ENSA_BOVIN
ID ENSA_BOVIN Reviewed; 121 AA.
AC P68210; O97976; Q2KID1; Q95105;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Alpha-endosulfine;
DE AltName: Full=ARPP-19e;
GN Name=ENSA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-31.
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), AND VARIANT ARG-31.
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-101.
RC TISSUE=Caudate nucleus;
RX PubMed=8687439; DOI=10.1006/bbrc.1996.0938;
RA Peyrollier K., Heron L., Virsolvy-Vergine A., Le Cam A., Bataille D.;
RT "Alpha endosulfine is a novel molecule, structurally related to a family of
RT phosphoproteins.";
RL Biochem. Biophys. Res. Commun. 223:583-586(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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P68210-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P68210-2; Sequence=VSP_019714;
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; X95958; CAA65196.1; -; mRNA.
DR EMBL; BC112682; AAI12683.1; -; mRNA.
DR EMBL; AJ005986; CAA06800.1; -; mRNA.
DR PIR; JC4878; JC4878.
DR RefSeq; NP_001300934.1; NM_001314005.1.
DR AlphaFoldDB; P68210; -.
DR BMRB; P68210; -.
DR STRING; 9913.ENSBTAP00000009379; -.
DR PaxDb; P68210; -.
DR PRIDE; P68210; -.
DR GeneID; 281142; -.
DR KEGG; bta:281142; -.
DR CTD; 2029; -.
DR eggNOG; KOG4076; Eukaryota.
DR HOGENOM; CLU_125025_0_1_1; -.
DR InParanoid; P68210; -.
DR OrthoDB; 1494565at2759; -.
DR TreeFam; TF314718; -.
DR Proteomes; UP000009136; 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 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:O43768"
FT CHAIN 2..121
FT /note="Alpha-endosulfine"
FT /id="PRO_0000146757"
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"
FT VAR_SEQ 118..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_019714"
FT VARIANT 31
FT /note="K -> R"
FT /evidence="ECO:0000269|PubMed:9653196, ECO:0000269|Ref.2"
FT CONFLICT 11
FT /note="A -> T (in Ref. 2; AAI12683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 121 AA; 13361 MW; A84629D3B9EFFC5A CRC64;
MSQKQEEENP AEETGEEKQD TQEKEGILPE KAEEAKLKAK YPSLGQKPGG SDFLMKRLQK
GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV
E
