RSC7_SCHPO
ID RSC7_SCHPO Reviewed; 390 AA.
AC O94522;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Chromatin structure-remodeling complex subunit rsc7;
DE AltName: Full=Remodel the structure of chromatin complex subunit 7;
GN Name=rsc7; ORFNames=SPCC1281.05;
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 SER-36 AND SER-37, AND
RP IDENTIFICATION BY 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 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 probably interacts with histone and histone variant
CC components of centromeric chromatin. {ECO:0000269|PubMed:18622392}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the RSC7/SWP82 family. RSC7 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA22826.1; -; Genomic_DNA.
DR PIR; T40924; T40924.
DR RefSeq; NP_588169.1; NM_001023158.2.
DR AlphaFoldDB; O94522; -.
DR BioGRID; 275417; 14.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-48393N; -.
DR IntAct; O94522; 12.
DR STRING; 4896.SPCC1281.05.1; -.
DR iPTMnet; O94522; -.
DR SwissPalm; O94522; -.
DR MaxQB; O94522; -.
DR PaxDb; O94522; -.
DR PRIDE; O94522; -.
DR EnsemblFungi; SPCC1281.05.1; SPCC1281.05.1:pep; SPCC1281.05.
DR GeneID; 2538836; -.
DR KEGG; spo:SPCC1281.05; -.
DR PomBase; SPCC1281.05; rsc7.
DR VEuPathDB; FungiDB:SPCC1281.05; -.
DR eggNOG; ENOG502QW07; Eukaryota.
DR HOGENOM; CLU_022149_2_1_1; -.
DR InParanoid; O94522; -.
DR OMA; CRTFTCL; -.
DR PhylomeDB; O94522; -.
DR Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR PRO; PR:O94522; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016586; C:RSC-type 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:0006357; P:regulation of transcription by RNA polymerase II; IC:PomBase.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:PomBase.
DR InterPro; IPR013933; CRC_Rsc7/Swp82.
DR Pfam; PF08624; CRC_subunit; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..390
FT /note="Chromatin structure-remodeling complex subunit rsc7"
FT /id="PRO_0000373988"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 390 AA; 44009 MW; 04123B06A14C7790 CRC64;
MDSTAGSDAS TPTNHTVSSK KRRGRPPKGS YAAYGSSDDD DEEYSGRTRR RNRNTRPRVS
APSSSSTVVP KDLYSHRATL EDDELNFGVV DPEGEKKVNE LGYLNGGREY RCRTFTCLGR
GNRLYMLSTE PARAMGYRDS YLLFLKHRSL HKIIVDDSEK WDLIERNIIP HSYKGRAVGI
VAARSIFREF GARIIVGGRR IVDDYWEGEF RARGFVEGEL ADPDDKLPPP GMPYNRNQYV
AWHGASAVYH PQPSLEAQLP AAARKRKKEP PKDATWLFQH AKATAAYNND ITKYLVQKQD
IGYFEPHTNL LHVPLNTQPT KTHWIQAKTG TECPAPKLDI LVALNSDVAP QVSIANIPPS
VYASCPLHVQ EAIRKRQEQE IRSIRLNSMY
