ARP19_RAT
ID ARP19_RAT Reviewed; 112 AA.
AC Q712U5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=cAMP-regulated phosphoprotein 19;
DE Short=ARPP-19;
GN Name=Arpp19;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ARPP-19).
RC TISSUE=Brain;
RA Bataille D.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ARPP-19).
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 59-69 (ISOFORMS ARPP-16/ARPP-19), AND FUNCTION.
RX PubMed=12221279; DOI=10.1073/pnas.152457399;
RA Irwin N., Chao S., Goritchenko L., Horiuchi A., Greengard P., Nairn A.C.,
RA Benowitz L.I.;
RT "Nerve growth factor controls GAP-43 mRNA stability via the phosphoprotein
RT ARPP-19.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12427-12431(2002).
RN [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=2158525; DOI=10.1523/jneurosci.10-04-01124.1990;
RA Girault J.-A., Horiuchi A., Gustafson E.L., Rosen N.L., Greengard P.;
RT "Differential expression of ARPP-16 and ARPP-19, two highly related cAMP-
RT regulated phosphoproteins, one of which is specifically associated with
RT dopamine-innervated brain regions.";
RL J. Neurosci. 10:1124-1133(1990).
RN [5]
RP PHOSPHORYLATION AT SER-104.
RX PubMed=11279279; DOI=10.1046/j.1471-4159.2001.t01-1-00191.x;
RA Dulubova I., Horiuchi A., Snyder G.L., Girault J.-A., Czernik A.J.,
RA Shao L., Ramabhadran R., Greengard P., Nairn A.C.;
RT "ARPP-16/ARPP-19: a highly conserved family of cAMP-regulated
RT phosphoproteins.";
RL J. Neurochem. 77:229-238(2001).
RN [6]
RP INDUCTION BY DENERVATION, AND SUBCELLULAR LOCATION.
RX PubMed=12944371; DOI=10.1093/jb/mvg113;
RA Yoshikawa A., Mitsuhashi H., Sasagawa N., Tsukahara T., Hayashi Y.,
RA Nishino I., Goto Y., Ishiura S.;
RT "Expression of ARPP-16/19 in rat denervated skeletal muscle.";
RL J. Biochem. 134:57-61(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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). May indirectly enhance GAP-43 expression by binding to
CC the NGF-regulatory region of its mRNA. {ECO:0000250,
CC ECO:0000269|PubMed:12221279}.
CC -!- SUBUNIT: Interacts (when phosphorylated at Ser-62) with PPP2R2D.
CC Interacts with SNCA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12944371,
CC ECO:0000269|PubMed:2158525}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=ARPP-19;
CC IsoId=Q712U5-1; Sequence=Displayed;
CC Name=ARPP-16;
CC IsoId=Q712U5-2; Sequence=VSP_018558;
CC -!- TISSUE SPECIFICITY: Whereas isoform ARPP-19 is ubiquitously expressed,
CC isoform ARPP-16 is found only in selected brain neurons.
CC {ECO:0000269|PubMed:2158525}.
CC -!- INDUCTION: Up-regulated in denervated skeletal muscle (at protein
CC level). {ECO:0000269|PubMed:12944371}.
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:11279279}.
CC -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR EMBL; AJ005982; CAA06796.1; -; mRNA.
DR EMBL; BC058461; AAH58461.1; -; mRNA.
DR RefSeq; NP_113848.1; NM_031660.1. [Q712U5-1]
DR RefSeq; XP_002727150.2; XM_002727104.4. [Q712U5-1]
DR RefSeq; XP_002730018.2; XM_002729972.4. [Q712U5-1]
DR AlphaFoldDB; Q712U5; -.
DR BMRB; Q712U5; -.
DR STRING; 10116.ENSRNOP00000035534; -.
DR BindingDB; Q712U5; -.
DR ChEMBL; CHEMBL2170; -.
DR iPTMnet; Q712U5; -.
DR PhosphoSitePlus; Q712U5; -.
DR jPOST; Q712U5; -.
DR PaxDb; Q712U5; -.
DR PRIDE; Q712U5; -.
DR Ensembl; ENSRNOT00000030221; ENSRNOP00000035534; ENSRNOG00000023086. [Q712U5-1]
DR GeneID; 100360828; -.
DR GeneID; 60336; -.
DR KEGG; rno:100360828; -.
DR KEGG; rno:60336; -.
DR UCSC; RGD:71054; rat. [Q712U5-1]
DR CTD; 10776; -.
DR RGD; 71054; Arpp19.
DR eggNOG; KOG4076; Eukaryota.
DR GeneTree; ENSGT00940000154555; -.
DR HOGENOM; CLU_125025_1_0_1; -.
DR InParanoid; Q712U5; -.
DR OMA; SKYPGGM; -.
DR OrthoDB; 1494565at2759; -.
DR PhylomeDB; Q712U5; -.
DR Reactome; R-RNO-2465910; MASTL Facilitates Mitotic Progression.
DR PRO; PR:Q712U5; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000023086; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q712U5; RN.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IEP:RGD.
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; ISO:RGD.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:RGD.
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:0000250|UniProtKB:Q28055"
FT CHAIN 2..112
FT /note="cAMP-regulated phosphoprotein 19"
FT /id="PRO_0000235988"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..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|UniProtKB:Q28055"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0000305"
FT MOD_RES 104
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:11279279"
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:0000305"
FT /id="VSP_018558"
FT MOD_RES Q712U5-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q28055"
SQ SEQUENCE 112 AA; 12293 MW; F18BE46E35C839AB CRC64;
MSAEVPEAAS AEEQKEMEDK VTSPEKAEEA KLKARYPHLG QKPGGSDFLR KRLQKGQKYF
DSGDYNMAKA KMKNKQLPAA APDKTEVTGD HIPTPQDLPQ RKPSLVASKL AG
