ID   ARP8_SCHPO              Reviewed;         662 AA.
AC   Q9US07; Q9UU33;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable actin-related protein 8;
GN   ORFNames=SPAC664.02c;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 419-632, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [4]
RP   IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA   Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA   Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT   "Chromatin Central: towards the comparative proteome by accurate mapping of
RT   the yeast proteomic environment.";
RL   Genome Biol. 9:R167.1-R167.22(2008).
CC   -!- FUNCTION: Probably involved in transcription regulation via its
CC       interaction with the INO80 complex, a chromatin remodeling complex.
CC       Exhibits low basal ATPase activity, and unable to polymerize. Strongly
CC       prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting
CC       it may act as a nucleosome recognition module within the complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the chromatin remodeling Ino80 complex. Exists as
CC       monomers and dimers, but the dimer is most probably the biologically
CC       relevant form required for stable interactions with histones that
CC       exploits the twofold symmetry of the nucleosome core (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB65803.2; -; Genomic_DNA.
DR   EMBL; AB027842; BAA87146.1; -; Genomic_DNA.
DR   PIR; T50232; T50232.
DR   RefSeq; NP_593450.2; NM_001018883.2.
DR   AlphaFoldDB; Q9US07; -.
DR   SMR; Q9US07; -.
DR   BioGRID; 279979; 212.
DR   STRING; 4896.SPAC664.02c.1; -.
DR   iPTMnet; Q9US07; -.
DR   MaxQB; Q9US07; -.
DR   PaxDb; Q9US07; -.
DR   PRIDE; Q9US07; -.
DR   EnsemblFungi; SPAC664.02c.1; SPAC664.02c.1:pep; SPAC664.02c.
DR   GeneID; 2543563; -.
DR   KEGG; spo:SPAC664.02c; -.
DR   PomBase; SPAC664.02c; -.
DR   VEuPathDB; FungiDB:SPAC664.02c; -.
DR   eggNOG; KOG0797; Eukaryota.
DR   HOGENOM; CLU_006974_0_1_1; -.
DR   InParanoid; Q9US07; -.
DR   OMA; CFIQESL; -.
DR   PRO; PR:Q9US07; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0031011; C:Ino80 complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:PomBase.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:PomBase.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:PomBase.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR027668; Arp8/plant_Arp9.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   PANTHER; PTHR11937:SF13; PTHR11937:SF13; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..662
FT                   /note="Probable actin-related protein 8"
FT                   /id="PRO_0000089127"
FT   REGION          50..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         339..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        419..423
FT                   /note="NSFFS -> IASFR (in Ref. 3; BAA87146)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   662 AA;  75193 MW;  6F7D99B34459C324 CRC64;
     MAPKRKQPYT EEGIDFKFTQ FQIVPPINQK NFYTEYLKRD DQMYIWRDSA GEKDAKETES
     ESANGDTKQD DSKKSQVEEE EDGIEESELG EEKDNKTIVL HIGSQNLRIG LASNKTPTTV
     PMVIARKMRA PFAQERCLLK DICHVNEDGN VAFDSEFDSN LKLLDSELKS WLKAQKKRSV
     PNGTQLVKNY NKISKPETVP PDDDPEKPDW IHFEQDDHVD VICGKEAFLL PLNEYPEYKL
     FYPIKSGVFN ESDYASSQQL LADIYEIFKY SITSLLQIPV SQLSQYSVIF IVPDLYDRVY
     VEKILDILFF DLHFGKAAIV QESLCTSFGA GMSAACVVDM GAQKTSISCV EEGVVVPNSR
     IKINYGGDDI TLLFMKLLMR SHFPYQDIDL KTPYDWSLAN ALKIKYCGLS EATYNVQLNS
     FFSRTPDKGT RKFTFKSLDE TMLAPLGFFR PDIFENENKL HDRYTLFPVP VDVYDNQPNN
     PESLAQTTLL QISTPISNIK ANGKDDEEKK EESDLVTPSV KFKPPRVVYC GSLAAPEIKN
     EKLIYPLDDA INQSIFSACD GNLSDEKAKN LYSSILIVGG AGQFPGFAHL LEERIHSKRA
     NIPTISVIPP PRSMDAQFVA WKGACIYNRI RIVSELWIKN SDWKMLGSRV LQYKTLGYFW
     TG