DRN1_YEAST
ID DRN1_YEAST Reviewed; 507 AA.
AC P53255; D6VUM5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=CWF19-like protein DRN1;
DE AltName: Full=Debranching enzyme-associated ribonuclease 1;
GN Name=DRN1; OrderedLocusNames=YGR093W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=22932476; DOI=10.1186/2045-3701-2-30;
RA Dastidar R.G., Hooda J., Shah A., Cao T.M., Henke R.M., Zhang L.;
RT "The nuclear localization of SWI/SNF proteins is subjected to oxygen
RT regulation.";
RL Cell Biosci. 2:30-30(2012).
RN [8]
RP FUNCTION, INTERACTION WITH DBR1 AND SYF1, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-269; CYS-272; HIS-366; ARG-459 AND TRP-474.
RX PubMed=24919400; DOI=10.1261/rna.044602.114;
RA Garrey S.M., Katolik A., Prekeris M., Li X., York K., Bernards S.,
RA Fields S., Zhao R., Damha M.J., Hesselberth J.R.;
RT "A homolog of lariat-debranching enzyme modulates turnover of branched
RT RNA.";
RL RNA 20:1337-1348(2014).
CC -!- FUNCTION: Involved in branched RNA metabolism, modulating the turnover
CC of lariat-intron pre-mRNAs by the lariat-debranching enzyme DBR1.
CC Enhances the debranching activity of DBR1 in vitro.
CC {ECO:0000269|PubMed:24919400}.
CC -!- SUBUNIT: Interacts with DBR1. Interacts with SYF1, a component of the
CC NTC complex. Interacts with lariat-introns and lariat-intermediates.
CC {ECO:0000269|PubMed:24919400}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Relocalizes to the
CC cytoplasm in response to hypoxia.
CC -!- DISRUPTION PHENOTYPE: Accumulates pre-mRNA splicing intermediates.
CC {ECO:0000269|PubMed:24919400}.
CC -!- MISCELLANEOUS: Present with 1270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CWF19 family. {ECO:0000305}.
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DR EMBL; Z72878; CAA97096.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08186.1; -; Genomic_DNA.
DR PIR; S64388; S64388.
DR RefSeq; NP_011607.3; NM_001181222.3.
DR AlphaFoldDB; P53255; -.
DR SMR; P53255; -.
DR BioGRID; 33336; 74.
DR IntAct; P53255; 2.
DR MINT; P53255; -.
DR STRING; 4932.YGR093W; -.
DR iPTMnet; P53255; -.
DR MaxQB; P53255; -.
DR PaxDb; P53255; -.
DR PRIDE; P53255; -.
DR EnsemblFungi; YGR093W_mRNA; YGR093W; YGR093W.
DR GeneID; 852985; -.
DR KEGG; sce:YGR093W; -.
DR SGD; S000003325; DRN1.
DR VEuPathDB; FungiDB:YGR093W; -.
DR eggNOG; KOG2476; Eukaryota.
DR GeneTree; ENSGT00940000156000; -.
DR HOGENOM; CLU_019955_0_0_1; -.
DR InParanoid; P53255; -.
DR OMA; FSGHCLI; -.
DR BioCyc; YEAST:G3O-30803-MON; -.
DR PRO; PR:P53255; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53255; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0061632; F:RNA lariat debranching enzyme activator activity; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR InterPro; IPR040194; Cwf19-like.
DR InterPro; IPR006768; Cwf19-like_C_dom-1.
DR InterPro; IPR006767; Cwf19-like_C_dom-2.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR12072; PTHR12072; 2.
DR Pfam; PF04677; CwfJ_C_1; 1.
DR Pfam; PF04676; CwfJ_C_2; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..507
FT /note="CWF19-like protein DRN1"
FT /id="PRO_0000202810"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 269
FT /note="C->A: Causes accumulation of pre-mRNA splicing
FT intermediates."
FT /evidence="ECO:0000269|PubMed:24919400"
FT MUTAGEN 272
FT /note="C->A: Causes accumulation of pre-mRNA splicing
FT intermediates."
FT /evidence="ECO:0000269|PubMed:24919400"
FT MUTAGEN 366
FT /note="H->A: Causes accumulation of pre-mRNA splicing
FT intermediates."
FT /evidence="ECO:0000269|PubMed:24919400"
FT MUTAGEN 459
FT /note="R->A: Causes accumulation of pre-mRNA splicing
FT intermediates."
FT /evidence="ECO:0000269|PubMed:24919400"
FT MUTAGEN 474
FT /note="W->A: Causes accumulation of pre-mRNA splicing
FT intermediates."
FT /evidence="ECO:0000269|PubMed:24919400"
SQ SEQUENCE 507 AA; 58206 MW; 80ADC9B5F9883A92 CRC64;
MTNAKILVAH ISESDADEAI RKIKKVNEKS GPFDLIIIFS NSYDENFELN TDGLPQLILL
SCDKANNSKS KKINENVTLL HNMGTYKLAN GITLSYFIYP DDTLQGEKKS ILDEFGKSED
QVDILLTKEW GLSISERCGR LSGSEVVDEL AKKLQARYHF AFSDEINFYE LEPFQWERER
LSRFLNIPKY GSGKKWAYAF NMPIGDNELK DEPEPPNLIA NPYNSVVTNS NKRPLETETE
NSFDGDKQVL ANREKNENKK IRTILPSSCH FCFSNPNLED HMIISIGKLV YLTTAKGPLS
VPKGDMDISG HCLIIPIEHI PKLDPSKNAE LTQSILAYEA SLVKMNYIKF DMCTIVFEIQ
SERSIHFHKQ VIPVPKYLVL KFCSALDRQV HFNNEKFTRN AKLEFQCYDS HSSKQYVDVI
NNQSNNYLQF TVYETPEADP KIYLATFNAS ETIDLQFGRR VLAFLLNLPR RVKWNSSTCL
QTKQQETIEA EKFQKAYRTY DISLTEN
