SN309_YEAST
ID SN309_YEAST Reviewed; 175 AA.
AC Q06091; D6W499;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Pre-mRNA-splicing factor SNT309;
DE AltName: Full=PRP19-associated complex protein 25;
DE AltName: Full=Synergistic to PRP19 mutation protein 309;
GN Name=SNT309; Synonyms=NTC25; OrderedLocusNames=YPR101W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX.
RX PubMed=9528791; DOI=10.1128/mcb.18.4.2196;
RA Chen H.-R., Jan S.-P., Tsao T.Y., Sheu Y.-J., Banroques J., Cheng S.-C.;
RT "Snt309p, a component of the Prp19p-associated complex that interacts with
RT Prp19p and associates with the spliceosome simultaneously with or
RT immediately after dissociation of U4 in the same manner as Prp19p.";
RL Mol. Cell. Biol. 18:2196-2204(1998).
RN [5]
RP FUNCTION.
RX PubMed=10318896; DOI=10.1073/pnas.96.10.5406;
RA Chen H.-R., Tsao T.Y., Chen C.-H., Tsai W.-Y., Her L.-S., Hsu M.M.-T.,
RA Cheng S.-C.;
RT "Snt309p modulates interactions of Prp19p with its associated components to
RT stabilize the Prp19p-associated complex essential for pre-mRNA splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5406-5411(1999).
RN [6]
RP INTERACTION WITH PRP19.
RX PubMed=11018040; DOI=10.1074/jbc.m006958200;
RA Chen C.-H., Tsai W.-Y., Chen H.-R., Wang C.-H., Cheng S.-C.;
RT "Identification and characterization of two novel components of the Prp19p-
RT associated complex, Ntc30p and Ntc20p.";
RL J. Biol. Chem. 276:488-494(2001).
RN [7]
RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [8]
RP INTERACTION WITH PRP19.
RX PubMed=12088152; DOI=10.1017/s1355838202025050;
RA Ohi M.D., Gould K.L.;
RT "Characterization of interactions among the Cef1p-Prp19p-associated
RT splicing complex.";
RL RNA 8:798-815(2002).
RN [9]
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 [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).
CC -!- FUNCTION: Involved in pre-mRNA splicing by stabilizing the NTC (or
CC PRP19-associated complex). As a component of the NTC complex,
CC associates to the spliceosome to mediate conformational rearrangement
CC or to stabilize the structure of the spliceosome after U4 snRNA
CC dissociation, which leads to spliceosome maturation.
CC {ECO:0000269|PubMed:10318896, ECO:0000269|PubMed:9528791}.
CC -!- SUBUNIT: Belongs to the NTC complex (or PRP19-associated complex),
CC composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and
CC PRP19. The NTC complex associates with the spliceosome after the
CC release of the U1 and U4 snRNAs and forms the CWC spliceosome
CC subcomplex (or CEF1-associated complex) reminiscent of a late-stage
CC spliceosome composed also of the U2, U5 and U6 snRNAs and at least
CC BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23,
CC CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11,
CC PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3,
CC SNU114, SPP2, RSE1 and YJU2. Interacts with PRP19.
CC {ECO:0000269|PubMed:11018040, ECO:0000269|PubMed:11884590,
CC ECO:0000269|PubMed:12088152, ECO:0000269|PubMed:9528791}.
CC -!- INTERACTION:
CC Q06091; Q12309: CLF1; NbExp=4; IntAct=EBI-818, EBI-484;
CC Q06091; P38302: NTC20; NbExp=2; IntAct=EBI-818, EBI-20921;
CC Q06091; P32523: PRP19; NbExp=8; IntAct=EBI-818, EBI-493;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 721 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U32445; AAB68071.1; -; Genomic_DNA.
DR EMBL; AY693233; AAT93252.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11515.1; -; Genomic_DNA.
DR PIR; S59766; S59766.
DR RefSeq; NP_015426.1; NM_001184198.1.
DR PDB; 5GM6; EM; 3.50 A; t=1-175.
DR PDB; 5GMK; EM; 3.40 A; t=1-175.
DR PDB; 5LJ5; EM; 3.80 A; s=1-175.
DR PDB; 5MQ0; EM; 4.17 A; s=1-175.
DR PDB; 5WSG; EM; 4.00 A; t=1-175.
DR PDB; 5Y88; EM; 3.70 A; G=1-175.
DR PDB; 5YLZ; EM; 3.60 A; G=1-175.
DR PDB; 6BK8; EM; 3.30 A; y=1-175.
DR PDB; 6EXN; EM; 3.70 A; s=1-175.
DR PDB; 6J6G; EM; 3.20 A; t=1-175.
DR PDB; 6J6H; EM; 3.60 A; t=1-175.
DR PDB; 6J6N; EM; 3.86 A; t=1-175.
DR PDB; 6J6Q; EM; 3.70 A; t=1-175.
DR PDBsum; 5GM6; -.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5WSG; -.
DR PDBsum; 5Y88; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR PDBsum; 6J6G; -.
DR PDBsum; 6J6H; -.
DR PDBsum; 6J6N; -.
DR PDBsum; 6J6Q; -.
DR AlphaFoldDB; Q06091; -.
DR SMR; Q06091; -.
DR BioGRID; 36267; 301.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-1885; NineTeen complex.
DR DIP; DIP-2864N; -.
DR IntAct; Q06091; 35.
DR MINT; Q06091; -.
DR STRING; 4932.YPR101W; -.
DR MaxQB; Q06091; -.
DR PaxDb; Q06091; -.
DR PRIDE; Q06091; -.
DR EnsemblFungi; YPR101W_mRNA; YPR101W; YPR101W.
DR GeneID; 856216; -.
DR KEGG; sce:YPR101W; -.
DR SGD; S000006305; SNT309.
DR VEuPathDB; FungiDB:YPR101W; -.
DR eggNOG; ENOG502S9WN; Eukaryota.
DR HOGENOM; CLU_119596_0_0_1; -.
DR InParanoid; Q06091; -.
DR OMA; YLRHQEL; -.
DR BioCyc; YEAST:G3O-34241-MON; -.
DR PRO; PR:Q06091; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06091; protein.
DR GO; GO:0000974; C:Prp19 complex; IDA:SGD.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Spliceosome.
FT CHAIN 1..175
FT /note="Pre-mRNA-splicing factor SNT309"
FT /id="PRO_0000071999"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 14..31
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 83..109
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 112..174
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 175 AA; 20709 MW; B781CA65BC9A1918 CRC64;
MDGLSFVDKG KIPDGYKNEI DQLVKKEFAN IKREPVHPEI RGILAKRKGA DNSVSTLTNA
LYTEYLKQRN NKKRRTPDFN DDDDTLFLEE YRRKYPRIDT SRYIPNESSE VSLLGIVDSY
LKHQEIVLDT LLPQTVSNQW RINNDYIRQT CTIVEEMNIQ QRKQINDLEI YRKRL
