ARP5_SCHPO
ID ARP5_SCHPO Reviewed; 721 AA.
AC Q9Y7X8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Actin-like protein arp5;
GN Name=arp5; ORFNames=SPBC365.10;
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 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: Component of the INO80 complex which remodels chromatin by
CC shifting nucleosomes and is involved in DNA repair.
CC -!- SUBUNIT: Component of the INO80 chromatin remodeling complex.
CC {ECO:0000269|PubMed:19040720}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; CU329671; CAB44762.1; -; Genomic_DNA.
DR PIR; T40317; T40317.
DR RefSeq; NP_596039.1; NM_001021949.2.
DR AlphaFoldDB; Q9Y7X8; -.
DR BioGRID; 277546; 3.
DR STRING; 4896.SPBC365.10.1; -.
DR MaxQB; Q9Y7X8; -.
DR PaxDb; Q9Y7X8; -.
DR PRIDE; Q9Y7X8; -.
DR EnsemblFungi; SPBC365.10.1; SPBC365.10.1:pep; SPBC365.10.
DR GeneID; 2541031; -.
DR KEGG; spo:SPBC365.10; -.
DR PomBase; SPBC365.10; arp5.
DR VEuPathDB; FungiDB:SPBC365.10; -.
DR eggNOG; KOG0681; Eukaryota.
DR HOGENOM; CLU_008246_1_0_1; -.
DR InParanoid; Q9Y7X8; -.
DR OMA; TNWNHQE; -.
DR PhylomeDB; Q9Y7X8; -.
DR PRO; PR:Q9Y7X8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IDA:PomBase.
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; IPR027664; Arp5.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF16; PTHR11937:SF16; 1.
DR Pfam; PF00022; Actin; 2.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; DNA damage; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..721
FT /note="Actin-like protein arp5"
FT /id="PRO_0000310307"
FT REGION 486..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 266..368
FT /evidence="ECO:0000255"
FT COMPBIAS 493..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 82364 MW; B847A16E87A9A148 CRC64;
MKIYAVREPV FSGPTPSFQN VSNDIPLVID NGSWQLRAGW GGEKDPKLVF DNLVSRYRDR
KLSRTSTLVG NDTLIEVGSR SIARSPFERN VISNWDLMEQ VLDYTFLKLG IDRMEHPICM
TEPLANPTYV RSTMTELLFE LYNAPSVAYG IDGLFSFYHN TKPSSSGIVL NLGNAASHVI
PVLNGERILS EAKRISWGGS QSSSYLLKLF QIKYPSFPIK MLPSQAELLM HDHCHVSSDY
THDIAHALDR DILERDEIVL QFPYTEAAAQ EKSQEELELI AERKRESGRR LQAQAAIKRK
EKAAERDREL ATLTELQQQS LVLSRRAFQR ALEEAGFEDE SQLNAQVKNV QAKIRRAQRD
QQRQEESEGS LDVTEIDVEQ AFPLLNVPDA ELDEAGLRQK RHQRLMKANY DARVRAKAEK
AIEEAAEAER AEADERLRLE NFSTWVNEKR ETHKILLEKI SKNKRLKFEL NDRKSHASQM
RMKSLATLAS EQPIQKRKRK DQSEDNFGAR DEDWKVYHDV LTAEQLEEER KKLLDQIYSL
EKQLLEYDSQ FTQANTYDTL NDPRATLLYA FTRGVSDFDV NDVAQAFQLH LNVEQIRVPE
VIFSPSIVGI DQAGILEIMR SILQRHSLEE QQKLVSNVLI TGGLGSLPGM ETRIKRELTS
IMPVGSSINV FRASNPLLDA WKGASEWSVT EKFKAAKVTR EEYLEKGPEY IKEHSLGNIN
S