RSE1_YEAST
ID RSE1_YEAST Reviewed; 1361 AA.
AC Q04693; D6VZC6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Pre-mRNA-splicing factor RSE1;
DE AltName: Full=RNA splicing and ER to Golgi transport factor 1;
DE AltName: Full=Spliceosome-associated protein 130;
GN Name=RSE1; Synonyms=SAP130; OrderedLocusNames=YML049C; ORFNames=YM9827.03C;
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 FUNCTION.
RX PubMed=9819400; DOI=10.1128/mcb.18.12.7139;
RA Chen E.J., Frand A.R., Chitouras E., Kaiser C.A.;
RT "A link between secretion and pre-mRNA processing defects in Saccharomyces
RT cerevisiae and the identification of a novel splicing gene, RSE1.";
RL Mol. Cell. Biol. 18:7139-7146(1998).
RN [4]
RP FUNCTION, AND ASSOCIATION WITH THE PRE-SPLICEOSOME.
RX PubMed=10369685; DOI=10.1093/emboj/18.12.3463;
RA Caspary F., Shevchenko A., Wilm M., Seraphin B.;
RT "Partial purification of the yeast U2 snRNP reveals a novel yeast pre-mRNA
RT splicing factor required for pre-spliceosome assembly.";
RL EMBO J. 18:3463-3474(1999).
RN [5]
RP IDENTIFICATION IN THE SPLICEOSOME, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA Fabrizio P.;
RT "Identification by mass spectrometry and functional analysis of novel
RT proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL EMBO J. 18:4535-4548(1999).
RN [6]
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 [7]
RP INTERACTION WITH RDS3.
RX PubMed=14517302; DOI=10.1128/mcb.23.20.7339-7349.2003;
RA Wang Q., Rymond B.C.;
RT "Rds3p is required for stable U2 snRNP recruitment to the splicing
RT apparatus.";
RL Mol. Cell. Biol. 23:7339-7349(2003).
RN [8]
RP IDENTIFICATION IN THE SF3B COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in G2/M transition (By similarity). Required for
CC pre-mRNA splicing and endoplasmic reticulum (ER) to Golgi secretion
CC pathway. U2 snRNPs associated protein required for the pre-spliceosome
CC assembly. The involvement in ER to Golgi secretion is probably indirect
CC and due to the splicing of the pre-mRNA coding for SAR1, a small GTP-
CC binding protein required for COPII vesicle formation from the ER.
CC {ECO:0000250, ECO:0000269|PubMed:10369685, ECO:0000269|PubMed:9819400}.
CC -!- SUBUNIT: Belongs to the SF3B complex, a U2 associated sub-complex of
CC the spliceosome. The SF3B complex is composed of at least CUS1, HSH49,
CC HSH155, RDS3 and RSE1. Belongs also to the CWC complex (or CEF1-
CC associated complex), a spliceosome sub-complex reminiscent of a late-
CC stage spliceosome composed of the U2, U5 and U6 snRNAs and at least
CC BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22,
CC CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1,
CC NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7,
CC SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2,
CC RSE1 and YJU2. Interacts with RDS3. {ECO:0000269|PubMed:10449419,
CC ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:14517302,
CC ECO:0000269|PubMed:15565172}.
CC -!- INTERACTION:
CC Q04693; P49955: HSH155; NbExp=3; IntAct=EBI-519, EBI-664;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RSE1 family. {ECO:0000305}.
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DR EMBL; Z47816; CAA87825.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09850.1; -; Genomic_DNA.
DR PIR; S50943; S50943.
DR RefSeq; NP_013663.1; NM_001182407.1.
DR PDB; 5GM6; EM; 3.50 A; F=1-1361.
DR PDB; 5LQW; EM; 5.80 A; X=1-1361.
DR PDB; 5NRL; EM; 7.20 A; P=1-1361.
DR PDB; 5ZWM; EM; 3.40 A; 3=1-1361.
DR PDB; 5ZWO; EM; 3.90 A; 3=1-1361.
DR PDB; 6G90; EM; 4.00 A; P=1-1361.
DR PDB; 7OQB; EM; 9.00 A; P=1-1361.
DR PDB; 7OQE; EM; 5.90 A; P=1-1361.
DR PDBsum; 5GM6; -.
DR PDBsum; 5LQW; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 6G90; -.
DR PDBsum; 7OQB; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; Q04693; -.
DR SMR; Q04693; -.
DR BioGRID; 35119; 224.
DR ComplexPortal; CPX-1647; SF3B complex.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR DIP; DIP-856N; -.
DR IntAct; Q04693; 32.
DR MINT; Q04693; -.
