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Protein

Myocardin-related transcription factor A

Gene

Mrtfa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Transcription coactivator that associates with the serum response factor (SRF) transcription factor to control expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration (PubMed:12019265, PubMed:12732141, PubMed:17588931, PubMed:19350017, PubMed:24732378). The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics (PubMed:24732378). MRTFA binds G-actin via its RPEL repeats, regulating activity of the MRTFA-SRF complex (PubMed:12732141, PubMed:17588931). Activity is also regulated by filamentous actin (F-actin) in the nucleus (PubMed:23558171, PubMed:25759381).7 Publications

Caution

Some publications use a protein sequence that is longer at the N-terminus and is based on an artificial construct (PubMed:12732141, PubMed:27304076). The sequence used in these publications modifies a non-canonical CTG leucine codon upstream of the initiator codon into ATG, generating a protein of 1021 residues (PubMed:12732141, PubMed:27304076). The existence of this form has not been confirmed in vivo and is therefore unsure (PubMed:12732141, PubMed:27304076). Similarly, the existence of the S33 ('Ser-33') phosphorylation site described in Panayiotou et al. is unsure (PubMed:27304076).2 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-3899300 SUMOylation of transcription cofactors
R-MMU-5663220 RHO GTPases Activate Formins

Names & Taxonomyi

Protein namesi
Recommended name:
Myocardin-related transcription factor ACurated
Short name:
MRTF-A1 Publication
Alternative name(s):
Basic SAP coiled-coil transcription activator1 Publication
MKL/myocardin-like protein 1
Megakaryoblastic leukemia 1 protein homolog
Megakaryocytic acute leukemia protein homolog2 Publications
Gene namesi
Name:Mrtfa
Synonyms:Bsac1 Publication, Mal2 Publications, Mkl1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2384495 Mkl1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24R → A in 123-1A: Reduced interaction with G-actin, leading to a constitutively active SRF-MRTFA complex; when associated with A-68 and A-112. 1 Publication1
Mutagenesisi45F → A or D: Induces a nuclear accumulation in unstimulated cells. 1 Publication1
Mutagenesisi48Q → A or D: Induces a nuclear accumulation in unstimulated cells. 1 Publication1
Mutagenesisi52L → A or D: Induces a nuclear accumulation in unstimulated cells. 1 Publication1
Mutagenesisi54R → A: Impaired interaction with G-actin, leading to nuclear accumulation in unstimulated cells. 1 Publication1
Mutagenesisi56R → A: Impaired interaction with G-actin, leading to nuclear accumulation in unstimulated cells. 1 Publication1
Mutagenesisi68R → A in 123-1A: Reduced interaction with G-actin, leading to a constitutively active SRF-MRTFA complex; when associated with A-24 and A-112. 1 Publication1
Mutagenesisi89L → A or D: Does not induce a nuclear accumulation in unstimulated cells. 1 Publication1
Mutagenesisi92K → A or D: Does not induce a nuclear accumulation in unstimulated cells. 1 Publication1
Mutagenesisi96L → A: Induces a nuclear accumulation in unstimulated cells. 1 Publication1
Mutagenesisi96L → D: Induces a nuclear decrease in unstimulated cells. 1 Publication1
Mutagenesisi98R → A: Impaired interaction with G-actin, leading to cytoplasmic accumulation. 1 Publication1
Mutagenesisi100R → A: Impaired interaction with G-actin, leading to cytoplasmic accumulation. 1 Publication1
Mutagenesisi112R → A in 123-1A: Reduced interaction with G-actin, leading to a constitutively active SRF-MRTFA complex; when associated with A-24 and A-68. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001266261 – 964Myocardin-related transcription factor AAdd BLAST964

