ARP4_DEBHA
ID ARP4_DEBHA Reviewed; 492 AA.
AC Q6BXN0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Actin-related protein 4;
DE AltName: Full=Actin-like protein ARP4;
DE Short=Actin-like protein 4;
GN Name=ARP4; OrderedLocusNames=DEHA2B01694g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Chromatin interaction component of the NuA4 histone
CC acetyltransferase complex which is involved in transcriptional
CC activation of selected genes principally by acetylation of nucleosomal
CC histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Is
CC required for NuA4 complex integrity. Component of the SWR1 complex
CC which mediates the ATP-dependent exchange of histone H2A for the H2A
CC variant HZT1 leading to transcriptional regulation of selected genes by
CC chromatin remodeling. Component of the INO80 complex which remodels
CC chromatin by shifting nucleosomes and is involved in DNA repair (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex, of
CC the INO80 chromatin remodeling complex, and of the SWR1 chromatin
CC remodeling complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the actin family. ARP4 subfamily. {ECO:0000305}.
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DR EMBL; CR382134; CAG85025.1; -; Genomic_DNA.
DR RefSeq; XP_457039.1; XM_457039.1.
DR AlphaFoldDB; Q6BXN0; -.
DR SMR; Q6BXN0; -.
DR STRING; 4959.XP_457039.1; -.
DR EnsemblFungi; CAG85025; CAG85025; DEHA2B01694g.
DR GeneID; 2913692; -.
DR KEGG; dha:DEHA2B01694g; -.
DR VEuPathDB; FungiDB:DEHA2B01694g; -.
DR eggNOG; KOG0679; Eukaryota.
DR HOGENOM; CLU_027965_6_2_1; -.
DR InParanoid; Q6BXN0; -.
DR OMA; GIVEKRC; -.
DR OrthoDB; 649708at2759; -.
DR Proteomes; UP000000599; Chromosome B.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00432; ACTINS_2; 1.
PE 3: Inferred from homology;
KW Activator; Chromatin regulator; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..492
FT /note="Actin-related protein 4"
FT /id="PRO_0000089095"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 55665 MW; 8990981361A12478 CRC64;
MSSSGNNASV YGGDEINAIV LDSSSFHTRI GYAGDDFPKI ITPSSYASPN EDAMELDNKK
KNGKSKSSKI FGESINIPRS NHNVSPILKD SVIIDWEAAI EQYHYYFDDV LTLNYKEQPI
LITEPVWCTP QYRQTLLETF YENFDFPALF LAKSPTCISF QQGRPNCLVV DIGHDSVSVT
PVIDGISLLK NSMKTNYGGQ YLNDQIEDML THKFSGVNFE NRYRIKSKTP TVYPEESKYT
VRDLSENITQ SFDDYQRQNI WHEFKETMLE VPEKKFNTSN TSQANSLKEI YSQDSNKRLF
ELPTGQSLEL CLERFQLADS LFDPQSYKFN NPDLATKYPP SNGELSLTNS YDDYKPLKRA
RKAESNQSTP PPSDAKKPSS KTSQIRGLTH LITHTLSTID IDLRSSVAHN IIVTGGVSLI
PQLTERLYSE LSNSNPGLKI RLHAVGNSSE RFNQAWIGGS VLASLGTFHQ MWVSKQEYEE
AGAERILNQR FR
