ARP19_PIG
ID ARP19_PIG Reviewed; 112 AA.
AC Q712U6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=cAMP-regulated phosphoprotein 19;
DE Short=ARPP-19;
GN Name=ARPP19;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ARPP-16 AND ARPP-19), AND TISSUE
RP SPECIFICITY.
RX PubMed=10875629; DOI=10.2527/2000.7861475x;
RA Janzen M.A., Kuhlers D.L., Jungst S.B., Louis C.F.;
RT "ARPP-16 mRNA is up-regulated in the longissimus muscle of pigs possessing
RT an elevated growth rate.";
RL J. Anim. Sci. 78:1475-1484(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ARPP-19).
RA Bataille D.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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=Q712U6-1; Sequence=Displayed;
CC Name=ARPP-16;
CC IsoId=Q712U6-2; Sequence=VSP_018557;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10875629}.
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. Phosphorylated by PKA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR EMBL; AJ005981; CAA06795.1; -; mRNA.
DR RefSeq; NP_999340.1; NM_214175.1. [Q712U6-1]
DR RefSeq; XP_005659645.1; XM_005659588.2. [Q712U6-1]
DR RefSeq; XP_005659646.1; XM_005659589.2. [Q712U6-1]
DR AlphaFoldDB; Q712U6; -.
DR BMRB; Q712U6; -.
DR STRING; 9823.ENSSSCP00000004976; -.
DR PaxDb; Q712U6; -.
DR PeptideAtlas; Q712U6; -.
DR Ensembl; ENSSSCT00000038541; ENSSSCP00000051686; ENSSSCG00000004620. [Q712U6-1]
DR Ensembl; ENSSSCT00025015200; ENSSSCP00025005951; ENSSSCG00025010333. [Q712U6-1]
DR Ensembl; ENSSSCT00030093990; ENSSSCP00030043318; ENSSSCG00030066368. [Q712U6-1]
DR Ensembl; ENSSSCT00040047541; ENSSSCP00040019877; ENSSSCG00040035185. [Q712U6-1]
DR Ensembl; ENSSSCT00045053752; ENSSSCP00045037381; ENSSSCG00045029944. [Q712U6-1]
DR Ensembl; ENSSSCT00050076064; ENSSSCP00050032784; ENSSSCG00050055696. [Q712U6-1]
DR Ensembl; ENSSSCT00065076493; ENSSSCP00065033291; ENSSSCG00065055540. [Q712U6-1]
DR Ensembl; ENSSSCT00070014722; ENSSSCP00070012162; ENSSSCG00070006926. [Q712U6-1]
DR GeneID; 397362; -.
DR KEGG; ssc:397362; -.
DR CTD; 10776; -.
DR eggNOG; KOG4076; Eukaryota.
DR GeneTree; ENSGT00940000155347; -.
DR HOGENOM; CLU_125025_1_0_1; -.
DR InParanoid; Q712U6; -.
DR OrthoDB; 1494565at2759; -.
DR TreeFam; TF314718; -.
DR Reactome; R-SSC-2465910; MASTL Facilitates Mitotic Progression.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000004620; Expressed in hippocampal formation and 44 other tissues.
DR ExpressionAtlas; Q712U6; baseline and differential.
DR Genevisible; Q712U6; SS.
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; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR InterPro; IPR006760; Endosulphine.
DR PANTHER; PTHR10358; PTHR10358; 1.
DR Pfam; PF04667; Endosulfine; 1.
PE 2: Evidence at transcript 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_0000235987"
FT REGION 1..49
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|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: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:10875629"
FT /id="VSP_018557"
FT MOD_RES Q712U6-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q28055"
SQ SEQUENCE 112 AA; 12323 MW; F19652B545C839AB CRC64;
MSAEVPEAAS AEEQKEMEDK VTSPEKAEEA KLKARYPHLG QKPGGSDFLR KRLQKGQKYF
DSGDYNMAKA KMKNKQLPTA APDKTEVTGD HIPTPQDLPQ RKPSLVASKL AG
