SPP42_SCHPO
ID SPP42_SCHPO Reviewed; 2363 AA.
AC O14187;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Pre-mRNA-splicing factor spp42;
DE AltName: Full=Complexed with cdc5 protein 6;
GN Name=spp42; Synonyms=cwf6; ORFNames=SPAC4F8.12c;
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, INTERACTION WITH PRP1, AND MUTAGENESIS OF GLY-2248.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2015, 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. May be involved in endoplasmic
CC reticulum-associated protein degradation (ERAD) and required for growth
CC at low and high temperatures (By similarity). Required for pre-
CC spliceosome formation, which is the first step of pre-mRNA splicing.
CC This protein is associated with snRNP U5. Has a role in branch site-3'
CC splice site selection. Associates with the branch site-3' splice 3'-
CC exon region. {ECO:0000250, ECO:0000269|PubMed:16133344}.
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. Interacts with prp1.
CC {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:16133344}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; CU329670; CAB11062.1; -; Genomic_DNA.
DR PIR; T38841; T38841.
DR RefSeq; NP_593861.1; NM_001019290.2.
DR PDB; 3JB9; EM; 3.60 A; A=1-2363.
DR PDBsum; 3JB9; -.
DR AlphaFoldDB; O14187; -.
DR SMR; O14187; -.
DR BioGRID; 279835; 35.
DR IntAct; O14187; 9.
DR STRING; 4896.SPAC4F8.12c.1; -.
DR iPTMnet; O14187; -.
DR MaxQB; O14187; -.
DR PaxDb; O14187; -.
DR PRIDE; O14187; -.
DR EnsemblFungi; SPAC4F8.12c.1; SPAC4F8.12c.1:pep; SPAC4F8.12c.
DR GeneID; 2543413; -.
DR KEGG; spo:SPAC4F8.12c; -.
DR PomBase; SPAC4F8.12c; spp42.
DR VEuPathDB; FungiDB:SPAC4F8.12c; -.
DR eggNOG; KOG1795; Eukaryota.
DR HOGENOM; CLU_000380_3_0_1; -.
DR InParanoid; O14187; -.
DR OMA; VCMRREK; -.
DR PhylomeDB; O14187; -.
DR Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
DR PRO; PR:O14187; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:PomBase.
DR GO; GO:0005682; C:U5 snRNP; IDA:PomBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISM:PomBase.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central.
DR GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000393; P:spliceosomal conformational changes to generate catalytic conformation; IGI:PomBase.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IBA:GO_Central.
DR CDD; cd13838; RNase_H_like_Prp8_IV; 1.
DR DisProt; DP02357; -.
DR Gene3D; 1.20.80.40; -; 1.
DR Gene3D; 3.30.420.230; -; 1.
DR Gene3D; 3.30.43.40; -; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR012591; PRO8NT.
DR InterPro; IPR012592; PROCN.
DR InterPro; IPR012984; PROCT.
DR InterPro; IPR027652; PRP8.
DR InterPro; IPR021983; PRP8_domainIV.
DR InterPro; IPR043173; Prp8_domainIV_fingers.
DR InterPro; IPR043172; Prp8_domainIV_palm.
DR InterPro; IPR019581; Prp8_U5-snRNA-bd.
DR InterPro; IPR042516; Prp8_U5-snRNA-bd_sf.
DR InterPro; IPR019580; Prp8_U6-snRNA-bd.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR019582; RRM_spliceosomal_PrP8.
DR PANTHER; PTHR11140; PTHR11140; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08082; PRO8NT; 1.
DR Pfam; PF08083; PROCN; 1.
DR Pfam; PF08084; PROCT; 1.
DR Pfam; PF12134; PRP8_domainIV; 1.
DR Pfam; PF10598; RRM_4; 1.
DR Pfam; PF10597; U5_2-snRNA_bdg; 1.
DR Pfam; PF10596; U6-snRNA_bdg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Spliceosome.
FT CHAIN 1..2363
FT /note="Pre-mRNA-splicing factor spp42"
FT /id="PRO_0000290646"
FT DOMAIN 2128..2261
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2015
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 2248
FT /note="G->D: In spp42-1."
