ID   PPR1A_RABIT             Reviewed;         166 AA.
AC   P01099;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   02-SEP-2026, entry version 112.
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   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   PROTEIN SEQUENCE, ACETYLATION AT MET-1, AND PHOSPHORYLATION AT THR-35 AND
RP   SER-67.
RX   PubMed=6290217; DOI=10.1111/j.1432-1033.1982.tb06771.x;
RA   Aitken A., Bilham T., Cohen P.;
RT   "Complete primary structure of protein phosphatase inhibitor-1 from rabbit
RT   skeletal muscle.";
RL   Eur. J. Biochem. 126:235-246(1982).
RN   [2]
RP   SEQUENCE REVISION TO 164.
RA   Aitken A.;
RL   Submitted (OCT-1988) to UniProtKB.
RN   [3]
RP   FUNCTION.
RX   PubMed=7140990; DOI=10.1016/0014-5793(82)81010-7;
RA   Aitken A., Cohen P.;
RT   "Isolation and characterisation of active fragments of protein phosphatase
RT   inhibitor-1 from rabbit skeletal muscle.";
RL   FEBS Lett. 147:54-58(1982).
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. {ECO:0000269|PubMed:7140990}.
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   PIR; A91120; PZRB1.
DR   AlphaFoldDB; P01099; -.
DR   SMR; P01099; -.
DR   FunCoup; P01099; 60.
DR   IntAct; P01099; 1.
DR   MINT; P01099; -.
DR   STRING; 9986.ENSOCUP00000039736; -.
DR   iPTMnet; P01099; -.
DR   PaxDb; 9986-ENSOCUP00000039736; -.
DR   eggNOG; ENOG502S1WG; Eukaryota.
DR   InParanoid; P01099; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0098723; C:skeletal muscle myofibril; IDA:CAFA.
DR   GO; GO:0140678; F:molecular function inhibitor activity; EXP:DisProt.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:CAFA.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter.
DR   DisProt; DP00325; -.
DR   InterPro; IPR008466; PPP1R1A/B/C.
DR   PANTHER; PTHR15417:SF4; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 1A; 1.
DR   PANTHER; PTHR15417; PROTEIN PHOSPHATASE INHIBITOR AND DOPAMINE- AND CAMP-REGULATED NEURONAL PHOSPHOPROTEIN; 1.
DR   Pfam; PF05395; DARPP-32; 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   CHAIN           1..166
FT                   /note="Protein phosphatase 1 regulatory subunit 1A"
FT                   /id="PRO_0000071479"
FT   REGION          1..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          9..12
FT                   /note="Essential for activity"
FT   REGION          42..54
FT                   /note="Essential for activity"
FT                   /evidence="ECO:0000305"
FT   REGION          143..166
FT                   /note="Interaction with PPP1R15A"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        19..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..114
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:6290217"
FT   MOD_RES         35
FT                   /note="Phosphothreonine; by PKA"
FT                   /evidence="ECO:0000269|PubMed:6290217"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ERT9"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ERT9"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ERT9"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:6290217"
FT   VARIANT         164..166
FT                   /note="Missing (in 40% of the molecules)"
SQ   SEQUENCE   166 AA;  18032 MW;  0D26A5FE0C617C88 CRC64;
     MEQDNSPRKI QFTVPLLEPH LDPEAAEQIR RRRPTPATLV LTSDQSSPEV DEDRIPNPLL
     KPSLAMSPRQ RKKMTRTTPT MKELQMMVEH HLGQQEQGEE PEGAAEGTGA QESQPPGTPG
     TGAESRLGPS ATAQKPAQPS PRAQERRGEE PSTAKTSQDS QGASAV
//