SDA1_YEAST
ID SDA1_YEAST Reviewed; 767 AA.
AC P53313; D6VV25;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein SDA1;
DE AltName: Full=Severe depolymerization of actin protein 1;
GN Name=SDA1; OrderedLocusNames=YGR245C;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9133742;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<373::aid-yea82>3.0.co;2-v;
RA Feroli F., Carignani G., Pavanello A., Guerreiro P., Azevedo D.,
RA Rodrigues-Pousada C., Melchioretto P., Panzeri L., Agostoni Carbone M.L.;
RT "Analysis of a 17.9 kb region from Saccharomyces cerevisiae chromosome VII
RT reveals the presence of eight open reading frames, including BRF1
RT (TFIIIB70) and GCN5 genes.";
RL Yeast 13:373-377(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 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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10704371; DOI=10.1242/jcs.113.7.1199;
RA Buscemi G., Saracino F., Masnada D., Carbone M.L.;
RT "The Saccharomyces cerevisiae SDA1 gene is required for actin cytoskeleton
RT organization and cell cycle progression.";
RL J. Cell Sci. 113:1199-1211(2000).
RN [6]
RP FUNCTION.
RX PubMed=11160833; DOI=10.1091/mbc.12.1.201;
RA Zimmerman Z.A., Kellogg D.R.;
RT "The Sda1 protein is required for passage through start.";
RL Mol. Biol. Cell 12:201-219(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11583615; DOI=10.1016/s1097-2765(01)00342-2;
RA Bassler J., Grandi P., Gadal O., Lessmann T., Petfalski E., Tollervey D.,
RA Lechner J., Hurt E.;
RT "Identification of a 60S preribosomal particle that is closely linked to
RT nuclear export.";
RL Mol. Cell 8:517-529(2001).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12374754; DOI=10.1093/emboj/cdf547;
RA Nissan T.A., Bassler J., Petfalski E., Tollervey D., Hurt E.;
RT "60S pre-ribosome formation viewed from assembly in the nucleolus until
RT export to the cytoplasm.";
RL EMBO J. 21:5539-5547(2002).
RN [9]
RP FUNCTION.
RX PubMed=15107621;
RA Saracino F., Bassler J., Muzzini D., Hurt E., Agostoni Carbone M.L.;
RT "The yeast kinase Swe1 is required for proper entry into cell cycle after
RT arrest due to ribosome biogenesis and protein synthesis defects.";
RL Cell Cycle 3:648-654(2004).
RN [10]
RP POSSIBLE FUNCTION.
RX PubMed=15116429; DOI=10.1002/yea.1063;
RA Davydenko S.G., Juselius J.K., Munder T., Bogengruber E., Jaentti J.,
RA Keraenen S.;
RT "Screening for novel essential genes of Saccharomyces cerevisiae involved
RT in protein secretion.";
RL Yeast 21:463-471(2004).
RN [11]
RP FUNCTION.
RX PubMed=16541108; DOI=10.1038/sj.emboj.7601035;
RA Dez C., Houseley J., Tollervey D.;
RT "Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar
RT region of Saccharomyces cerevisiae.";
RL EMBO J. 25:1534-1546(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, 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).
CC -!- FUNCTION: Required for 60S pre-ribosomal subunits export to the
CC cytoplasm. May also be required for 60S ribosomal subunit maturation
CC and accumulation. Involved in G1 events and passage through start, and
CC possibly actin cytoskeleton organization. {ECO:0000269|PubMed:10704371,
CC ECO:0000269|PubMed:11160833, ECO:0000269|PubMed:12374754,
CC ECO:0000269|PubMed:15107621, ECO:0000269|PubMed:16541108}.
CC -!- SUBUNIT: Associated with the 60S pre-ribosomal particles. Interacts
CC with NAP1.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10704371,
CC ECO:0000269|PubMed:12374754}.
CC -!- MISCELLANEOUS: Present with 3640 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SDA1 family. {ECO:0000305}.
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DR EMBL; Y07703; CAA68967.1; -; Genomic_DNA.
