PRP18_YEAST
ID PRP18_YEAST Reviewed; 251 AA.
AC P33411; D6VUE3; Q02459; Q05724;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Pre-mRNA-splicing factor 18;
GN Name=PRP18; OrderedLocusNames=YGR006W;
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=8474454; DOI=10.1128/mcb.13.5.2959-2970.1993;
RA Horowitz D.S., Abelson J.N.;
RT "A U5 small nuclear ribonucleoprotein particle protein involved only in the
RT second step of pre-mRNA splicing in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:2959-2970(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 208279 / BJ926;
RX PubMed=7995524; DOI=10.1101/gad.8.23.2868;
RA Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A., Kornberg R.D.;
RT "TFIIF-TAF-RNA polymerase II connection.";
RL Genes Dev. 8:2868-2878(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 130-251.
RC STRAIN=S288c / GRF88;
RX PubMed=8982874; DOI=10.1093/oxfordjournals.jbchem.a021497;
RA Min-Seok R., Kawamata Y., Nakamura H., Ohta A., Takagi M.;
RT "Isolation and characterization of ECT1 gene encoding CTP:
RT phosphoethanolamine cytidylyltransferase of Saccharomyces cerevisiae.";
RL J. Biochem. 120:1040-1047(1996).
RN [6]
RP SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA Fabrizio P.;
RT "Identification by mass spectrometry and functional analysis of novel
RT proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL EMBO J. 18:4535-4548(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 79-251.
RX PubMed=10737784; DOI=10.1073/pnas.97.7.3022;
RA Jiang J., Horowitz D.S., Xu R.-M.;
RT "Crystal structure of the functional domain of the splicing factor Prp18.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3022-3027(2000).
CC -!- FUNCTION: Component of the U4/U5/U6 snRNP, binding principally to the
CC u5 snRNP. It is not absolutely required for the second step of pre-mRNA
CC splicing at low temperatures but is required at higher temperatures. It
CC may stabilize a particular conformation of the U5 snRNP or orient the
CC U5 snRNP within the U4/U5/U6 snRNP or within the spliceosome.
CC -!- SUBUNIT: Homodimer. Component of the U4/U6-U5 tri-snRNP complex
CC composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6,
CC PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1,
CC SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8,
CC BRR2 and DIB1. {ECO:0000269|PubMed:10449419}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the PRP18 family. {ECO:0000305}.
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DR EMBL; L03536; AAA34915.1; -; Genomic_DNA.
DR EMBL; U13016; AAA61643.1; -; Genomic_DNA.
DR EMBL; Z72791; CAA96989.1; -; Genomic_DNA.
DR EMBL; D50644; BAA09309.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08104.1; -; Genomic_DNA.
DR PIR; S64295; S64295.
DR RefSeq; NP_011520.2; NM_001181135.1.
DR PDB; 1DVK; X-ray; 2.15 A; A/B=79-251.
DR PDB; 5MPS; EM; 3.85 A; a=1-251.
DR PDB; 5MQ0; EM; 4.17 A; a=1-251.
DR PDB; 5WSG; EM; 4.00 A; f=1-251.
DR PDB; 5YLZ; EM; 3.60 A; U=1-251.
DR PDB; 6BK8; EM; 3.30 A; N=1-251.
DR PDB; 6EXN; EM; 3.70 A; a=1-251.
DR PDBsum; 1DVK; -.
DR PDBsum; 5MPS; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5WSG; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR AlphaFoldDB; P33411; -.
DR SMR; P33411; -.
DR BioGRID; 33250; 426.
DR DIP; DIP-1110N; -.
DR IntAct; P33411; 3.
DR MINT; P33411; -.
DR STRING; 4932.YGR006W; -.
DR iPTMnet; P33411; -.
DR MaxQB; P33411; -.
DR PaxDb; P33411; -.
DR PRIDE; P33411; -.
DR EnsemblFungi; YGR006W_mRNA; YGR006W; YGR006W.
DR GeneID; 852889; -.
DR KEGG; sce:YGR006W; -.
DR SGD; S000003238; PRP18.
DR VEuPathDB; FungiDB:YGR006W; -.
DR eggNOG; KOG2808; Eukaryota.
DR GeneTree; ENSGT00390000015073; -.
DR HOGENOM; CLU_081028_0_0_1; -.
DR InParanoid; P33411; -.
DR OMA; PIGVTQI; -.
DR BioCyc; YEAST:G3O-30737-MON; -.
DR EvolutionaryTrace; P33411; -.
DR PRO; PR:P33411; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P33411; protein.
DR GO; GO:0071021; C:U2-type post-spliceosomal complex; IDA:SGD.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR GO; GO:0005682; C:U5 snRNP; IDA:SGD.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR DisProt; DP02073; -.
DR InterPro; IPR004098; Prp18.
DR InterPro; IPR039979; PRPF18.
DR PANTHER; PTHR13007; PTHR13007; 1.
DR Pfam; PF02840; Prp18; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Spliceosome.
FT CHAIN 1..251
FT /note="Pre-mRNA-splicing factor 18"
FT /id="PRO_0000058586"
FT REGION 17..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 194..249
FT /note="PIGVTSVGIHARSAHSKIQGGRNAANIMIDERTRLWITSIKRLITFEEWYTS
FT NHDS -> LLVL (in Ref. 2; AAA61643)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..251
FT /note="GIHARSAHSKIQGGRNAANIMIDERTRLWITSIKRLITFEEWYTSNHDSLA
FT -> AFMLVVHIRKFKEAGMLLT (in Ref. 3)"
FT /evidence="ECO:0000305"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1DVK"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1DVK"
FT HELIX 106..126
FT /evidence="ECO:0007829|PDB:1DVK"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1DVK"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1DVK"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:1DVK"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:1DVK"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1DVK"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:1DVK"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 224..245
FT /evidence="ECO:0007829|PDB:1DVK"
SQ SEQUENCE 251 AA; 28377 MW; B50D9B9A99D9711B CRC64;
MDLDLASILK GEISKKKKEL ANSKGVQPPC TEKFQPHESA NIDETPRQVE QESTDEENLS
DNQSDDIRTT ISKLENRPER IQEAIAQDKT ISVIIDPSQI GSTEGKPLLS MKCNLYIHEI
LSRWKASLEA YHPELFLDTK KALFPLLLQL RRNQLAPDLL ISLATVLYHL QQPKEINLAV
QSYMKLSIGN VAWPIGVTSV GIHARSAHSK IQGGRNAANI MIDERTRLWI TSIKRLITFE
EWYTSNHDSL A
