ID SLT11_YEAST Reviewed; 364 AA. AC P38241; D6VQ64; P89497; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 05-JUN-2019, entry version 142. DE RecName: Full=Pre-mRNA-splicing factor SLT11; DE AltName: Full=Extracellular mutant protein 2; DE AltName: Full=Synthetic lethality with U2 protein 11; GN Name=ECM2; Synonyms=SLT11; OrderedLocusNames=YBR065C; GN ORFNames=YBR0614; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., RA Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., RA Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., RA Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., RA Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., RA Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., RA Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., RA Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., RA Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., RA Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., RA Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., RA van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., RA Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., RA Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP FUNCTION. RX PubMed=9528778; DOI=10.1128/MCB.18.4.2055; RA Xu D., Field D.J., Tang S.-J., Moris A., Bobechko B.P., Friesen J.D.; RT "Synthetic lethality of yeast slt mutations with U2 small nuclear RNA RT mutations suggests functional interactions between U2 and U5 snRNPs RT that are important for both steps of pre-mRNA splicing."; RL Mol. Cell. Biol. 18:2055-2066(1998). RN [4] RP FUNCTION, AND INTERACTION WITH SLU7. RX PubMed=11158289; DOI=10.1128/MCB.21.4.1011-1023.2001; RA Xu D., Friesen J.D.; RT "Splicing factor slt11p and its involvement in formation of U2/U6 RT helix II in activation of the yeast spliceosome."; RL Mol. Cell. Biol. 21:1011-1023(2001). RN [5] RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS RP 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 RT fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel RT pre-mRNA splicing factors, and snRNAs."; RL Mol. Cell. Biol. 22:2011-2024(2002). RN [6] 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., RA Riffle M., Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., RA Snydsman B.E., Bradley P., Muller E.G.D., Fields S., Baker D., RA Yates J.R. III, Davis T.N.; RT "Assigning function to yeast proteins by integration of RT technologies."; RL Mol. Cell 12:1353-1365(2003). RN [7] 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 [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., RA Dephoure N., 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. Facilitates the CC cooperative formation of U2/U6 helix II in association with stem CC II in the spliceosome. Binds to RNA. {ECO:0000269|PubMed:11158289, CC ECO:0000269|PubMed:9528778}. CC -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), CC a spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and CC at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CC CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, CC ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, CC PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, CC SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with SLU7. CC {ECO:0000269|PubMed:11158289, ECO:0000269|PubMed:11884590}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 4260 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the SLT11 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z35934; CAA85008.1; -; Genomic_DNA. DR EMBL; Z35935; CAA85009.