IWR1_YEAST
ID IWR1_YEAST Reviewed; 353 AA.
AC Q07532; A2TBP4; D6VRN5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=RNA polymerase II nuclear localization protein IWR1;
DE AltName: Full=Interacting with RNA polymerase II protein 1;
GN Name=IWR1; OrderedLocusNames=YDL115C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-227.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 114-353.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=12663529; DOI=10.1093/genetics/163.3.875;
RA Page N., Gerard-Vincent M., Menard P., Beaulieu M., Azuma M.,
RA Dijkgraaf G.J.P., Li H., Marcoux J., Nguyen T., Dowse T., Sdicu A.-M.,
RA Bussey H.;
RT "A Saccharomyces cerevisiae genome-wide mutant screen for altered
RT sensitivity to K1 killer toxin.";
RL Genetics 163:875-894(2003).
RN [6]
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 [7]
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 [8]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH RPB1; RBP2; RPB3; RPB4;
RP RPB5; RPB7; SPT5 AND DST1.
RX PubMed=16554755; DOI=10.1038/nature04670;
RA Krogan N.J., Cagney G., Yu H., Zhong G., Guo X., Ignatchenko A., Li J.,
RA Pu S., Datta N., Tikuisis A.P., Punna T., Peregrin-Alvarez J.M., Shales M.,
RA Zhang X., Davey M., Robinson M.D., Paccanaro A., Bray J.E., Sheung A.,
RA Beattie B., Richards D.P., Canadien V., Lalev A., Mena F., Wong P.,
RA Starostine A., Canete M.M., Vlasblom J., Wu S., Orsi C., Collins S.R.,
RA Chandran S., Haw R., Rilstone J.J., Gandi K., Thompson N.J., Musso G.,
RA St Onge P., Ghanny S., Lam M.H., Butland G., Altaf-Ul A.M., Kanaya S.,
RA Shilatifard A., O'Shea E.K., Weissman J.S., Ingles C.J., Hughes T.R.,
RA Parkinson J., Gerstein M., Wodak S.J., Emili A., Greenblatt J.F.;
RT "Global landscape of protein complexes in the yeast Saccharomyces
RT cerevisiae.";
RL Nature 440:637-643(2006).
RN [9]
RP IDENTIFICATION OF INTRON.
RX PubMed=17101987; DOI=10.1073/pnas.0605645103;
RA Miura F., Kawaguchi N., Sese J., Toyoda A., Hattori M., Morishita S.,
RA Ito T.;
RT "A large-scale full-length cDNA analysis to explore the budding yeast
RT transcriptome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17846-17851(2006).
RN [10]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=19679657; DOI=10.1074/jbc.m109.012153;
RA Peiro-Chova L., Estruch F.;
RT "The yeast RNA polymerase II-associated factor Iwr1p is involved in the
RT basal and regulated transcription of specific genes.";
RL J. Biol. Chem. 284:28958-28967(2009).
RN [11]
RP FUNCTION.
RX PubMed=20010803; DOI=10.1038/embor.2009.246;
RA Kanno T., Bucher E., Daxinger L., Huettel B., Kreil D.P., Breinig F.,
RA Lind M., Schmitt M.J., Simon S.A., Gurazada S.G., Meyers B.C.,
RA Lorkovic Z.J., Matzke A.J., Matzke M.;
RT "RNA-directed DNA methylation and plant development require an IWR1-type
RT transcription factor.";
RL EMBO Rep. 11:65-71(2010).
RN [12]
RP FUNCTION, ASSOCIATION WITH RNA POLYMERASE II, NUCLEAR LOCALIZATION SIGNAL,
RP AND SUBCELLULAR LOCATION.
RX PubMed=21504834; DOI=10.1016/j.molcel.2011.02.033;
RA Czeko E., Seizl M., Augsberger C., Mielke T., Cramer P.;
RT "Iwr1 directs RNA polymerase II nuclear import.";
RL Mol. Cell 42:261-266(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Directs RNA polymerase II nuclear import. Binds RNA
CC polymerase II in the active center cleft between the two largest
CC subunits in the cytoplasm. Then uses an N-terminal bipartite nuclear
CC localization signal that may be recognized by karyopherin alpha to
CC direct the polymerase II complex nuclear import. In the nucleus, is
CC displaced from polymerase II complex by transcription initiation
CC factors and nucleic acids, enabling its export and recycling.
