ID   ENSA_XENLA              Reviewed;         125 AA.
AC   Q7ZXH9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Alpha-endosulfine;
GN   Name=ensa;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, INTERACTION WITH PPP2R2D, PHOSPHORYLATION AT THR-28; SER-67;
RP   THR-99 AND SER-109, AND MUTAGENESIS OF SER-67.
RX   PubMed=21164013; DOI=10.1126/science.1195689;
RA   Mochida S., Maslen S.L., Skehel M., Hunt T.;
RT   "Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is
RT   essential for mitosis.";
RL   Science 330:1670-1673(2010).
RN   [3]
RP   FUNCTION, INTERACTION WITH PPP2R2D, PHOSPHORYLATION AT SER-67, AND
RP   MUTAGENESIS OF SER-67.
RX   PubMed=21164014; DOI=10.1126/science.1197048;
RA   Gharbi-Ayachi A., Labbe J.C., Burgess A., Vigneron S., Strub J.M.,
RA   Brioudes E., Van-Dorsselaer A., Castro A., Lorca T.;
RT   "The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting
RT   protein phosphatase 2A.";
RL   Science 330:1673-1677(2010).
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. {ECO:0000269|PubMed:21164013, ECO:0000269|PubMed:21164014}.
CC   -!- SUBUNIT: Interacts (when phosphorylated at Ser-67) with ppp2r2d.
CC       {ECO:0000269|PubMed:21164013, ECO:0000269|PubMed:21164014}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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. {ECO:0000269|PubMed:21164013,
CC       ECO:0000269|PubMed:21164014}.
CC   -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR   EMBL; BC044986; AAH44986.1; -; mRNA.
DR   RefSeq; NP_001080074.1; NM_001086605.1.
DR   AlphaFoldDB; Q7ZXH9; -.
DR   iPTMnet; Q7ZXH9; -.
DR   DNASU; 379766; -.
DR   GeneID; 379766; -.
DR   KEGG; xla:379766; -.
DR   CTD; 379766; -.
DR   Xenbase; XB-GENE-6077899; ensa.S.
DR   OMA; VWSTISY; -.
DR   OrthoDB; 1494565at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 379766; Expressed in camera-type eye and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0019212; F:phosphatase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; IDA:UniProtKB.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IDA:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR   InterPro; IPR006760; Endosulphine.
DR   PANTHER; PTHR10358; PTHR10358; 1.
DR   Pfam; PF04667; Endosulfine; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein;
KW   Protein phosphatase inhibitor; Reference proteome.
FT   CHAIN           1..125
FT                   /note="Alpha-endosulfine"
FT                   /id="PRO_0000371566"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..107
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   MOD_RES         28
FT                   /note="Phosphothreonine; by CDK2"
FT                   /evidence="ECO:0000269|PubMed:21164013"
FT   MOD_RES         67
FT                   /note="Phosphoserine; by GWL"
FT                   /evidence="ECO:0000269|PubMed:21164013,
FT                   ECO:0000269|PubMed:21164014"
FT   MOD_RES         99
FT                   /note="Phosphothreonine; by CDK2"
FT                   /evidence="ECO:0000269|PubMed:21164013"
FT   MOD_RES         109
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000269|PubMed:21164013"
FT   MUTAGEN         67
FT                   /note="S->A: Abolishes phosphorylation by GWL and ability
FT                   to regulate mitosis."
FT                   /evidence="ECO:0000269|PubMed:21164013,
FT                   ECO:0000269|PubMed:21164014"
SQ   SEQUENCE   125 AA;  13946 MW;  A94479F6FDB6E183 CRC64;
     MSDKYIGDSH LEETGEEKQD SQEKEAVTPE KAEEQKLKAK YPNLGQKPGG SDFLMKRLQK
     GQKYFDSGDY NMAKAKIKNK QLPCAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGHVE
     DLHHV