DRI1_SCHPO
ID DRI1_SCHPO Reviewed; 604 AA.
AC O13801;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=RNA-binding protein involved in heterochromatin assembly dri1 {ECO:0000312|PomBase:SPAC17H9.04c};
DE AltName: Full=Dpb4-interacting, RRM, and IDR-containing factor {ECO:0000303|PubMed:33693625};
GN Name=dri1 {ECO:0000303|PubMed:33693625};
GN Synonyms=nrp1 {ECO:0000312|PomBase:SPAC17H9.04c};
GN ORFNames=SPAC17H9.04c {ECO:0000312|PomBase:SPAC17H9.04c};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-437, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [3]
RP FUNCTION, INTERACTION WITH DPB4 AND CHP1, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=33693625; DOI=10.1093/genetics/iyab032;
RA Ban H., Sun W., Chen Y.H., Chen Y., Li F.;
RT "Dri1 mediates heterochromatin assembly via RNAi and histone
RT deacetylation.";
RL Genetics 217:iyab032-iyab032(2021).
CC -!- FUNCTION: Mediates heterochromatin assembly by promoting RNAi-mediated
CC heterochromatin silencing and histone deacetylation (PubMed:33693625).
CC Binds pericetromeric transcripts and recruits the RNA-induced
CC transcriptional silencing (RITS) complex to heterochromatin
CC (PubMed:33693625). Recruits sir2 to chromatin to promote deacetylation
CC of 'Lys-9' of histone H3 (PubMed:33693625).
CC {ECO:0000269|PubMed:33693625}.
CC -!- SUBUNIT: Interacts with dpb4 (PubMed:33693625). Interacts with chp1
CC (PubMed:33693625). {ECO:0000269|PubMed:33693625}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:33693625}. Nucleus
CC {ECO:0000269|PubMed:33693625}.
CC -!- DISRUPTION PHENOTYPE: Abolishes siRNA production from the centromeric
CC outer repeat region (PubMed:33693625). Decreases H3K9 methylation and
CC impairs heterochromatin silencing; simultaneous disruption of dpb4
CC exacerbates the effect (PubMed:33693625).
CC {ECO:0000269|PubMed:33693625}.
CC -!- MISCELLANEOUS: Shown to localize to the nucleolus in PMID:16823372 by
CC overexpression of a C-terminally tagged allele, however this allele was
CC subsequently shown to be non-functional in PMID:33693625.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11213.1; -; Genomic_DNA.
DR PIR; T37870; T37870.
DR RefSeq; NP_593574.1; NM_001019006.2.
DR AlphaFoldDB; O13801; -.
DR BioGRID; 278723; 50.
DR IntAct; O13801; 1.
DR STRING; 4896.SPAC17H9.04c.1; -.
DR iPTMnet; O13801; -.
DR MaxQB; O13801; -.
DR PaxDb; O13801; -.
DR PRIDE; O13801; -.
DR EnsemblFungi; SPAC17H9.04c.1; SPAC17H9.04c.1:pep; SPAC17H9.04c.
DR GeneID; 2542253; -.
DR KEGG; spo:SPAC17H9.04c; -.
DR PomBase; SPAC17H9.04c; -.
DR VEuPathDB; FungiDB:SPAC17H9.04c; -.
DR eggNOG; KOG4198; Eukaryota.
DR HOGENOM; CLU_022834_1_0_1; -.
DR InParanoid; O13801; -.
DR OMA; IVIHVAT; -.
DR PhylomeDB; O13801; -.
DR PRO; PR:O13801; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; EXP:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0140453; C:protein aggregate center; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; EXP:PomBase.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IMP:PomBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0031445; P:regulation of heterochromatin assembly; IMP:PomBase.
DR CDD; cd12452; RRM_ARP_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034351; Nrp1_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 2.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00547; ZnF_RBZ; 3.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90209; SSF90209; 3.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing; Zinc;
KW Zinc-finger.
FT CHAIN 1..604
FT /note="RNA-binding protein involved in heterochromatin
FT assembly dri1"
FT /id="PRO_0000314102"
FT DOMAIN 244..322
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 343..372
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 445..476
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 560..588
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 604 AA; 66396 MW; F4DE6C459D062716 CRC64;
MSKLPSPTMP LPESVGDLVV LHFETNLDDH GISIGRAPCE IHEICWVILD GKTLEKQHCE
SCSIREDSSR HGICGSASSL TEAIFTLDNS IQERLNFQGK PFTFVVMNGR ELRVLLPKEA
RDQGITLPSY MRHPRLFDLS SEYAKWQIRM GAVPPYTITL SHIFGKLDVD SLPPITESKA
IELSPSDAPY ITKGLTQCWR LANATTLLLR KAEKDSRGHS LPSVLTQPIN CQADARSFYA
ERSKIVHVAG LTNDVTQLEL ESWFTNHGVH PVALWTLKTP EPYKSTGTGF VLFASHEDAA
DALAFNGYCL GDRMLEIIPS STKVLDKASD ILIPFPSSKN RPRPGDWNCP MCGFSNFQRR
TSCFRCSFPG PTHVSAATGS NTFSPDFPYG NSYGNGSSHF IANYGGSVHH SNENTMQSDL
QHQNGNNAVN HHHSSRSFGG NVPFRAGDWK CGSEGCGYHN FAKNVCCLRC GASRATAAVV
ADHASGPVNG SYSHNSYSHI PPVMSTSPPN HSVYPYSQLS INSVTANHGQ NFGGQNGGNV
SRFDDHGRFK EVSRPSVTTD QGDWLCECGF TNFRRRSNCL RCNAPHYSNM QIPASLPSDF
NAYV