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07184.1; -; Genomic_DNA. DR PIR; S45925; S45925. DR RefSeq; NP_009621.3; NM_001178413.3. DR PDB; 5GM6; EM; 3.50 A; Q=1-364. DR PDB; 5GMK; EM; 3.40 A; Q=1-364. DR PDB; 5LJ3; EM; 3.80 A; N=1-364. DR PDB; 5LJ5; EM; 3.80 A; N=1-364. DR PDB; 5LQW; EM; 5.80 A; D=1-364. DR PDB; 5MPS; EM; 3.85 A; N=1-364. DR PDB; 5MQ0; EM; 4.17 A; N=1-364. DR PDB; 5WSG; EM; 4.00 A; Q=1-364. DR PDB; 5Y88; EM; 3.70 A; M=1-364. DR PDB; 5YLZ; EM; 3.60 A; M=1-364. DR PDB; 6BK8; EM; 3.30 A; F=1-364. DR PDB; 6EXN; EM; 3.70 A; N=1-364. DR PDB; 6J6G; EM; 3.20 A; Q=1-364. DR PDB; 6J6H; EM; 3.60 A; Q=1-364. DR PDB; 6J6N; EM; 3.86 A; Q=1-364. DR PDB; 6J6Q; EM; 3.70 A; Q=1-364. DR PDBsum; 5GM6; -. DR PDBsum; 5GMK; -. DR PDBsum; 5LJ3; -. DR PDBsum; 5LJ5; -. DR PDBsum; 5LQW; -. DR PDBsum; 5MPS; -. 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 SMR; P38241; -. DR BioGrid; 32768; 176. DR ComplexPortal; CPX-1651; PRP19-associated complex. DR DIP; DIP-5359N; -. DR IntAct; P38241; 12. DR MINT; P38241; -. DR STRING; 4932.YBR065C; -. DR iPTMnet; P38241; -. DR MaxQB; P38241; -. DR PaxDb; P38241; -. DR PRIDE; P38241; -. DR EnsemblFungi; YBR065C_mRNA; YBR065C_mRNA; YBR065C. DR GeneID; 852357; -. DR KEGG; sce:YBR065C; -. DR EuPathDB; FungiDB:YBR065C; -. DR SGD; S000000269; ECM2. DR HOGENOM; HOG000154338; -. DR InParanoid; P38241; -. DR KO; K12872; -. DR OMA; RNVCQCC; -. DR BioCyc; YEAST:G3O-29034-MONOMER; -. DR PRO; PR:P38241; -. DR Proteomes; UP000002311; Chromosome II. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central. DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central. DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IBA:GO_Central. DR GO; GO:0036002; F:pre-mRNA binding; IBA:GO_Central. DR GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IGI:SGD. DR CDD; cd12265; RRM_SLT11; 1. DR InterPro; IPR039171; Cwc2/Slt11. DR InterPro; IPR034356; Slt11-like_RRM. DR PANTHER; PTHR14089; PTHR14089; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; mRNA processing; mRNA splicing; KW Nucleus; Reference proteome; RNA-binding; Spliceosome. FT CHAIN 1 364 Pre-mRNA-splicing factor SLT11. FT /FTId=PRO_0000212432. FT TURN 4 6 {ECO:0000244|PDB:5GMK}. FT HELIX 14 17 {ECO:0000244|PDB:6BK8}. FT STRAND 23 28 {ECO:0000244|PDB:6BK8}. FT TURN 35 37 {ECO:0000244|PDB:6BK8}. FT STRAND 43 46 {ECO:0000244|PDB:6BK8}. FT STRAND 48 51 {ECO:0000244|PDB:5GMK}. FT HELIX 62 68 {ECO:0000244|PDB:6BK8}. FT STRAND 72 74 {ECO:0000244|PDB:6BK8}. FT TURN 78 80 {ECO:0000244|PDB:6BK8}. FT HELIX 84 93 {ECO:0000244|PDB:6BK8}. FT STRAND 94 97 {ECO:0000244|PDB:5GMK}. FT HELIX 107 113 {ECO:0000244|PDB:6BK8}. FT HELIX 123 126 {ECO:0000244|PDB:6BK8}. FT HELIX 129 146 {ECO:0000244|PDB:6BK8}. FT STRAND 204 207 {ECO:0000244|PDB:6BK8}. FT STRAND 212 214 {ECO:0000244|PDB:5GMK}. FT HELIX 216 225 {ECO:0000244|PDB:6BK8}. FT STRAND 240 243 {ECO:0000244|PDB:5GMK}. FT TURN 244 247 {ECO:0000244|PDB:6BK8}. FT STRAND 249 252 {ECO:0000244|PDB:6BK8}. FT HELIX 256 265 {ECO:0000244|PDB:6BK8}. SQ SEQUENCE 364 AA; 40925 MW; BF21E687817A42B4 CRC64; MNDEINEPPP NICEQCLGDE ANIRMTKIPQ GSECKICTLP FTLYHFKTSK RSNNIIKTLI CVRCATQRNI CQCCMLDSRW HIPIQLRDHL ISLVNEENVM TEEAKNDMMK RFLSLKNVKL GGAQITSDPS EADNIVDKLK NILLRATSDG PSTPLIKNTT ALYKNEKGAN EVKNLEKYAS VDISHILKKL PLNESFLKNP STKSFFLYNI DASIPEWKIT DTVSQLLGIK KWKDGNSLSL IVNHKAKCGG LRFQSSELGE RFVSKISETL VTPKGLKRGV LLIDRFRIFI IPWSSGFSAA SFGTNTAENI KLSLSLNKLI QLELGLSFPT KSTDNAKNDK KKTSKKVHKD RSKKSKPRAN KLTI //