ID   ENSA_XENTR              Reviewed;         125 AA.
AC   Q6NVR1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Alpha-endosulfine;
GN   Name=ensa; ORFNames=TTpA018o10.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2004) 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-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 phase
CC       (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR   EMBL; CR760899; CAJ82927.1; -; mRNA.
DR   EMBL; BC067944; AAH67944.1; -; mRNA.
DR   RefSeq; NP_998845.1; NM_213680.1.
DR   AlphaFoldDB; Q6NVR1; -.
DR   STRING; 8364.ENSXETP00000056121; -.
DR   PaxDb; Q6NVR1; -.
DR   PRIDE; Q6NVR1; -.
DR   DNASU; 407936; -.
DR   GeneID; 407936; -.
DR   KEGG; xtr:407936; -.
DR   CTD; 2029; -.
DR   Xenbase; XB-GENE-943824; ensa.
DR   eggNOG; KOG4076; Eukaryota.
DR   HOGENOM; CLU_125025_0_1_1; -.
DR   InParanoid; Q6NVR1; -.
DR   OMA; NQDTETH; -.
DR   OrthoDB; 1494565at2759; -.
DR   PhylomeDB; Q6NVR1; -.
DR   TreeFam; TF314718; -.
DR   Reactome; R-XTR-2465910; MASTL Facilitates Mitotic Progression.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000026684; Expressed in skeletal muscle tissue and 18 other tissues.
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   Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein;
KW   Protein phosphatase inhibitor; Reference proteome.
FT   CHAIN           1..125
FT                   /note="Alpha-endosulfine"
FT                   /id="PRO_0000371567"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..108
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:0000250"
FT   MOD_RES         67
FT                   /note="Phosphoserine; by GWL"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         99
FT                   /note="Phosphothreonine; by CDK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         109
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   125 AA;  13955 MW;  AE4824473DB6E183 CRC64;
     MSDKYIGDSH LEETGEEKQD SQEKEAVTPE KAEEQKLKAK YPNLGQKPGG SDFLMKRLQK
     GQKYFDSGDY NMAKAKMKNK QLPCAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGHVE
     DLHQV