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei41Phosphoserine1 Publication1
Modified residuei159Phosphoserine1 Publication1
Modified residuei174Phosphoserine1 Publication1
Modified residuei191Phosphoserine1 Publication1
Modified residuei349Phosphoserine1 Publication1
Modified residuei351Phosphoserine1 Publication1
Modified residuei352Phosphothreonine1 Publication1
Modified residuei355Phosphoserine1 Publication1
Modified residuei358Phosphoserine1 Publication1
Modified residuei360Phosphothreonine1 Publication1
Modified residuei371PhosphoserineBy similarity1
Modified residuei423Phosphoserine1 Publication1
Modified residuei484Phosphoserine1 Publication1
Modified residuei485Phosphothreonine1 Publication1
Modified residuei487Phosphoserine1 Publication1
Modified residuei488Phosphothreonine1 Publication1
Modified residuei492Phosphoserine1 Publication1
Modified residuei494Phosphothreonine1 Publication1
Modified residuei496Phosphoserine1 Publication1
Modified residuei520Phosphoserine1 Publication1
Modified residuei530Phosphoserine1 Publication1
Modified residuei544Phosphoserine1 Publication1
Modified residuei548Phosphoserine1 Publication1
Modified residuei605Phosphoserine1 Publication1
Modified residuei606Phosphoserine1 Publication1
Modified residuei651Phosphoserine1 Publication1
Modified residuei687Phosphoserine1 Publication1
Modified residuei718Phosphoserine1 Publication1
Modified residuei724Phosphoserine1 Publication1
Modified residuei728Phosphoserine1 Publication1
Modified residuei810Phosphoserine1 Publication1
Modified residuei822Phosphothreonine1 Publication1
Modified residuei826Phosphoserine1 Publication1
Modified residuei840Phosphoserine1 Publication1
Modified residuei842Phosphothreonine1 Publication1
Modified residuei892Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylation at Ser-41 by Erk inhibits binding of globular actin (G-actin), unmasking the nuclear localization signal (NLS) and promoting nuclear import.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8K4J6
PaxDbiQ8K4J6
PRIDEiQ8K4J6

PTM databases

iPTMnetiQ8K4J6
PhosphoSitePlusiQ8K4J6

Expressioni

Tissue specificityi

Expressed in heart, brain, spleen, lung, liver, muscle, kidney and testis.1 Publication

Developmental stagei

Detected throughout the embryo at 10.5 dpc; higher expression is found at 13.5 dpc in neural mesenchymal cells, skeletal muscle of the tongue, and epithelial cells of the colon and small intestine; at 15.5 dpc, expression in epithelial cells of lung, kidney, bladder, and colon is also detected.1 Publication

Gene expression databases

BgeeiENSMUSG00000042292 Expressed in 277 organ(s), highest expression level in dentate gyrus granule cell layer
CleanExiMM_MKL1
ExpressionAtlasiQ8K4J6 baseline and differential
GenevisibleiQ8K4J6 MM

Interactioni

Subunit structurei

Interacts with SRF, forming the SRF-MRTFA nuclear complex which binds the 5'-CArG-3' consensus motif (CArG box) on DNA via SRF (PubMed:12732141, PubMed:19350017). Interacts (via RPEL repeats) with globular actin (G-actin), thereby regulating its subcellular location and activity of the complex formed with SRF (PubMed:12732141, PubMed:17588931, PubMed:19350017, PubMed:19008859, PubMed:27304076, PubMed:21673315). Either forms a trivalent (by binding three G-actin monomers) or pentavalent (by binding five G-actin monomers) complex with G-actin (PubMed:21673315). Forms a nuclear ternary complex with SCAI and SRF, leading to suppress MRTFA-induced SRF transcriptional activity (PubMed:19350017). Interacts with beta-actin (ACTB); interaction with ACTB prevents interaction with SCAI (PubMed:19350017). Interacts with MRTFB (By similarity).By similarity6 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi230180, 2 interactors
DIPiDIP-60884N
ELMiQ8K4J6
IntActiQ8K4J6, 6 interactors
MINTiQ8K4J6
STRINGi10090.ENSMUSP00000105207

Structurei

Secondary structure

1964
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ8K4J6
SMRiQ8K4J6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8K4J6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati15 – 40RPEL 1Add BLAST26
Repeati59 – 84RPEL 2Add BLAST26
Repeati103 – 128RPEL 3Add BLAST26
Domaini385 – 419SAPPROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 291Mediates interaction with SCAI and ACTB1 PublicationAdd BLAST291
Regioni41 – 58Intervening spacer sequence 11 PublicationAdd BLAST18
Regioni85 – 102Intervening spacer sequence 21 PublicationAdd BLAST18

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili552 – 600Sequence analysisAdd BLAST49

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi299 – 325Gln-richAdd BLAST27
Compositional biasi712 – 844Pro-richAdd BLAST133

Domaini

The N-terminal region is required for nuclear localization and the C-terminal region mediates transcriptional activity.1 Publication
The RPEL repeats mediate binding to globular actin (G-actin); each RPEL repeat-binding to one G-actin monomer (PubMed:19008859, PubMed:21673315). In addition, each intervening spacer sequence region can bind one G-actin monomer, to reach a pentavalent complex (PubMed:21673315).2 Publications

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IFJX Eukaryota
ENOG41101AM LUCA
GeneTreeiENSGT00530000063195
HOGENOMiHOG000038001
HOVERGENiHBG036493
InParanoidiQ8K4J6
KOiK22525
OMAiSELHFAH
OrthoDBiEOG091G01ZY
PhylomeDBiQ8K4J6
TreeFamiTF326024

