SSR3_SCHPO
ID SSR3_SCHPO Reviewed; 425 AA.
AC Q9P7S3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=SWI/SNF and RSC complexes subunit ssr3;
GN Name=ssr3; ORFNames=SPAC23G3.10c;
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 SMARCD family. {ECO:0000305}.
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DR EMBL; CU329670; CAB72235.1; -; Genomic_DNA.
DR PIR; T50184; T50184.
DR RefSeq; NP_593110.1; NM_001018507.2.
DR AlphaFoldDB; Q9P7S3; -.
DR SMR; Q9P7S3; -.
DR BioGRID; 277943; 50.
DR ComplexPortal; CPX-6362; SWI/SNF chromatin remodelling complex.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-48385N; -.
DR IntAct; Q9P7S3; 10.
DR STRING; 4896.SPAC23G3.10c.1; -.
DR MaxQB; Q9P7S3; -.
DR PaxDb; Q9P7S3; -.
DR EnsemblFungi; SPAC23G3.10c.1; SPAC23G3.10c.1:pep; SPAC23G3.10c.
DR GeneID; 2541438; -.
DR KEGG; spo:SPAC23G3.10c; -.
DR PomBase; SPAC23G3.10c; ssr3.
DR VEuPathDB; FungiDB:SPAC23G3.10c; -.
DR eggNOG; KOG2570; Eukaryota.
DR HOGENOM; CLU_023529_2_1_1; -.
DR InParanoid; Q9P7S3; -.
DR OMA; PYFWNSD; -.
DR PhylomeDB; Q9P7S3; -.
DR PRO; PR:Q9P7S3; -.
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; IPI:PomBase.
DR Gene3D; 1.10.245.10; -; 1.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR Pfam; PF02201; SWIB; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..425
FT /note="SWI/SNF and RSC complexes subunit ssr3"
FT /id="PRO_0000317337"
FT DOMAIN 201..278
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 49759 MW; 26D420E6CEF71058 CRC64;
MSNNSRLPEN GVQSGNGEDA ELKKSMRIIE REIPDSLLEK IPEAEDYIAL QDLERKLDSL
IVRKRFDLQD SLSRNSHKTR ILRMYIHSTV ANQSWQQKGE NQENNSGDIN SLPIPEWTLH
IEGRLLVNPD DEDDKAFELA PFTNFFRKIA IQILRSDDLY PSGNYVEWNK LPDNSNTSNG
ITVTRKGDQS VDVKIMLYPE EHPERYKLSK AFANILGIRE GTRPDIVSYL WQYIKFHRLQ
DMEEKRLINC DKALRDLFEA DRLYFPRIPE LMNRFLEPID PIVIPYTINV SEHTVEKVTI
FDIRINTEDP RHSQIRSFLA TMMSQDKIRS IDDKLTELIQ AITYSQSKYD FMKKFSESPI
EFINEWIESQ SRDLEIVLDG TNMNYAEKRS ADYYQQPWVH ESAFHYLNLL NSKKQQSVLN
ASAKK
