ENSA_RAT
ID ENSA_RAT Reviewed; 121 AA.
AC P60841; Q6PCU7; Q9CQZ9; Q9Z0G1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Alpha-endosulfine;
DE AltName: Full=ARPP-19e;
GN Name=Ensa;
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 1).
RC TISSUE=Brain;
RX PubMed=9653196; DOI=10.1073/pnas.95.14.8387;
RA Heron L., Virsolvy A., Peyrollier K., Gribble F.M., Le Cam A.,
RA Ashcroft F.M., Bataille D.;
RT "Human alpha-endosulfine, a possible regulator of sulfonylurea-sensitive
RT K(ATP) channel: molecular cloning, expression and biological properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8387-8391(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-109.
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 [4]
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-67 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. Also acts as a stimulator of insulin secretion by interacting
CC with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea
CC from binding to its receptor and reducing K(ATP) channel currents (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (when phosphorylated at Ser-67) with PPP2R2D.
CC Interacts with ABCC8. Interacts with SNCA; interaction is disrupted
CC when phosphorylated at Ser-109 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11279279}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60841-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60841-2; Sequence=VSP_037070;
CC -!- TISSUE SPECIFICITY: Present in brain (at protein level).
CC {ECO:0000269|PubMed:11279279}.
CC -!- PTM: Phosphorylation at Ser-67 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; AJ005984; CAA06798.1; -; mRNA.
DR EMBL; BC059135; AAH59135.1; -; mRNA.
DR RefSeq; NP_001029146.1; NM_001033974.2. [P60841-2]
DR RefSeq; NP_068614.1; NM_021842.3. [P60841-1]
DR AlphaFoldDB; P60841; -.
DR BMRB; P60841; -.
DR STRING; 10116.ENSRNOP00000063946; -.
DR iPTMnet; P60841; -.
DR PhosphoSitePlus; P60841; -.
DR jPOST; P60841; -.
DR PaxDb; P60841; -.
DR PRIDE; P60841; -.
DR Ensembl; ENSRNOT00000075511; ENSRNOP00000063946; ENSRNOG00000048617. [P60841-1]
DR Ensembl; ENSRNOT00000104132; ENSRNOP00000083613; ENSRNOG00000048617. [P60841-2]
DR GeneID; 60334; -.
DR KEGG; rno:60334; -.
DR CTD; 2029; -.
DR RGD; 62007; Ensa.
DR eggNOG; KOG4076; Eukaryota.
DR GeneTree; ENSGT00940000155413; -.
DR InParanoid; P60841; -.
DR OMA; VWSTISY; -.
DR OrthoDB; 1494565at2759; -.
DR PhylomeDB; P60841; -.
DR Reactome; R-RNO-2465910; MASTL Facilitates Mitotic Progression.
DR PRO; PR:P60841; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000048617; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; P60841; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0019212; F:phosphatase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0019870; F:potassium channel inhibitor activity; ISO:RGD.
DR GO; GO:0015459; F:potassium channel regulator activity; NAS: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: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:0050796; P:regulation of insulin secretion; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; IEP: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 Mitosis; Phosphoprotein; Protein phosphatase inhibitor; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43768"
FT CHAIN 2..121
FT /note="Alpha-endosulfine"
FT /id="PRO_0000146761"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O43768"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43768"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43768"
FT MOD_RES 67
FT /note="Phosphoserine; by GWL"
FT /evidence="ECO:0000250"
FT MOD_RES 109
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000305|PubMed:11279279"
FT VAR_SEQ 118..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037070"
SQ SEQUENCE 121 AA; 13335 MW; A84632C9085FFC5A CRC64;
MSQKQEEENP AEETGEEKQD TQEKEGILPE KAEEAKLKAK YPSLGQKPGG SDFLMKRLQK
GQKYFDSGDY NMAKAKMKNK QLPSAGADKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV
E
