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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
 
 
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