ID DRE4_SCHPO Reviewed; 411 AA.
AC Q09685;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 24-JAN-2024, entry version 144.
DE RecName: Full=Pre-mRNA-splicing factor dre4;
DE AltName: Full=DNA replication protein 4;
DE AltName: Full=Hyphal growth protein 1;
GN Name=dre4; Synonyms=hgp1; ORFNames=SPAC13C5.02;
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].
RA Yao J., Leung S.W., Uzawa S., Lee C.S., Joshi H.C.;
RT "Hyphal growth in S. pombe: a plausible model to study infectious yeast.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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 DISRUPTION PHENOTYPE.
RX PubMed=15466421; DOI=10.1534/genetics.104.034231;
RA Gomez E.B., Angeles V.T., Forsburg S.L.;
RT "A screen for Schizosaccharomyces pombe mutants defective in rereplication
RT identifies new alleles of rad4+, cut9+ and psf2+.";
RL Genetics 169:77-89(2005).
RN [4]
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 [5]
RP INTERACTION WITH PRP19, IDENTIFICATION IN THE SPLICEOSOME, AND FUNCTION.
RX PubMed=21386897; DOI=10.1371/journal.pone.0016719;
RA Ren L., McLean J.R., Hazbun T.R., Fields S., Vander Kooi C., Ohi M.D.,
RA Gould K.L.;
RT "Systematic two-hybrid and comparative proteomic analyses reveal novel
RT yeast pre-mRNA splicing factors connected to Prp19.";
RL PLoS ONE 6:E16719-E16719(2011).
CC -!- FUNCTION: Component of the spliceosome involved in mRNA processing.
CC {ECO:0000269|PubMed:21386897}.
CC -!- SUBUNIT: Component of the spliceosomal complex. Interacts with prp19.
CC {ECO:0000269|PubMed:21386897}.
CC -!- INTERACTION:
CC Q09685; O14011: prp19; NbExp=6; IntAct=EBI-4408349, EBI-590830;
CC Q09685; O74517: saf1; NbExp=4; IntAct=EBI-4408349, EBI-4421067;
CC Q09685; Q9P7H6: SPAC1782.03; NbExp=3; IntAct=EBI-4408349, EBI-4421106;
CC Q09685; O14097: SPAC2F3.14c; NbExp=3; IntAct=EBI-4408349, EBI-4420697;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Cells are defective in DNA replication, S-phase
CC progression, chromatin structure and cytokinesis. Dre4-54 truncated
CC temperature-sensitive mutant has 'Trp-117' changed to a stop codon.
CC {ECO:0000269|PubMed:15466421}.
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DR EMBL; AY227798; AAO73008.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA90453.1; -; Genomic_DNA.
DR PIR; S58094; S58094.
DR RefSeq; NP_592930.1; NM_001018331.2.
DR AlphaFoldDB; Q09685; -.
DR SMR; Q09685; -.
DR BioGRID; 278651; 40.
DR IntAct; Q09685; 35.
DR STRING; 284812.Q09685; -.
DR iPTMnet; Q09685; -.
DR MaxQB; Q09685; -.
DR PaxDb; 4896-SPAC13C5-02-1; -.
DR EnsemblFungi; SPAC13C5.02.1; SPAC13C5.02.1:pep; SPAC13C5.02.
DR GeneID; 2542176; -.
DR KEGG; spo:SPAC13C5.02; -.
DR PomBase; SPAC13C5.02; dre4.
DR VEuPathDB; FungiDB:SPAC13C5.02; -.
DR eggNOG; KOG0155; Eukaryota.
DR HOGENOM; CLU_013872_0_0_1; -.
DR InParanoid; Q09685; -.
DR OMA; MLKSTYT; -.
DR PhylomeDB; Q09685; -.
DR PRO; PR:Q09685; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0070063; F:RNA polymerase binding; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 1.10.10.440; FF domain; 1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR045148; TCRG1-like.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR15377; TRANSCRIPTION ELONGATION REGULATOR 1; 1.
DR PANTHER; PTHR15377:SF3; WW DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01846; FF; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00441; FF; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF81698; FF domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS51676; FF; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW Spliceosome.
FT CHAIN 1..411
FT /note="Pre-mRNA-splicing factor dre4"
FT /id="PRO_0000076095"
FT DOMAIN 3..36
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 89..122
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 239..293
FT /note="FF"
FT REGION 65..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 48519 MW; 7A89C5F7397B8AAF CRC64;
MSQPLPPGWT EHKAPSGIPY YWNAELKKST YQRPSFIEKN HSSSVTASQA SLAFNTSEKL
FVNENAEERK NSRDLRKQLP DRPKFKKRIP NNDSWVVVFT KKNRYFFHNL KSHESYWEPP
LEISKDLKIL RLPIRKQISK DSSQSQNVDS GKTNHEEIHE SRHLQTEIEE PSGLEESSEE
SVLYSEEFYE KSDEEEDEEK SHSAEELEFG EEDIMYQLQQ LDDETVSYDI QEQATNLSTD
DARRVFTELL KDKNIGAYQP WELVYPKLLD DDRFYVLDSG ERRKEVFEEY CKSVVSTKKI
TRRKNTLSDF WTLLHSLPST LLWPQFKRKY RKSSTLQIPG YSERDFEKLF REFQILRKQP
MQDKLLNFKK LCKSKTVDPK NPDEFTESIL NDTRYAVLTR EELDSLACSS N
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