SLT11_YEAST
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 03-AUG-2022, entry version 157.
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; ORFNames=YBR0614;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
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., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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 that
RT 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 helix II
RT 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 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 [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., 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 [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., 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. Facilitates the cooperative
CC formation of U2/U6 helix II in association with stem II in the
CC spliceosome. Binds to RNA. {ECO:0000269|PubMed:11158289,
CC ECO:0000269|PubMed:9528778}.
CC -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), a
CC spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and at
CC least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21,
CC CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1,
CC MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46,
CC SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1,
CC SYF2, RSE1 and YJU2. Interacts with SLU7. {ECO:0000269|PubMed:11158289,
CC ECO:0000269|PubMed:11884590}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 4260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SLT11 family. {ECO:0000305}.
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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 AlphaFoldDB; P38241; -.
DR SMR; P38241; -.
DR BioGRID; 32768; 178.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-5359N; -.
DR IntAct; P38241; 13.
DR MINT; P38241; -.
DR STRING; 4932.YBR065C; -.
DR iPTMnet; P38241; -.
DR MaxQB; P38241; -.
DR PaxDb; P38241; -.
DR PRIDE; P38241; -.
DR EnsemblFungi; YBR065C_mRNA; YBR065C; YBR065C.
DR GeneID; 852357; -.
DR KEGG; sce:YBR065C; -.
DR SGD; S000000269; ECM2.
DR VEuPathDB; FungiDB:YBR065C; -.
DR eggNOG; KOG0153; Eukaryota.
DR HOGENOM; CLU_027112_1_1_1; -.
DR InParanoid; P38241; -.
DR OMA; RNVCQCC; -.
DR BioCyc; YEAST:G3O-29034-MON; -.
DR PRO; PR:P38241; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38241; protein.
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_RRM.
DR PANTHER; PTHR14089; PTHR14089; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW RNA-binding; Spliceosome.
FT CHAIN 1..364
FT /note="Pre-mRNA-splicing factor SLT11"
FT /id="PRO_0000212432"
FT REGION 331..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..364
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 244..255
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 306..324
FT /evidence="ECO:0007829|PDB:6J6G"
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
