CEF1_YEAST
ID CEF1_YEAST Reviewed; 590 AA.
AC Q03654; D6W038; Q6B1D8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Pre-mRNA-splicing factor CEF1;
DE AltName: Full=PRP nineteen-associated complex protein 85;
DE AltName: Full=PRP19-associated complex protein 85;
GN Name=CEF1; Synonyms=NTC85; OrderedLocusNames=YMR213W; ORFNames=YM8261.07;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 PROTEIN SEQUENCE OF 3-16, FUNCTION, DOMAIN, AND IDENTIFICATION IN THE
RP PRP19-ASSOCIATED COMPLEX.
RX PubMed=10092627; DOI=10.1074/jbc.274.14.9455;
RA Tsai W.-Y., Chow Y.-T., Chen H.-R., Huang K.-T., Hong R.-I., Jan S.-P.,
RA Kuo N.-Y., Tsao T.Y., Chen C.-H., Cheng S.-C.;
RT "Cef1p is a component of the Prp19p-associated complex and essential for
RT pre-mRNA splicing.";
RL J. Biol. Chem. 274:9455-9462(1999).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF TRP-52 AND TRP-84.
RX PubMed=11784857; DOI=10.1128/mcb.22.3.801-815.2002;
RA Burns C.G., Ohi R., Mehta S., O'Toole E.T., Winey M., Clark T.A.,
RA Sugnet C.W., Ares M. Jr., Gould K.L.;
RT "Removal of a single alpha-tubulin gene intron suppresses cell cycle arrest
RT phenotypes of splicing factor mutations in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 22:801-815(2002).
RN [6]
RP INTERACTION WITH PRP19, 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 [7]
RP FUNCTION, AND MUTAGENESIS OF TRP-33; TRP-52; TRP-84 AND TYR-102.
RX PubMed=9632794; DOI=10.1128/mcb.18.7.4097;
RA Ohi R., Feoktistova A., McCann S., Valentine V., Look A.T., Lipsick J.S.,
RA Gould K.L.;
RT "Myb-related Schizosaccharomyces pombe cdc5p is structurally and
RT functionally conserved in eukaryotes.";
RL Mol. Cell. Biol. 18:4097-4108(1998).
RN [8]
RP FUNCTION.
RX PubMed=10570151; DOI=10.1073/pnas.96.24.13789;
RA Burns C.G., Ohi R., Krainer A.R., Gould K.L.;
RT "Evidence that Myb-related CDC5 proteins are required for pre-mRNA
RT splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13789-13794(1999).
RN [9]
RP INTERACTION WITH CLF1; ISY1; NTC20; SYF1 AND SYF2.
RX PubMed=11102353; DOI=10.1093/genetics/156.4.1503;
RA Ben-Yehuda S., Dix I., Russell C.S., McGarvey M., Beggs J.D., Kupiec M.;
RT "Genetic and physical interactions between factors involved in both cell
RT cycle progression and pre-mRNA splicing in Saccharomyces cerevisiae.";
RL Genetics 156:1503-1517(2000).
RN [10]
RP INTERACTION WITH ISY1; NTC20 AND 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 [11]
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 [12]
RP INTERACTION WITH PRP19; PRP46 AND SYF1.
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 [13]
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 [14]
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 [15]
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 and cell cycle control.
CC Required for the binding of the NTC complex (or PRP19-associated
CC complex) components to the spliceosome to mediate conformational
CC rearrangement or to stabilize the structure of the spliceosome after U4
CC snRNA dissociation, which leads to spliceosome maturation. Its absence
CC leads to an arrest of the cell cycle, possibly due to the inefficient
CC splicing of TUB1. {ECO:0000269|PubMed:10092627,
CC ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:11784857,
CC ECO:0000269|PubMed:9632794}.
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 CLF1, ISY1, NTC20, PRP19,
CC PRP46, SYF1 and SYF2. {ECO:0000269|PubMed:10092627,
CC ECO:0000269|PubMed:11018040, ECO:0000269|PubMed:11102353,
CC ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:12088152,
CC ECO:0000269|PubMed:9528791}.
CC -!- INTERACTION:
CC Q03654; P25337: BUD31; NbExp=12; IntAct=EBI-476, EBI-547;
CC Q03654; Q12309: CLF1; NbExp=8; IntAct=EBI-476, EBI-484;
CC Q03654; Q03772: CWC15; NbExp=3; IntAct=EBI-476, EBI-36780;
CC Q03654; P38302: NTC20; NbExp=4; IntAct=EBI-476, EBI-20921;
CC Q03654; P32523: PRP19; NbExp=9; IntAct=EBI-476, EBI-493;
CC Q03654; Q06411: SPP382; NbExp=3; IntAct=EBI-476, EBI-576;
CC Q03654; Q04048: SYF1; NbExp=5; IntAct=EBI-476, EBI-540;
CC Q03654; P53277: SYF2; NbExp=3; IntAct=EBI-476, EBI-23308;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CEF1 family. {ECO:0000305}.
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DR EMBL; Z49809; CAA89928.1; -; Genomic_DNA.
DR EMBL; AY693142; AAT93161.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10112.1; -; Genomic_DNA.
DR PIR; S55095; S55095.
DR RefSeq; NP_013940.1; NM_001182720.1.
DR PDB; 5GM6; EM; 3.50 A; c=1-253, c=482-587.
DR PDB; 5GMK; EM; 3.40 A; c=1-253, c=482-587.
DR PDB; 5LJ3; EM; 3.80 A; O=1-590.
DR PDB; 5LJ5; EM; 3.80 A; O=1-590.
DR PDB; 5LQW; EM; 5.80 A; W=1-590.