DR EMBL; Z73030; CAA97274.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08336.1; -; Genomic_DNA.
DR PIR; S64571; S64571.
DR RefSeq; NP_011761.3; NM_001181374.3.
DR PDB; 5FL8; EM; 9.50 A; r=1-767.
DR PDB; 5JCS; EM; 9.50 A; r=1-767.
DR PDB; 6YLG; EM; 3.00 A; t=1-767.
DR PDB; 6YLH; EM; 3.10 A; t=1-767.
DR PDBsum; 5FL8; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR AlphaFoldDB; P53313; -.
DR SMR; P53313; -.
DR BioGRID; 33496; 276.
DR DIP; DIP-5267N; -.
DR IntAct; P53313; 38.
DR MINT; P53313; -.
DR STRING; 4932.YGR245C; -.
DR iPTMnet; P53313; -.
DR MaxQB; P53313; -.
DR PaxDb; P53313; -.
DR PRIDE; P53313; -.
DR EnsemblFungi; YGR245C_mRNA; YGR245C; YGR245C.
DR GeneID; 853160; -.
DR KEGG; sce:YGR245C; -.
DR SGD; S000003477; SDA1.
DR VEuPathDB; FungiDB:YGR245C; -.
DR eggNOG; KOG2229; Eukaryota.
DR GeneTree; ENSGT00390000010355; -.
DR HOGENOM; CLU_009161_2_1_1; -.
DR InParanoid; P53313; -.
DR OMA; AMYKTYK; -.
DR BioCyc; YEAST:G3O-30920-MON; -.
DR PRO; PR:P53313; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53313; protein.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027312; Sda1.
DR InterPro; IPR007949; SDA1_dom.
DR InterPro; IPR012977; Uncharacterised_NUC130/133_N.
DR PANTHER; PTHR12730; PTHR12730; 1.
DR Pfam; PF08158; NUC130_3NT; 1.
DR Pfam; PF05285; SDA1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Ribosome biogenesis; Transport.
FT CHAIN 1..767
FT /note="Protein SDA1"
FT /id="PRO_0000202858"
FT REGION 500..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..576
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..628
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 767 AA; 86618 MW; 3EC5065338385346 CRC64;
MGRRSRAAML PTNIILLQNL VKRDPESYQE EFLQQYAHYE SLRDIFMLNG LAGGDSAAAT
NGLDVGNGSS TMAGTNGTTM STSTSQLIEL VGFVSQVCSC FPRETANFPS ELKQLLLEHH
KSLPFELKEK ILSCLTMLRN KDVITAEELI QSLFPLLVAY SSHGNSLGVN SHAKELRKII
YTNLISLLKS CNTNGKNQKL NKSTQAVCFN LLDQPDSQGI WATKLTRELW RRGIWDDSRT
VEIMTQAALH QDVKIVMSGV MFFLDADRER EENFEENSED EDGFDLDALR HKMQVNKKTG
RRGKKLENAI KTVKKKKKNG PGAPQGYLNF SAIHLLRDPQ GFAEKLFKEH LSGKTKNKFD
MEQKISLMQL LSRLIGTHKL IVLGIYTFFL KYLTPKQRDV TRIMSACAQA CHDLVPPEVI
NVMVRKIADE FVSDGVANEV AAAGINTIRE ICSRAPLAID EILLQDLVEY KGSKAKGVNM
AAKSLIALYR DVAPEMLKKK DRGKNAAMEV QEAKKGGKDS KRPQFGADNS VQGIAGIELL
AKWKKEHGEE SENEDADANW EVDVDSEEDD VDGEWVTMDS DKEYDVDMED SDDEKDNAKG
KESDSDLELS DDDDEKEVKD EQEDADIDPE AAFREIASTR ILTPADFAKL QELRNEESVA
KIMGIHKQDK REELVDASTL TGPIKYKQSR EERLQKVLEG REGRDKFGSR RGKRDNMRST
TNREKERRKN FVMSIHKRSV RGKQKMSLRD KQKVLRAHIT KQKKKGY
