NSA1_YEAST
ID NSA1_YEAST Reviewed; 463 AA.
AC P53136; D6VU36;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ribosome biogenesis protein NSA1;
DE AltName: Full=NOP7-associated protein 1;
GN Name=NSA1; OrderedLocusNames=YGL111W; ORFNames=G2990;
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].
RX PubMed=9046090;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<85::aid-yea53>3.0.co;2-e;
RA Paoluzi S., Minenkova O., Castagnoli L.;
RT "The genes encoding the transcription factor yTAFII60, the G4p1 protein and
RT a putative glucose transporter are contained in a 12.3 kb DNA fragment on
RT the left arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:85-91(1997).
RN [2]
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 [3]
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 [4]
RP IDENTIFICATION IN THE PRE-66S RIBOSOMAL PARTICLE, INTERACTION WITH NOP7,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11583614; DOI=10.1016/s1097-2765(01)00344-6;
RA Harnpicharnchai P., Jakovljevic J., Horsey E., Miles T., Roman J., Rout M.,
RA Meagher D., Imai B., Guo Y., Brame C.J., Shabanowitz J., Hunt D.F.,
RA Woolford J.L. Jr.;
RT "Composition and functional characterization of yeast 66S ribosome assembly
RT intermediates.";
RL Mol. Cell 8:505-515(2001).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION IN THE PRE-66S RIBOSOMAL PARTICLE, INTERACTION WITH RRP1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15100437; DOI=10.1261/rna.5255804;
RA Horsey E.W., Jakovljevic J., Miles T.D., Harnpicharnchai P.,
RA Woolford J.L. Jr.;
RT "Role of the yeast Rrp1 protein in the dynamics of pre-ribosome
RT maturation.";
RL RNA 10:813-827(2004).
RN [8]
RP INTERACTION WITH RRP5, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15769876; DOI=10.1261/rna.7200205;
RA De Marchis M.L., Giorgi A., Schinina M.E., Bozzoni I., Fatica A.;
RT "Rrp15p, a novel component of pre-ribosomal particles required for 60S
RT ribosome subunit maturation.";
RL RNA 11:495-502(2005).
RN [9]
RP FUNCTION.
RX PubMed=16544271; DOI=10.1002/yea.1353;
RA Wade C.H., Umbarger M.A., McAlear M.A.;
RT "The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains
RT over 200 genes.";
RL Yeast 23:293-306(2006).
RN [10]
RP INTERACTION WITH NOP7, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17443350; DOI=10.1007/s00438-007-0233-1;
RA Fuentes J.L., Datta K., Sullivan S.M., Walker A., Maddock J.R.;
RT "In vivo functional characterization of the Saccharomyces cerevisiae 60S
RT biogenesis GTPase Nog1.";
RL Mol. Genet. Genomics 278:105-123(2007).
RN [11] {ECO:0007744|PDB:5SUI, ECO:0007744|PDB:5SUM}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 1-434.
RX PubMed=28416111; DOI=10.1016/j.str.2017.03.008;
RA Lo Y.H., Romes E.M., Pillon M.C., Sobhany M., Stanley R.E.;
RT "Structural Analysis Reveals Features of Ribosome Assembly Factor
RT Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2.";
RL Structure 25:762-772(2017).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit.
CC {ECO:0000269|PubMed:16544271}.
CC -!- SUBUNIT: Component of the pre-66S ribosomal particle. Interacts with
CC NOP7, RRP1 and RRP5. {ECO:0000269|PubMed:11583614,
CC ECO:0000269|PubMed:15100437, ECO:0000269|PubMed:15769876,
CC ECO:0000269|PubMed:17443350}.
CC -!- INTERACTION:
CC P53136; Q02892: NOG1; NbExp=4; IntAct=EBI-23920, EBI-12105;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2740 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NSA1 family. {ECO:0000305}.
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DR EMBL; X97644; CAA66241.1; -; Genomic_DNA.
DR EMBL; Z72633; CAA96818.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07997.1; -; Genomic_DNA.
DR PIR; S64119; S64119.