DR PDB; 5MPS; EM; 3.85 A; O=1-590.
DR PDB; 5MQ0; EM; 4.17 A; O=1-590.
DR PDB; 5WSG; EM; 4.00 A; c=9-253, c=482-587.
DR PDB; 5Y88; EM; 3.70 A; J=1-590.
DR PDB; 5YLZ; EM; 3.60 A; J=1-590.
DR PDB; 6BK8; EM; 3.30 A; S=1-590.
DR PDB; 6EXN; EM; 3.70 A; O=1-590.
DR PDB; 6J6G; EM; 3.20 A; c=1-590.
DR PDB; 6J6H; EM; 3.60 A; c=1-590.
DR PDB; 6J6N; EM; 3.86 A; c=1-590.
DR PDB; 6J6Q; EM; 3.70 A; c=1-590.
DR PDB; 7DCO; EM; 2.50 A; L=1-590.
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 PDBsum; 7DCO; -.
DR AlphaFoldDB; Q03654; -.
DR SMR; Q03654; -.
DR BioGRID; 35391; 311.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-1885; NineTeen complex.
DR DIP; DIP-1113N; -.
DR IntAct; Q03654; 51.
DR MINT; Q03654; -.
DR STRING; 4932.YMR213W; -.
DR iPTMnet; Q03654; -.
DR MaxQB; Q03654; -.
DR PaxDb; Q03654; -.
DR PRIDE; Q03654; -.
DR EnsemblFungi; YMR213W_mRNA; YMR213W; YMR213W.
DR GeneID; 855253; -.
DR KEGG; sce:YMR213W; -.
DR SGD; S000004826; CEF1.
DR VEuPathDB; FungiDB:YMR213W; -.
DR eggNOG; KOG0050; Eukaryota.
DR GeneTree; ENSGT00550000074922; -.
DR HOGENOM; CLU_009082_2_1_1; -.
DR InParanoid; Q03654; -.
DR OMA; RLPNQWR; -.
DR BioCyc; YEAST:G3O-32896-MON; -.
DR PRO; PR:Q03654; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03654; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000974; C:Prp19 complex; IDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR021786; Cdc5p/Cef1_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF11831; Myb_Cef; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW Spliceosome.
FT CHAIN 1..590
FT /note="Pre-mRNA-splicing factor CEF1"
FT /id="PRO_0000197107"
FT DOMAIN 1..60
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 63..110
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 33..56
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 84..106
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 244..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..490
FT /note="Interaction with PRP19 and self-interaction"
FT COMPBIAS 244..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 33
FT /note="W->G: No effect. Slower growth and
FT thermosensitivity; when associated with G-84. Complete loss
FT of function; when associated with G-52 and G-84. Complete
FT loss of function; when associated with G-52; G-84 and G-
FT 102."
FT /evidence="ECO:0000269|PubMed:9632794"
FT MUTAGEN 52
FT /note="W->G: No effect. Slower growth and
FT thermosensitivity; when associated with G-84. Complete loss
FT of function; when associated with G-33 and G-84. Complete
FT loss of function; when associated with G-33; G-84 and G-
FT 102."
FT /evidence="ECO:0000269|PubMed:11784857,
FT ECO:0000269|PubMed:9632794"
FT MUTAGEN 84
FT /note="W->G: No effect. Slower growth and
FT thermosensitivity; when associated with G-33 or G-52.
FT Complete loss of function; when associated with G-33 and G-
FT 52 or G-52 and Y-102. Complete loss of function; when
FT associated with G-33; G-52 and G-102."
FT /evidence="ECO:0000269|PubMed:11784857,
FT ECO:0000269|PubMed:9632794"
FT MUTAGEN 102
FT /note="Y->G: No effect. Slower growth and
FT thermosensitivity; when associated with G-52 or G-84.
FT Complete loss of function; when associated with G-33; G-52
FT and G-84."
FT /evidence="ECO:0000269|PubMed:9632794"
FT CONFLICT 11
FT /note="G -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="K -> E (in Ref. 3; AAT93161)"
FT /evidence="ECO:0000305"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 165..193
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 232..251
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 338..355
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 374..379
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 426..437
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 445..468
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 483..581
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 583..586
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 590 AA; 67731 MW; A4C417A8B330EA9C CRC64;
MPPVPIYVKG GVWTNVEDQI LKAAVQKYGT HQWSKVASLL QKKTARQSEL RWNEYLNPKL
NFTEFSKEED AQLLDLAREL PNQWRTIADM MARPAQVCVE RYNRLLESED SGGAALSTGV
TDLKAGDINP NAETQMARPD NGDLEDEEKE MLAEARARLL NTQGKKATRK IRERMLEESK
RIAELQKRRE LKQAGINVAI KKPKKKYGTD IDYNEDIVYE QAPMPGIYDT STEDRQIKKK
FEQFERKVNR KGLDGNKDKP SKKNKDKKRK HDENEHVEKA ALGESTTLTD EYKKPKLILS
APGTKQGKVT YKKKLESKRQ KLIEAQATGT VLTPKELLPH DSGQEDNERS NIKSGKQLKS
RIRKFLVQMF ASLPSPKNDF EIVLSEDEKE EDAEIAEYEK EFENERAMNE EDNFIEPPSQ
NDAPRVSLVA VPLAYSTLPI PEFKNNPQSA IDNKYNLLVA NAINKEPHMV PEDTVDFLKE
VESRMQHITQ GRTSMKIQFK TAMPPTEVLL ESIQSKVESI EQLQRKLQHV QPLEQQNNEM
CSTLCHHSLP ALIEGQRKYY ADYYAYRQEI RSLEGRRKRL QAMLNSSSSI