Family and domain databases

Gene3Di1.10.720.30, 1 hit
InterProiView protein in InterPro
IPR029992 MRTF-A
IPR004018 RPEL_repeat
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
PANTHERiPTHR22793:SF6 PTHR22793:SF6, 2 hits
PfamiView protein in Pfam
PF02755 RPEL, 3 hits
PF02037 SAP, 1 hit
SMARTiView protein in SMART
SM00707 RPEL, 3 hits
SM00513 SAP, 1 hit
SUPFAMiSSF68906 SSF68906, 1 hit
PROSITEiView protein in PROSITE
PS51073 RPEL, 3 hits
PS50800 SAP, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8K4J6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MTLLEPEMLM MAVQSVLQLK LQQRRTREEL VSQGIMPPLK SPAAFHEQRR
60 70 80 90 100
SLERARTEDY LKRKIRSRPE RAELVRMHIL EETSAEPSLQ AKQLKLKRAR
110 120 130 140 150
LADDLNEKIA QRPGPMELVE KNILPVESSL KEAIIVGQVN YPKVADSSSF
160 170 180 190 200
DEDSSDALSP EQPASHESQG SVPSPLESRV SDPLPSATSI SPTQVLSQLP
210 220 230 240 250
MAPDPGETLF LAEQPPLPPA PLLPPSLANG SIVPTAKPAP TLIKQSQPKS
260 270 280 290 300
ASEKSQRSKK AKELKPKVKK LKYHQYIPPD QKQDKGAPAM DSSYAKILQQ
310 320 330 340 350
QQLFLQLQIL NQQQQQQQQQ HYNYQAILPA PPKPSAETPG SSAPTPSRSL
360 370 380 390 400
STSSSPSSGT PGPSGLARQS STALAAKPGA LPANLDDMKV AELKQELKLR
410 420 430 440 450
SLPVSGTKTE LIERLRAYQD QVSPAPGAPK APATTSVLSK AGEVVVAFPA
460 470 480 490 500
ALLSTGSALV TAGLAPAEMV VATVTSNGMV KFGSTGSTPP VSPTPSERSL
510 520 530 540 550
LSTGDENSTP GDAFGEMVTS PLTQLTLQAS PLQIVKEEGA RAASCCLSPG
560 570 580 590 600
ARAELEGLDK DQMLQEKDKQ IEELTRMLQQ KQQLVELLRL QLEQQKRAQQ
610 620 630 640 650
PAPASSPVKR ESGFSSCQLS CQPQGSAHAF GSGLVVPTTN HGDTQAPAPE
660 670 680 690 700
SPPVVVKQEA GPPEPDLAPS SQLLLGSQGT SFLKRVSPPT LVTDSTGTHL
710 720 730 740 750
ILTVTNKSAD GPGLPAGSPQ QPLSQPGSPA PGPPAQMDLE HPPQPPFATP
760 770 780 790 800
TSLLKKEPPG YEETVTQQPK QQENGSSSQH MDDLFDILIQ SGEISADFKE
810 820 830 840 850
PPSLPGKEKS PPAAAAYGPP LTPQPSPLSE LPQAAPPPGS PTLPGRLEDF
860 870 880 890 900
LESSTGLPLL TSGHEGPEPL SLIDDLHSQM LSSSAILDHP PSPMDTSELH
910 920 930 940 950
FAPEPSSGMG LDLAVGHLDS MDWLELSSGG PVLSLAPLST AAPSLFSMDF
960
LDGHDLQLHW DSCL
Length:964
Mass (Da):102,546
Last modified:June 27, 2003 - v2
Checksum:iAFAEA328A1860CE5
GO
Isoform 2 (identifier: Q8K4J6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Show »
Length:929
Mass (Da):98,463
Checksum:iB13D0985013B6E49
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3YUG5D3YUG5_MOUSE
MKL (megakaryoblastic leukemia)/myo...
Mkl1
705Annotation score:
D3YUI2D3YUI2_MOUSE
MKL (megakaryoblastic leukemia)/myo...
Mkl1
879Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53E → Q in BAC31809 (PubMed:16141072).Curated1
Sequence conflicti724S → D in BAC40873 (PubMed:16141072).Curated1
Sequence conflicti728S → F in AAM94258 (PubMed:12019265).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0076521 – 35Missing in isoform 2. 3 PublicationsAdd BLAST35

