PRP17_YEAST
ID PRP17_YEAST Reviewed; 455 AA.
AC P40968; D6VSZ3; Q06341;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Pre-mRNA-processing factor 17;
DE AltName: Full=Cell division control protein 40;
GN Name=CDC40; Synonyms=PRP17, SLU4, XRS2; OrderedLocusNames=YDR364C;
GN ORFNames=D9481.11;
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=7753021; DOI=10.1007/bf00705642;
RA Vaisman N., Tsouladze A., Robzyk K., Ben-Yehuda S., Kupiec M., Kassir Y.;
RT "The role of Saccharomyces cerevisiae Cdc40p in DNA replication and mitotic
RT spindle formation and/or maintenance.";
RL Mol. Gen. Genet. 247:123-136(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [5]
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 [6]
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: May function in the second step of pre-mRNA splicing.
CC Regulatory protein involved in replication and mitotic spindle
CC formation and/or maintenance. Required for initiation and completion of
CC S-phase and for initiation and completion of DNA replication. Might be
CC required for the maintenance of microtubules. Essential only at
CC elevated temperatures.
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.
CC {ECO:0000269|PubMed:11884590}.
CC -!- INTERACTION:
CC P40968; P32523: PRP19; NbExp=7; IntAct=EBI-13834, EBI-493;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U17018; AAA86875.1; -; Genomic_DNA.
DR EMBL; U28373; AAB64800.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12203.1; -; Genomic_DNA.
DR PIR; S61159; S61159.
DR RefSeq; NP_010652.3; NM_001180672.3.
DR PDB; 5GM6; EM; 3.50 A; n=1-455.
DR PDB; 5GMK; EM; 3.40 A; n=1-455.
DR PDB; 5MPS; EM; 3.85 A; o=1-455.
DR PDB; 5MQ0; EM; 4.17 A; o=1-455.
DR PDB; 5WSG; EM; 4.00 A; n=1-455.
DR PDB; 5Y88; EM; 3.70 A; S=1-455.
DR PDB; 5YLZ; EM; 3.60 A; T=1-455.
DR PDB; 6BK8; EM; 3.30 A; M=1-455.
DR PDB; 6EXN; EM; 3.70 A; o=1-455.
DR PDB; 6J6G; EM; 3.20 A; n=1-455.
DR PDB; 6J6H; EM; 3.60 A; n=1-455.
DR PDB; 6J6N; EM; 3.86 A; n=1-455.
DR PDB; 6J6Q; EM; 3.70 A; n=1-455.
DR PDBsum; 5GM6; -.
DR PDBsum; 5GMK; -.
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; P40968; -.
DR SMR; P40968; -.
DR BioGRID; 32421; 164.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-1111N; -.
DR IntAct; P40968; 9.
DR MINT; P40968; -.
DR STRING; 4932.YDR364C; -.
DR iPTMnet; P40968; -.
DR MaxQB; P40968; -.
DR PaxDb; P40968; -.
DR PRIDE; P40968; -.
DR EnsemblFungi; YDR364C_mRNA; YDR364C; YDR364C.
DR GeneID; 851968; -.
DR KEGG; sce:YDR364C; -.
DR SGD; S000002772; CDC40.
DR VEuPathDB; FungiDB:YDR364C; -.
DR eggNOG; KOG0282; Eukaryota.
DR GeneTree; ENSGT00530000063583; -.
DR HOGENOM; CLU_022571_0_0_1; -.
DR InParanoid; P40968; -.
DR OMA; VQVYDHH; -.
DR BioCyc; YEAST:G3O-29914-MON; -.
DR PRO; PR:P40968; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P40968; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IMP:SGD.
DR GO; GO:0000389; P:mRNA 3'-splice site recognition; IGI:SGD.
DR GO; GO:0000348; P:mRNA branch site recognition; IGI:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR032847; PRPF17.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR43979; PTHR43979; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Spliceosome; WD repeat.
FT CHAIN 1..455
FT /note="Pre-mRNA-processing factor 17"
FT /id="PRO_0000051144"
FT REPEAT 160..200
FT /note="WD 1"
FT REPEAT 204..243
FT /note="WD 2"
FT REPEAT 291..330
FT /note="WD 3"
FT REPEAT 334..373
FT /note="WD 4"
FT REPEAT 379..422
FT /note="WD 5"
FT REPEAT 424..454
FT /note="WD 6"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 390
FT /note="A -> T (in Ref. 1; AAA86875)"
FT /evidence="ECO:0000305"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 455 AA; 52048 MW; 40AED5DB35319147 CRC64;
MGLVDGYDTS SDSDLNFDEG KSVHEKKNGN LHEDTSYEPS SNNIHKRKSH FTKSELKRRR
KTRKGDGPWG SWSSSDDETS QASETQKEDQ DIFVHALAED NLDSEQIEVE EVSHFYGKSE
KDYQGRGYLY PPNDVDVDLR EERISFRCYL PKKVIRNYPG HPEGTTALKF LPKTGHLILS
GGNDHTIKIW DFYHDYECLR DFQGHNKPIK ALRFTEDCQS FLSSSFDRSV KIWDTETGKV
KTRLHLNSTP ADVESRPTNP HEFIVGLSNS KILHYDDRVS ENQGLVQTYD HHLSSILALK
YFPDGSKFIS SSEDKTVRIW ENQINVPIKQ ISDTAQHSMP FLNVHPSQNY FCAQSMDNRI
YSFSLKPKYK RHPKKIFKGH SSAGYGISLA FSGDGRYICS GDSKSRLFTW DWNTSRLLNN
IKIPGNKPIT QVDWHPQETS KVICSGAAGK IYVCD
