PPR1B_RAT
ID PPR1B_RAT Reviewed; 205 AA.
AC Q6J4I0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 1B;
DE AltName: Full=DARPP-32;
DE AltName: Full=Dopamine- and cAMP-regulated neuronal phosphoprotein;
GN Name=Ppp1r1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Liu Q.-R., Uhl G.R.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-46; SER-102 AND
RP SER-137, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Inhibitor of protein-phosphatase 1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylation of Thr-34 is required for activity. {ECO:0000250}.
CC -!- PTM: Dopamine- and cyclic AMP-regulated neuronal phosphoprotein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family.
CC {ECO:0000305}.
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DR EMBL; AY601872; AAT11858.1; -; mRNA.
DR EMBL; BC078954; AAH78954.1; -; mRNA.
DR RefSeq; NP_612530.1; NM_138521.1.
DR AlphaFoldDB; Q6J4I0; -.
DR BMRB; Q6J4I0; -.
DR STRING; 10116.ENSRNOP00000034614; -.
DR iPTMnet; Q6J4I0; -.
DR PhosphoSitePlus; Q6J4I0; -.
DR PaxDb; Q6J4I0; -.
DR PRIDE; Q6J4I0; -.
DR Ensembl; ENSRNOT00000037752; ENSRNOP00000034614; ENSRNOG00000028404.
DR GeneID; 360616; -.
DR KEGG; rno:360616; -.
DR UCSC; RGD:621859; rat.
DR CTD; 84152; -.
DR RGD; 621859; Ppp1r1b.
DR eggNOG; ENOG502S19Z; Eukaryota.
DR HOGENOM; CLU_092269_3_0_1; -.
DR InParanoid; Q6J4I0; -.
DR OMA; EDPCEGD; -.
DR OrthoDB; 1412891at2759; -.
DR PhylomeDB; Q6J4I0; -.
DR TreeFam; TF332576; -.
DR Reactome; R-RNO-180024; DARPP-32 events.
DR PRO; PR:Q6J4I0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000028404; Expressed in stomach and 16 other tissues.
DR Genevisible; Q6J4I0; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0044327; C:dendritic spine head; IDA:RGD.
DR GO; GO:0044326; C:dendritic spine neck; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
DR GO; GO:0031749; F:D2 dopamine receptor binding; IPI:RGD.
DR GO; GO:0031750; F:D3 dopamine receptor binding; IPI:RGD.
DR GO; GO:0031751; F:D4 dopamine receptor binding; IPI:RGD.
DR GO; GO:0031752; F:D5 dopamine receptor binding; IPI:RGD.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; ISO:RGD.
DR GO; GO:0048148; P:behavioral response to cocaine; ISO:RGD.
DR GO; GO:0071314; P:cellular response to cocaine; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
DR GO; GO:0007626; P:locomotory behavior; IDA:RGD.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0007621; P:negative regulation of female receptivity; ISO:RGD.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:0001975; P:response to amphetamine; ISO:RGD.
DR GO; GO:0042220; P:response to cocaine; IDA:RGD.
DR GO; GO:0043278; P:response to morphine; ISO:RGD.
DR GO; GO:0035094; P:response to nicotine; IDA:RGD.
DR GO; GO:0006351; P:transcription, DNA-templated; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR InterPro; IPR015670; DARPP-32.
DR InterPro; IPR008466; PPP1R1A/B/C.
DR PANTHER; PTHR15417; PTHR15417; 1.
DR PANTHER; PTHR15417:SF2; PTHR15417:SF2; 1.
DR Pfam; PF05395; DARPP-32; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Phosphoprotein; Protein phosphatase inhibitor;
KW Reference proteome.
FT CHAIN 1..205
FT /note="Protein phosphatase 1 regulatory subunit 1B"
FT /id="PRO_0000286442"
FT REGION 1..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..197
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:P07516"
FT MOD_RES 34
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P07516"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 75
FT /note="Phosphothreonine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:Q9UD71"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 205 AA; 22913 MW; 38B587BFEBAC692A CRC64;
MDPKDRKKIQ FSVPAPPSQL DPRQVEMIRR RRPTPALLFR VSEHSSPEEE SSPHQRTSGE
GHHPKSKRPN PCAYTPPSLK AVQRIAESHL QTISNLSENQ ASEEEDELGE LRELGYPQED
DEEDEDEDEE EDEEEDSQAE VLKGSRGTAG QKLTSGQGLE GPWERPPPLD EPQRDGNSED
QGEGRATQSE PGEEPRHPTP PESGT
