RAF2_SCHPO
ID RAF2_SCHPO Reviewed; 636 AA.
AC O74560;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Rik1-associated factor 2;
DE AltName: Full=Cryptic loci regulator 7;
DE AltName: Full=De-localization of swi6 protein 2;
GN Name=raf2; Synonyms=clr7, cmc2, dos2; ORFNames=SPCC970.07c;
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 PARTIAL PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION IN THE RIK1-ASSOCIATED
RP E3 UBIQUITIN LIGASE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=16024659; DOI=10.1101/gad.1328005;
RA Horn P.J., Bastie J.-N., Peterson C.L.;
RT "A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for
RT heterochromatin formation.";
RL Genes Dev. 19:1705-1714(2005).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16040243; DOI=10.1016/j.cub.2005.07.021;
RA Li F., Goto D.B., Zaratiegui M., Tang X., Martienssen R., Cande W.Z.;
RT "Two novel proteins, dos1 and dos2, interact with rik1 to regulate
RT heterochromatic RNA interference and histone modification.";
RL Curr. Biol. 15:1448-1457(2005).
RN [4]
RP FUNCTION, AND INTERACTION WITH CUL4.
RX PubMed=16157682; DOI=10.1534/genetics.105.048298;
RA Thon G., Hansen K.R., Altes S.P., Sidhu D., Singh G., Verhein-Hansen J.,
RA Bonaduce M.J., Klar A.J.;
RT "The Clr7 and Clr8 directionality factors and the Pcu4 cullin mediate
RT heterochromatin formation in the fission yeast Schizosaccharomyces pombe.";
RL Genetics 171:1583-1595(2005).
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18345014; DOI=10.1038/nsmb.1406;
RA Zhang K., Mosch K., Fischle W., Grewal S.I.;
RT "Roles of the Clr4 methyltransferase complex in nucleation, spreading and
RT maintenance of heterochromatin.";
RL Nat. Struct. Mol. Biol. 15:381-388(2008).
RN [7]
RP FUNCTION.
RX PubMed=31468675; DOI=10.15252/embr.201948111;
RA Oya E., Nakagawa R., Yoshimura Y., Tanaka M., Nishibuchi G., Machida S.,
RA Shirai A., Ekwall K., Kurumizaka H., Tagami H., Nakayama J.I.;
RT "H3K14 ubiquitylation promotes H3K9 methylation for heterochromatin
RT assembly.";
RL EMBO Rep. 20:E48111-E48111(2019).
CC -!- FUNCTION: Component of the Clr4 methyltransferase complex (ClrC) which
CC contributes to the establishment of heterochromatin by specifically
CC methylating histone H3 to form H3K9me (PubMed:16024659,
CC PubMed:16040243, PubMed:16157682). ClrC preferentially ubiquitylates
CC H3K14 and ClrC-mediated H3 ubiquitination promotes clr4
CC methyltransferase activity for the methylation of H3K9
CC (PubMed:31468675). H3K9me represents a specific tag for epigenetic
CC transcriptional repression by recruiting swi6/HP1 to methylated
CC histones which leads to transcriptional silencing within centromeric
CC heterochromatin, telomeric regions and at the silent mating-type loci
CC (PubMed:16024659, PubMed:16040243, PubMed:16157682, PubMed:18345014).
CC Has a role in both mitotic and meiotic chromosome segregation
CC (PubMed:16040243). {ECO:0000269|PubMed:16024659,
CC ECO:0000269|PubMed:16040243, ECO:0000269|PubMed:16157682,
CC ECO:0000269|PubMed:18345014, ECO:0000269|PubMed:31468675}.
CC -!- SUBUNIT: Component of the Clr4 methyltransferase complex (ClrC)
CC composed of at least clr4, rik1, pcu4, rbx1, raf1 and raf2. The cullin
CC pcu4, rik1, raf1, raf2 and the ring-box protein rbx1 are components of
CC an E3 ubiquitin ligase, whose activity is essential for heterochromatin
CC assembly (PubMed:16024659). Interacts with pcu4 (PubMed:16157682).
CC {ECO:0000269|PubMed:16024659, ECO:0000269|PubMed:16157682}.
CC -!- INTERACTION:
CC O74560; Q9UTR1: mms19; NbExp=2; IntAct=EBI-904886, EBI-15934093;
CC O74560; P87154: pol2; NbExp=2; IntAct=EBI-904886, EBI-876811;
CC O74560; O94276: SPBP8B7.28c; NbExp=3; IntAct=EBI-904886, EBI-2651917;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Mitochondrion {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16040243, ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:18345014}. Chromosome {ECO:0000269|PubMed:16040243,
CC ECO:0000269|PubMed:18345014}.
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DR EMBL; CU329672; CAA20700.1; -; Genomic_DNA.
DR PIR; T41673; T41673.
DR RefSeq; NP_587848.1; NM_001022841.2.
DR AlphaFoldDB; O74560; -.
DR BioGRID; 275985; 255.
DR DIP; DIP-37848N; -.
DR IntAct; O74560; 6.
DR STRING; 4896.SPCC970.07c.1; -.
DR PaxDb; O74560; -.
DR EnsemblFungi; SPCC970.07c.1; SPCC970.07c.1:pep; SPCC970.07c.
DR GeneID; 2539420; -.
DR KEGG; spo:SPCC970.07c; -.
DR PomBase; SPCC970.07c; raf2.
DR VEuPathDB; FungiDB:SPCC970.07c; -.
DR HOGENOM; CLU_430309_0_0_1; -.
DR InParanoid; O74560; -.
DR OMA; IRSSYEH; -.
DR PRO; PR:O74560; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0043494; C:CLRC complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; TAS:PomBase.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IC:PomBase.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:PomBase.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:PomBase.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:PomBase.
DR InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR Pfam; PF12047; DNMT1-RFD; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Cytoplasm; Direct protein sequencing;
KW Mitochondrion; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..636
FT /note="Rik1-associated factor 2"
FT /id="PRO_0000116561"
SQ SEQUENCE 636 AA; 73293 MW; C3FF8306DD764CFB CRC64;
MPPVRAEKKR KTDLIEQVCV TNKAGELVDL EDVLEYGPYS LTGILSSEKD EQEPLFDESI
VLGYSIKISP VWTYNLKDVP EKETMSIWIV TPQRRYGILS PSSEYKAIYE QISEKNRLFY
LIKTKFKDDM ISGTLEDYDN YIEVLKEKLE LPSCFQAILL VQKHIRFLLT QMVATSSLHV
WSESPFFIRI RSSYEHLILQ INKNIYNARQ ERKKSKLSSN NPSDNNTTMK SSLNQALTLI
NLPEQPFSIS SPTATPQLGV VKRTSPLRFP LNDIWLSGLR IVDPNIESIS LWKRIQVSTS
PKHQRYISLQ EVCSVIAQQL QITNLEALNK LSSHGETLLQ IMHTAFTWRG TKLFNDIKHA
IGFRSSVQQA RSQFRGYCYD YLFMHCNNGE KTSLHLLRTL ICMKLDFSNA QLAAKILFHF
LLFDIGSGLS GSDYTYEQYI NHSAVAFSFT EEIFEKNFVT VLPDFVKLFS ISFGYWPAFS
FYDELLKLLR NKYPKVYSST PNLCDQVWLD RTNLFPCNRS TRSTLPYRPT KLLDLASASS
CLSKKETDFK QDTGLYSYNL EKVEALKVSP DLQTGIWSCP VQNCLYFAVC DNPYKPSQVI
YDHLLGHVDS KFIFKTPSNS VRSFTNKLEH IMYNIN
