MASTR_MOUSE
ID MASTR_MOUSE Reviewed; 421 AA.
AC Q0ZCJ7; A1L0X1; E9QM68; Q3B818;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=MEF2-activating motif and SAP domain-containing transcriptional regulator;
DE AltName: Full=MEF2-activating SAP transcriptional regulatory protein;
GN Name=Mamstr; Synonyms=Mastr;
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), FUNCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=16818234; DOI=10.1016/j.molcel.2006.05.026;
RA Creemers E.E., Sutherland L.B., Oh J., Barbosa A.C., Olson E.N.;
RT "Coactivation of MEF2 by the SAP domain proteins myocardin and MASTR.";
RL Mol. Cell 23:83-96(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-348 (ISOFORM 2).
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).
CC -!- FUNCTION: Transcriptional coactivator. Stimulates the transcriptional
CC activity of MEF2C. Stimulates MYOD1 activity in part via MEF2,
CC resulting in an enhancement of skeletal muscle differentiation.
CC {ECO:0000269|PubMed:16818234}.
CC -!- SUBUNIT: Interacts with MEF2C. {ECO:0000269|PubMed:16818234}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16818234}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0ZCJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0ZCJ7-2; Sequence=VSP_031556, VSP_031557;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, placenta and
CC spleen. {ECO:0000269|PubMed:16818234}.
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DR EMBL; DQ534901; ABF85692.1; -; mRNA.
DR EMBL; AC149057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC107175; AAI07176.1; -; mRNA.
DR EMBL; BC107176; AAI07177.1; -; mRNA.
DR EMBL; BC119481; AAI19482.1; -; mRNA.
DR EMBL; BC119482; AAI19483.1; -; mRNA.
DR EMBL; BC127227; AAI27228.1; -; mRNA.
DR EMBL; BC127228; AAI27229.1; -; mRNA.
DR CCDS; CCDS21257.2; -. [Q0ZCJ7-1]
DR RefSeq; NP_766006.2; NM_172418.2. [Q0ZCJ7-1]
DR RefSeq; XP_006541297.1; XM_006541234.3. [Q0ZCJ7-1]
DR AlphaFoldDB; Q0ZCJ7; -.
DR SMR; Q0ZCJ7; -.
DR STRING; 10090.ENSMUSP00000114686; -.
DR PhosphoSitePlus; Q0ZCJ7; -.
DR PaxDb; Q0ZCJ7; -.
DR PRIDE; Q0ZCJ7; -.
DR Antibodypedia; 45786; 88 antibodies from 14 providers.
DR Ensembl; ENSMUST00000148532; ENSMUSP00000114686; ENSMUSG00000042918. [Q0ZCJ7-1]
DR GeneID; 74490; -.
DR KEGG; mmu:74490; -.
DR UCSC; uc009gwk.2; mouse. [Q0ZCJ7-1]
DR CTD; 284358; -.
DR MGI; MGI:1921740; Mamstr.
DR VEuPathDB; HostDB:ENSMUSG00000042918; -.
DR eggNOG; ENOG502RJE6; Eukaryota.
DR GeneTree; ENSGT00940000154181; -.
DR HOGENOM; CLU_055830_0_0_1; -.
DR InParanoid; Q0ZCJ7; -.
DR OMA; PKISQHW; -.
DR OrthoDB; 1127316at2759; -.
DR PhylomeDB; Q0ZCJ7; -.
DR BioGRID-ORCS; 74490; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q0ZCJ7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q0ZCJ7; protein.
DR Bgee; ENSMUSG00000042918; Expressed in hindlimb stylopod muscle and 111 other tissues.
DR ExpressionAtlas; Q0ZCJ7; baseline and differential.
DR Genevisible; Q0ZCJ7; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..421
FT /note="MEF2-activating motif and SAP domain-containing
FT transcriptional regulator"
FT /id="PRO_0000319982"
FT DOMAIN 165..199
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 104..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..421
FT /note="Transcription activation"
FT REGION 322..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 12..28
FT /note="MEF2-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 197..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..135
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031556"
FT VAR_SEQ 136..139
FT /note="RPHP -> MPVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031557"
FT CONFLICT 53
FT /note="T -> P (in Ref. 1; ABF85692)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="S -> P (in Ref. 1; ABF85692)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="K -> R (in Ref. 1; ABF85692)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="P -> R (in Ref. 3; AAI27229/AAI27228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 45403 MW; 8E32B80765E9A3E1 CRC64;
MTLAASSQRS QIIRSKFRSV LQLRIHRRNQ DCTSDSDPWI SASGPALAPA LPTVPASFLV
SPGVLSPEPA YCPWRAPKKE SPKNSQHWKE PKVRGNLTYH LYMPPEQRQG PRANLQVERS
TLGPPDPPLW EKNSQRPHPR MKPSSAGVSS PSPPSHKLEL QTLKLEELTV SELRQQLRLR
GLPVSGTKAM LLERMRGGTP PRERPKPRRE DKEAAAPWPR LKPKALGTTR LPSTVKASAT
NRRLKFSGAT DPLGAAPAPA SVPAPTPSPA LAPTPTPAPV PAPAPAPFPT PPASLTLEEE
LQEAIRRAQL LPNRNIDDIL EDQVEPDDLL PPVPLDFPGS FDLLSPSPDS EGFSSVFSSS
LPSPTSSLSP SPRALTDSLD WLEALSGGPP LGSGPPGPSI FSADLSDPSG SLLWELLPDP
W
