MRTFA_XENLA
ID MRTFA_XENLA Reviewed; 936 AA.
AC Q8AYC2;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Myocardin-related transcription factor A;
DE Short=MRTF-A;
DE AltName: Full=MKL/myocardin-like protein 1;
DE AltName: Full=Megakaryoblastic leukemia 1 protein;
GN Name=mrtfa; Synonyms=mkl1;
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 [MRNA].
RX PubMed=12397177; DOI=10.1073/pnas.222561499;
RA Wang D.-Z., Li S., Hockemeyer D., Sutherland L., Wang Z., Schratt G.,
RA Richardson J.A., Nordheim A., Olson E.N.;
RT "Potentiation of serum response factor activity by a family of myocardin-
RT related transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14855-14860(2002).
CC -!- FUNCTION: Transcription coactivator that associates with the serum
CC response factor (srf) transcription factor to control expression of
CC genes regulating the cytoskeleton during development, morphogenesis and
CC cell migration. The srf-mrtfa complex activity responds to Rho GTPase-
CC induced changes in cellular globular actin (G-actin) concentration,
CC thereby coupling cytoskeletal gene expression to cytoskeletal dynamics.
CC Mrtfa binds G-actin via its RPEL repeats, regulating activity of the
CC mrtfa-srf complex. Activity is also regulated by filamentous actin (F-
CC actin) in the nucleus. {ECO:0000250|UniProtKB:Q8K4J6}.
CC -!- SUBUNIT: Interacts with srf, forming the srf-mrtfa nuclear complex
CC which binds the 5'-CArG-3' consensus motif (CArG box) on DNA via srf.
CC Interacts (via RPEL repeats) with globular actin (G-actin), thereby
CC regulating its subcellular location and activity of the complex formed
CC with srf. {ECO:0000250|UniProtKB:Q8K4J6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K4J6}. Nucleus
CC {ECO:0000250|UniProtKB:Q8K4J6}. Note=Subcellular location is tightly
CC regulated by actin both in cytoplasm and nucleus: high levels of G-
CC actin in the nucleus observed during serum deprivation lead to low
CC levels of nuclear mrtfa, while reduced levels of nuclear G-actin result
CC in accumulation of mrtfa in the nucleus.
CC {ECO:0000250|UniProtKB:Q8K4J6}.
CC -!- DOMAIN: The N-terminal region is required for nuclear localization and
CC the C-terminal region mediates transcriptional activity.
CC {ECO:0000250|UniProtKB:Q8K4J6}.
CC -!- DOMAIN: The RPEL repeats mediate binding to globular actin (G-actin);
CC each RPEL repeat-binding to one G-actin monomer. In addition, each
CC intervening spacer sequence region can bind one G-actin monomer, to
CC reach a pentavalent complex. {ECO:0000250|UniProtKB:Q8K4J6}.
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DR EMBL; AF532599; AAN33043.1; -; mRNA.
DR AlphaFoldDB; Q8AYC2; -.
DR SMR; Q8AYC2; -.
DR PRIDE; Q8AYC2; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0010735; P:positive regulation of transcription via serum response element binding; ISS:UniProtKB.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR029992; MRTF-A.
DR InterPro; IPR043451; Myocardin-like.
DR InterPro; IPR004018; RPEL_repeat.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR22793; PTHR22793; 1.
DR PANTHER; PTHR22793:SF6; PTHR22793:SF6; 1.
DR Pfam; PF02755; RPEL; 3.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00707; RPEL; 3.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51073; RPEL; 3.
DR PROSITE; PS50800; SAP; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Coiled coil; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..936
FT /note="Myocardin-related transcription factor A"
FT /id="PRO_0000126627"
FT REPEAT 15..40
FT /note="RPEL 1"
FT REPEAT 59..84
FT /note="RPEL 2"
FT REPEAT 103..128
FT /note="RPEL 3"
FT DOMAIN 368..402
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 146..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 497..542
FT /evidence="ECO:0000255"
FT COMPBIAS 149..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..727
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 103238 MW; 51E9C6E2DC11E348 CRC64;
MTLLDTEQAL LAIHTVLQLK LQQRRTREEL ENQGIMPPLK SPAAFHEQRR SLERARTEDY
LKRKIRSRPE RAELVRMHIL EETSAEPSLQ AKQIKLKRAR LADDLNEKIS QRPGPMELVV
KNILPVETSL KEVIIDVDYP EVVDNSSFDE DSSDALSPEQ PASQESQGSI PSPIENRPSE
TTQIPALSPS HAFSCVQFGT DAFNQDSLQS TAITISNGLT ASICKSLPAL VKQSQPKPSF
EKSQRIKKPK EPKPKVKKLK YHQYIPPDQK QKGTPAMDSS YAKLLQQQQL FLQLQIINQQ
QHQHYNYQTI LPAPPKPLPD QQNTNSSSTT TVRSMSTVAP STLATPTITR QNSNVAVGGR
TGPLPHNLDE MKVAELKLEL KHRGLPVSGT KIDLIERLKA SQDPSTATAA SAKPTPVQQA
KPPEVVPIVS SSCLTTREPI KLCSTSSTPP GSPCPSEVSV VSMDEVSMIS DALGETVACP
VTQQVQQNPA AEKSPPDARD KDLMLREKDR QIEELTQRLK QKQELVERLR QQLEQEKRTP
QHSTDDQQAL ILAVKQEPLP LTVDSINKKA SSIVKQELNT AIICQQEPQL LIGPVSSGIE
GKVDNSAGTK LVFTLTNPSS QLPEENRQIV LQKVPTPPSS LHPNNSLPKQ EVLLSCCALQ
NQKPALQLVP GTVLSLSSSN LQPMLNMNGF QKWHGEALDS LQKQLVHNES PATPPQQPEP
EPPPHSIFLT HSSPQWSKNP PGYDEAMKQQ PNSCEDGRPG CLQAVDFFDV LIKNLDIPSE
FKDYLVPCLK QTSPSHQAAQ MVPQVEMAPP PSPIHSALGR LEDFLESSTG TPLLRGHQDG
PSSMPLIDDL HSQMLSSLAI LDHPPSPMDT SDLHFSPIGN SLGLDISEPP LDGMDWLELS
EPPAMNLTPL STFTPSVFST DFLDSHDLHL HWDSCL
