CWC26_YEAST
ID CWC26_YEAST Reviewed; 266 AA.
AC P46947; D6VTX8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Pre-mRNA-splicing factor CWC26;
DE AltName: Full=Bud site selection protein 13;
DE AltName: Full=Complexed with CEF1 protein 26;
DE AltName: Full=Synthetic lethal with CLF1 protein 7;
GN Name=BUD13; Synonyms=CWC26, SLC7; OrderedLocusNames=YGL174W;
GN ORFNames=G1642;
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=8619317; DOI=10.1002/yea.320111209;
RA Bertani I., Coglievina M., Zaccaria P., Klima R., Bruschi C.V.;
RT "The sequence of an 11.1 kb fragment on the left arm of Saccharomyces
RT cerevisiae chromosome VII reveals six open reading frames including NSP49,
RT KEM1 and four putative new genes.";
RL Yeast 11:1187-1194(1995).
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 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 [5]
RP FUNCTION.
RX PubMed=8657162; DOI=10.1128/mcb.16.4.1857;
RA Zahner J.E., Harkins H.A., Pringle J.R.;
RT "Genetic analysis of the bipolar pattern of bud site selection in the yeast
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:1857-1870(1996).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11452010; DOI=10.1091/mbc.12.7.2147;
RA Ni L., Snyder M.;
RT "A genomic study of the bipolar bud site selection pattern in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 12:2147-2170(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 FUNCTION.
RX PubMed=12871902; DOI=10.1093/genetics/164.3.895;
RA Vincent K., Wang Q., Jay S., Hobbs K., Rymond B.C.;
RT "Genetic interactions with CLF1 identify additional pre-mRNA splicing
RT factors and a link between activators of yeast vesicular transport and
RT splicing.";
RL Genetics 164:895-907(2003).
RN [9]
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 [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH IST3
RP AND PML1.
RX PubMed=15565172; DOI=10.1038/sj.emboj.7600482;
RA Dziembowski A., Ventura A.-P., Rutz B., Caspary F., Faux C., Halgand F.,
RA Laprevote O., Seraphin B.;
RT "Proteomic analysis identifies a new complex required for nuclear pre-mRNA
RT retention and splicing.";
RL EMBO J. 23:4847-4856(2004).
CC -!- FUNCTION: Required for efficient splicing and pre-mRNA nuclear
CC retention. May also be involved in positioning the proximal bud pole
CC signal. {ECO:0000269|PubMed:11452010, ECO:0000269|PubMed:12871902,
CC ECO:0000269|PubMed:15565172, ECO:0000269|PubMed:8657162}.
CC -!- SUBUNIT: Belongs to the pre-mRNA retention and splicing (RES) complex
CC composed of at least BUD13, IST3 and PML1. May also belong to the CWC
CC complex (or CEF1-associated complex) composed of the U2, U5 and U6
CC snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2,
CC CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3,
CC ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45,
CC PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2,
CC SYF1, SYF2, RSE1 and YJU2. Interacts with IST3 and PML1.
CC {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:15565172}.
CC -!- INTERACTION:
CC P46947; P40565: IST3; NbExp=13; IntAct=EBI-24073, EBI-25387;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the CWC26 family. {ECO:0000305}.
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DR EMBL; X84705; CAA59179.1; -; Genomic_DNA.
DR EMBL; Z72696; CAA96886.1; -; Genomic_DNA.
DR EMBL; AY558504; AAS56830.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07939.1; -; Genomic_DNA.
DR PIR; S59237; S59237.
DR RefSeq; NP_011341.3; NM_001181039.3.
DR PDB; 2MKC; NMR; -; C=215-245.
DR PDB; 2MY2; NMR; -; B=215-255.
DR PDB; 4UQT; NMR; -; B=222-256.
DR PDB; 5GM6; EM; 3.50 A; W=1-266.
DR PDB; 5LQW; EM; 5.80 A; L=1-266.
DR PDB; 5ZWM; EM; 3.40 A; Y=1-266.
DR PDB; 5ZWO; EM; 3.90 A; Y=1-266.
DR PDBsum; 2MKC; -.
DR PDBsum; 2MY2; -.
DR PDBsum; 4UQT; -.
DR PDBsum; 5GM6; -.
DR PDBsum; 5LQW; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR AlphaFoldDB; P46947; -.
DR BMRB; P46947; -.
DR SMR; P46947; -.
DR BioGRID; 33079; 390.
DR ComplexPortal; CPX-1649; RES complex.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR DIP; DIP-2075N; -.
DR IntAct; P46947; 15.
DR MINT; P46947; -.
DR STRING; 4932.YGL174W; -.
DR iPTMnet; P46947; -.
DR MaxQB; P46947; -.
DR PaxDb; P46947; -.
DR PRIDE; P46947; -.
DR EnsemblFungi; YGL174W_mRNA; YGL174W; YGL174W.
DR GeneID; 852701; -.
DR KEGG; sce:YGL174W; -.
DR SGD; S000003142; BUD13.
DR VEuPathDB; FungiDB:YGL174W; -.
DR eggNOG; KOG2654; Eukaryota.
DR GeneTree; ENSGT00390000014500; -.
DR HOGENOM; CLU_086127_0_0_1; -.
DR InParanoid; P46947; -.
DR OMA; GYAPPNR; -.
DR BioCyc; YEAST:G3O-30662-MON; -.
DR PRO; PR:P46947; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P46947; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0070274; C:RES complex; IDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005686; C:U2 snRNP; IC:ComplexPortal.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0051237; P:maintenance of RNA location; IMP:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:SGD.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR InterPro; IPR018609; Bud13.
DR Pfam; PF09736; Bud13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Spliceosome.
FT CHAIN 1..266
FT /note="Pre-mRNA-splicing factor CWC26"
FT /id="PRO_0000079610"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2MY2"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:2MY2"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4UQT"
SQ SEQUENCE 266 AA; 30472 MW; 1584B390121325CD CRC64;
MALHQYLSET YGPTKPKNKT KKKKKESKSD ANSDKTSLIV KERLSTLQQE QEKSGVASFS
KFDKQKSKNI WKNLETNELS HAITHPSASS ITGNESKNDL KEIRAQEPLV TVADKSKTRK
TIYRDAQGHK IQEDSKIDDS SFSRSKYEDE KAAEREQYLK NLNMGDVQKL GINVDAHDKK
KNQTASSLTI EDPAITFTHD KERTVKTSLL GRKLYDKPAP ENRFAIMPGS RWDGVHRSNG
FEEKWFAKQN EINEKKVQSY TLQEDY