CC {ECO:0000269|PubMed:12663529, ECO:0000269|PubMed:16554755,
CC ECO:0000269|PubMed:20010803, ECO:0000269|PubMed:21504834}.
CC -!- SUBUNIT: Associates with RNA polymerase II. Part of a complex
CC consisting of RPB1, RBP2, RPB3, RPB4, RPB5, RPB7, SPT5, DST1 and IWR1.
CC {ECO:0000269|PubMed:16554755}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC nucleus and cytoplasm.
CC -!- DISRUPTION PHENOTYPE: Leads to a K1 killer toxin hypersensitivity and
CC pleiotropic effects on gene expression. {ECO:0000269|PubMed:19679657}.
CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the IWR1/SLC7A6OS family. {ECO:0000305}.
CC -!- CAUTION: Due to the effects of deletion on gene expression, was
CC originally thought to be a general transcription factor
CC (PubMed:19679657). Further studies clearly suggest that it is involved
CC in nuclear localization of the RNA polymerase II complex
CC (PubMed:21504834). {ECO:0000305|PubMed:19679657,
CC ECO:0000305|PubMed:21504834}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM97491.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA98683.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z74163; CAA98683.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY558163; AAS56489.1; -; Genomic_DNA.
DR EMBL; EF123147; ABM97491.1; ALT_INIT; mRNA.
DR EMBL; BK006938; DAA11745.1; -; Genomic_DNA.
DR PIR; S67658; S67658.
DR RefSeq; NP_010168.4; NM_001180174.1.
DR AlphaFoldDB; Q07532; -.
DR BioGRID; 31947; 279.
DR DIP; DIP-6726N; -.
DR IntAct; Q07532; 16.
DR MINT; Q07532; -.
DR STRING; 4932.YDL115C; -.
DR iPTMnet; Q07532; -.
DR MaxQB; Q07532; -.
DR PaxDb; Q07532; -.
DR PRIDE; Q07532; -.
DR EnsemblFungi; YDL115C_mRNA; YDL115C; YDL115C.
DR GeneID; 851442; -.
DR KEGG; sce:YDL115C; -.
DR SGD; S000002273; IWR1.
DR VEuPathDB; FungiDB:YDL115C; -.
DR eggNOG; KOG4852; Eukaryota.
DR HOGENOM; CLU_044104_0_0_1; -.
DR InParanoid; Q07532; -.
DR OMA; EYPRNEF; -.
DR BioCyc; YEAST:G3O-29515-MON; -.
DR PRO; PR:Q07532; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07532; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR InterPro; IPR040150; Iwr1.
DR InterPro; IPR013883; TF_Iwr1_dom.
DR PANTHER; PTHR28063; PTHR28063; 2.
DR Pfam; PF08574; Iwr1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..353
FT /note="RNA polymerase II nuclear localization protein IWR1"
FT /id="PRO_0000255269"
FT REGION 77..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 10..43
FT /note="Bipartite nuclear localization signal"
FT COMPBIAS 77..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 353 AA; 40640 MW; 243B018B36F60D76 CRC64;
MSTISTTTAP EFIRVKRRRD EDSVQALLID EGKRVKKQKF IFKLSKTVSS ESYQSEQESS
TPLLKLAHED HRHFVLEQRK KSRRDSDDEK SQQRLAAEGS TVDDDGLPPE INQMVNDYLK
LNKGVEKTER KKPSRKYFTG DSAKIASLPS LDYVFDIYHL EKIHDDEVAR YNNEKNIGFV
KIIEHIDLAL DEESDPNEAR SDDEDSNDEN YYQNDYPEDE DDDRSILFGS EGEDIAALGE
EIVIGVNKSR FSSWNDDKIQ GSNGYHDVEE EYGDLFNRLG GKSDVLKSIN SSNFIDLDGQ
EGEIEISDNE DDSDEGDDIE YPRNEFFPTD VDDPLAHHRD RIFHQLQKKI NRS
