ARP19_BOVIN
ID ARP19_BOVIN Reviewed; 112 AA.
AC Q28055; Q28054;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=cAMP-regulated phosphoprotein 19;
DE Short=ARPP-19;
GN Name=ARPP19;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ARPP-16 AND ARPP-19), PARTIAL PROTEIN
RP SEQUENCE, PHOSPHORYLATION, ACETYLATION AT SER-2, ACETYLATION AT MET-1
RP (ISOFORM ARPP-16), AND MASS SPECTROMETRY.
RC TISSUE=Caudate nucleus;
RX PubMed=2160982; DOI=10.1016/s0021-9258(19)38874-x;
RA Horiuchi A., Williams K.R., Kurihara T., Nairn A.C., Greengard P.;
RT "Purification and cDNA cloning of ARPP-16, a cAMP-regulated phosphoprotein
RT enriched in basal ganglia, and of a related phosphoprotein, ARPP-19.";
RL J. Biol. Chem. 265:9476-9484(1990).
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
CC phase. May indirectly enhance GAP-43 expression (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (when phosphorylated at Ser-62) with PPP2R2D.
CC Interacts with SNCA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=ARPP-19;
CC IsoId=Q28055-1; Sequence=Displayed;
CC Name=ARPP-16;
CC IsoId=Q28055-2; Sequence=VSP_018554;
CC -!- TISSUE SPECIFICITY: Isoform ARPP-19 is found in all brain regions and
CC also present in non-neuronal tissues. Isoform ARPP-16 is enriched in
CC the caudate nucleus, found in low levels in cerebral cortex.
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 (By similarity). Phosphorylated by PKA. {ECO:0000250,
CC ECO:0000269|PubMed:2160982}.
CC -!- MASS SPECTROMETRY: Mass=10708; Mass_error=1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:2160982};
CC -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR EMBL; M33618; AAA30386.1; -; mRNA.
DR EMBL; M33617; AAA30385.1; -; mRNA.
DR PIR; B35308; B35308.
DR RefSeq; NP_001106726.1; NM_001113255.1. [Q28055-1]
DR RefSeq; NP_777130.1; NM_174705.1. [Q28055-2]
DR RefSeq; XP_005211845.2; XM_005211788.3.
DR RefSeq; XP_010807630.1; XM_010809328.2. [Q28055-1]
DR AlphaFoldDB; Q28055; -.
DR BMRB; Q28055; -.
DR STRING; 9913.ENSBTAP00000022929; -.
DR iPTMnet; Q28055; -.
DR PaxDb; Q28055; -.
DR PRIDE; Q28055; -.
DR Ensembl; ENSBTAT00000014642; ENSBTAP00000014642; ENSBTAG00000011022. [Q28055-2]
DR Ensembl; ENSBTAT00000022929; ENSBTAP00000022929; ENSBTAG00000011022. [Q28055-1]
DR GeneID; 282658; -.
DR KEGG; bta:282658; -.
DR CTD; 10776; -.
DR VEuPathDB; HostDB:ENSBTAG00000011022; -.
DR eggNOG; KOG4076; Eukaryota.
DR GeneTree; ENSGT00940000154555; -.
DR HOGENOM; CLU_125025_1_0_1; -.
DR InParanoid; Q28055; -.
DR OMA; SKYPGGM; -.
DR OrthoDB; 1494565at2759; -.
DR TreeFam; TF314718; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000011022; Expressed in occipital lobe and 105 other tissues.
DR ExpressionAtlas; Q28055; baseline and differential.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Direct protein sequencing; Mitosis; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2160982"
FT CHAIN 2..112
FT /note="cAMP-regulated phosphoprotein 19"
FT /id="PRO_0000008039"
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 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:2160982"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56211"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56211"
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|UniProtKB:P56212"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56211"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform ARPP-16)"
FT /evidence="ECO:0000303|PubMed:2160982"
FT /id="VSP_018554"
FT MOD_RES Q28055-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:2160982"
SQ SEQUENCE 112 AA; 12353 MW; 874D22B545C839BF CRC64;
MSAEVPEAAS AEEQKEMEDK VTSPEKAEEA KLKARYPHLG QKPGGSDFLR KRLQKGQKYF
DSGDYNMAKA KMKNKQLPTA TPDKTEVTGD HIPTPQDLPQ RKPSLVASKL AG
