ID A0A3B5B317_9TELE Unreviewed; 211 AA.
AC A0A3B5B317;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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|Ensembl:ENSSPAP00000027161.1};
GN Synonyms=ppp1r1a {ECO:0000313|RefSeq:XP_008280318.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000027161.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000027161.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008280318.1}
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_008280318.1; XM_008282096.1.
DR AlphaFoldDB; A0A3B5B317; -.
DR STRING; 144197.ENSSPAP00000027161; -.
DR Ensembl; ENSSPAT00000027606.1; ENSSPAP00000027161.1; ENSSPAG00000020484.1.
DR GeneID; 103357510; -.
DR CTD; 5502; -.
DR GeneTree; ENSGT00940000161232; -.
DR OrthoDB; 5350621at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; 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:UP000694891}.
FT REGION 16..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 23291 MW; 1653AC38C131C1B0 CRC64;
METGSPRKIQ FTVPLLDTHL DPEAAEQIRR RRPTPATLVA SSDQSSPEID EDRLPNQLYK
AALLNSPRQR RKGQKGTPTM KELQFMVEHH LYRQQQGAGD ECSSESCLSD RPSPDSVPTG
EELPHDDEAT AEAFEKLRCQ MEEFSRESLL EAAGGLECPL SKEKEDCSSV ANVADPSSQQ
NYAQADTKAG ASSASQPAEE KTKKCSLEKE K
//
