PRP45_YEAST
ID PRP45_YEAST Reviewed; 379 AA.
AC P28004; D6VPI6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Pre-mRNA-processing protein 45;
GN Name=PRP45; Synonyms=FUN20; OrderedLocusNames=YAL032C;
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].
RX PubMed=1583694; DOI=10.1016/0022-2836(92)91025-k;
RA Harris S.D., Cheng J., Pugh T.A., Pringle J.R.;
RT "Molecular analysis of Saccharomyces cerevisiae chromosome I. On the number
RT of genes and the identification of essential genes using temperature-
RT sensitive-lethal mutations.";
RL J. Mol. Biol. 225:53-65(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
RP SEQUENCE REVISION.
RA Vo D.T.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=12359070; DOI=10.1093/oxfordjournals.jbchem.a003257;
RA Martinkova K., Lebduska P., Skruzny M., Folk P., Puta F.;
RT "Functional mapping of Saccharomyces cerevisiae Prp45 identifies the SNW
RT domain as essential for viability.";
RL J. Biochem. 132:557-563(2002).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SPP382.
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 [8]
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 [9]
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).
RN [10]
RP FUNCTION, INTERACTION WITH CLF1; PRP22 AND PRP46, AND ASSOCIATION WITH THE
RP SPLICEOSOME.
RX PubMed=12554883; DOI=10.1261/rna.2119903;
RA Albers M., Diment A., Muraru M., Russell C.S., Beggs J.D.;
RT "Identification and characterization of Prp45p and Prp46p, essential pre-
RT mRNA splicing factors.";
RL RNA 9:138-150(2003).
CC -!- FUNCTION: Involved in pre-mRNA splicing. Associated with the
CC spliceosome throughout the splicing reactions, until after the second
CC catalytic step. {ECO:0000269|PubMed:12359070,
CC ECO:0000269|PubMed:12554883}.
CC -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2,
CC CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24,
CC CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9,
CC PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts
CC with CLF1, PRP22 and PRP46. Interacts with SPP382.
CC {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:12554883,
CC ECO:0000269|PubMed:14690591}.
CC -!- INTERACTION:
CC P28004; Q12417: PRP46; NbExp=4; IntAct=EBI-20640, EBI-710;
CC P28004; Q04048: SYF1; NbExp=3; IntAct=EBI-20640, EBI-540;
CC P28004; Q06137: YLR345W; NbExp=3; IntAct=EBI-20640, EBI-33827;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12359070,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1670 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNW family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA44455.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X62577; CAA44455.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U12980; AAC05000.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06956.1; -; Genomic_DNA.
DR PIR; S23409; S23409.
DR RefSeq; NP_009370.1; NM_001178177.1.
DR PDB; 5GM6; EM; 3.50 A; P=1-379.
DR PDB; 5GMK; EM; 3.40 A; P=1-379.
DR PDB; 5LJ3; EM; 3.80 A; K=1-379.
DR PDB; 5LJ5; EM; 3.80 A; K=1-379.
DR PDB; 5LQW; EM; 5.80 A; M=1-379.
DR PDB; 5MPS; EM; 3.85 A; K=1-379.
DR PDB; 5MQ0; EM; 4.17 A; K=1-379.
DR PDB; 5WSG; EM; 4.00 A; P=1-379.
DR PDB; 5Y88; EM; 3.70 A; Q=1-379.
DR PDB; 5YLZ; EM; 3.60 A; Q=1-379.
DR PDB; 6BK8; EM; 3.30 A; E=1-379.
DR PDB; 6EXN; EM; 3.70 A; K=1-379.
DR PDB; 6J6G; EM; 3.20 A; P=1-379.
DR PDB; 6J6H; EM; 3.60 A; P=1-379.
DR PDB; 6J6N; EM; 3.86 A; P=1-379.
DR PDB; 6J6Q; EM; 3.70 A; P=1-379.
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; P28004; -.
DR SMR; P28004; -.
DR BioGRID; 31734; 255.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-2774N; -.
DR IntAct; P28004; 38.
DR MINT; P28004; -.
DR STRING; 4932.YAL032C; -.
DR iPTMnet; P28004; -.
DR MaxQB; P28004; -.
DR PaxDb; P28004; -.
DR PRIDE; P28004; -.
DR EnsemblFungi; YAL032C_mRNA; YAL032C; YAL032C.
DR GeneID; 851201; -.
DR KEGG; sce:YAL032C; -.
DR SGD; S000000030; PRP45.
DR VEuPathDB; FungiDB:YAL032C; -.
DR eggNOG; KOG2441; Eukaryota.
DR GeneTree; ENSGT00390000010423; -.
DR HOGENOM; CLU_006601_3_1_1; -.
DR InParanoid; P28004; -.
DR OMA; NGFTIAL; -.
DR BioCyc; YEAST:G3O-28843-MON; -.
DR PRO; PR:P28004; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P28004; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:SGD.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:SGD.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IMP:SGD.
DR InterPro; IPR017862; SKI-int_prot_SKIP.
DR InterPro; IPR004015; SKI-int_prot_SKIP_SNW-dom.
DR PANTHER; PTHR12096; PTHR12096; 1.
DR Pfam; PF02731; SKIP_SNW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Spliceosome.
FT CHAIN 1..379
FT /note="Pre-mRNA-processing protein 45"
FT /id="PRO_0000084825"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 60..84
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 199..244
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 379 AA; 42483 MW; FE5A724186D7FE84 CRC64;
MFSNRLPPPK HSQGRVSTAL SSDRVEPAIL TDQIAKNVKL DDFIPKRQSN FELSVPLPTK
AEIQECTART KSYIQRLVNA KLANSNNRAS SRYVTETHQA PANLLLNNSH HIEVVSKQMD
PLLPRFVGKK ARKVVAPTEN DEVVPVLHMD GSNDRGEADP NEWKIPAAVS NWKNPNGYTV
ALERRVGKAL DNENNTINDG FMKLSEALEN ADKKARQEIR SKMELKRLAM EQEMLAKESK
LKELSQRARY HNGTPQTGAI VKPKKQTSTV ARLKELAYSQ GRDVSEKIIL GAAKRSEQPD
LQYDSRFFTR GANASAKRHE DQVYDNPLFV QQDIESIYKT NYEKLDEAVN VKSEGASGSH
GPIQFTKAES DDKSDNYGA
