SSR4_SCHPO
ID SSR4_SCHPO Reviewed; 395 AA.
AC Q9P7Y0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=SWI/SNF and RSC complexes subunit ssr4;
GN Name=ssr4; ORFNames=SPBP23A10.05;
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 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 SSR4 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB66433.1; -; Genomic_DNA.
DR PIR; T50392; T50392.
DR RefSeq; NP_595817.1; NM_001021721.2.
DR PDB; 7K7V; X-ray; 1.88 A; A=2-180.
DR PDB; 7K7W; X-ray; 1.77 A; A=2-180.
DR PDB; 7K82; X-ray; 2.10 A; A=2-180.
DR PDBsum; 7K7V; -.
DR PDBsum; 7K7W; -.
DR PDBsum; 7K82; -.
DR AlphaFoldDB; Q9P7Y0; -.
DR SMR; Q9P7Y0; -.
DR BioGRID; 277813; 13.
DR ComplexPortal; CPX-6362; SWI/SNF chromatin remodelling complex.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-48386N; -.
DR IntAct; Q9P7Y0; 10.
DR STRING; 4896.SPBP23A10.05.1; -.
DR iPTMnet; Q9P7Y0; -.
DR MaxQB; Q9P7Y0; -.
DR PaxDb; Q9P7Y0; -.
DR EnsemblFungi; SPBP23A10.05.1; SPBP23A10.05.1:pep; SPBP23A10.05.
DR GeneID; 2541301; -.
DR KEGG; spo:SPBP23A10.05; -.
DR PomBase; SPBP23A10.05; ssr4.
DR VEuPathDB; FungiDB:SPBP23A10.05; -.
DR eggNOG; ENOG502S04K; Eukaryota.
DR HOGENOM; CLU_040576_0_0_1; -.
DR InParanoid; Q9P7Y0; -.
DR OMA; AGQKVYP; -.
DR PhylomeDB; Q9P7Y0; -.
DR PRO; PR:Q9P7Y0; -.
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: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 InterPro; IPR013859; Ssr4.
DR Pfam; PF08549; SWI-SNF_Ssr4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Cytoplasm; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..395
FT /note="SWI/SNF and RSC complexes subunit ssr4"
FT /id="PRO_0000349433"
FT REGION 182..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:7K7W"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7K7W"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:7K7W"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:7K7W"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:7K7W"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:7K7W"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:7K7W"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:7K7W"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:7K7W"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:7K7W"
FT STRAND 101..112
FT /evidence="ECO:0007829|PDB:7K7W"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:7K7W"
FT STRAND 122..133
FT /evidence="ECO:0007829|PDB:7K7W"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:7K7W"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:7K7W"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:7K7W"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7K7V"
SQ SEQUENCE 395 AA; 44255 MW; 4A2586D0D72A55CE CRC64;
MAATMAAQSL LSIPVEYRSQ VWCRANLPYP PAPQLPIPAV VDILTKASQA LPQISFSWTL
IDQPPDGSLF LVWQAPTLPS PPDGMHFMSN ERFFNMDVAG KVLEIHEAKH GFYPLSETRT
MHVRCRYRLL GVGFDNFWLV HYFQGSETDS IPANISVAKP PHLRRYPLPD VKTSPFLLQE
PKKHIPEGTA LSQRETLPNM GSAQMKSQSR TPSFSNVTTS PVPPINSNAT AQTAEGHMGA
TNMTVDNMNK PSIPPNGNTS ILMQEDLEIE KGDVMDKLSP QQICTARFIK HAEWMSQVLL
TLQSVKDIEP PALWQEPNSM EELGKELKDN KEQLVKQDQK YQSLQGDLSY TDSMSNLLKE
FSNIKSAEEC DVLQKKIEEF AEAKIVPLSH VTERS
