SP381_YEAST
ID SP381_YEAST Reviewed; 291 AA.
AC P38282; D6VQE7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Pre-mRNA-splicing factor SPP381;
DE AltName: Full=Suppressor of PRP38-1 mutation;
GN Name=SPP381; OrderedLocusNames=YBR152W; ORFNames=YBR1202;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 157-169, SUBUNIT, IDENTIFICATION IN THE U4/U5/U6
RP TRI-SNRNP COMPLEX, AND 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 [5]
RP FUNCTION, IDENTIFICATION IN U4/U6.U5 TRI-SNRNP COMPLEX, AND INTERACTION
RP WITH PRP38.
RX PubMed=9858581; DOI=10.1128/mcb.19.1.577;
RA Lybarger S., Beickman K., Brown V., Dembla-Rajpal N., Morey K., Seipelt R.,
RA Rymond B.C.;
RT "Elevated levels of a U4/U6.U5 snRNP-associated protein, Spp381p, rescue a
RT mutant defective in spliceosome maturation.";
RL Mol. Cell. Biol. 19:577-584(1999).
RN [6]
RP IDENTIFICATION IN U1.U2.U4/U6.U5 PENTA-SNRNP COMPLEX, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=11804584; DOI=10.1016/s1097-2765(02)00436-7;
RA Stevens S.W., Ryan D.E., Ge H.Y., Moore R.E., Young M.K., Lee T.D.,
RA Abelson J.;
RT "Composition and functional characterization of the yeast spliceosomal
RT penta-snRNP.";
RL Mol. Cell 9:31-44(2002).
RN [7]
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 [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).
CC -!- FUNCTION: Component of the spliceosome and rRNA processing machinery.
CC In association with the spliceosomal U4/U6.U5 tri-snRNP particle,
CC required for splicing of pre-mRNA. {ECO:0000269|PubMed:9858581}.
CC -!- SUBUNIT: Component of the U4/U6-U5 tri-snRNP complex composed of the
CC U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31,
CC PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
CC Interacts with PRP38. {ECO:0000269|PubMed:10449419,
CC ECO:0000269|PubMed:11804584, ECO:0000269|PubMed:9858581}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPP381 family. {ECO:0000305}.
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DR EMBL; Z36021; CAA85111.1; -; Genomic_DNA.
DR EMBL; AY693054; AAT93073.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07267.1; -; Genomic_DNA.
DR PIR; S46023; S46023.
DR RefSeq; NP_009710.3; NM_001178500.3.
DR PDB; 5NRL; EM; 7.20 A; N=1-291.
DR PDB; 5ZWO; EM; 3.90 A; 9=1-291.
DR PDBsum; 5NRL; -.
DR PDBsum; 5ZWO; -.
DR AlphaFoldDB; P38282; -.
DR SMR; P38282; -.
DR BioGRID; 32851; 157.
DR ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR DIP; DIP-2461N; -.
DR IntAct; P38282; 24.
DR MINT; P38282; -.
DR STRING; 4932.YBR152W; -.
DR iPTMnet; P38282; -.
DR MaxQB; P38282; -.
DR PaxDb; P38282; -.
DR PRIDE; P38282; -.
DR EnsemblFungi; YBR152W_mRNA; YBR152W; YBR152W.
DR GeneID; 852449; -.
DR KEGG; sce:YBR152W; -.
DR SGD; S000000356; SPP381.
DR VEuPathDB; FungiDB:YBR152W; -.
DR eggNOG; ENOG502S80M; Eukaryota.
DR HOGENOM; CLU_1107827_0_0_1; -.
DR InParanoid; P38282; -.
DR OMA; WFERQNE; -.
DR BioCyc; YEAST:G3O-29103-MON; -.
DR PRO; PR:P38282; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38282; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IGI:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..291
FT /note="Pre-mRNA-splicing factor SPP381"
FT /id="PRO_0000202498"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 33772 MW; B65D0F00DE860A83 CRC64;
MSFRHFKRRL DTSSADESSS ADEEHPDQNV SLTEKSASLS HSDLGGEILN GTGKNRTPND
GQESNESDGS PESDESPESE ESSDNSDSSD SDDMRPLPRP LFMKKKANNL QKATKIDQPW
NAQDDARVLQ TKKENMIKNI DKANQVAKNY ETMKLRLNTN YSTNEELIKQ CLLLDDNDEV
DSEKERQKWF ERQNERKQKH RRIQLAKQRE SEEYEAKRFE AMQKGKDGNT KYDVILDKEK
EKLDHKKQRS AEKVEKSHNN NRYKITRTKN VEFGDLGKNS RDYEETEYSV I
