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Nucleolar protein 3 (Mitochondrial targeting suppressor 1 protein) (Nuclear polyadenylated RNA-binding protein 1)

 NOP3_YEAST              Reviewed;         414 AA.
Q01560; D6VT60;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
25-APR-2018, entry version 190.
RecName: Full=Nucleolar protein 3;
AltName: Full=Mitochondrial targeting suppressor 1 protein;
AltName: Full=Nuclear polyadenylated RNA-binding protein 1;
Name=NPL3; Synonyms=MTR13, MTS1, NAB1, NOP3;
OrderedLocusNames=YDR432W; ORFNames=D9461.19;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1429834; DOI=10.1083/jcb.119.4.737;
Russell I.D., Tollervey D.;
"NOP3 is an essential yeast protein which is required for pre-rRNA
processing.";
J. Cell Biol. 119:737-747(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1392078; DOI=10.1091/mbc.3.8.875;
Bossie M.A., Dehoratious C., Barcelo G., Silver P.;
"A mutant nuclear protein with similarity to RNA binding proteins
interferes with nuclear import in yeast.";
Mol. Biol. Cell 3:875-893(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8224861; DOI=10.1016/0378-1119(93)90193-7;
Ellis E.M., Reid G.A.;
"The Saccharomyces cerevisiae MTS1 gene encodes a putative RNA-binding
protein involved in mitochondrial protein targeting.";
Gene 132:175-183(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
SUBCELLULAR LOCATION, AND BINDING TO POLYADENYLATED RNA.
PubMed=7962083; DOI=10.1083/jcb.127.5.1173;
Wilson S.M., Datar K.V., Paddy M.R., Swedlow J.R., Swanson M.S.;
"Characterization of nuclear polyadenylated RNA-binding proteins in
Saccharomyces cerevisiae.";
J. Cell Biol. 127:1173-1184(1994).
[7]
INTERACTION WITH RRP6.
PubMed=10611239; DOI=10.1128/MCB.20.2.604-616.2000;
Burkard K.T.D., Butler J.S.;
"A nuclear 3'-5' exonuclease involved in mRNA degradation interacts
with Poly(A) polymerase and the hnRNA protein Npl3p.";
Mol. Cell. Biol. 20:604-616(2000).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-224, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Required for pre-rRNA processing and nuclear import as
well as mitochondrial protein targeting. Binds to poly(A).
-!- SUBUNIT: Interacts with RRP6. {ECO:0000269|PubMed:10611239}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-12114, EBI-12114;
P40507:AIR1; NbExp=3; IntAct=EBI-12114, EBI-25083;
P38074:HMT1; NbExp=9; IntAct=EBI-12114, EBI-8394;
P04456:RPL25; NbExp=2; IntAct=EBI-12114, EBI-15308;
P39940:RSP5; NbExp=2; IntAct=EBI-12114, EBI-16219;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:7962083}.
-!- MISCELLANEOUS: Present with 78700 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the RRM GAR family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X66019; CAA46817.1; -; Genomic_DNA.
EMBL; M86731; AAA34818.1; -; Genomic_DNA.
EMBL; X70951; CAA50291.1; -; Genomic_DNA.
EMBL; U33007; AAB64865.1; -; Genomic_DNA.
EMBL; BK006938; DAA12270.1; -; Genomic_DNA.
PIR; JN0866; JN0866.
RefSeq; NP_010720.3; NM_001180740.3.
PDB; 2JD5; X-ray; 2.50 A; C=408-414.
PDB; 2JVO; NMR; -; A=116-201.
PDB; 2JVR; NMR; -; A=193-282.
PDB; 2OSQ; NMR; -; A=121-194.
PDB; 2OSR; NMR; -; A=194-280.
PDBsum; 2JD5; -.
PDBsum; 2JVO; -.
PDBsum; 2JVR; -.
PDBsum; 2OSQ; -.
PDBsum; 2OSR; -.
ProteinModelPortal; Q01560; -.
SMR; Q01560; -.
BioGrid; 32489; 1142.
DIP; DIP-6464N; -.
IntAct; Q01560; 56.
MINT; Q01560; -.
STRING; 4932.YDR432W; -.
iPTMnet; Q01560; -.
MaxQB; Q01560; -.
PaxDb; Q01560; -.
PRIDE; Q01560; -.
EnsemblFungi; YDR432W; YDR432W; YDR432W.
GeneID; 852042; -.
KEGG; sce:YDR432W; -.
EuPathDB; FungiDB:YDR432W; -.
SGD; S000002840; NPL3.
GeneTree; ENSGT00910000144049; -.
InParanoid; Q01560; -.
KO; K14651; -.
OMA; YYDSTGY; -.
OrthoDB; EOG092C5ATD; -.
BioCyc; YEAST:G3O-29970-MONOMER; -.
Reactome; R-SCE-72165; mRNA Splicing - Minor Pathway.
EvolutionaryTrace; Q01560; -.
PRO; PR:Q01560; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IMP:SGD.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003729; F:mRNA binding; IDA:SGD.
GO; GO:0008143; F:poly(A) binding; IDA:SGD.
GO; GO:0000993; F:RNA polymerase II core binding; IPI:SGD.
GO; GO:0006406; P:mRNA export from nucleus; IGI:SGD.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
GO; GO:2000805; P:negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled; IDA:SGD.
GO; GO:0017148; P:negative regulation of translation; IDA:SGD.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
GO; GO:0006415; P:translational termination; IMP:SGD.
CDD; cd12340; RBD_RRM1_NPL3; 1.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR034166; Npl3_RRM1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ribonucleoprotein; Ribosome biogenesis;
RNA-binding; rRNA processing.
CHAIN 1 414 Nucleolar protein 3.
/FTId=PRO_0000081676.
DOMAIN 125 195 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 200 275 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 280 398 Arg/Gly-rich.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
STRAND 125 129 {ECO:0000244|PDB:2JVO}.
HELIX 138 145 {ECO:0000244|PDB:2JVO}.
TURN 146 148 {ECO:0000244|PDB:2JVO}.
STRAND 153 157 {ECO:0000244|PDB:2JVO}.
STRAND 160 164 {ECO:0000244|PDB:2JVO}.
HELIX 168 178 {ECO:0000244|PDB:2JVO}.
STRAND 189 192 {ECO:0000244|PDB:2JVO}.
STRAND 200 205 {ECO:0000244|PDB:2JVR}.
HELIX 213 223 {ECO:0000244|PDB:2JVR}.
STRAND 228 231 {ECO:0000244|PDB:2JVR}.
STRAND 236 238 {ECO:0000244|PDB:2JVR}.
STRAND 241 247 {ECO:0000244|PDB:2JVR}.
HELIX 248 257 {ECO:0000244|PDB:2JVR}.
STRAND 261 263 {ECO:0000244|PDB:2JVR}.
STRAND 266 273 {ECO:0000244|PDB:2JVR}.
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


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