ID   ARP19_XENTR             Reviewed;         117 AA.
AC   Q28GU6; Q05B03; Q6DIM8;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=cAMP-regulated phosphoprotein 19;
DE            Short=ARPP-19;
GN   Name=arpp19; ORFNames=TEgg006a24.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-117.
RC   STRAIN=N6; TISSUE=Oviduct;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein phosphatase inhibitor that specifically inhibits
CC       protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at
CC       Ser-67 during mitosis, specifically interacts with ppp2r2d (PR55-delta)
CC       and inhibits its activity, leading to inactivation of PP2A, an
CC       essential condition to keep cyclin-B1-CDK1 activity high during M phase
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (when phosphorylated at Ser-67) with ppp2r2d.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Ser-67 by gwl during mitosis is essential for
CC       interaction with PPP2R2D (PR55-delta) and subsequent inactivation of
CC       PP2A. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR   EMBL; CR761222; CAJ83731.1; -; mRNA.
DR   EMBL; BC075509; AAH75509.1; -; mRNA.
DR   EMBL; BC123052; AAI23053.1; -; mRNA.
DR   RefSeq; NP_001032337.1; NM_001037260.1.
DR   AlphaFoldDB; Q28GU6; -.
DR   STRING; 8364.ENSXETP00000056806; -.
DR   PaxDb; Q28GU6; -.
DR   GeneID; 447957; -.
DR   KEGG; xtr:447957; -.
DR   CTD; 10776; -.
DR   Xenbase; XB-GENE-953906; arpp19.
DR   eggNOG; KOG4076; Eukaryota.
DR   HOGENOM; CLU_125025_1_0_1; -.
DR   InParanoid; Q28GU6; -.
DR   OrthoDB; 1494565at2759; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0019212; F:phosphatase inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0035308; P:negative regulation of protein dephosphorylation; IBA:GO_Central.
DR   InterPro; IPR006760; Endosulphine.
DR   PANTHER; PTHR10358; PTHR10358; 1.
DR   Pfam; PF04667; Endosulfine; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein;
KW   Protein phosphatase inhibitor; Reference proteome.
FT   CHAIN           1..117
FT                   /note="cAMP-regulated phosphoprotein 19"
FT                   /id="PRO_0000408323"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         28
FT                   /note="Phosphoserine; by CDK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         67
FT                   /note="Phosphoserine; by GWL"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         99
FT                   /note="Phosphothreonine; by CDK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         109
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   117 AA;  12915 MW;  DBBF49EBAB2E9B2B CRC64;
     MSGDNQESRA PEESSAEEQK EMDDKVISPE KSEEIKLKAR YPNLGPKPGG SDFLRKRLQK
     GQKYFDSGDY NVAKAKMKNK QLSTAAPDKT EVTGDHIPTP QDLPQRKPSL VASKLAG