ENSA_PIG
ID ENSA_PIG Reviewed; 121 AA.
AC P68211; O97976; Q95105;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Alpha-endosulfine;
DE AltName: Full=ARPP-19e;
GN Name=ENSA;
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].
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 PROTEIN SEQUENCE OF 25-36; 39-57; 59-74 AND 81-106, MASS SPECTROMETRY, AND
RP CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=8635664; DOI=10.1007/bf00403955;
RA Virsolvy-Vergine A., Salazar G., Sillard R., Denoroy L., Mutt V.,
RA Bataille D.;
RT "Endosulfine, endogenous ligand for the sulphonylurea receptor: isolation
RT from porcine brain and partial structural determination of the alpha
RT form.";
RL Diabetologia 39:135-141(1996).
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:0000250}.
CC -!- PTM: The N-terminus is blocked.
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 -!- MASS SPECTROMETRY: Mass=13196; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8635664};
CC -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR EMBL; AJ005987; CAA06801.1; -; mRNA.
DR RefSeq; NP_999339.1; NM_214174.1.
DR AlphaFoldDB; P68211; -.
DR BMRB; P68211; -.
DR STRING; 9823.ENSSSCP00000007095; -.
DR PaxDb; P68211; -.
DR PeptideAtlas; P68211; -.
DR PRIDE; P68211; -.
DR GeneID; 397361; -.
DR CTD; 2029; -.
DR eggNOG; KOG4076; Eukaryota.
DR InParanoid; P68211; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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; 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:O43768"
FT CHAIN 2..121
FT /note="Alpha-endosulfine"
FT /id="PRO_0000146760"
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:0000250|UniProtKB:O43768"
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:0000250|UniProtKB:O43768"
SQ SEQUENCE 121 AA; 13361 MW; A84629D3B9EFFC5A CRC64;
MSQKQEEENP AEETGEEKQD TQEKEGILPE KAEEAKLKAK YPSLGQKPGG SDFLMKRLQK
GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV
E
