ARP9_SCHPO
ID ARP9_SCHPO Reviewed; 523 AA.
AC Q9UTQ7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=SWI/SNF and RSC complexes subunit arp9;
DE AltName: Full=Actin-like protein arp9;
DE AltName: Full=Actin-related protein 9;
DE AltName: Full=Chromatin structure-remodeling complex subunit arp9;
GN Name=arp9; ORFNames=SPAC1071.06;
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 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 [3]
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; CAB59882.1; -; Genomic_DNA.
DR PIR; T37488; T37488.
DR RefSeq; NP_594356.1; NM_001019777.2.
DR AlphaFoldDB; Q9UTQ7; -.
DR BioGRID; 278040; 16.
DR ComplexPortal; CPX-6362; SWI/SNF chromatin remodelling complex.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-48381N; -.
DR IntAct; Q9UTQ7; 18.
DR STRING; 4896.SPAC1071.06.1; -.
DR MaxQB; Q9UTQ7; -.
DR PaxDb; Q9UTQ7; -.
DR EnsemblFungi; SPAC1071.06.1; SPAC1071.06.1:pep; SPAC1071.06.
DR GeneID; 2541540; -.
DR KEGG; spo:SPAC1071.06; -.
DR PomBase; SPAC1071.06; arp9.
DR VEuPathDB; FungiDB:SPAC1071.06; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_531127_0_0_1; -.
DR InParanoid; Q9UTQ7; -.
DR OMA; RYIFEKT; -.
DR PhylomeDB; Q9UTQ7; -.
DR PRO; PR:Q9UTQ7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; HDA: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:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IC:ComplexPortal.
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; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..523
FT /note="SWI/SNF and RSC complexes subunit arp9"
FT /id="PRO_0000310305"
FT REGION 56..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 59139 MW; D51F4D57B4228FF7 CRC64;
MPSFRDDHII VIQTGSLYHR ATFGLAESLE PPTIRVRTRV GKNDNGEYVF TNKEDINMED
PNVKTDETKV ETSESTSEQP SNSNVTEEKN MGSSFHSECK VDDFTPLPNE IQPIQRGRVV
DWEALKAFWK HLYSLLLKDP NDTTFRYPVC LVIPTYWSLY DRELATQFFF EECQVPGFTI
AYEPLMGLYA IGILHGLVID IGYEKTDITP ILDGQIIFTA TQQLPLGGRY MTQHLQNLLR
ESLPTLKSSG QYVSKEDITE LFAEQVKCSE IAQVVRDEQD TAKDPVKALT STNNVEEEDP
AEDIGKIIAS GQTRAYLAQK EREKNGESEK DEKPDNTDVE FQTIAIEPLG DCIVGRERFK
ICEPIFHRPS NETVSLPEAI YITIKNYAAN YKRRNDLWEN IIVLGCGSRI RGFRECLIQQ
LQFKYQLSGS LEPYYAAQGT DSILGMTTMP PTPYPALINP CKILPDYFPS WKPDAGTNAM
FEELAFLGGS IVAKTSFNES VSSHYVTLEE YAQHGPTAIH TKQ
