NOP3_YEAST
ID NOP3_YEAST Reviewed; 414 AA.
AC Q01560; D6VT60;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Serine/arginine (SR)-type shuttling mRNA binding protein NPL3 {ECO:0000305};
DE AltName: Full=Mitochondrial targeting suppressor 1 protein {ECO:0000303|PubMed:8224861};
DE AltName: Full=Nuclear polyadenylated RNA-binding protein 1 {ECO:0000303|PubMed:7962083};
DE AltName: Full=Nuclear protein localization protein 3 {ECO:0000303|PubMed:1392078};
DE AltName: Full=Polyadenylate-binding protein NPL3 {ECO:0000305};
GN Name=NPL3 {ECO:0000303|PubMed:1392078};
GN Synonyms=MTR13, MTS1 {ECO:0000303|PubMed:8224861},
GN NAB1 {ECO:0000303|PubMed:7962083}, NOP3 {ECO:0000303|PubMed:1429834};
GN OrderedLocusNames=YDR432W; ORFNames=D9461.19;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=1429834; DOI=10.1083/jcb.119.4.737;
RA Russell I.D., Tollervey D.;
RT "NOP3 is an essential yeast protein which is required for pre-rRNA
RT processing.";
RL J. Cell Biol. 119:737-747(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1392078; DOI=10.1091/mbc.3.8.875;
RA Bossie M.A., Dehoratious C., Barcelo G., Silver P.;
RT "A mutant nuclear protein with similarity to RNA binding proteins
RT interferes with nuclear import in yeast.";
RL Mol. Biol. Cell 3:875-893(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8224861; DOI=10.1016/0378-1119(93)90193-7;
RA Ellis E.M., Reid G.A.;
RT "The Saccharomyces cerevisiae MTS1 gene encodes a putative RNA-binding
RT protein involved in mitochondrial protein targeting.";
RL Gene 132:175-183(1993).
RN [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION, AND BINDING TO POLYADENYLATED RNA.
RX PubMed=7962083; DOI=10.1083/jcb.127.5.1173;
RA Wilson S.M., Datar K.V., Paddy M.R., Swedlow J.R., Swanson M.S.;
RT "Characterization of nuclear polyadenylated RNA-binding proteins in
RT Saccharomyces cerevisiae.";
RL J. Cell Biol. 127:1173-1184(1994).
RN [7]
RP FUNCTION.
RX PubMed=8675010; DOI=10.1101/gad.10.10.1233;
RA Lee M.S., Henry M., Silver P.A.;
RT "A protein that shuttles between the nucleus and the cytoplasm is an
RT important mediator of RNA export.";
RL Genes Dev. 10:1233-1246(1996).
RN [8]
RP SUBCELLULAR LOCATION, AND METHYLATION BY HMT1.
RX PubMed=9499403; DOI=10.1101/gad.12.5.679;
RA Shen E.C., Henry M.F., Weiss V.H., Valentini S.R., Silver P.A., Lee M.S.;
RT "Arginine methylation facilitates the nuclear export of hnRNP proteins.";
RL Genes Dev. 12:679-691(1998).
RN [9]
RP INTERACTION WITH RRP6.
RX PubMed=10611239; DOI=10.1128/mcb.20.2.604-616.2000;
RA Burkard K.T.D., Butler J.S.;
RT "A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with
RT Poly(A) polymerase and the hnRNA protein Npl3p.";
RL Mol. Cell. Biol. 20:604-616(2000).
RN [10]
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 [11]
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 [12]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-411.
RX PubMed=14676199; DOI=10.1074/jbc.c300522200;
RA Haecker S., Krebber H.;
RT "Differential export requirements for shuttling serine/arginine-type mRNA-
RT binding proteins.";
RL J. Biol. Chem. 279:5049-5052(2004).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15542855; DOI=10.1128/mcb.24.23.10479-10491.2004;
RA Windgassen M., Sturm D., Cajigas I.J., Gonzalez C.I., Seedorf M.,
RA Bastians H., Krebber H.;
RT "Yeast shuttling SR proteins Npl3p, Gbp2p, and Hrb1p are part of the
RT translating mRNPs, and Npl3p can function as a translational repressor.";
RL Mol. Cell. Biol. 24:10479-10491(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [15]
RP FUNCTION.
RX PubMed=19061647; DOI=10.1016/j.molcel.2008.11.013;
RA Kress T.L., Krogan N.J., Guthrie C.;
RT "A single SR-like protein, Npl3, promotes pre-mRNA splicing in budding
RT yeast.";
RL Mol. Cell 32:727-734(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-224, AND
RP IDENTIFICATION BY 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, 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 [18]
RP FUNCTION.
RX PubMed=23209445; DOI=10.1371/journal.pgen.1003101;
RA Moehle E.A., Ryan C.J., Krogan N.J., Kress T.L., Guthrie C.;
RT "The yeast SR-like protein Npl3 links chromatin modification to mRNA
RT processing.";
RL PLoS Genet. 8:e1003101-e1003101(2012).