DR RefSeq; NP_011404.1; NM_001180976.1.
DR PDB; 5SUI; X-ray; 1.30 A; A=1-434.
DR PDB; 5SUM; X-ray; 2.80 A; A/B=1-463.
DR PDB; 5Z3G; EM; 3.65 A; V=1-463.
DR PDB; 6C0F; EM; 3.70 A; A=1-463.
DR PDB; 6CB1; EM; 4.60 A; A=1-463.
DR PDB; 6EM1; EM; 3.60 A; 5=1-463.
DR PDB; 6EM3; EM; 3.20 A; 5=1-463.
DR PDB; 6EM4; EM; 4.10 A; 5=1-463.
DR PDB; 6EM5; EM; 4.30 A; 5=1-463.
DR PDB; 6EN7; X-ray; 2.40 A; A=1-463.
DR PDB; 7OHS; EM; 4.38 A; 5=1-463.
DR PDB; 7OHW; EM; 3.50 A; 5=1-463.
DR PDB; 7OHX; EM; 3.30 A; 5=1-463.
DR PDBsum; 5SUI; -.
DR PDBsum; 5SUM; -.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6EN7; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR AlphaFoldDB; P53136; -.
DR SMR; P53136; -.
DR BioGRID; 33140; 212.
DR DIP; DIP-6415N; -.
DR IntAct; P53136; 34.
DR MINT; P53136; -.
DR STRING; 4932.YGL111W; -.
DR MaxQB; P53136; -.
DR PaxDb; P53136; -.
DR PRIDE; P53136; -.
DR EnsemblFungi; YGL111W_mRNA; YGL111W; YGL111W.
DR GeneID; 852767; -.
DR KEGG; sce:YGL111W; -.
DR SGD; S000003079; NSA1.
DR VEuPathDB; FungiDB:YGL111W; -.
DR eggNOG; KOG3881; Eukaryota.
DR GeneTree; ENSGT00390000015119; -.
DR HOGENOM; CLU_033769_4_0_1; -.
DR InParanoid; P53136; -.
DR OMA; IWEAKNV; -.
DR BioCyc; YEAST:G3O-30609-MON; -.
DR PRO; PR:P53136; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53136; protein.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR DisProt; DP02195; -.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR037379; WDR74/Nsa1.
DR PANTHER; PTHR16038; PTHR16038; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Ribosome biogenesis;
KW rRNA processing.
FT CHAIN 1..463
FT /note="Ribosome biogenesis protein NSA1"
FT /id="PRO_0000202748"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:5SUI"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:5SUI"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5SUI"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 102..114
FT /evidence="ECO:0007829|PDB:5SUI"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:5SUM"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:5SUI"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:5SUI"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:5SUI"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 332..340
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:5SUI"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:5SUI"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:5SUI"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:5SUI"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:5SUI"
SQ SEQUENCE 463 AA; 51907 MW; 4BF4BECDBB689F1A CRC64;
MRLLVSCVDS GSIKEVLCNI GTDTSVQSAL QPFHVAPHLA EGLKAYVDRM WVISEDEAIL
ARNSGVVELV KISKHLKENE ALQVDPKGES KNEKSLSDDL PKFDISEFEI TSSVSDLFDD
AKLESLSSKS VKRTKLVDGF VTLCPIKKDS SNNTFVAATK SGLLHIIKKG EDKKLIKLAS
LGLKAPVEFL QLYDLEDTDT DKYIFAYGGE ENLIKLVEID SSFQSLKQIW EAKNVKNDRL
DMRVPVWPMA LRFLEPSPGK TEKGKLNYQF AAITRWSHLT KYSTQHGRKP FAQIDLLPNR
EPLSQMEVFD AKGENVVSSL GNFQSETFNE LNVITTDYKK NVFKFDGNGR MLGKVGRDDI
TGSSTYIHVH DGKYLLQGGL DRYVRIFDIK TNKMLVKVYV GSRINFIVML DDVEIEMPLS
PSAKAAKGKQ KRKVTELEED ADELWNKLEG KVAASKASKK SKI
