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CLR1_SCHPO
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   03-AUG-2022, entry version 120.
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.
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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; 4896.SPBC2D10.17.1; -.
DR   iPTMnet; O74808; -.
DR   MaxQB; O74808; -.
DR   PaxDb; O74808; -.
DR   PRIDE; O74808; -.
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:0110129; C:SHREC2 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 assembly; IMP:PomBase.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; 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
 
 
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