ARP19_TAEGU
ID ARP19_TAEGU Reviewed; 112 AA.
AC B5G1C4; B5G1C5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=cAMP-regulated phosphoprotein 19;
DE Short=ARPP-19;
GN Name=ARPP19;
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=17018643; DOI=10.1073/pnas.0607098103;
RA Wada K., Howard J.T., McConnell P., Whitney O., Lints T., Rivas M.V.,
RA Horita H., Patterson M.A., White S.A., Scharff C., Haesler S., Zhao S.,
RA Sakaguchi H., Hagiwara M., Shiraki T., Hirozane-Kishikawa T., Skene P.,
RA Hayashizaki Y., Carninci P., Jarvis E.D.;
RT "A molecular neuroethological approach for identifying and characterizing a
RT cascade of behaviorally regulated genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15212-15217(2006).
CC -!- FUNCTION: Protein phosphatase inhibitor that specifically inhibits
CC protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at
CC Ser-62 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-62) with PPP2R2D.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B5G1C4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B5G1C4-2; Sequence=VSP_041056;
CC -!- PTM: Phosphorylation at Ser-62 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; DQ215487; ACH45085.1; -; mRNA.
DR EMBL; DQ215488; ACH45086.1; -; mRNA.
DR EMBL; DQ215489; ACH45087.1; -; mRNA.
DR RefSeq; NP_001232557.1; NM_001245628.2. [B5G1C4-2]
DR RefSeq; XP_012428224.1; XM_012572770.1. [B5G1C4-2]
DR AlphaFoldDB; B5G1C4; -.
DR STRING; 59729.ENSTGUP00000026693; -.
DR GeneID; 100190388; -.
DR KEGG; tgu:100190388; -.
DR CTD; 10776; -.
DR InParanoid; B5G1C4; -.
DR OMA; SKYPGGM; -.
DR OrthoDB; 1494565at2759; -.
DR Proteomes; UP000007754; Unplaced.
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 Alternative splicing; Cell cycle; Cell division; Cytoplasm; Mitosis;
KW Phosphoprotein; Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..112
FT /note="cAMP-regulated phosphoprotein 19"
FT /id="PRO_0000408320"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine; by GWL"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17018643"
FT /id="VSP_041056"
FT CONFLICT 67..68
FT /note="MA -> FF (in Ref. 1; ACH45085)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..72
FT /note="KM -> PP (in Ref. 1; ACH45085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 112 AA; 12349 MW; 402C77DC585DE4A6 CRC64;
MSAESPEPAS AEEQKEMEDK VLSPEKAEEA KLKARYPHLG QKPGGSDFLR KRLQKGQKYF
DSGDYNMAKA KMKNKQLPTA APDKTEVTGD HIPTPQDLPQ RKPSLVASKL AG
