ENSA_MOUSE
ID ENSA_MOUSE Reviewed; 121 AA.
AC P60840; Q5D069; Q6PBG4; Q9CQZ9; Q9Z0G1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Alpha-endosulfine;
DE AltName: Full=ARPP-19e;
GN Name=Ensa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=FVB/N; TISSUE=Colon, and Testis;
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 [5]
RP TISSUE SPECIFICITY, 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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. 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=3;
CC Name=1; Synonyms=Alpha;
CC IsoId=P60840-1, Q9Z0G1-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=P60840-2, Q9Z0G1-2;
CC Sequence=VSP_001444;
CC Name=3;
CC IsoId=P60840-3, Q9Z0G1-3;
CC Sequence=VSP_037068, VSP_037069;
CC -!- TISSUE SPECIFICITY: Present in striatum (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 -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR EMBL; AJ005985; CAA06799.1; -; mRNA.
DR EMBL; AK006149; BAB24433.1; -; mRNA.
DR EMBL; AK011334; BAB27552.1; -; mRNA.
DR EMBL; AK149726; BAE29049.1; -; mRNA.
DR EMBL; AK161290; BAE36298.1; -; mRNA.
DR EMBL; AK019170; BAB31584.1; -; mRNA.
DR EMBL; CH466620; EDL38827.1; -; Genomic_DNA.
DR EMBL; BC058802; AAH58802.1; -; mRNA.
DR EMBL; BC059724; AAH59724.1; -; mRNA.
DR CCDS; CCDS17617.1; -. [P60840-2]
DR CCDS; CCDS50993.1; -.
DR RefSeq; NP_001021383.1; NM_001026212.1. [P60840-2]
DR RefSeq; NP_062507.1; NM_019561.2. [P60840-1]
DR AlphaFoldDB; P60840; -.
DR BMRB; P60840; -.
DR BioGRID; 207841; 1.
DR STRING; 10090.ENSMUSP00000051799; -.
DR iPTMnet; P60840; -.
DR PhosphoSitePlus; P60840; -.
DR EPD; P60840; -.
DR jPOST; P60840; -.
DR MaxQB; P60840; -.
DR PaxDb; P60840; -.
DR PeptideAtlas; P60840; -.
DR PRIDE; P60840; -.
DR ProteomicsDB; 275913; -.
DR ProteomicsDB; 275914; -. [P60840-2]
DR ProteomicsDB; 275915; -. [P60840-3]
DR Antibodypedia; 34035; 241 antibodies from 27 providers.
DR Ensembl; ENSMUST00000037983; ENSMUSP00000045937; ENSMUSG00000038619. [P60840-2]
DR Ensembl; ENSMUST00000058230; ENSMUSP00000051799; ENSMUSG00000038619. [P60840-1]
DR GeneID; 56205; -.
DR KEGG; mmu:56205; -.
DR UCSC; uc008qki.1; mouse. [P60840-3]
DR UCSC; uc008qkj.1; mouse.
DR CTD; 2029; -.
DR MGI; MGI:1891189; Ensa.
DR VEuPathDB; HostDB:ENSMUSG00000038619; -.
DR eggNOG; KOG4076; Eukaryota.
DR GeneTree; ENSGT00940000155413; -.
DR HOGENOM; CLU_125025_0_1_1; -.
DR InParanoid; P60840; -.
DR OMA; VWSTISY; -.
DR OrthoDB; 1494565at2759; -.
DR PhylomeDB; P60840; -.
DR TreeFam; TF314718; -.
DR Reactome; R-MMU-2465910; MASTL Facilitates Mitotic Progression.
DR BioGRID-ORCS; 56205; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ensa; mouse.
DR PRO; PR:P60840; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P60840; protein.
DR Bgee; ENSMUSG00000038619; Expressed in dentate gyrus of hippocampal formation granule cell and 259 other tissues.
DR Genevisible; P60840; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0019212; F:phosphatase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0019870; F:potassium channel inhibitor activity; ISO:MGI.
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:MGI.
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:MGI.
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_0000146759"
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 108
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11279279"
FT VAR_SEQ 62..72
FT /note="QKYFDSGDYNM -> VWDTLILWHLG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037068"
FT VAR_SEQ 73..121
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037069"
FT VAR_SEQ 118..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_001444"
FT CONFLICT 24
FT /note="K -> E (in Ref. 2; BAB27552/BAB31584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 121 AA; 13335 MW; A84632C9085FFC5A CRC64;
MSQKQEEENP AEETGEEKQD TQEKEGILPE KAEEAKLKAK YPSLGQKPGG SDFLMKRLQK
GQKYFDSGDY NMAKAKMKNK QLPSAGADKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV
E
