PPR1A_RABIT
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 25-MAY-2022, entry version 97.
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 IntAct; P01099; 1.
DR MINT; P01099; -.
DR STRING; 9986.ENSOCUP00000011659; -.
DR iPTMnet; P01099; -.
DR eggNOG; ENOG502S1WG; Eukaryota.
DR InParanoid; P01099; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0098723; C:skeletal muscle myofibril; IDA: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:0007165; P:signal transduction; IEA:InterPro.
DR DisProt; DP00325; -.
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; 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 111..139
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