ID CLR1_SCHPO Reviewed; 1238 AA. AC O74808; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=Cryptic loci regulator protein 1; GN Name=clr1; ORFNames=SPBC2D10.17; 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 [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 FUNCTION. RX PubMed=1644273; DOI=10.1093/genetics/131.2.287; RA Thon G., Klar A.J.S.; RT "The clr1 locus regulates the expression of the cryptic mating-type loci of RT fission yeast."; RL Genetics 131:287-296(1992). RN [3] 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 [4] 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: Regulates silencing of the mat2 and mat3 loci. Organizes the CC chromatin structure of the mating-type region where it also CC participates in establishing the 'cold spot' for recombination. CC Required for proper positioning of nucleosomes at heterochromatic loci CC and for transcriptional gene silencing (TGS) function of the Snf2/Hdac- CC containing repressor complex (SHREC). {ECO:0000269|PubMed:1644273, CC ECO:0000269|PubMed:17289569}. CC -!- SUBUNIT: Interacts with clr3. {ECO:0000269|PubMed:17289569}. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Chromosome, CC telomere. Note=Associates with major heterochromatin, centromeres, sub- CC 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; CU329671; CAA21175.1; -; Genomic_DNA. DR PIR; T40120; T40120. DR RefSeq; NP_596236.1; NM_001022156.2. DR PDB; 5IKF; X-ray; 2.80 A; B=357-500. DR PDB; 5IKJ; X-ray; 2.30 A; B=1151-1238. DR PDBsum; 5IKF; -. DR PDBsum; 5IKJ; -. DR AlphaFoldDB; O74808; -. DR SMR; O74808; -. DR BioGRID; 277085; 107. DR STRING; 284812.O74808; -. DR iPTMnet; O74808; -. DR MaxQB; O74808; -. DR PaxDb; 4896-SPBC2D10-17-1; -. DR EnsemblFungi; SPBC2D10.17.1; SPBC2D10.17.1:pep; SPBC2D10.17. DR GeneID; 2540558; -. DR KEGG; spo:SPBC2D10.17; -. DR PomBase; SPBC2D10.17; clr1. DR VEuPathDB; FungiDB:SPBC2D10.17; -. DR eggNOG; KOG1721; Eukaryota. DR HOGENOM; CLU_260175_0_0_1; -. DR InParanoid; O74808; -. DR OMA; LKHRRFN; -. DR PRO; PR:O74808; -. DR Proteomes; UP000002485; Chromosome II. DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase. DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase. DR GO; GO:0005634; C:nucleus; HDA: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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; IMP:PomBase. DR GO; GO:0031507; P:heterochromatin formation; IMP:PomBase. DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IMP:PomBase. DR InterPro; IPR013087; Znf_C2H2_type. DR SMART; SM00355; ZnF_C2H2; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Centromere; Chromatin regulator; Chromosome; Metal-binding; KW Nucleus; Reference proteome; Telomere; Zinc; Zinc-finger. FT CHAIN 1..1238 FT /note="Cryptic loci regulator protein 1" FT /id="PRO_0000290637" FT ZN_FING 1062..1087 FT /note="C2H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 133..156 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 196..237 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 277..303 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 546..568 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 696..735 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 784..824 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 696..722 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT TURN 361..363 FT /evidence="ECO:0007829|PDB:5IKF" FT HELIX 364..372 FT /evidence="ECO:0007829|PDB:5IKF" FT STRAND 377..379 FT /evidence="ECO:0007829|PDB:5IKF" FT HELIX 387..395 FT /evidence="ECO:0007829|PDB:5IKF" FT TURN 396..399 FT /evidence="ECO:0007829|PDB:5IKF" FT HELIX 404..408 FT /evidence="ECO:0007829|PDB:5IKF" FT HELIX 411..413 FT /evidence="ECO:0007829|PDB:5IKF" FT HELIX 417..426 FT /evidence="ECO:0007829|PDB:5IKF" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:5IKF" FT HELIX 447..464 FT /evidence="ECO:0007829|PDB:5IKF" FT HELIX 469..478 FT /evidence="ECO:0007829|PDB:5IKF" FT STRAND 485..490 FT /evidence="ECO:0007829|PDB:5IKF" FT HELIX 1163..1173 FT /evidence="ECO:0007829|PDB:5IKJ" FT STRAND 1212..1215 FT /evidence="ECO:0007829|PDB:5IKJ" FT HELIX 1221..1226 FT /evidence="ECO:0007829|PDB:5IKJ" FT STRAND 1227..1231 FT /evidence="ECO:0007829|PDB:5IKJ" FT STRAND 1234..1238 FT /evidence="ECO:0007829|PDB:5IKJ" SQ SEQUENCE 1238 AA; 136677 MW; 5C6F2213478758CC CRC64; MAEPDISSSE TLTELQQLRL LYFFCFYHAA PFNVKTLVHS LIPPGALSYL LSTYDILRPW LMALRVREGP VNDISTIVQL YEEIVKTGFF INPPPFESYS QTLVARITTL GRPKLQVQQE AQSEVYQRAS TNTQQQVSNV SHGNFKPNSS VNTEPNTSIL SNSKYAGIKP FDFQSSSQNP GLVCEQKTFY QHQFRPFSNL PSNKSSPVKH VSPNVKNNSK KTASSVNSNH SSIPSSITKS NISSLDVYGS EKLISSGSQQ PGHGMVQTTS DKVNASASLY DRSPSKKDIT SSRNTSSYNL GSMRNPSTLK NAAHANPFEG LRFQGSSAVL KEGLNSTVKK TFFDNLNSEK VCPSVSPFLT PDNIASSILY STASFSRSKP DRPRLNLSLE LKLMQNELNK GQLKKQFKGD LRNLADWNNL SLVSSKFPSL PITNLRPDGS FLKHRRFNEE IAYNRQTLEK AIKQLDLSPD KVIQLREQNG VAVNGRVCYP TRNKHSEISA QSSSSLGVTK SLASEVYSSS TVDTISKLNT DKDNYLIKSK KEPIQQKSVS SETTLVKPSS TSSYIDTTNN VLKTNSSFKS SGLTSGPRNE KELLPEGIPT SHNNSETQAQ TADVSNIAAS ADGIYNSDQE KPPEKLDVTK RAFGREIENS NEKELLTSTF LSPSAESQVC LAEIKTIRPG LVPKKQFSVD QNNVISDNTD CSLPKPSNSK LSSISSDGDA SSNRMAVPDK SPFVHAAPNS KALTKDSFST HISVSSLLHS DNEISPIDST RKDYFTSKDS NLQTLKEDAS STKQAKDSGT NDFDKLISGN DVSKNNSGEE QSRSALKPLI SGKLSSCESI NLTKDISTVK RKEYFGIEST SSKQPFHDTG SIKIPAKRSF DTIDKDFRSS NIPFADKIKE DGGDKNVISS IHITTELPKS MPVEVPTNAG AQSDQSNVVD SESLNLRENI STSVADVSLS QAGNEAVLSK KACKPLVLID PFEEKVLKAF NMLSKGYAEY RCQWEGCLAN LHSLENFIKH VLLLHHPKSC SVVKCLWASC DMVLPSEEFE MHLRGHLNNI RLNCEVSNCK KCFSNYEDMF KHLQHSHLPF KFTPESFIKI RNGNVKEEAR RTRNAYTQKS GEVECFMETC TPIAKPAPAN WYPVPPPGFN SSLLSRLTQS NQSKDKIIAA LAKRNVYKSF AGLYDSKGKN DNTGYDFDSN YARVGRHGSF ILPVSKSVPT PSLLIEGSIV QRKNIKIE //