DR STRING; 4932.YML049C; -.
DR iPTMnet; Q04693; -.
DR MaxQB; Q04693; -.
DR PaxDb; Q04693; -.
DR PRIDE; Q04693; -.
DR TopDownProteomics; Q04693; -.
DR EnsemblFungi; YML049C_mRNA; YML049C; YML049C.
DR GeneID; 854956; -.
DR KEGG; sce:YML049C; -.
DR SGD; S000004513; RSE1.
DR VEuPathDB; FungiDB:YML049C; -.
DR eggNOG; KOG1898; Eukaryota.
DR GeneTree; ENSGT00950000183151; -.
DR HOGENOM; CLU_003246_0_1_1; -.
DR InParanoid; Q04693; -.
DR OMA; FFLVQTE; -.
DR BioCyc; YEAST:G3O-32646-MON; -.
DR PRO; PR:Q04693; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04693; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005686; C:U2 snRNP; IDA:SGD.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0000245; P:spliceosomal complex assembly; IDA:SGD.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Spliceosome.
FT CHAIN 1..1361
FT /note="Pre-mRNA-splicing factor RSE1"
FT /id="PRO_0000218638"
FT REGION 788..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..806
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1361 AA; 153784 MW; 4D92837F5C267D67 CRC64;
MWGGGKMAVV SLSPHTAKMR KLFGQASTTM AYDGLKREAE RRTRSDHNIT MVAKDDELYL
YHLTLKKQTN FVHSCIGHFV DLEAGSKREQ SQLCVATETH LELYDTADGE LKLIAKFQNL
FATITSMKSL DLPHSGSRAK ASNWPTFLAL TSDSGNLSIV QIIMHAGALR LKTLVNQPLT
RTTLRRVSPI SYMEIDPNGR CIILSSVEQN KLCFLVDYAQ KLRISSPLEI IRPHMVTLDM
AVVDVNFNNP CFVTLEIDNA ATQLSVHLIF YVLELGLNHI VKKADYLVNP SANFVLSLPD
LSRYNITTSL SDNNYDADYD TLFNPFVVIG FENHILVKDM NGFFSLKVEI PKRSITNSRH
KNVTIISGIV QKLKNDFFVL LQSNHGDLFK LTVSPDTNDR NRPLVQLSYF DTIQNSHQLH
IFKNGYLFAL SEMNNNFLFQ FEKLGVEKND FSNVLTSKDP NKSLVFEPSI KLQNLSILSQ
QLNLNPSIKS QIVSDSPLSI ATKHFTNNKI ITLTNAVNYS NLISTSLPPN ATKLWLIPDP
ATTGDNNTLL FITFPKKTMI LQIDNESMEE LTPDEATRSA FKLSQDTTIH TCLMGSHSII
QVCTAELRHI VPTGKSRYSN KLTWVPPAGI RIVCATSSKT QLIISLSNYE LVYFKIDVSS
DSLIELTTHP ELDTMPSKVA IVQDTQHADL LAIADNEGMI KIMSLKDQKE DFLTVISLQL
VSEKISDMIM VRDSSIGQLN LHVGLENGVY MKFHIGDVDG SFTDIKRRFL GLKPVSLSYL
REISVSLNNE EEEEEEEDDD DEKEEEEINS SGAKWMSCVV CHSSSTWVSY TWKNVWTIRQ
LKDQNMLSCS KFVNADVAIN GVCSISSSGR LNIGRVSNFP TLDNWFHVHE SSVNKQENGG
GDESNEEEED EMEEEMEMLQ ISTFRPRTIL SFPNNPKSIL FIDNHSGKKQ CRISLQIDGE
CLKFGSSDHL YKILDDIDCV SAAIIDFTRQ ADHLIICAGD KRLLTYKILV NKDKLSFDIE
LLHQTEIISP IHAMLKFKNF LLTAMGSTIV LYGLGKKQLL RRSVTQTPVS ITKIVSMHQW
NYERLAVGDI HESVTLFIWD PAGNVFIPYV DDSVKRHVTV LKFLDEATVI GADRYGNAWT
LRSPPECEKI MSNHDPSELS NGAIKYPLDV ITLQQKLPNT YDCKFKFQLL NHFFVNDIIT
DFHILDSLSN SDRPGCIYMG LQGTVGCFIP LLSKGNVFMM GNIENIMAEA DDTFYLDYES
RKKNNNMRKE DDEEESGSVV LQGRHGIEDE IICEGSCSIL GRDHQEYRSY YAPVRKVIDG
DLCENFLRLS LNEQEFLAKN LKSVQVEDII QTINEVRTNY M
