 143..171
FT /note="Interaction with PPP1R15A"
FT /evidence="ECO:0000250"
FT COMPBIAS 60..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P01099"
FT MOD_RES 35
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q13522"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERT9"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 171 AA; 18738 MW; 4D26478008245956 CRC64;
MEPDNSPRKI QFTVPLLEPH LDPEAAEQIR RRRPTPATLV LTSDQSSPEV DEDRIPNPLL
KSTLSMSPRQ RKKMTRTTPT MKELQTMVEH HLGQQKQGEE PEGATESTGN QESCPPGIPD
TGSASRPDTS GTAQKPAESK PKTQEQRGVE PSTEDLSAHM LPLDSQGASL V
