PRP31_YEAST
ID PRP31_YEAST Reviewed; 494 AA.
AC P49704; D6VUM3; Q66R99;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Pre-mRNA-processing factor 31;
GN Name=PRP31; OrderedLocusNames=YGR091W;
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 FUNCTION.
RX PubMed=8604353; DOI=10.1093/nar/24.6.1164;
RA Weidenhammer E.M., Singh M., Ruiz-Noriega M., Woolford J.L. Jr.;
RT "The PRP31 gene encodes a novel protein required for pre-mRNA splicing in
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 24:1164-1170(1996).
RN [2]
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 [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 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 [5]
RP IDENTIFICATION IN U4/U6.U5 TRI-SNRNP COMPLEX.
RX PubMed=9199293; DOI=10.1128/mcb.17.7.3580;
RA Weidenhammer E.M., Ruiz-Noriega M., Woolford J.L. Jr.;
RT "Prp31p promotes the association of the U4/U6.U5 tri-snRNP with
RT prespliceosomes to form spliceosomes in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:3580-3588(1997).
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 IDENTIFICATION IN U4/U6.U5 TRI-SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=10377396; DOI=10.1073/pnas.96.13.7226;
RA Stevens S.W., Abelson J.;
RT "Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein
RT particle and identification of its proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7226-7231(1999).
RN [8]
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 [9]
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 [10]
RP SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND ELECTRON
RP MICROSCOPY.
RX PubMed=18953335; DOI=10.1038/nsmb.1506;
RA Hacker I., Sander B., Golas M.M., Wolf E., Karagoz E., Kastner B.,
RA Stark H., Fabrizio P., Luhrmann R.;
RT "Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-
RT snRNP by electron microscopy.";
RL Nat. Struct. Mol. Biol. 15:1206-1212(2008).
CC -!- FUNCTION: Promotes the association of the U4/U6.U5 tri-snRNP particle
CC with pre-spliceosomes to form the mature spliceosomal complex.
CC {ECO:0000269|PubMed:8604353}.
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 {ECO:0000269|PubMed:10377396, ECO:0000269|PubMed:10449419,
CC ECO:0000269|PubMed:11804584, ECO:0000269|PubMed:18953335,
CC ECO:0000269|PubMed:9199293}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Interacts with the snRNP via the Nop domain. {ECO:0000250}.
CC -!- DOMAIN: The coiled coil domain is formed by two non-contiguous helices.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PRP31 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74984.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U31970; AAA74984.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z72876; CAA97094.1; -; Genomic_DNA.
DR EMBL; AY723814; AAU09731.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08184.1; -; Genomic_DNA.
DR PIR; S64386; S64386.
DR RefSeq; NP_011605.1; NM_001181220.1.
DR PDB; 3JCM; EM; 3.80 A; I=1-494.
DR PDB; 5GAN; EM; 3.60 A; F=1-494.
DR PDB; 5GAP; EM; 3.60 A; F=1-494.
DR PDB; 5NRL; EM; 7.20 A; F=1-494.
DR PDB; 5ZWM; EM; 3.40 A; L=1-494.
DR PDB; 5ZWO; EM; 3.90 A; L=1-494.
DR PDBsum; 3JCM; -.
DR PDBsum; 5GAN; -.
DR PDBsum; 5GAP; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR AlphaFoldDB; P49704; -.
DR SMR; P49704; -.
DR BioGRID; 33334; 229.
DR ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-32; U4/U6 small nuclear ribonucleoprotein complex.
DR DIP; DIP-5355N; -.
DR IntAct; P49704; 32.
DR MINT; P49704; -.
DR STRING; 4932.YGR091W; -.
DR MaxQB; P49704; -.
DR PaxDb; P49704; -.
DR PRIDE; P49704; -.
DR EnsemblFungi; YGR091W_mRNA; YGR091W; YGR091W.
DR GeneID; 852983; -.
DR KEGG; sce:YGR091W; -.
DR SGD; S000003323; PRP31.
DR VEuPathDB; FungiDB:YGR091W; -.
DR eggNOG; KOG2574; Eukaryota.
DR GeneTree; ENSGT00550000075069; -.
DR HOGENOM; CLU_026337_3_0_1; -.
DR InParanoid; P49704; -.
DR OMA; IIGNGPM; -.
DR BioCyc; YEAST:G3O-30801-MON; -.
DR PRO; PR:P49704; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P49704; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005687; C:U4 snRNP; IBA:GO_Central.
DR GO; GO:0071001; C:U4/U6 snRNP; 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:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:SGD.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IEA:InterPro.
DR Gene3D; 1.10.246.90; -; 1.
DR InterPro; IPR042239; Nop_C.
DR InterPro; IPR002687; Nop_dom.
DR InterPro; IPR036070; Nop_dom_sf.
DR InterPro; IPR012976; NOSIC.
DR InterPro; IPR027105; Prp31.
DR InterPro; IPR019175; Prp31_C.
DR PANTHER; PTHR13904; PTHR13904; 1.
DR Pfam; PF01798; Nop; 1.
DR Pfam; PF09785; Prp31_C; 1.
DR SMART; SM00931; NOSIC; 1.
DR SUPFAM; SSF89124; SSF89124; 1.
DR PROSITE; PS51358; NOP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..494
FT /note="Pre-mRNA-processing factor 31"
FT /id="PRO_0000058589"
FT DOMAIN 225..346
FT /note="Nop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00690"
FT REGION 344..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 88..122
FT /evidence="ECO:0000250"
FT COILED 191..225
FT /evidence="ECO:0000250"
FT SITE 257
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250"
FT CONFLICT 31
FT /note="L -> F (in Ref. 2; AAU09731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56303 MW; E39AC6247859FB3B CRC64;
MSSEEDYFDE LEYDLADEVN EEKEDIQTKK LTTVNCQTEK FNPFEILPES IELFRTLALI
SPDRLSLSET AQILPKIVDL KRILQQQEID FIKLLPFFNE IIPLIKSNIK LMHNFLISLY
SRRFPELSSL IPSPLQYSKV ISILENENYS KNESDELFFH LENKAKLTRE QILVLTMSMK
TSFKNKEPLD IKTRTQILEA NSILENLWKL QEDIGQYIAS KISIIAPNVC FLVGPEIAAQ
LIAHAGGVLE FSRIPSCNIA SIGKNKHLSH ELHTLESGVR QEGYLFASDM IQKFPVSVHK
QMLRMLCAKV SLAARVDAGQ KNGDRNTVLA HKWKAELSKK ARKLSEAPSI SETKALPIPE
DQPKKKRAGR KFRKYKEKFR LSHVRQLQNR MEFGKQEQTV LDSYGEEVGL GMSNTSLQQA
VGATSGSRRS AGNQAKLTKV MKHRISEANQ QADEFLISLG HNTEQPNLSP EMVQMHKKQH
TNPEEETNWF SGHG
