ID A0A1S3W5A7_ERIEU Unreviewed; 138 AA.
AC A0A1S3W5A7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 1A {ECO:0000256|ARBA:ARBA00040692};
DE AltName: Full=Protein phosphatase inhibitor 1 {ECO:0000256|ARBA:ARBA00042082};
GN Name=PPP1R1A {ECO:0000313|RefSeq:XP_016041512.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016041512.1};
RN [1] {ECO:0000313|RefSeq:XP_016041512.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037661}.
CC -!- SUBUNIT: Interacts with PPP1R15A. {ECO:0000256|ARBA:ARBA00038671}.
CC -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family.
CC {ECO:0000256|ARBA:ARBA00007775}.
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DR RefSeq; XP_016041512.1; XM_016186026.1.
DR AlphaFoldDB; A0A1S3W5A7; -.
DR GeneID; 103109126; -.
DR CTD; 5502; -.
DR OrthoDB; 5350621at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase inhibitor {ECO:0000256|ARBA:ARBA00023272};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 138 AA; 15378 MW; C3E2FDC6E7CC7327 CRC64;
MEPDNSPRKI QFTVPLLEPH LDPEAAEQIR RRRPTPATLV LTSDQSSPEI DEDRIPNPLL
KTTLTMSPRQ RKKVTRTTPT MKELQMMVEH HLGQQQQEEE PEGASSSTGT QESFPPETTE
VEPRLGASGK AQSASPEA
//
