CLR2_SCHPO
ID CLR2_SCHPO Reviewed; 537 AA.
AC O13881;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cryptic loci regulator 2;
GN Name=clr2; ORFNames=SPAC1B3.17;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=15317867; DOI=10.1093/nar/gkh780;
RA Bjerling P., Ekwall K., Egel R., Thon G.;
RT "A novel type of silencing factor, Clr2, is necessary for transcriptional
RT silencing at various chromosomal locations in the fission yeast
RT Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 32:4421-4428(2004).
RN [2]
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 [3]
RP FUNCTION, INTERACTION WITH CLR3, AND SUBCELLULAR LOCATION.
RX PubMed=17289569; DOI=10.1016/j.cell.2006.12.035;
RA Sugiyama T., Cam H.P., Sugiyama R., Noma K., Zofall M., Kobayashi R.,
RA Grewal S.I.S.;
RT "SHREC, an effector complex for heterochromatic transcriptional
RT silencing.";
RL Cell 128:491-504(2007).
CC -!- FUNCTION: Required for deacetylation in the mating-type region and the
CC centromere. Acts upstream of the histone deacetylases to promote
CC transcriptional silencing. Required for proper positioning of
CC nucleosomes at heterochromatic loci and for transcriptional gene
CC silencing (TGS) function of the Snf2/Hdac-containing repressor complex
CC (SHREC). {ECO:0000269|PubMed:15317867, ECO:0000269|PubMed:17289569}.
CC -!- SUBUNIT: Interacts with clr3. {ECO:0000269|PubMed:17289569}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17289569}.
CC Chromosome, centromere {ECO:0000269|PubMed:17289569}. Chromosome,
CC telomere {ECO:0000269|PubMed:17289569}. Note=Associates with major
CC heterochromatin, centromeres, sub-telomeres, rDNA and the mat locus.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB11243.1; -; Genomic_DNA.
DR PIR; T38036; T38036.
DR RefSeq; NP_594802.1; NM_001020230.2.
DR PDB; 5IKJ; X-ray; 2.30 A; A=1-537.
DR PDBsum; 5IKJ; -.
DR AlphaFoldDB; O13881; -.
DR SMR; O13881; -.
DR BioGRID; 279050; 29.
DR STRING; 4896.SPAC1B3.17.1; -.
DR iPTMnet; O13881; -.
DR SwissPalm; O13881; -.
DR MaxQB; O13881; -.
DR PaxDb; O13881; -.
DR EnsemblFungi; SPAC1B3.17.1; SPAC1B3.17.1:pep; SPAC1B3.17.
DR GeneID; 2542596; -.
DR KEGG; spo:SPAC1B3.17; -.
DR PomBase; SPAC1B3.17; clr2.
DR VEuPathDB; FungiDB:SPAC1B3.17; -.
DR eggNOG; ENOG502S16G; Eukaryota.
DR HOGENOM; CLU_560382_0_0_1; -.
DR InParanoid; O13881; -.
DR OMA; GRWYEPW; -.
DR PRO; PR:O13881; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0061638; C:CENP-A containing chromatin; IDA:PomBase.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:PomBase.
DR GO; GO:0070824; C:SHREC complex; IDA:PomBase.
DR GO; GO:0110129; C:SHREC2 complex; IDA:PomBase.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:PomBase.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:PomBase.
DR InterPro; IPR038986; Clr2.
DR InterPro; IPR031915; Clr2_N.
DR InterPro; IPR018839; Tscrpt-silencing_Clr2_C.
DR PANTHER; PTHR38046; PTHR38046; 2.
DR Pfam; PF10383; Clr2; 1.
DR Pfam; PF16761; Clr2_transil; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Centromere; Chromatin regulator; Chromosome; Nucleus;
KW Reference proteome; Repressor; Telomere; Transcription;
KW Transcription regulation.
FT CHAIN 1..537
FT /note="Cryptic loci regulator 2"
FT /id="PRO_0000089869"
FT REGION 96..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 39..56
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 203..224
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 244..256
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:5IKJ"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 400..408
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 412..425
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 450..458
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 459..465
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:5IKJ"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 507..511
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:5IKJ"
FT HELIX 520..529
FT /evidence="ECO:0007829|PDB:5IKJ"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:5IKJ"
SQ SEQUENCE 537 AA; 61971 MW; B4EF6EA63FAF75CA CRC64;
MPAITCVWSD GRSDTWPNVN GHSRTRSVPS LKPLPHQDSK NLLYRQICGR LLAQHVFGGA
GSTQPILNQL CKRLSTGNPN NTNASTVVTA PEKNVVSARH VRPNPKSSKD TLEKQPKYSS
QIYLTDSFEN YYLASLPTNY QLYQRDSNRE NGNGKREFWL YGHPSGRPFR SVNDFLHHLY
WLISDLTRNE STCCCVLCSG NMTRVRKNLQ KENERMFHEC KDDTYTWPSS YRLGEVVWID
INNELIPAII VARNLINYES NQMDAVKLIS DTFVEPYQYH CKQLGNSRYY FDMAAADIEP
WSRHPLDLQK QEHLVAHSIC QTWNLFGIFQ PLEGIDMEEP KFHDENYSIP LTVLPTFGGE
SNSLDDHFYG IFRGAEKLWI NDLCVISTSS LPSVLQKTSF MYISDIYVNE DDIVCFQGSL
WTQIDKNALD YNDSADNIDE HKDDLKELPR RLQMVSKLSN TYFRCLHDKS VEYVCPFADV
LGRWYEPWFV KGDLNYTSEV KERTSSRLSA VGSENWVDDD FYEYLLSEID MVSAVVM
