PRP45_SCHPO
ID PRP45_SCHPO Reviewed; 557 AA.
AC Q09882;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Pre-mRNA-processing protein 45;
DE AltName: Full=Complexed with cdc5 protein 13;
DE AltName: Full=Transcriptional coregulator snw1;
GN Name=prp45; Synonyms=cwf13, snw1; ORFNames=SPCC188.11, SPCC584.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP HOMODIMERIZATION, AND INTERACTION WITH U2AF23.
RX PubMed=11414703; DOI=10.1006/bbrc.2001.5108;
RA Ambrozkova M., Puta F., Fukova I., Skruzny M., Brabek J., Folk P.;
RT "The fission yeast ortholog of the coregulator SKIP interacts with the
RT small subunit of U2AF.";
RL Biochem. Biophys. Res. Commun. 284:1148-1154(2001).
RN [3]
RP INTERACTION WITH CYP1.
RX PubMed=11690648; DOI=10.1016/s0167-4781(01)00301-3;
RA Skruzny M., Ambrozkova M., Fukova I., Martinkova K., Blahuskova A.,
RA Hamplova L., Puta F., Folk P.;
RT "Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in
RT Dictyostelium discoideum and Schizosaccharomyces pombe.";
RL Biochim. Biophys. Acta 1521:146-151(2001).
RN [4]
RP IDENTIFICATION IN THE CWF 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228; SER-236 AND SER-376, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in pre-mRNA splicing.
CC -!- SUBUNIT: Homodimer. Interacts with cyp1 and the small 23 kDa subunit of
CC the splicing factor U2AF (u2af23). Belongs to the 40S cdc5-associated
CC complex (or cwf complex), a spliceosome sub-complex reminiscent of a
CC late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at
CC least brr2, cdc5, cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2,
CC spp42/cwf6, cwf7/spf27, cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13,
CC cwf14, cwf15, cwf16, cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23,
CC cwf24, cwf25, cwf26, cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1,
CC prp5/cwf1, prp10, prp12/sap130, prp17, prp22, sap61, sap62, sap114,
CC sap145, slu7, smb1, smd1, smd3, smf1, smg1 and syf2.
CC {ECO:0000269|PubMed:11414703, ECO:0000269|PubMed:11690648,
CC ECO:0000269|PubMed:11884590}.
CC -!- INTERACTION:
CC Q09882; P39964: cdc5; NbExp=3; IntAct=EBI-457758, EBI-538771;
CC Q09882; P87051: ppi1; NbExp=4; IntAct=EBI-457758, EBI-1810686;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SNW family. {ECO:0000305}.
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DR EMBL; CU329672; CAB41231.1; -; Genomic_DNA.
DR PIR; T39128; S62522.
DR RefSeq; NP_588213.1; NM_001023203.2.
DR PDB; 3JB9; EM; 3.60 A; M=1-557.
DR PDBsum; 3JB9; -.
DR AlphaFoldDB; Q09882; -.
DR SMR; Q09882; -.
DR BioGRID; 275562; 28.
DR IntAct; Q09882; 7.
DR STRING; 4896.SPCC188.11.1; -.
DR iPTMnet; Q09882; -.
DR MaxQB; Q09882; -.
DR PaxDb; Q09882; -.
DR PRIDE; Q09882; -.
DR EnsemblFungi; SPCC188.11.1; SPCC188.11.1:pep; SPCC188.11.
DR GeneID; 2538988; -.
DR KEGG; spo:SPCC188.11; -.
DR PomBase; SPCC188.11; prp45.
DR VEuPathDB; FungiDB:SPCC188.11; -.
DR eggNOG; KOG2441; Eukaryota.
DR HOGENOM; CLU_006601_2_0_1; -.
DR InParanoid; Q09882; -.
DR OMA; WRDSNTL; -.
DR PhylomeDB; Q09882; -.
DR PRO; PR:Q09882; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0000974; C:Prp19 complex; IDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; IDA:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IPI:PomBase.
DR DisProt; DP01658; -.
DR InterPro; IPR017862; SKI-int_prot_SKIP.
DR InterPro; IPR004015; SKI-int_prot_SKIP_SNW-dom.
DR PANTHER; PTHR12096; PTHR12096; 1.
DR Pfam; PF02731; SKIP_SNW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT CHAIN 1..557
FT /note="Pre-mRNA-processing protein 45"
FT /id="PRO_0000084822"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 557 AA; 62697 MW; 916673DA5F9FE192 CRC64;
MALLSEELSS ILPNPDFDDE EEDYVERETS HADERQIGVK FHIPPYGQRK GWFPSSPEDF
GDGGAFPEIH VAQYPLDMGR KRSAKSAGNT LALQVTSSGA VDYNAIARQG HEHGELVQAS
FRDLIPLRAR LGVGEISLEK PSDEQKQEVA NKTKLALQKI LSKQIAQSQP KSAVVQQRDD
PVYIRYTPSN QMGQALSKQR IIKMVTAEQD PMEPPKFRHK KVPRGPPSPP PPVLHSPPRK
VSAQEQQDWQ IPPSISNWKN PKGYTIPLDK RLAADGRGLN DVEINDGFAK FSEALYTVER
QAREEVRYRA IMRQKMAEKE KQEKEQRLFM LAQKAREDRM GRNAASSGPS HAKPRSTSVS
SEERSRSRAG SFSHHSESEN EDEDSEAFRR RQELRRERRR QAEKDLRLSR MGAEKRAKLA
EKDRPRDVAE RVALGLSKPS MSSDTMIDSR LFNQASGLGS GFQDEDSYNV YDKPWRAAPS
STLYRPGATL SRQVDASAEL ERITSESRYD VLGNAHKKFK GSDEVVESRA GPVTFEKDIA
DPFGVDTFLN NVSSKKT
