PRP46_YEAST
ID PRP46_YEAST Reviewed; 451 AA.
AC Q12417; D6W3L8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Pre-mRNA-splicing factor PRP46;
DE AltName: Full=Complexed with CEF1 protein 1;
DE AltName: Full=PRP nineteen-associated complex protein 50;
DE AltName: Full=PRP19-associated complex protein 50;
DE AltName: Full=Pre-mRNA-processing protein 46;
GN Name=PRP46; Synonyms=CWC1, NTC50; OrderedLocusNames=YPL151C;
GN ORFNames=P2594;
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 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11079560;
RX DOI=10.1002/1522-2683(20001001)21:16<3396::aid-elps3396>3.0.co;2-j;
RA Pardo M., Ward M., Bains S., Molina M., Blackstock W., Gil C., Nombela C.;
RT "A proteomic approach for the study of Saccharomyces cerevisiae cell wall
RT biogenesis.";
RL Electrophoresis 21:3396-3410(2000).
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 INTERACTION WITH CEF1; CLF1; NTC20 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 [7]
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 [8]
RP FUNCTION, AND INTERACTION WITH PRP45.
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).
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 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. May also be required for cell
CC cycle progression at G2/M (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12554883}.
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 CEF1, CLF1, NTC20, PRP45 and SYF1.
CC {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:12088152,
CC ECO:0000269|PubMed:12554883}.
CC -!- INTERACTION:
CC Q12417; P28004: PRP45; NbExp=4; IntAct=EBI-710, EBI-20640;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1770 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat PRL1/PRL2 family. {ECO:0000305}.
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DR EMBL; X96770; CAA65570.1; -; Genomic_DNA.
DR EMBL; Z73507; CAA97856.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11284.1; -; Genomic_DNA.
DR PIR; S65162; S65162.
DR RefSeq; NP_015174.1; NM_001183965.1.
DR PDB; 5GM6; EM; 3.50 A; O=1-451.
DR PDB; 5GMK; EM; 3.40 A; O=1-451.
DR PDB; 5LJ3; EM; 3.80 A; J=1-451.
DR PDB; 5LJ5; EM; 3.80 A; J=1-451.
DR PDB; 5LQW; EM; 5.80 A; K=1-451.
DR PDB; 5MPS; EM; 3.85 A; J=1-451.
DR PDB; 5MQ0; EM; 4.17 A; J=1-451.
DR PDB; 5WSG; EM; 4.00 A; O=1-451.
DR PDB; 5Y88; EM; 3.70 A; O=1-451.
DR PDB; 5YLZ; EM; 3.60 A; O=1-451.
DR PDB; 6BK8; EM; 3.30 A; D=1-451.
DR PDB; 6EXN; EM; 3.70 A; J=1-451.
DR PDB; 6J6G; EM; 3.20 A; O=1-451.
DR PDB; 6J6H; EM; 3.60 A; O=1-451.
DR PDB; 6J6N; EM; 3.86 A; O=1-451.
DR PDB; 6J6Q; EM; 3.70 A; O=1-451.
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; Q12417; -.
DR SMR; Q12417; -.
DR BioGRID; 36032; 226.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-3994N; -.
DR IntAct; Q12417; 45.
DR MINT; Q12417; -.
DR STRING; 4932.YPL151C; -.
DR iPTMnet; Q12417; -.
DR COMPLUYEAST-2DPAGE; Q12417; -.
DR MaxQB; Q12417; -.
DR PaxDb; Q12417; -.
DR PRIDE; Q12417; -.
DR EnsemblFungi; YPL151C_mRNA; YPL151C; YPL151C.
DR GeneID; 855952; -.
DR KEGG; sce:YPL151C; -.
DR SGD; S000006072; PRP46.
DR VEuPathDB; FungiDB:YPL151C; -.
DR eggNOG; KOG0285; Eukaryota.
DR GeneTree; ENSGT00940000155316; -.
DR HOGENOM; CLU_000288_72_0_1; -.
DR InParanoid; Q12417; -.
DR OMA; HPLEWKP; -.
DR BioCyc; YEAST:G3O-34048-MON; -.
DR PRO; PR:Q12417; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12417; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000974; C:Prp19 complex; IPI:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR045241; Prp46/PLRG1-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19923; PTHR19923; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Repeat; Spliceosome; WD repeat.
FT CHAIN 1..451
FT /note="Pre-mRNA-splicing factor PRP46"
FT /id="PRO_0000051169"
FT REPEAT 137..168
FT /note="WD 1"
FT REPEAT 180..210
FT /note="WD 2"
FT REPEAT 222..252
FT /note="WD 3"
FT REPEAT 264..294
FT /note="WD 4"
FT REPEAT 306..335
FT /note="WD 5"
FT REPEAT 348..377
FT /note="WD 6"
FT REPEAT 397..427
FT /note="WD 7"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 154..168
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 192..201
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 409..418
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 421..428
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 451 AA; 50700 MW; 0E888F566A5414BD CRC64;
MDGNDHKVEN LGDVDKFYSR IRWNNQFSYM ATLPPHLQSE MEGQKSLLMR YDTYRKESSS
FSGEGKKVTL QHVPTDFSEA SQAVISKKDH DTHASAFVNK IFQPEVAEEL IVNRYEKLLS
QRPEWHAPWK LSRVINGHLG WVRCVAIDPV DNEWFITGSN DTTMKVWDLA TGKLKTTLAG
HVMTVRDVAV SDRHPYLFSV SEDKTVKCWD LEKNQIIRDY YGHLSGVRTV SIHPTLDLIA
TAGRDSVIKL WDMRTRIPVI TLVGHKGPIN QVQCTPVDPQ VVSSSTDATV RLWDVVAGKT
MKVLTHHKRS VRATALHPKE FSVASACTDD IRSWGLAEGS LLTNFESEKT GIINTLSINQ
DDVLFAGGDN GVLSFYDYKS GHKYQSLATR EMVGSLEGER SVLCSTFDKT GLRLITGEAD
KSIKIWKQDE TATKESEPGL AWNPNLSAKR F
