ID   ARP4_SCHPO              Reviewed;         433 AA.
AC   Q9P7X7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Actin-related protein 4;
DE   AltName: Full=Actin-like protein arp4;
DE            Short=Actin-like protein 4;
DE   AltName: Full=Altered polarity protein 5;
GN   Name=alp5; Synonyms=arp4; ORFNames=SPBP23A10.08;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; CU329671; CAB66436.1; -; Genomic_DNA.
DR   PIR; T50395; T50395.
DR   RefSeq; NP_595820.1; NM_001021724.2.
DR   AlphaFoldDB; Q9P7X7; -.
DR   SMR; Q9P7X7; -.
DR   BioGRID; 277830; 15.
DR   IntAct; Q9P7X7; 1.
DR   MINT; Q9P7X7; -.
DR   STRING; 4896.SPBP23A10.08.1; -.
DR   MaxQB; Q9P7X7; -.
DR   PaxDb; Q9P7X7; -.
DR   PRIDE; Q9P7X7; -.
DR   EnsemblFungi; SPBP23A10.08.1; SPBP23A10.08.1:pep; SPBP23A10.08.
DR   GeneID; 2541318; -.
DR   KEGG; spo:SPBP23A10.08; -.
DR   PomBase; SPBP23A10.08; alp5.
DR   VEuPathDB; FungiDB:SPBP23A10.08; -.
DR   eggNOG; KOG0679; Eukaryota.
DR   HOGENOM; CLU_027965_6_2_1; -.
DR   InParanoid; Q9P7X7; -.
DR   OMA; GIVEKRC; -.
DR   PhylomeDB; Q9P7X7; -.
DR   PRO; PR:Q9P7X7; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0043189; C:H4/H2A histone acetyltransferase complex; IDA:PomBase.
DR   GO; GO:0031011; C:Ino80 complex; IDA:PomBase.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0000812; C:Swr1 complex; IDA:PomBase.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:PomBase.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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..433
FT                   /note="Actin-related protein 4"
FT                   /id="PRO_0000089100"
FT   REGION          289..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  48773 MW;  976A7E47819E91D2 CRC64;
     MTSAFYGGDE VSAIVIDPGS KWTRIGFSGE DIPKCVLPSY CGEFSDGRRL FGEEYIYKSN
     PGMEIKNAIR NGWVENWDVT VDLWRYGLEQ QLKTNPLEHP ILITEPFDNP PENRVKTLET
     MFESLRCPAT YLAKQETCAA FASGKGTACL VDIGAERSSV SAIYDGFVLQ KGYQVQHFSG
     NAINDILAQT LRDKNFEVMP KYLVKSKNPV EIGQPANCEL RPRDTTDSYH QFQVQRVYDE
     WKEECALISD VPFSSETTIA ESEFEFPDGS RMMFGAERYQ IPEHLFVPGS DEEMNEEPSK
     PIEQTENNEV SQQDSSVTNT SSRILGIPQL FQNCISECDV DIRASLLNNV IVCGGTSLMQ
     GFSLRLQNEL SKLYPGSRLK IHASGHVVER SYASWLGGSI LSSLGTFHQL WISRQEYEEH
     GSDRLALIEK RCK