ID   ARP42_SCHPO             Reviewed;         424 AA.
AC   Q09849;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=SWI/SNF and RSC complexes subunit arp42;
DE   AltName: Full=Actin-related protein 42;
DE   AltName: Full=Chromatin structure-remodeling complex subunit arp42;
GN   Name=arp42; Synonyms=arp4; ORFNames=SPAC23D3.09;
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).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   IDENTIFICATION IN THE SWI/SNF AND RSC COMPLEXES, FUNCTION OF THE SWI/SNF
RP   AND RSC COMPLEXES, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18622392; DOI=10.1038/nsmb.1452;
RA   Monahan B.J., Villen J., Marguerat S., Baehler J., Gygi S.P., Winston F.;
RT   "Fission yeast SWI/SNF and RSC complexes show compositional and functional
RT   differences from budding yeast.";
RL   Nat. Struct. Mol. Biol. 15:873-880(2008).
CC   -!- FUNCTION: Component of the chromatin structure remodeling complex
CC       (RSC), which is involved in transcription regulation and nucleosome
CC       positioning. Controls particularly membrane and organelle development
CC       genes. Part of the SWI/SNF complex, an ATP-dependent chromatin
CC       remodeling complex, required for the positive and negative regulation
CC       of gene expression of a large number of genes. It changes chromatin
CC       structure by altering DNA-histone contacts within a nucleosome, leading
CC       eventually to a change in nucleosome position, thus facilitating or
CC       repressing binding of gene-specific transcription factors.
CC       {ECO:0000269|PubMed:18622392}.
CC   -!- SUBUNIT: Component of the RSC complex composed of at least arp9, arp42,
CC       rsc1, rsc4, rsc7, rsc9, rsc58, sfh1, snf21, ssr1, ssr2, ssr3 and ssr4.
CC       The complex interacts with histone and histone variant components of
CC       centromeric chromatin (By similarity). Component of the SWI/SNF global
CC       transcription activator complex composed of at least arp9, arp42, snf5,
CC       snf22, snf30, sbf59, sol1, ssr1, ssr2, ssr3, ssr4 and tfg3.
CC       {ECO:0000250, ECO:0000269|PubMed:18622392}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA91244.2; -; Genomic_DNA.
DR   PIR; S62500; S62500.
DR   RefSeq; NP_594546.2; NM_001019975.2.
DR   AlphaFoldDB; Q09849; -.
DR   SMR; Q09849; -.
DR   BioGRID; 277998; 438.
DR   ComplexPortal; CPX-6362; SWI/SNF chromatin remodelling complex.
DR   ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR   DIP; DIP-48384N; -.
DR   IntAct; Q09849; 18.
DR   STRING; 4896.SPAC23D3.09.1; -.
DR   MaxQB; Q09849; -.
DR   PaxDb; Q09849; -.
DR   PRIDE; Q09849; -.
DR   EnsemblFungi; SPAC23D3.09.1; SPAC23D3.09.1:pep; SPAC23D3.09.
DR   GeneID; 2541496; -.
DR   KEGG; spo:SPAC23D3.09; -.
DR   PomBase; SPAC23D3.09; arp42.
DR   VEuPathDB; FungiDB:SPAC23D3.09; -.
DR   eggNOG; KOG0679; Eukaryota.
DR   HOGENOM; CLU_027965_6_2_1; -.
DR   InParanoid; Q09849; -.
DR   OMA; MWLSRQE; -.
DR   PRO; PR:Q09849; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0031011; C:Ino80 complex; ISO:PomBase.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0016586; C:RSC-type complex; IDA:PomBase.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:PomBase.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IC:ComplexPortal.
DR   GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
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   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..424
FT                   /note="SWI/SNF and RSC complexes subunit arp42"
FT                   /id="PRO_0000089146"
SQ   SEQUENCE   424 AA;  47100 MW;  97F0C4B746A10748 CRC64;
     MEEIPSLVID PGSCWTRFGY AGEESPMTIL PSYYGVRSDV TGRNKYVVDE LQIHAPIPGM
     EVKNGKSNGI IQDWESTLYT WERGLKEKLQ VNPTEYAMMI TEPSWNPQSV RQQIMEAAFE
     QLHVPAFYLT KQAVCVAFAN SKSTALIVDI GSDNASVTPV VDGLIIRKGI FKQSLAGDFL
     NANIEQLFNT MNIEFPPHYR IARKSVAIQQ SGNMANGSAD AVKPAVLYPP IQDLTSSYEI
     FQKRRVIEEW KESVLDVLDT PFDEAKASSR NPKPFEFPDG VTHKFGQERF RISEILFNPS
     FSASRSAETT PPQGSVGLHE LVYQSILACD SELRSPLLNN IVVTGGTSLI PGLSERLQAE
     VQRLATGSRI NVHTAETASA TSNAVWFGGS ILASLDNFQH LWVSKQEYDE VGVDRALFVE
     KRCK