ARP19_MOUSE
ID ARP19_MOUSE Reviewed; 112 AA.
AC P56212; Q543L2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=cAMP-regulated phosphoprotein 19;
DE Short=ARPP-19;
GN Name=Arpp19;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ARPP-16 AND ARPP-19), AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RA Girault J.-A., Horiuchi A., Gustafson E., Rosen N., Greengard P.;
RT "Differential expression of ARPP-16 and ARPP-19, two highly related
RT phosphoproteins, one of which is specifically associated with dopamine-
RT innervated brain regions.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ARPP-19).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ARPP-19).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION.
RX PubMed=2845422; DOI=10.1073/pnas.85.20.7790;
RA Girault J.-A., Shalaby I.A., Rosen N.L., Greengard P.;
RT "Regulation by cAMP and vasoactive intestinal peptide of phosphorylation of
RT specific proteins in striatal cells in culture.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7790-7794(1988).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 binding to the NGF-
CC regulatory region of its mRNA (By similarity). {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=P56212-1; Sequence=Displayed;
CC Name=ARPP-16;
CC IsoId=P56212-2; Sequence=VSP_018556;
CC -!- DEVELOPMENTAL STAGE: Isoform ARPP-19 is highly expressed in the embryo
CC and its levels decrease progressively as development proceeds. In
CC contrast, isoform ARPP-16 appears in the brain at the end of the first
CC postnatal week and increases to reach a plateau. {ECO:0000269|Ref.1}.
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, ECO:0000269|PubMed:2845422}.
CC -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR EMBL; AJ005983; CAA06797.1; -; mRNA.
DR EMBL; AK049760; BAC33908.1; -; mRNA.
DR EMBL; BC040206; AAH40206.1; -; mRNA.
DR CCDS; CCDS23340.1; -. [P56212-1]
DR CCDS; CCDS90623.1; -. [P56212-2]
DR RefSeq; NP_067523.1; NM_021548.4. [P56212-1]
DR RefSeq; XP_006511390.1; XM_006511327.1.
DR AlphaFoldDB; P56212; -.
DR BMRB; P56212; -.
DR STRING; 10090.ENSMUSP00000007800; -.
DR iPTMnet; P56212; -.
DR PhosphoSitePlus; P56212; -.
DR EPD; P56212; -.
DR jPOST; P56212; -.
DR MaxQB; P56212; -.
DR PaxDb; P56212; -.
DR PeptideAtlas; P56212; -.
DR PRIDE; P56212; -.
DR ProteomicsDB; 283231; -. [P56212-1]
DR ProteomicsDB; 283232; -. [P56212-2]
DR Antibodypedia; 42667; 57 antibodies from 19 providers.
DR Ensembl; ENSMUST00000007800; ENSMUSP00000007800; ENSMUSG00000007656. [P56212-1]
DR Ensembl; ENSMUST00000164467; ENSMUSP00000130730; ENSMUSG00000007656. [P56212-1]
DR Ensembl; ENSMUST00000166549; ENSMUSP00000131987; ENSMUSG00000007656. [P56212-2]
DR Ensembl; ENSMUST00000167885; ENSMUSP00000131597; ENSMUSG00000007656. [P56212-2]
DR Ensembl; ENSMUST00000168166; ENSMUSP00000126618; ENSMUSG00000007656. [P56212-1]
DR Ensembl; ENSMUST00000170308; ENSMUSP00000132350; ENSMUSG00000007656. [P56212-1]
DR Ensembl; ENSMUST00000170310; ENSMUSP00000125825; ENSMUSG00000007656. [P56212-2]
DR GeneID; 59046; -.
DR KEGG; mmu:59046; -.
DR UCSC; uc009qro.1; mouse. [P56212-1]
DR CTD; 10776; -.
DR MGI; MGI:1891691; Arpp19.
DR VEuPathDB; HostDB:ENSMUSG00000007656; -.
DR eggNOG; KOG4076; Eukaryota.
DR GeneTree; ENSGT00940000154555; -.
DR HOGENOM; CLU_125025_1_0_1; -.
DR InParanoid; P56212; -.
DR TreeFam; TF314718; -.
DR Reactome; R-MMU-2465910; MASTL Facilitates Mitotic Progression.
DR BioGRID-ORCS; 59046; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Arpp19; mouse.
DR PRO; PR:P56212; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P56212; protein.
DR Bgee; ENSMUSG00000007656; Expressed in caudate-putamen and 261 other tissues.
DR ExpressionAtlas; P56212; baseline and differential.
DR Genevisible; P56212; MM.
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:MGI.
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:MGI.
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; ISO:MGI.
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 Mitosis; Phosphoprotein; 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_0000146762"
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: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:0000269|PubMed:11279279,
FT ECO:0007744|PubMed:21183079"
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|Ref.1"
FT /id="VSP_018556"
FT MOD_RES P56212-2:1
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