RN [19]
RP METHYLATION AT ARG-307; ARG-314 AND ARG-321.
RX PubMed=26081071; DOI=10.1002/pmic.201500075;
RA Yagoub D., Hart-Smith G., Moecking J., Erce M.A., Wilkins M.R.;
RT "Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively
RT methylated and are substrates of the arginine methyltransferase Hmt1p.";
RL Proteomics 15:3209-3218(2015).
RN [20]
RP METHYLATION AT ARG-307; ARG-314; ARG-321; ARG-329; ARG-337; ARG-344;
RP ARG-351; ARG-358; ARG-363; ARG-377; ARG-384 AND ARG-391.
RX PubMed=26046779; DOI=10.1002/pmic.201500032;
RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA Pears C., Schofield C.J., Kessler B.M.;
RT "Expanding the yeast protein arginine methylome.";
RL Proteomics 15:3232-3243(2015).
RN [21]
RP SUBCELLULAR LOCATION.
RX PubMed=26777405; DOI=10.1016/j.cell.2015.12.038;
RA Jain S., Wheeler J.R., Walters R.W., Agrawal A., Barsic A., Parker R.;
RT "ATPase-modulated stress granules contain a diverse proteome and
RT substructure.";
RL Cell 164:487-498(2016).
RN [22]
RP METHYLATION AT ARG-288; ARG-290; ARG-294; ARG-298; ARG-302; ARG-307;
RP ARG-314; ARG-344; ARG-351; ARG-358; ARG-363; ARG-377; ARG-384 AND ARG-391,
RP AND PHOSPHORYLATION AT SER-15; SER-79; SER-212; SER-224 AND SER-356.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
RN [23] {ECO:0007744|PDB:2JD5}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 408-414.
RX PubMed=17239901; DOI=10.1016/j.jmb.2006.12.031;
RA Lukasiewicz R., Nolen B., Adams J.A., Ghosh G.;
RT "The RGG domain of Npl3p recruits Sky1p through docking interactions.";
RL J. Mol. Biol. 367:249-261(2007).
RN [24] {ECO:0007744|PDB:2OSQ, ECO:0007744|PDB:2OSR}
RP STRUCTURE BY NMR OF 194-280.
RX PubMed=18022637; DOI=10.1016/j.jmb.2007.09.029;
RA Deka P., Bucheli M.E., Moore C., Buratowski S., Varani G.;
RT "Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end
RT processing signals.";
RL J. Mol. Biol. 375:136-150(2008).
RN [25] {ECO:0007744|PDB:2JVO, ECO:0007744|PDB:2JVR}
RP STRUCTURE BY NMR OF 193-282.
RX PubMed=17936301; DOI=10.1016/j.jmb.2007.09.030;
RA Skrisovska L., Allain F.H.;
RT "Improved segmental isotope labeling methods for the NMR study of
RT multidomain or large proteins: application to the RRMs of Npl3p and hnRNP
RT L.";
RL J. Mol. Biol. 375:151-164(2008).
CC -!- FUNCTION: Involved in mRNA processing and export (PubMed:1429834,
CC PubMed:8675010, PubMed:15542855, PubMed:19061647). Required for
CC efficient splicing of a large set of pre-mRNAs by efficient co-
CC transcriptional recruitment of the splicing machinery (PubMed:19061647,
CC PubMed:23209445). Remains associated with the mRNP during early steps
CC of translation elongation (PubMed:15542855).
CC {ECO:0000269|PubMed:1429834, ECO:0000269|PubMed:15542855,
CC ECO:0000269|PubMed:19061647, ECO:0000269|PubMed:23209445,
CC ECO:0000269|PubMed:8675010}.
CC -!- SUBUNIT: Interacts with RRP6. {ECO:0000269|PubMed:10611239}.
CC -!- INTERACTION:
CC Q01560; P40507: AIR1; NbExp=3; IntAct=EBI-12114, EBI-25083;
CC Q01560; P25555: GBP2; NbExp=3; IntAct=EBI-12114, EBI-7410;
CC Q01560; P38074: HMT1; NbExp=9; IntAct=EBI-12114, EBI-8394;
CC Q01560; Q01560: NPL3; NbExp=3; IntAct=EBI-12114, EBI-12114;
CC Q01560; P04456: RPL25; NbExp=2; IntAct=EBI-12114, EBI-15308;
CC Q01560; P39940: RSP5; NbExp=2; IntAct=EBI-12114, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14676199,
CC ECO:0000269|PubMed:9499403}. Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14676199, ECO:0000269|PubMed:7962083,
CC ECO:0000269|PubMed:9499403}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:26777405}. Note=Nuclear at steady state and its
CC import is mediated by the karyopherin MTR10 (PubMed:14676199,
CC PubMed:15542855). Export is dependent on active transcription and the
CC export of mRNAs in general (PubMed:8675010, PubMed:14676199).
CC {ECO:0000269|PubMed:14676199, ECO:0000269|PubMed:15542855,
CC ECO:0000269|PubMed:8675010}.
