NSR1_YEAST
ID NSR1_YEAST Reviewed; 414 AA.
AC P27476; D6VUT9;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Nuclear localization sequence-binding protein {ECO:0000305};
DE AltName: Full=p67 {ECO:0000303|PubMed:1706724};
GN Name=NSR1 {ECO:0000303|PubMed:1706724}; OrderedLocusNames=YGR159C;
GN ORFNames=G7001;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1706724; DOI=10.1083/jcb.113.1.1;
RA Lee W.-C., Xue Z., Melese T.;
RT "The NSR1 gene encodes a protein that specifically binds nuclear
RT localization sequences and has two RNA recognition motifs.";
RL J. Cell Biol. 113:1-12(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1644811; DOI=10.1016/s0021-9258(18)41993-x;
RA Kondo K., Inouye M.;
RT "Yeast NSR1 protein that has structural similarity to mammalian nucleolin
RT is involved in pre-rRNA processing.";
RL J. Biol. Chem. 267:16252-16258(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8585325; DOI=10.1002/yea.320111410;
RA Skala J., Nawrocki A., Goffeau A.;
RT "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT NSR1 genes and ten new open reading frames.";
RL Yeast 11:1421-1427(1995).
RN [4]
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 [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 DNA-BINDING.
RX PubMed=7800479; DOI=10.1093/nar/22.23.4906;
RA Lin J.-J., Zakian V.A.;
RT "Isolation and characterization of two Saccharomyces cerevisiae genes that
RT encode proteins that bind to (TG1-3)n single strand telomeric DNA in
RT vitro.";
RL Nucleic Acids Res. 22:4906-4913(1994).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [8]
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 [9]
RP SUBCELLULAR LOCATION, AND METHYLATION BY HMT1.
RX PubMed=12756332; DOI=10.1261/rna.5020803;
RA Xu C., Henry P.A., Setya A., Henry M.F.;
RT "In vivo analysis of nucleolar proteins modified by the yeast arginine
RT methyltransferase Hmt1/Rmt1p.";
RL RNA 9:746-759(2003).
RN [10]
RP PYROPHOSPHORYLATION.
RX PubMed=15604408; DOI=10.1126/science.1103344;
RA Saiardi A., Bhandari R., Resnick A.C., Snowman A.M., Snyder S.H.;
RT "Phosphorylation of proteins by inositol pyrophosphates.";
RL Science 306:2101-2105(2004).
RN [11]
RP PYROPHOSPHORYLATION.
RX PubMed=17873058; DOI=10.1073/pnas.0707338104;
RA Bhandari R., Saiardi A., Ahmadibeni Y., Snowman A.M., Resnick A.C.,
RA Kristiansen T.Z., Molina H., Pandey A., Werner J.K. Jr., Juluri K.R.,
RA Xu Y., Prestwich G.D., Parang K., Snyder S.H.;
RT "Protein pyrophosphorylation by inositol pyrophosphates is a
RT posttranslational event.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15305-15310(2007).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=23222640; DOI=10.1038/nsmb.2468;
RA Mitchell S.F., Jain S., She M., Parker R.;
RT "Global analysis of yeast mRNPs.";
RL Nat. Struct. Mol. Biol. 20:127-133(2013).
RN [13]
RP METHYLATION AT ARG-353; ARG-357; ARG-375; ARG-379 AND ARG-382.
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 [14]
RP METHYLATION AT ARG-353; ARG-379; ARG-382 AND ARG-386.
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 [15]
RP METHYLATION AT ARG-353; ARG-357; ARG-362; ARG-366; ARG-370; ARG-375;
RP ARG-379 AND ARG-382, AND PHOSPHORYLATION AT SER-93; SER-95; SER-96; SER-97;
RP SER-116; SER-127; SER-129; SER-131 AND SER-143.
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).
CC -!- FUNCTION: Involved in pre-rRNA processing (PubMed:1644811).
CC Specifically binds nuclear localization sequences (PubMed:1706724).
CC Candidate for a receptor at the nucleus that may be involved in both
CC RNA and protein transport (Probable). Binds telomeric sequences of the
CC type (TG[1-3])n in vitro (PubMed:7800479). {ECO:0000269|PubMed:1644811,
CC ECO:0000269|PubMed:1706724, ECO:0000269|PubMed:7800479,
CC ECO:0000305|PubMed:1706724}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1706724,
CC ECO:0000269|PubMed:23222640}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:12756332}.
