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ARP19_CHICK
ID   ARP19_CHICK             Reviewed;         112 AA.
AC   Q5ZLY8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=cAMP-regulated phosphoprotein 19;
DE            Short=ARPP-19;
GN   Name=ARPP19; ORFNames=RCJMB04_4f12;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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   -!- 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; AJ719596; CAG31255.1; -; mRNA.
DR   RefSeq; NP_001075176.1; NM_001081707.1.
DR   AlphaFoldDB; Q5ZLY8; -.
DR   STRING; 9031.ENSGALP00000038292; -.
DR   PaxDb; Q5ZLY8; -.
DR   Ensembl; ENSGALT00000039081; ENSGALP00000038292; ENSGALG00000017370.
DR   GeneID; 768853; -.
DR   KEGG; gga:768853; -.
DR   CTD; 10776; -.
DR   VEuPathDB; HostDB:geneid_768853; -.
DR   eggNOG; KOG4076; Eukaryota.
DR   GeneTree; ENSGT00940000154555; -.
DR   HOGENOM; CLU_125025_1_0_1; -.
DR   InParanoid; Q5ZLY8; -.
DR   OMA; SKYPGGM; -.
DR   OrthoDB; 1494565at2759; -.
DR   PhylomeDB; Q5ZLY8; -.
DR   PRO; PR:Q5ZLY8; -.
DR   Proteomes; UP000000539; Chromosome 10.
DR   Bgee; ENSGALG00000017370; Expressed in spermatocyte and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0019212; F:phosphatase inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0015459; F:potassium channel regulator activity; ISS:AgBase.
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:0005102; F:signaling receptor binding; ISS:AgBase.
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   GO; GO:0045722; P:positive regulation of gluconeogenesis; ISS:AgBase.
DR   InterPro; IPR006760; Endosulphine.
DR   PANTHER; PTHR10358; PTHR10358; 1.
DR   Pfam; PF04667; Endosulfine; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein;
KW   Protein phosphatase inhibitor; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..112
FT                   /note="cAMP-regulated phosphoprotein 19"
FT                   /id="PRO_0000235989"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..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         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         62
FT                   /note="Phosphoserine; by GWL"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         104
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   112 AA;  12349 MW;  305C72895D0DB1A3 CRC64;
     MSAESPEPAS AEEQKEMEDK VISPEKAEEA KLKARYPHLG QKPGGSDFLR KRLQKGQKYF
     DSGDYNMAKA KMKNKQLPTA APDKTEVTGD HIPTPQDLPQ RKPSLVASKL AG
 
 
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