PPR1A_CANLF
ID PPR1A_CANLF Reviewed; 171 AA.
AC Q8WMS3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 63.
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;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Mishra S., Tiwari N., Sabbah H.N., Gupta R.C.;
RT "Cloning of inhibitor-1 of protein phosphatase type 1 from adult dog
RT heart.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 EMBL; AY063765; AAL48320.1; -; mRNA.
DR AlphaFoldDB; Q8WMS3; -.
DR BMRB; Q8WMS3; -.
DR InParanoid; Q8WMS3; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR InterPro; IPR008466; PPP1R1A/B/C.
DR PANTHER; PTHR15417; PTHR15417; 1.
DR Pfam; PF05395; DARPP-32; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..171
FT /note="Protein phosphatase 1 regulatory subunit 1A"
FT /id="PRO_0000071476"
FT REGION 1..171
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..171
FT /note="Interaction with PPP1R15A"
FT /evidence="ECO:0000250"
FT COMPBIAS 100..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P01099"
FT MOD_RES 35
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q13522"
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:0000250|UniProtKB:Q13522"
SQ SEQUENCE 171 AA; 18999 MW; 6F7EEC68E430552B CRC64;
MEQDNSPRKI QFTVPLLEPH LDPEAAEQIR RRRPTPATLV LTSDQSSPEI DEDRIPNPHL
KSTLAMSPRQ RKKMTRITPT MKELQMMVEH HLGQQQQGEE PEGAAESTGT QESRPPGIPD
TEVESRLGTS GTAKKTAECI PKTHERGSKE PSTKEPSTHI PPLDSKGANF V