CC -!- INDUCTION: In response to low temperature (By cold-shock).
CC -!- PTM: Methylated by HMT1, forming asymmetric dimethylarginines (DMA)
CC within a domain referred to as an RGG box, made up of repeated Gly-Gly
CC dipeptides interspersed with Arg and aromatic residues.
CC {ECO:0000269|PubMed:12756332}.
CC -!- PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) (PubMed:15604408). Serine pyrophosphorylation is achieved by
CC Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate
CC from a inositol pyrophosphate to a pre-phosphorylated serine residue
CC (PubMed:15604408, PubMed:17873058). {ECO:0000269|PubMed:15604408,
CC ECO:0000269|PubMed:17873058}.
CC -!- MISCELLANEOUS: Present with 77400 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; X57185; CAA40472.1; -; Genomic_DNA.
DR EMBL; X85807; CAA59817.1; -; Genomic_DNA.
DR EMBL; Z72944; CAA97173.1; -; Genomic_DNA.
DR EMBL; Z72946; CAA97180.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08250.1; -; Genomic_DNA.
DR PIR; A39205; A39205.
DR RefSeq; NP_011675.1; NM_001181288.1.
DR AlphaFoldDB; P27476; -.
DR SMR; P27476; -.
DR BioGRID; 33407; 135.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-5537N; -.
DR IntAct; P27476; 52.
DR MINT; P27476; -.
DR STRING; 4932.YGR159C; -.
DR iPTMnet; P27476; -.
DR MaxQB; P27476; -.
DR PaxDb; P27476; -.
DR PRIDE; P27476; -.
DR EnsemblFungi; YGR159C_mRNA; YGR159C; YGR159C.
DR GeneID; 853064; -.
DR KEGG; sce:YGR159C; -.
DR SGD; S000003391; NSR1.
DR VEuPathDB; FungiDB:YGR159C; -.
DR eggNOG; KOG4210; Eukaryota.
DR GeneTree; ENSGT00940000170607; -.
DR HOGENOM; CLU_026791_0_0_1; -.
DR InParanoid; P27476; -.
DR OMA; NYGQEAS; -.
DR BioCyc; YEAST:G3O-30859-MON; -.
DR PRO; PR:P27476; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P27476; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000028; P:ribosomal small subunit assembly; TAS:SGD.
DR GO; GO:0006364; P:rRNA processing; TAS:SGD.
DR CDD; cd12447; RRM1_gar2; 1.
DR CDD; cd12448; RRM2_gar2; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034272; Gar2_RRM1.
DR InterPro; IPR034276; Gar2_RRM2.
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 DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; rRNA processing; Stress response.
FT CHAIN 1..414
FT /note="Nuclear localization sequence-binding protein"
FT /id="PRO_0000081690"
FT DOMAIN 168..246
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 267..345
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..384
FT /note="RGG-box"
FT REGION 366..384
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 353
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:26081071, ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 357
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 357
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 362
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 362
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 366
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 366
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 370
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 375
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 375
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 379
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 379
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 382
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 382
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:26081071, ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 386
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779"
SQ SEQUENCE 414 AA; 44535 MW; 90DEEE7BBC20BC0C CRC64;
MAKTTKVKGN KKEVKASKQA KEEKAKAVSS SSSESSSSSS SSSESESESE SESESSSSSS
SSDSESSSSS SSDSESEAET KKEESKDSSS SSSDSSSDEE EEEEKEETKK EESKESSSSD
SSSSSSSDSE SEKEESNDKK RKSEDAEEEE DEESSNKKQK NEETEEPATI FVGRLSWSID
DEWLKKEFEH IGGVIGARVI YERGTDRSRG YGYVDFENKS YAEKAIQEMQ GKEIDGRPIN
CDMSTSKPAG NNDRAKKFGD TPSEPSDTLF LGNLSFNADR DAIFELFAKH GEVVSVRIPT
HPETEQPKGF GYVQFSNMED AKKALDALQG EYIDNRPVRL DFSSPRPNND GGRGGSRGFG
GRGGGRGGNR GFGGRGGARG GRGGFRPSGS GANTAPLGRS RNTASFAGSK KTFD
