PRP9_YEAST
ID PRP9_YEAST Reviewed; 530 AA.
AC P19736; D6VRW2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Pre-mRNA-splicing factor PRP9;
GN Name=PRP9; OrderedLocusNames=YDL030W; ORFNames=D2773;
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=S288c / GRF88;
RX PubMed=2118103; DOI=10.1002/j.1460-2075.1990.tb07465.x;
RA Legrain P., Choulika A.;
RT "The molecular characterization of PRP6 and PRP9 yeast genes reveals a new
RT cysteine/histidine motif common to several splicing factors.";
RL EMBO J. 9:2775-2781(1990).
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 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: mRNA splicing factors, PRP9, PRP11, and PRP21, are necessary
CC for binding of the U2 snRNP to the pre-mRNA in an early step of
CC spliceosome assembly.
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 -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 3920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SF3A3 family. {ECO:0000305}.
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DR EMBL; X53466; CAA37560.1; -; Genomic_DNA.
DR EMBL; Z71781; CAA96459.1; -; Genomic_DNA.
DR EMBL; Z74078; CAA98589.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11822.1; -; Genomic_DNA.
DR PIR; S12320; S12320.
DR RefSeq; NP_010254.1; NM_001180089.1.
DR PDB; 4DGW; X-ray; 3.11 A; A=1-389.
DR PDB; 5NRL; EM; 7.20 A; T=1-530.
DR PDB; 5ZWM; EM; 3.40 A; u=1-530.
DR PDB; 5ZWO; EM; 3.90 A; u=1-530.
DR PDB; 6G90; EM; 4.00 A; T=1-530.
DR PDB; 7OQB; EM; 9.00 A; T=1-530.
DR PDB; 7OQE; EM; 5.90 A; T=1-530.
DR PDBsum; 4DGW; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 6G90; -.
DR PDBsum; 7OQB; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; P19736; -.
DR SMR; P19736; -.
DR BioGRID; 32026; 520.
DR ComplexPortal; CPX-1648; SF3A complex.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR DIP; DIP-651N; -.
DR IntAct; P19736; 23.
DR MINT; P19736; -.
DR STRING; 4932.YDL030W; -.
DR MaxQB; P19736; -.
DR PaxDb; P19736; -.
DR PRIDE; P19736; -.
DR EnsemblFungi; YDL030W_mRNA; YDL030W; YDL030W.
DR GeneID; 851531; -.
DR KEGG; sce:YDL030W; -.
DR SGD; S000002188; PRP9.
DR VEuPathDB; FungiDB:YDL030W; -.
DR eggNOG; KOG2636; Eukaryota.
DR GeneTree; ENSGT00530000063402; -.
DR HOGENOM; CLU_027160_1_1_1; -.
DR InParanoid; P19736; -.
DR OMA; KDAHRRN; -.
DR BioCyc; YEAST:G3O-29456-MON; -.
DR PRO; PR:P19736; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P19736; protein.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005686; C:U2 snRNP; IC:ComplexPortal.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IMP:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:SGD.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR031590; PRP9_N.
DR InterPro; IPR031776; SF3A3.
DR InterPro; IPR031774; SF3A3_dom.
DR InterPro; IPR024598; SF3a60/Prp9_C.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12786:SF2; PTHR12786:SF2; 1.
DR Pfam; PF16958; PRP9_N; 1.
DR Pfam; PF16837; SF3A3; 1.
DR Pfam; PF11931; SF3a60_Prp9_C; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50171; ZF_MATRIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..530
FT /note="Pre-mRNA-splicing factor PRP9"
FT /id="PRO_0000174321"
FT ZN_FING 280..310
FT /note="Matrin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT ZN_FING 421..452
FT /note="Matrin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 367..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..27
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 69..96
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4DGW"
FT TURN 172..178
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 227..247
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:4DGW"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:4DGW"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 312..327
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 329..343
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 347..361
FT /evidence="ECO:0007829|PDB:4DGW"
SQ SEQUENCE 530 AA; 63029 MW; 9020885E620488F3 CRC64;
MNLLETRRSL LEEMEIIENA IAERIQRNPE LYYHYIQESS KVFPDTKLPR SSLIAENKIY
KFKKVKRKRK QIILQQHEIN IFLRDYQEKQ QTFNKINRPE ETQEDDKDLP NFERKLQQLE
KELKNEDENF ELDINSKKDK YALFSSSSDP SRRTNILSDR ARDLDLNEIF TRDEQYGEYM
ELEQFHSLWL NVIKRGDCSL LQFLDILELF LDDEKYLLTP PMDRKNDRYM AFLLKLSKYV
ETFFFKSYAL LDAAAVENLI KSDFEHSYCR GSLRSEAKGI YCPFCSRWFK TSSVFESHLV
GKIHKKNESK RRNFVYSEYK LHRYLKYLND EFSRTRSFVE RKLAFTANER MAEMDILTQK
YEAPAYDSTE KEGAEQVDGE QRDGQLQEEH LSGKSFDMPL GPDGLPMPYW LYKLHGLDRE
YRCEICSNKV YNGRRTFERH FNEERHIYHL RCLGIEPSSV FKGITKIKEA QELWKNMQGQ
SQLTSIAAVP PKPNPSQLKV PTELELEEED EEGNVMSKKV YDELKKQGLV
