ID A0A096LXB6_POEFO Unreviewed; 211 AA.
AC A0A096LXB6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 1A {ECO:0000256|ARBA:ARBA00040692};
DE AltName: Full=Protein phosphatase inhibitor 1 {ECO:0000256|ARBA:ARBA00042082};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000023807.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000023807.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 EMBL; AYCK01000357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01000358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007549152.1; XM_007549090.2.
DR AlphaFoldDB; A0A096LXB6; -.
DR STRING; 48698.ENSPFOP00000023807; -.
DR Ensembl; ENSPFOT00000025298.1; ENSPFOP00000023807.1; ENSPFOG00000022867.1.
DR GeneID; 103136015; -.
DR KEGG; pfor:103136015; -.
DR eggNOG; ENOG502S1WG; Eukaryota.
DR GeneTree; ENSGT00940000161232; -.
DR OMA; AWGTEDK; -.
DR OrthoDB; 5350621at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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:UP000028760}.
FT REGION 16..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..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..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 23195 MW; 6B573EED58D1C261 CRC64;
METGSPRKIQ FTVPLLDTHL DPEAAEQIRR RRPTPATLVA SSDQSSPEID EDRLPNQLYK
AALLNSPRQR RKGQKGTPTM KELQFLVEHH LYRQQQGAGD ECSSESCLSD RPSPDSVPTG
EELPHDDEAT AEAFEKLRCQ MEEFSRESLL DAGGELECPL SEEKNDCSSV ATVADPSSQK
ENALTDTKAG ASSANQPSGK KTNKVSLETK K
//
