Q9Z2N8 (ACL6A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin-like protein 6A

Alternative name(s):
53 kDa BRG1-associated factor A
Actin-related protein Baf53a
BRG1-associated factor 53A
Short name=BAF53A

Gene names

Name:	Actl6a
Synonyms:	Actl6, Baf53a

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene By similarity. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair By similarity. Ref.4
Subunit structure	Component of numerous complexes with chromatin remodeling and histone acetyltransferase activity. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of the BAF53 complex, at least composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM/BAF190B, and TRRAP/PAF400, and which may also include a HAT activity related to, but distinct from, that of KAT5. ACTL6A interacts with SMARCA4/BRG1/BAF190A. Component of the chromatin-remodeling INO80 complex; specifically part of a complex module associated with the DBINO domain of INO80. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B By similarity. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Interacts with PHF10/BAF45A. Ref.4
Subcellular location	Nucleus By similarity.
Tissue specificity	Widely expressed. Expressed selectively in neural stem and progenitor cells (at protein level). Ref.4
Developmental stage	Expressed predominantly in E10.5-E11.5 neural cells. In the developing spinal cord (E10.5-E16.5), is specifically expressed in proliferating neural progenitors of the ventricular zone. In the developing forebrain and cerebellar primordium, expression is restricted to proliferating neuroepithelial progenitors and cerebellar granule precursors. Ref.4
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Growth regulation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Activator Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin remodeling Inferred from direct assay Ref.1. Source: MGI histone H2A acetylation Inferred from sequence or structural similarity. Source: UniProtKB histone H4 acetylation Inferred from sequence or structural similarity. Source: UniProtKB nervous system development Inferred from mutant phenotype Ref.4. Source: UniProtKB neural retina development Inferred from electronic annotation. Source: Compara regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Ino80 complex Inferred from electronic annotation. Source: Compara NuA4 histone acetyltransferase complex Inferred from sequence or structural similarity. Source: UniProtKB SWI/SNF complex Inferred from electronic annotation. Source: Compara npBAF complex Inferred from direct assay Ref.4. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro chromatin binding Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 429	428	Actin-like protein 6A		PRO_0000089134
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	233	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	38	1	P → H in BAC41116. Ref.2
	Sequence conflict	153	1	K → Q in BAC41116. Ref.2
	Sequence conflict	322	1	M → I in AAC94992. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9Z2N8 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: F3FF706C69808B13	FASTA	429	47,448
	10 20 30 40 50 60 MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGVVLERDDG STMMEIDGDK 70 80 90 100 110 120 GKQGGPTYYI DTNALRVPRE NMEAISPLKN GMVEDWDSFQ AILDHTYKMH VKSEASLHPV 130 140 150 160 170 180 LMSEAPWNTR AKREKLTELM FEHYSIPAFF LCKTAVLTAF ANGRSTGLIL DSGATHTTAI 190 200 210 220 230 240 PVHDGYVLQQ GIVKSPLAGD FITMQCRELF QEMNIELIPP YMIASKEAVR EGSPANWKRK 250 260 270 280 290 300 EKLPQVTRSW HNYMCNCVIQ DFQASVLQVS DSTYDEQVAA QMPTVHYEFP NGYNCDFGAE 310 320 330 340 350 360 RLKIPEGLFD PSNVKGLSGN TMLGVSHVVT TSVGMCDIDI RPGLYGSVIV AGGNTLIQSF 370 380 390 400 410 420 TDRLNRELSQ KTPPSMRLKL IANNTTVERR FSSWIGGSIL ASLGTFQQMW ISKQEYEEGG KQCVERKCP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling." Zhao K., Wang W., Rando O.J., Xue Y., Swiderek K., Kuo A., Crabtree G.R. Cell 95:625-636(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryonic brain.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
[4]	"An essential switch in subunit composition of a chromatin remodeling complex during neural development." Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H., Aebersold R., Graef I.A., Crabtree G.R. Neuron 55:201-215(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NPBAF COMPLEX, INTERACTION WITH PHF10, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF041476 mRNA. Translation: AAC94992.1. AK090154 mRNA. Translation: BAC41116.1. BC001994 mRNA. Translation: AAH01994.1.
IPI	IPI00323660.
RefSeq	NP_062647.2. NM_019673.2.
UniGene	Mm.41077.
3D structure databases
ProteinModelPortal	Q9Z2N8.
SMR	Q9Z2N8. Positions 8-428.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z2N8. 7 interactions.
STRING	10090.ENSMUSP00000029214.
PTM databases
PhosphoSite	Q9Z2N8.
2D gel databases
REPRODUCTION-2DPAGE	Q9Z2N8.
Proteomic databases
PaxDb	Q9Z2N8.
PRIDE	Q9Z2N8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029214; ENSMUSP00000029214; ENSMUSG00000027671.
GeneID	56456.
KEGG	mmu:56456.
Organism-specific databases
CTD	86.
MGI	MGI:1861453. Actl6a.
Phylogenomic databases
eggNOG	COG5277.
GeneTree	ENSGT00660000095557.
HOGENOM	HOG000233340.
HOVERGEN	HBG003771.
InParanoid	Q9Z2N8.
KO	K11340.
OMA	DFGSERF.
OrthoDB	EOG4XKV6Z.
Gene expression databases
ArrayExpress	Q9Z2N8.
Bgee	Q9Z2N8.
CleanEx	MM_ACTL6A.
Genevestigator	Q9Z2N8.
GermOnline	ENSMUSG00000027671. Mus musculus.
Family and domain databases
InterPro	IPR004000. Actin-related. IPR004001. Actin_CS. [Graphical view]
PANTHER	PTHR11937. PTHR11937. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
PRINTS	PR00190. ACTIN.
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS00406. ACTINS_1. False negative. PS00432. ACTINS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	312690.
SOURCE	Search...

Entry information

Entry name

ACL6A_MOUSE

Accession

Primary (citable) accession number: Q9Z2N8
Secondary accession number(s): Q8C1W3, Q99M56

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	September 19, 2002
Last modified:	April 3, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program