PRP21_YEAST
ID PRP21_YEAST Reviewed; 280 AA.
AC P32524; D6VVZ1; Q6Q5G7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Pre-mRNA-splicing factor PRP21;
GN Name=PRP21; Synonyms=SPP91; OrderedLocusNames=YJL203W; ORFNames=J0322;
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], AND MUTANT SPP91-1.
RC STRAIN=CY183;
RX PubMed=1505518; DOI=10.1002/j.1460-2075.1992.tb05406.x;
RA Chapon C., Legrain P.;
RT "A novel gene, spp91-1, suppresses the splicing defect and the pre-mRNA
RT nuclear export in the prp9-1 mutant.";
RL EMBO J. 11:3279-3288(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8341697; DOI=10.1073/pnas.90.14.6771;
RA Arenas J.E., Abelson J.N.;
RT "The Saccharomyces cerevisiae PRP21 gene product is an integral component
RT of the prespliceosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6771-6775(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7754713; DOI=10.1002/yea.320100912;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of a 36 kb segment on the left arm of yeast chromosome X
RT identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6,
RT CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two
RT homologues to chromosome III genes.";
RL Yeast 10:1235-1249(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
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 [8]
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 [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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 -!- INTERACTION:
CC P32524; Q07350: PRP11; NbExp=7; IntAct=EBI-603, EBI-688;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 2490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X67564; CAA47860.1; -; Genomic_DNA.
DR EMBL; L07744; AAB09601.1; -; Genomic_DNA.
DR EMBL; X77688; CAA54754.1; -; Genomic_DNA.
DR EMBL; Z49478; CAA89497.1; -; Genomic_DNA.
DR EMBL; AY558079; AAS56405.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08607.1; -; Genomic_DNA.
DR PIR; S23553; S23553.
DR RefSeq; NP_012332.1; NM_001181636.1.
DR PDB; 4DGW; X-ray; 3.11 A; B=87-237.
DR PDB; 5NRL; EM; 7.20 A; V=1-280.
DR PDB; 5ZWM; EM; 3.40 A; w=1-280.
DR PDB; 5ZWO; EM; 3.90 A; w=1-280.
DR PDB; 6G90; EM; 4.00 A; V=1-280.
DR PDB; 7DCO; EM; 2.50 A; w=1-280.
DR PDB; 7OQB; EM; 9.00 A; V=1-280.
DR PDB; 7OQE; EM; 5.90 A; V=1-280.
DR PDBsum; 4DGW; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 6G90; -.
DR PDBsum; 7DCO; -.
DR PDBsum; 7OQB; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; P32524; -.
DR SMR; P32524; -.
DR BioGRID; 33555; 335.
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-689N; -.
DR IntAct; P32524; 26.
DR MINT; P32524; -.
DR STRING; 4932.YJL203W; -.
DR iPTMnet; P32524; -.
DR MaxQB; P32524; -.
DR PaxDb; P32524; -.
DR PRIDE; P32524; -.
DR EnsemblFungi; YJL203W_mRNA; YJL203W; YJL203W.
DR GeneID; 853227; -.
DR KEGG; sce:YJL203W; -.
DR SGD; S000003739; PRP21.
DR VEuPathDB; FungiDB:YJL203W; -.
DR eggNOG; KOG0007; Eukaryota.
DR GeneTree; ENSGT00730000111077; -.
DR HOGENOM; CLU_013259_0_0_1; -.
DR InParanoid; P32524; -.
DR OMA; MEPEDTQ; -.
DR BioCyc; YEAST:G3O-31631-MON; -.
DR PRO; PR:P32524; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P32524; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:SGD.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR Gene3D; 1.10.10.790; -; 2.
DR InterPro; IPR045146; SF3A1.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR PANTHER; PTHR15316; PTHR15316; 1.
DR Pfam; PF01805; Surp; 2.
DR SMART; SM00648; SWAP; 2.
DR SUPFAM; SSF109905; SSF109905; 2.
DR PROSITE; PS50128; SURP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Spliceosome.
FT CHAIN 1..280
FT /note="Pre-mRNA-splicing factor PRP21"
FT /id="PRO_0000174322"
FT REPEAT 11..49
FT /note="SURP motif 1"
FT REPEAT 95..135
FT /note="SURP motif 2"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..280
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 168
FT /note="T->A: In SPP91-1; corrects the PRP9-1 growth defect
FT through partial restoration of splicing and by a complete
FT reversion of the pre-mRNA escape phenotype."
FT CONFLICT 205
FT /note="K -> N (in Ref. 6; AAS56405)"
FT /evidence="ECO:0000305"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 157..193
FT /evidence="ECO:0007829|PDB:4DGW"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:4DGW"
SQ SEQUENCE 280 AA; 33052 MW; 2E9DBA6F06759B3F CRC64;
MEPEDTQLKE DIKTTVNYIK QHGVEFENKL LEDERFSFIK KDDPLHEYYT KLMNEPTDTV
SGEDNDRKSE REIARPPDFL FSQYDTGISR RDMEVIKLTA RYYAKDKSIV EQMISKDGEA
RLNFMNSSHP LHKTFTDFVA QYKRVYSFTG QEIKKSKRTI LDNCFERTQY WEFEKDKDRE
HDKLVELCKI QFAAIPWDKF TQVAKFSIPE DTEIFEGSLD LEQMRLRRVQ TGIKLFDSIK
PTNEEEKIVS DQGKQKGGDS KGKKRKIRAV GETRLKKSKK
