ARP4_CANGA
ID ARP4_CANGA Reviewed; 493 AA.
AC Q6FJV8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Actin-related protein 4;
DE AltName: Full=Actin-like protein ARP4;
DE Short=Actin-like protein 4;
GN Name=ARP4; OrderedLocusNames=CAGL0M03201g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380959; CAG62462.1; -; Genomic_DNA.
DR RefSeq; XP_449486.1; XM_449486.1.
DR AlphaFoldDB; Q6FJV8; -.
DR SMR; Q6FJV8; -.
DR STRING; 5478.XP_449486.1; -.
DR EnsemblFungi; CAG62462; CAG62462; CAGL0M03201g.
DR GeneID; 2891494; -.
DR KEGG; cgr:CAGL0M03201g; -.
DR CGD; CAL0137375; CAGL0M03201g.
DR VEuPathDB; FungiDB:CAGL0M03201g; -.
DR eggNOG; KOG0679; Eukaryota.
DR HOGENOM; CLU_027965_6_2_1; -.
DR InParanoid; Q6FJV8; -.
DR OMA; CKETLCQ; -.
DR Proteomes; UP000002428; Chromosome M.
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; IPR020902; Actin/actin-like_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; PS01132; ACTINS_ACT_LIKE; 1.
PE 3: Inferred from homology;
KW Activator; Chromatin regulator; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..493
FT /note="Actin-related protein 4"
FT /id="PRO_0000089094"
FT REGION 333..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 55187 MW; 180CBA44ABA8B114 CRC64;
MSNSALQVYG GDEITAVIID PGSYTTNIGY AGTDCPQSIL PSSFGEIHEA EESTSEDNTE
KTRKTRKVFS EQSIPIPRPD YEVKRVVENG QVCDWDSAVE QWSWALRNEL HIESNRGIPA
MLTEPLWNSK ENRSKSLEIL LEGMEFEACY LTATSTAVSF ATGRPNSLIV DIGHDIASVT
PVIDGMSLSK STRCNHFAGR FLNKLLTDYL KPREIIPLFE VEQRKPEFKR RSFSYSVADS
LYDYANSRGF FQECKETIFQ VATTPIAQEK NNQATSTGRT IESPWNEVIE FESNDRYQFA
EQLINPLKES VPDDWPVNVA GVVETWRNDY VPMKRNKVGS GNNKEKEGTK ESTPLDSNTA
TPLPESSSTT NENGKRTAED IKREELPGIV DLISSSISSC DVDIRASLAH NLVITGGSST
IPGLSDRILN ELNMKFPALK FRVLATGQSI ERQYQSWLGG SILSSLGTFH QLWIGKKEYE
EVGSERLLHD RLR