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF385582 mRNA Translation: AAM94258.1
AF532597 mRNA Translation: AAN33041.1
AK044188 mRNA Translation: BAC31809.1
AK089416 mRNA Translation: BAC40873.1
BC050941 mRNA Translation: AAH50941.1
CCDSiCCDS37147.1 [Q8K4J6-1]
CCDS49674.1 [Q8K4J6-2]
RefSeqiNP_001076005.1, NM_001082536.1 [Q8K4J6-2]
NP_694629.2, NM_153049.3 [Q8K4J6-1]
UniGeneiMm.439814

Genome annotation databases

EnsembliENSMUST00000109579; ENSMUSP00000105207; ENSMUSG00000042292 [Q8K4J6-1]
ENSMUST00000134469; ENSMUSP00000119530; ENSMUSG00000042292 [Q8K4J6-2]
ENSMUST00000149582; ENSMUSP00000117745; ENSMUSG00000042292 [Q8K4J6-2]
GeneIDi223701
KEGGimmu:223701
UCSCiuc007wwc.2 mouse [Q8K4J6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF385582 mRNA Translation: AAM94258.1
AF532597 mRNA Translation: AAN33041.1
AK044188 mRNA Translation: BAC31809.1
AK089416 mRNA Translation: BAC40873.1
BC050941 mRNA Translation: AAH50941.1
CCDSiCCDS37147.1 [Q8K4J6-1]
CCDS49674.1 [Q8K4J6-2]
RefSeqiNP_001076005.1, NM_001082536.1 [Q8K4J6-2]
NP_694629.2, NM_153049.3 [Q8K4J6-1]
UniGeneiMm.439814

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V51X-ray2.35E/F16-41[»]
2V52X-ray1.45M54-85[»]
2YJEX-ray3.10M16-142[»]
2YJFX-ray3.50M16-142[»]
ProteinModelPortaliQ8K4J6
SMRiQ8K4J6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230180, 2 interactors
DIPiDIP-60884N
ELMiQ8K4J6
IntActiQ8K4J6, 6 interactors
MINTiQ8K4J6
STRINGi10090.ENSMUSP00000105207

PTM databases

iPTMnetiQ8K4J6
PhosphoSitePlusiQ8K4J6

Proteomic databases

EPDiQ8K4J6
PaxDbiQ8K4J6
PRIDEiQ8K4J6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000109579; ENSMUSP00000105207; ENSMUSG00000042292 [Q8K4J6-1]
ENSMUST00000134469; ENSMUSP00000119530; ENSMUSG00000042292 [Q8K4J6-2]
ENSMUST00000149582; ENSMUSP00000117745; ENSMUSG00000042292 [Q8K4J6-2]
GeneIDi223701
KEGGimmu:223701
UCSCiuc007wwc.2 mouse [Q8K4J6-1]

Organism-specific databases

CTDi223701
MGIiMGI:2384495 Mkl1

Phylogenomic databases

eggNOGiENOG410IFJX Eukaryota
ENOG41101AM LUCA
GeneTreeiENSGT00530000063195
HOGENOMiHOG000038001
HOVERGENiHBG036493
InParanoidiQ8K4J6
KOiK22525
OMAiSELHFAH
OrthoDBiEOG091G01ZY
PhylomeDBiQ8K4J6
TreeFamiTF326024

Enzyme and pathway databases

ReactomeiR-MMU-3899300 SUMOylation of transcription cofactors
R-MMU-5663220 RHO GTPases Activate Formins

Miscellaneous databases

ChiTaRSiMkl1 mouse
EvolutionaryTraceiQ8K4J6
PROiPR:Q8K4J6
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000042292 Expressed in 277 organ(s), highest expression level in dentate gyrus granule cell layer
CleanExiMM_MKL1
ExpressionAtlasiQ8K4J6 baseline and differential
GenevisibleiQ8K4J6 MM

Family and domain databases

Gene3Di1.10.720.30, 1 hit
InterProiView protein in InterPro
IPR029992 MRTF-A
IPR004018 RPEL_repeat
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
PANTHERiPTHR22793:SF6 PTHR22793:SF6, 2 hits
PfamiView protein in Pfam
PF02755 RPEL, 3 hits
PF02037 SAP, 1 hit
SMARTiView protein in SMART
SM00707 RPEL, 3 hits
SM00513 SAP, 1 hit
SUPFAMiSSF68906 SSF68906, 1 hit
PROSITEiView protein in PROSITE
PS51073 RPEL, 3 hits
PS50800 SAP, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMRTFA_MOUSE
AccessioniPrimary (citable) accession number: Q8K4J6
Secondary accession number(s): Q642U1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 27, 2003
Last modified: November 7, 2018
This is version 148 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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