CC -!- PTM: Methylated by HMT1. The methylation is required for nuclear
CC export. {ECO:0000269|PubMed:9499403}.
CC -!- MISCELLANEOUS: Present with 78700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRM GAR family. {ECO:0000305}.
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DR EMBL; X66019; CAA46817.1; -; Genomic_DNA.
DR EMBL; M86731; AAA34818.1; -; Genomic_DNA.
DR EMBL; X70951; CAA50291.1; -; Genomic_DNA.
DR EMBL; U33007; AAB64865.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12270.1; -; Genomic_DNA.
DR PIR; JN0866; JN0866.
DR RefSeq; NP_010720.3; NM_001180740.3.
DR PDB; 2JD5; X-ray; 2.50 A; C=408-414.
DR PDB; 2JVO; NMR; -; A=116-201.
DR PDB; 2JVR; NMR; -; A=193-282.
DR PDB; 2OSQ; NMR; -; A=121-194.
DR PDB; 2OSR; NMR; -; A=194-280.
DR PDBsum; 2JD5; -.
DR PDBsum; 2JVO; -.
DR PDBsum; 2JVR; -.
DR PDBsum; 2OSQ; -.
DR PDBsum; 2OSR; -.
DR AlphaFoldDB; Q01560; -.
DR BMRB; Q01560; -.
DR SMR; Q01560; -.
DR BioGRID; 32489; 1174.
DR DIP; DIP-6464N; -.
DR IntAct; Q01560; 40.
DR MINT; Q01560; -.
DR STRING; 4932.YDR432W; -.
DR iPTMnet; Q01560; -.
DR MaxQB; Q01560; -.
DR PaxDb; Q01560; -.
DR PRIDE; Q01560; -.
DR EnsemblFungi; YDR432W_mRNA; YDR432W; YDR432W.
DR GeneID; 852042; -.
DR KEGG; sce:YDR432W; -.
DR SGD; S000002840; NPL3.
DR VEuPathDB; FungiDB:YDR432W; -.
DR eggNOG; KOG0106; Eukaryota.
DR HOGENOM; CLU_054994_1_0_1; -.
DR InParanoid; Q01560; -.
DR OMA; HRMQISG; -.
DR BioCyc; YEAST:G3O-29970-MON; -.
DR EvolutionaryTrace; Q01560; -.
DR PRO; PR:Q01560; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q01560; protein.
DR GO; GO:0005737; C:cytoplasm; IMP:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0008143; F:poly(A) binding; IDA:SGD.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IPI:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:2000805; P:negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled; IDA:SGD.
DR GO; GO:0017148; P:negative regulation of translation; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006415; P:translational termination; IMP:SGD.
DR CDD; cd12340; RBD_RRM1_NPL3; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034166; Npl3_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methylation; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding.
FT CHAIN 1..414
FT /note="Serine/arginine (SR)-type shuttling mRNA binding
FT protein NPL3"
FT /id="PRO_0000081676"
FT DOMAIN 125..195
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 200..275
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..64
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 288
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 290
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 294
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 298
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 302
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 307
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 307
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:26081071, ECO:0000269|PubMed:33856219"
FT MOD_RES 314
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 314
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:26081071, ECO:0000269|PubMed:33856219"
FT MOD_RES 321
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:26081071"
FT MOD_RES 329
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779"
FT MOD_RES 337
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779"
FT MOD_RES 344
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 351
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 351
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 358
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 358
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 363
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 363
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 377
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 377
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 384
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 384
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 391
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MUTAGEN 411
FT /note="S->A: Shifts localization of the protein to the
FT cytoplasm at steady state."
FT /evidence="ECO:0000269|PubMed:15542855"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:2JVO"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:2JVO"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2JVO"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2JVO"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2JVO"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:2JVO"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2JVO"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2JVR"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:2JVR"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:2JVR"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2JVR"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:2JVR"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:2JVR"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2JVR"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:2JVR"
SQ SEQUENCE 414 AA; 45407 MW; 024439E4B6578787 CRC64;
MSEAQETHVE QLPESVVDAP VEEQHQEPPQ APDAPQEPQV PQESAPQESA PQEPPAPQEQ
NDVPPPSNAP IYEGEESHSV QDYQEAHQHH QPPEPQPYYP PPPPGEHMHG RPPMHHRQEG
ELSNTRLFVR PFPLDVQESE LNEIFGPFGP MKEVKILNGF AFVEFEEAES AAKAIEEVHG
KSFANQPLEV VYSKLPAKRY RITMKNLPEG CSWQDLKDLA RENSLETTFS SVNTRDFDGT
GALEFPSEEI LVEALERLNN IEFRGSVITV ERDDNPPPIR RSNRGGFRGR GGFRGGFRGG
FRGGFSRGGF GGPRGGFGGP RGGYGGYSRG GYGGYSRGGY GGSRGGYDSP RGGYDSPRGG
YSRGGYGGPR NDYGPPRGSY GGSRGGYDGP RGDYGPPRDA YRTRDAPRER SPTR
