AR19A_XENLA
ID AR19A_XENLA Reviewed; 117 AA.
AC Q6DEB4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=cAMP-regulated phosphoprotein 19-A;
DE Short=ARPP-19-A;
GN Name=arpp19-a; Synonyms=arpp19;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, INTERACTION WITH PPP2R2D, AND PHOSPHORYLATION AT SER-28; SER-67;
RP THR-99 AND SER-109.
RX PubMed=21164013; DOI=10.1126/science.1195689;
RA Mochida S., Maslen S.L., Skehel M., Hunt T.;
RT "Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is
RT essential for mitosis.";
RL Science 330:1670-1673(2010).
RN [3]
RP FUNCTION, INTERACTION WITH PPP2R2D, PHOSPHORYLATION AT SER-67, AND
RP MUTAGENESIS OF SER-2; SER-51; SER-67; THR-93; THR-99; SER-109 AND SER-113.
RX PubMed=21164014; DOI=10.1126/science.1197048;
RA Gharbi-Ayachi A., Labbe J.C., Burgess A., Vigneron S., Strub J.M.,
RA Brioudes E., Van-Dorsselaer A., Castro A., Lorca T.;
RT "The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting
RT protein phosphatase 2A.";
RL Science 330:1673-1677(2010).
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
CC phase. {ECO:0000269|PubMed:21164013, ECO:0000269|PubMed:21164014}.
CC -!- SUBUNIT: Interacts (when phosphorylated at Ser-67) with ppp2r2d.
CC {ECO:0000269|PubMed:21164013, ECO:0000269|PubMed:21164014}.
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. Phosphorylated by PKA. {ECO:0000269|PubMed:21164013,
CC ECO:0000269|PubMed:21164014}.
CC -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR EMBL; BC077215; AAH77215.1; -; mRNA.
DR RefSeq; NP_001086634.1; NM_001093165.1.
DR AlphaFoldDB; Q6DEB4; -.
DR iPTMnet; Q6DEB4; -.
DR DNASU; 446469; -.
DR GeneID; 446469; -.
DR KEGG; xla:446469; -.
DR CTD; 446469; -.
DR Xenbase; XB-GENE-953914; arpp19.L.
DR OMA; EQQEMDD; -.
DR OrthoDB; 1494565at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 446469; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0019212; F:phosphatase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR InterPro; IPR006760; Endosulphine.
DR PANTHER; PTHR10358; PTHR10358; 1.
DR Pfam; PF04667; Endosulfine; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..117
FT /note="cAMP-regulated phosphoprotein 19-A"
FT /id="PRO_0000408321"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..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:0000269|PubMed:21164013"
FT MOD_RES 67
FT /note="Phosphoserine; by GWL"
FT /evidence="ECO:0000269|PubMed:21164013,
FT ECO:0000269|PubMed:21164014"
FT MOD_RES 99
FT /note="Phosphothreonine; by CDK2"
FT /evidence="ECO:0000269|PubMed:21164013"
FT MOD_RES 109
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:21164013"
FT MUTAGEN 2
FT /note="S->A: Does not affect phosphorylation by GWL."
FT /evidence="ECO:0000269|PubMed:21164014"
FT MUTAGEN 51
FT /note="S->A: Does not affect phosphorylation by GWL."
FT /evidence="ECO:0000269|PubMed:21164014"
FT MUTAGEN 67
FT /note="S->A: Abolishes phosphorylation by GWL and ability
FT to regulate mitosis."
FT /evidence="ECO:0000269|PubMed:21164014"
FT MUTAGEN 93
FT /note="T->A: Does not affect phosphorylation by GWL."
FT /evidence="ECO:0000269|PubMed:21164014"
FT MUTAGEN 99
FT /note="T->A: Does not affect phosphorylation by GWL."
FT /evidence="ECO:0000269|PubMed:21164014"
FT MUTAGEN 109
FT /note="S->A: Does not affect phosphorylation by GWL."
FT /evidence="ECO:0000269|PubMed:21164014"
FT MUTAGEN 113
FT /note="S->A: Does not affect phosphorylation by GWL."
FT /evidence="ECO:0000269|PubMed:21164014"
SQ SEQUENCE 117 AA; 12931 MW; A958E15E494B8D45 CRC64;
MSGENQETKA QEESSALEQK EIDDKVVSPE KSEEIKLKAR YPNLGPKPGG SDFLRKRLQK
GQKYFDSGDY NMAKAKMKNK QLPTAASDKT EVTGDHIPTP QDLPQRKPSL VASKLAG
