AR19B_XENLA
ID AR19B_XENLA Reviewed; 117 AA.
AC Q6GQG3; Q7ZXC1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=cAMP-regulated phosphoprotein 19-B;
DE Short=ARPP-19-B;
GN Name=arpp19-b;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH45060.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC045060; AAH45060.1; ALT_INIT; mRNA.
DR EMBL; BC072781; AAH72781.1; -; mRNA.
DR RefSeq; NP_001083756.1; NM_001090287.1.
DR AlphaFoldDB; Q6GQG3; -.
DR iPTMnet; Q6GQG3; -.
DR PRIDE; Q6GQG3; -.
DR DNASU; 399099; -.
DR GeneID; 399099; -.
DR KEGG; xla:399099; -.
DR CTD; 399099; -.
DR Xenbase; XB-GENE-17336028; arpp19.S.
DR OMA; SKYPGGM; -.
DR OrthoDB; 1494565at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 399099; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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 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-B"
FT /id="PRO_0000408322"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..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"
FT CONFLICT 39
FT /note="S -> T (in Ref. 1; AAH45060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 117 AA; 13043 MW; F097126C3ED4B1AC CRC64;
MSRDNQEIKA PEESSAEEQK EMDDKVTSPE KAEEIKLKSR YPNIGPKPGG SDFLRKRLQK
GQKYFDSGDY NMAKAKMKNK QLPTAAPDKT EVTGDHIPTP QDLPQRKPSL VASKLAG
