RSC9_SCHPO
ID RSC9_SCHPO Reviewed; 780 AA.
AC Q9P7W8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Chromatin structure-remodeling complex subunit rsc9;
DE AltName: Full=RSC complex subunit rsc9;
DE AltName: Full=Remodel the structure of chromatin complex subunit 9;
GN Name=rsc9; ORFNames=SPBC1703.02;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP IDENTIFICATION IN THE RSC COMPLEX, FUNCTION OF THE RSC COMPLEX, AND
RP 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. {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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-
CC ProRule:PRU00858, ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the RSC9 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB66446.1; -; Genomic_DNA.
DR PIR; T50315; T50315.
DR RefSeq; NP_596197.1; NM_001022116.2.
DR AlphaFoldDB; Q9P7W8; -.
DR BioGRID; 276492; 6.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-48390N; -.
DR IntAct; Q9P7W8; 6.
DR STRING; 4896.SPBC1703.02.1; -.
DR iPTMnet; Q9P7W8; -.
DR MaxQB; Q9P7W8; -.
DR PaxDb; Q9P7W8; -.
DR PRIDE; Q9P7W8; -.
DR EnsemblFungi; SPBC1703.02.1; SPBC1703.02.1:pep; SPBC1703.02.
DR GeneID; 2539948; -.
DR KEGG; spo:SPBC1703.02; -.
DR PomBase; SPBC1703.02; rsc9.
DR VEuPathDB; FungiDB:SPBC1703.02; -.
DR eggNOG; ENOG502QVTM; Eukaryota.
DR HOGENOM; CLU_008152_1_0_1; -.
DR InParanoid; Q9P7W8; -.
DR OMA; IRNMVML; -.
DR PhylomeDB; Q9P7W8; -.
DR PRO; PR:Q9P7W8; -.
DR Proteomes; UP000002485; Chromosome II.
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:0000976; F:transcription cis-regulatory region 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003150; DNA-bd_RFX.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; rRNA processing; Transcription;
KW Transcription regulation.
FT CHAIN 1..780
FT /note="Chromatin structure-remodeling complex subunit rsc9"
FT /id="PRO_0000318104"
FT DOMAIN 20..112
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DNA_BIND 530..609
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 780 AA; 87995 MW; 76416645839716BC CRC64;
MSQVIQGAVE EPVYSNKSLT NENDSFLSLI ESFSQERGVP IDINPKIGRK PILLYELYKK
VIKRGGYDAV SATEDGWTNI AEEFNQSDPA RSAGILQNVY FKYLISWEIH DHWHLLLPPP
STLELSENRQ NVLERVKVFN SCSPPKPTNP ITIIDNDKTH SFKKFYKSLV KEDEENGIEK
KINEAMNSSA SQPLPNSTNF ASTTFPSVPF HPLPVDSGLQ KYIDRNSNLT PPALGAGVPG
PPLLVRVALA LKSQQDKEVD WAIGHLIKIS FERHQEFKLE RLPSLAECLV YSLGFQVTKA
KQVSDLTDIS LCMDRAIGIA LVLRNSVLSV ENAKHVAQTK LVISVLEASI RCAKTFNNLE
FLHYCLDISE MISSYLHVED EKNVFYLALC EFLNSSDYSI LIATLRTLAR LALNDRNNRL
LQDLKSNVIA NIIALVETDN EEIVAAALDF LYQYTTYRTN TSNLLASQEA WMLVDQLIRL
MMYQAQERFM TVTIENSESN PAVKHEATSS ISLPMEELQQ LVAMREPERS VKWMRCCFEP
SSDDYVLQTD IWQLYCSDME RAQGPNVMGI SPADFIKVSS HAFYNARAMT VSTPQLPVEY
VINGIKRRKF PTSVNGMRYQ PCRWCLDSGK ECGELLLGTP LLHSHLQEMH IFPQILETGK
CRWSDCKYEI QRLTPASELS HYQLLSHIVT HLHDDSLETL VEGRKLSPSR EFRIPLLLTA
VDDQGDATGI ALTATLVLRN LVRSKQGKML FSAIESRVLE VSSLNPAVAP YVSEMLLGQI
