ID   PRP1_SCHPO              Reviewed;         906 AA.
AC   Q12381;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 156.
DE   RecName: Full=Pre-mRNA-splicing factor prp1;
GN   Name=prp1; Synonyms=zer1; ORFNames=SPBC6B1.07;
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 [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF LEU-616.
RX   PubMed=9286671; DOI=10.1093/genetics/147.1.101;
RA   Urushiyama S., Tani T., Ohshima Y.;
RT   "The prp1+ gene required for pre-mRNA splicing in Schizosaccharomyces pombe
RT   encodes a protein that contains TPR motifs and is similar to Prp6p of
RT   budding yeast.";
RL   Genetics 147:101-115(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF PRO-875.
RA   Okazaki K., Okayama H.;
RT   "Fission yeast TPR gene involved in G0 transition.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   FUNCTION, AND INTERACTION WITH BRR2 AND SPP42.
RX   PubMed=16133344; DOI=10.1007/s00294-005-0013-6;
RA   Bottner C.A., Schmidt H., Vogel S., Michele M., Kaeufer N.F.;
RT   "Multiple genetic and biochemical interactions of Brr2, Prp8, Prp31, Prp1
RT   and Prp4 kinase suggest a function in the control of the activation of
RT   spliceosomes in Schizosaccharomyces pombe.";
RL   Curr. Genet. 48:151-161(2005).
RN   [5]
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).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY
RP   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. Interacts with prp6 and prp13.
CC       May also be involved in the regulation of the G0-G1/G2 transition.
CC       Required for pre-spliceosome formation, which is the first step of pre-
CC       mRNA splicing. This protein is associated with snRNP U5. Has a role in
CC       branch site-3' splice site selection. Associates with the branch site-
CC       3' splice 3'-exon region. {ECO:0000269|PubMed:16133344,
CC       ECO:0000269|PubMed:9286671}.
CC   -!- SUBUNIT: Interacts with brr2 and spp42. {ECO:0000269|PubMed:16133344}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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DR   EMBL; D83743; BAA12094.1; -; Genomic_DNA.
DR   EMBL; D83659; BAA12033.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA17050.1; -; Genomic_DNA.
DR   PIR; T45158; T45158.
DR   RefSeq; NP_596086.1; NM_001022000.2.
DR   AlphaFoldDB; Q12381; -.
DR   SMR; Q12381; -.
DR   BioGRID; 277699; 139.
DR   IntAct; Q12381; 1.
DR   STRING; 4896.SPBC6B1.07.1; -.
DR   iPTMnet; Q12381; -.
DR   MaxQB; Q12381; -.
DR   PaxDb; Q12381; -.
DR   PRIDE; Q12381; -.
DR   EnsemblFungi; SPBC6B1.07.1; SPBC6B1.07.1:pep; SPBC6B1.07.
DR   GeneID; 2541185; -.
DR   KEGG; spo:SPBC6B1.07; -.
DR   PomBase; SPBC6B1.07; prp1.
DR   VEuPathDB; FungiDB:SPBC6B1.07; -.
DR   eggNOG; KOG0495; Eukaryota.
DR   HOGENOM; CLU_007010_0_0_1; -.
DR   InParanoid; Q12381; -.
DR   OMA; DGWAWYY; -.
DR   PhylomeDB; Q12381; -.
DR   Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
DR   PRO; PR:Q12381; -.
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:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:PomBase.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IBA:GO_Central.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR010491; PRP1_N.
DR   InterPro; IPR027108; Prp6/Prp1/STA1.
DR   InterPro; IPR045075; Syf1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR11246; PTHR11246; 1.
DR   PANTHER; PTHR11246:SF1; PTHR11246:SF1; 1.
DR   Pfam; PF06424; PRP1_N; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00386; HAT; 14.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; SSF48452; 3.
PE   1: Evidence at protein level;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..906
FT                   /note="Pre-mRNA-splicing factor prp1"
FT                   /id="PRO_0000205755"
FT   REPEAT          258..290
FT                   /note="HAT 1"
FT   REPEAT          322..353
FT                   /note="HAT 2"
FT   REPEAT          354..384
FT                   /note="HAT 3"
FT   REPEAT          385..416
FT                   /note="HAT 4"
FT   REPEAT          524..556
FT                   /note="HAT 5"
FT   REPEAT          558..590
FT                   /note="HAT 6"
FT   REPEAT          592..624
FT                   /note="HAT 7"
FT   REPEAT          693..725
FT                   /note="HAT 8"
FT   REPEAT          726..758
FT                   /note="HAT 9"
FT   REPEAT          760..792
FT                   /note="HAT 10"
FT   REPEAT          824..856
FT                   /note="HAT 11"
FT   REGION          50..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MUTAGEN         616
FT                   /note="L->I: Defect in poly(A)+ RNA nuclear export."
FT                   /evidence="ECO:0000269|PubMed:9286671"
FT   MUTAGEN         875
FT                   /note="P->L: In zer1-C5; temperature-sensitive growth
FT                   arrest showing G0 state like terminal phenotype."
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   906 AA;  103004 MW;  4690EDBCA9F1AA3B CRC64;
     MANFYPDFLN MQPPPNYVAG LGRGATGFTT RSDLGPAQEL PSQESIKAAI EQRKSEIEEE
     EDIDPRYQDP DNEVALFATA PYDHEDEEAD KIYQSVEEHL SKRRKSQREK QEQLQKEKYE
     KENPKVSSQF ADLKRGLSTL TDEDWNNIPE PGDLTRKKRT KQPRRERFYA TSDFVLASAR
     NENQAISNFA VDTQAGTETP DMNGTKTNFV EIGAARDKVL GIKLAQASSN LTSPSTIDPK
     GYLTSLNSMV PKNANDLGDI RKARKLLQSV IETNPKHASG WVAAARLEEV ANKLSQAQSL
     ILKGCENCSR SEDVWLEAIR LHPAAEAKVI IANAVKKLPK SVTLWLEAEK LENQAQHKKR
     IIKKALEFNP TSVSLWKEAV NLEEEVDNAR ILLARAVELI PMSIDLWLAL ARLETYENAK
     KVLNKARQTI RTSHEVWIAA ARLEEQQGNV SRVEKIMARG VSELQATGGM LQRDQWLSEA
     EKCETEGAVI TAQAIINTCL GVGLDEEDQF DTWLDDAQSF IARKCIDCAR AVFAFSLRVY
     PKSEKLWLRA VELEKLYGTT ESVCSILEKA VESCPKAEIL WLLYAKERKN VNDIAGARNI
     LGRAFEYNSN SEEIWLAAVR IEFVNNENER ARKLLARARI ESGTERIWTK SISLERILDE
     KDRALQLLEN ALKIYPHYDK LYMMKGQIFE DKEQIELARD AYLAGTKVCP YSIPLWLLLA
     KLEEKQSVIR ARVVFDRAKV KNPKNEFLWL ELIKMELRAG NISQVRAALA KALQECPSSG
     LLWTEAIWLE PRAQRKTRAT DALRKCEGNA HLLCTIARML WLEKKADKAR SWFLKAVKAD
     QDNGDVWCWF YKYSLEAGNE DQQKEVLTSF ETADPHHGYF WPSITKDIKN SRKTPQELLH
     LAINVL