PRP17_SCHPO
ID PRP17_SCHPO Reviewed; 558 AA.
AC O43071;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Pre-mRNA-processing factor 17;
GN Name=prp17; ORFNames=SPBC6B1.10;
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 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 [3]
RP FUNCTION.
RX PubMed=15452114; DOI=10.1074/jbc.m408815200;
RA Sapra A.K., Arava Y., Khandelia P., Vijayraghavan U.;
RT "Genome-wide analysis of pre-mRNA splicing: intron features govern the
RT requirement for the second-step factor, Prp17 in Saccharomyces cerevisiae
RT and Schizosaccharomyces pombe.";
RL J. Biol. Chem. 279:52437-52446(2004).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Functions in the second step of pre-mRNA splicing. Involved
CC in splicing intron which are longer than 200 nucleotides.
CC {ECO:0000269|PubMed:15452114}.
CC -!- SUBUNIT: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5,
CC cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27,
CC cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16,
CC cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26,
CC cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10,
CC prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1,
CC smd1, smd3, smf1, smg1 and syf2. {ECO:0000269|PubMed:11884590}.
CC -!- INTERACTION:
CC O43071; O14011: prp19; NbExp=5; IntAct=EBI-538927, EBI-590830;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAA17053.1; -; Genomic_DNA.
DR PIR; T40651; T40651.
DR RefSeq; NP_596089.1; NM_001022004.2.
DR PDB; 3JB9; EM; 3.60 A; g=1-558.
DR PDBsum; 3JB9; -.
DR AlphaFoldDB; O43071; -.
DR SMR; O43071; -.
DR BioGRID; 277683; 86.
DR IntAct; O43071; 41.
DR STRING; 4896.SPBC6B1.10.1; -.
DR iPTMnet; O43071; -.
DR MaxQB; O43071; -.
DR PaxDb; O43071; -.
DR PRIDE; O43071; -.
DR EnsemblFungi; SPBC6B1.10.1; SPBC6B1.10.1:pep; SPBC6B1.10.
DR PomBase; SPBC6B1.10; prp17.
DR VEuPathDB; FungiDB:SPBC6B1.10; -.
DR eggNOG; KOG0282; Eukaryota.
DR HOGENOM; CLU_022571_2_1_1; -.
DR InParanoid; O43071; -.
DR OMA; EQTCYIP; -.
DR PhylomeDB; O43071; -.
DR Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SPO-72187; mRNA 3'-end processing.
DR PRO; PR:O43071; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR032847; PRPF17.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR43979; PTHR43979; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Spliceosome; WD repeat.
FT CHAIN 1..558
FT /note="Pre-mRNA-processing factor 17"
FT /id="PRO_0000278391"
FT REPEAT 264..304
FT /note="WD 1"
FT REPEAT 308..349
FT /note="WD 2"
FT REPEAT 351..391
FT /note="WD 3"
FT REPEAT 394..433
FT /note="WD 4"
FT REPEAT 437..476
FT /note="WD 5"
FT REPEAT 484..523
FT /note="WD 6"
FT REPEAT 526..558
FT /note="WD 7"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 63132 MW; 78859607D4460195 CRC64;
MLVANYSSDS EEQENSQSPN IQPLLHTENL APAVVDNVKD DLIVSKGGNS RELARNVPVN
EMVQPALGPA NPFVTKEQDS IKNSITGYAE REYVPNFVFN QEYYANTHAI YGKRNFDDNE
ATTSTDLKRK SQKIKERRED PGDPSILEGD GAYKGPWAGY GSEQSSSPLE YSEYEEVESL
DVKSEKDTES NNLGQNELLK EQLATPEVET HRSKEETILH KDRLFDYQNR SYMHVPNDVG
INLSEEPGEQ TCYIPKKHIF TWKGHTKGIS CLRFFPISGH LLLSGSMDNQ IKIWEVYHDR
SLLRTFQGHA RPIRDLSFSQ DGRSFLSTSF DKTIKLWDTE LGKCLNCFNS DRLTNCVKFQ
VDPDKPNEFL AGTADKRILQ FDIRSPDIVQ AYDHHLGGIN SITFLENGKR FVTTSDDSSM
RFWEYGTPVP IKFVADIAMH SMPRVALRPN GKSIACQSLD NCIYVYSAYE KYRQNKKKVF
KGYSCSGYSL EVGFSPDGRF VFSGDSSGNA CFWDWKTCKL MAKLPAHSGP VQSMAFHPQE
TSKVATSSIV DGSIKYWD
