ID   ARP4_KLULA              Reviewed;         520 AA.
AC   Q6CSB9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Actin-related protein 4;
DE   AltName: Full=Actin-like protein ARP4;
DE            Short=Actin-like protein 4;
GN   Name=ARP4; OrderedLocusNames=KLLA0D02288g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382124; CAH00266.1; -; Genomic_DNA.
DR   RefSeq; XP_453170.1; XM_453170.1.
DR   AlphaFoldDB; Q6CSB9; -.
DR   SMR; Q6CSB9; -.
DR   STRING; 28985.XP_453170.1; -.
DR   EnsemblFungi; CAH00266; CAH00266; KLLA0_D02288g.
DR   GeneID; 2892798; -.
DR   KEGG; kla:KLLA0_D02288g; -.
DR   eggNOG; KOG0679; Eukaryota.
DR   HOGENOM; CLU_027965_6_2_1; -.
DR   InParanoid; Q6CSB9; -.
DR   OMA; CKETLCQ; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0031011; C:Ino80 complex; IEA:EnsemblFungi.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0000812; C:Swr1 complex; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0051382; P:kinetochore assembly; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 2.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; DNA damage; DNA repair; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..520
FT                   /note="Actin-related protein 4"
FT                   /id="PRO_0000089098"
FT   REGION          320..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  57976 MW;  F07C5E5E76BF45EA CRC64;
     MSNPALQVYG GDEINAIVID PGSFVTNIGY SGTDCPQSIM PSSYGNVETD GDTKRIFNEQ
     PLLFPRAGME IKPIVENSTI VDWDRAQEQW EYALNTDLKF ESNKGTPVLL TEPIWNSEAS
     RKKSLEILLE SMEFEACYLA ANSSAVSFAM GRPTCLVVDI GHDVSTVSPV IDGMTLSKSS
     TRNYVAGKYL NHLIAKNLKP REIVPIFQVL KKKPDFVKRT LSFDVNESVI NFANERQFFQ
     EFKETLLHIA PKSLSSFKDE LATQTKRSLE APWGEELIFD ADTRYSFAEQ LFRPVKEDFP
     EGWPASTDGI VKTWHNDYVP LKRTKPGTST NTKEKENTAE STPVPASTEQ EAVDSPSQEP
     NENGKRPVEN KEDSSNNEQN SNEIKNEDAN SNESSAKATV PSNGIQAKGE DEVAGIVDLI
     NKSMMEADVD LRATLAHNVV LTGGTSKIPG LSDRIMHELN KSLPALKFRM LSSGHLRERQ
     YQGWLGGSIL ASLGTFHQLW VGREEYEEVG PERLLKDRFR