FT /evidence="ECO:0000269|PubMed:16133344"
SQ SEQUENCE 2363 AA; 274556 MW; 128DB6CF3B22EC29 CRC64;
MASLPPGNPP PPPPPPGFEP PSQPPPPPPP GYVKKRKNKT PAQSGNLEKQ LNERARKWRA
SQKSKFGVKR KQGYVQTEKA DLPPEHLRKI MKDRGDMSSR KFRADKRSYL GALKYLPHAV
LKLLENMPMP WEEYREVKVL YHVTGAITFV NESPRVIEPH FIAQWGTMWM MMRREKRDRK
NFKRLRFPPF DDEEPPFSID QLLDLEPLEA IRMDLDEEDD APVMDWFYEN KALEDTPHVN
GPTYRRWKLN LPQMANLHRL GYQLLSDLRD DNYFYLFNDN SFFTAKALNV AIPGGPKFEP
LYKDEAPEME DWNEFNDIYK LIIRHPIKTE YRIAFPYLYN SRARSVALSE YHQPSNVFVP
PEDPDLPAFF WDPIINPITS RQLTLHELDT SPEDSAIEED PNFEIPFDPF FHSEDIEFEH
TASALILLWA PHPFNKRSGA TKRAQDVPLI KHWYLEHCPP NQPVKVRVSY QKLLKSHVMN
KLHMAHPKSH TNRSLLRQLK NTKFFQSTSI DWVEAGLQVC RQGYNMLQLL IHRKGLTYLH
LDYNCNLKPT KTLTTKERKK SRFGNAFHLM REILRLTKLI VDSHVQYRLG NIDAYQLADG
LHYIFNHVGQ LTGMYRYKYR LMRQIRACKD FKHLIYYRFN TGPVGKGPGC GFWAPSWRVW
LFFLRGIVPL LERWLGNLLA RQFEGRHSTG VAKQITKQRV DSHQDLELRA AVMNDILDMI
PEGIRQGKSK TILQHLSEAW RCWKANIPWK VPGLPAPIEN MILRYVKSKA DWWTSVAHFN
RERIRRGATV DKTVAKKNLG RLTRLWLKAE QERQHNYLKD GPYVTADEAV AIYTTFVHWL
ESRRFQPIPF PPLSYKHDTK LLVLALERLK EAYSVKGRLN QSQREELALV EQAYDNPHEM
LSQIKRRLLT MRTFKEVGIE FMDMYSHLIP VYSVDPMEKI CDAYLDQYLW FEADRRHLFP
SWVKPSDSEP PPLLVYKWCQ GINNLTDVWE TSNGECNVLM ETRLSKVFEK VDLTLLNRLM
SLLMDTNLAS YASAKNNVVL SYKDMSHTNS YGLVRGLQFS SFIWQFYGLV LDLLILGLQR
ATEIAGPADA PNDFLHFKDQ ATETSHPIRL YTRYIDKVYI MFRFTDEESR DLIQRFLNEN
PDPTNSNVVN YSKGKKNCWP RDARMRLMKH DVNLGRAVFW EIRNRLPRSL TTLEWEDTFP
SVYSKDNPNL LFSMTGFEVR ILPKIRQNEE FSLKDGVWNL TDNRTKQRTA QAFIRVTEDG
INQFGNRIRQ ILMSSGSTTF TKIANKWNTA LIALMTYYRE AAISTPELLD LLVKCESKIQ
TRVKISLNSK MPSRFPPAVF YSPKELGGLG MLSMGHVLIP QSDLRWSKQT DTGITHFRSG
MTTNGEHLIP NLYRYIQPWE SEFIDSQRVW AEYAMKRQEA LQQNRRLTLE DLEDSWDRGI
PRINTLFQKD RHTLAYDKGW RVRTEFKQYQ LLKNNPFWWT SQRHDGKLWQ LNNYRVDVIQ
ALGGVEGILE HTMFKATGFP SWEGLFWEKA SGFEESMKFK KLTNAQRSGL NQIPNRRFTL
WWSPTINRAN VYVGFQVQLD LTGIMMHGKI PTLKISLIQI FRSHLWQKIH ESVVWDLCQV
LDQELESLQI ETVQKETIHP RKSYKMNSSC ADILLLAAYK WNVSRPSLLN DNRDVLDNTT
TNKYWIDVQL RFGDYDSHDI ERYTRAKFLD YSTDAQSMYP SPTGVLIGID LCYNMHSAYG
NWIPGMKPLI QQSMNKIMKA NPALYVLRER IRKGLQLYAS EPQEQYLSSS NYAELFSNQI
QLFVDDTNVY RVTIHKTFEG NLTTKPINGA IFIFNPRTGQ LFLKVIHTSV WAGQKRLGQL
AKWKTAEEVA ALIRSLPVEE QPRQIIVTRK GMLDPLEVHL LDFPNITIKG SELQLPFQAI
IKLDKINDLI LRATEPQMVL FNLYDDWLQS VSSYTAFSRL ILILRALNVN TEKTKLILRP
DKSIITKENH VWPNLDDQQW LDVEPKLRDL ILADYAKKNN INVASLTNSE VRDIILGMTI
TAPSLQRQQI AEIEKQGREN AQVTAVTTKT TNVHGDEMVV TTTSAYENEK FSSKTEWRNR
AISSISLPLR TKNIYVNSDN ISETFPYTYI LPQNLLRKFV TISDLRTQVA GYMYGKSPSD
NPQIKEIRCI ALVPQLGSIR NVQLPSKLPH DLQPSILEDL EPLGWIHTQS SELPYLSSVD
VTTHAKILSS HPEWDTKAVT LTVSYIPGSI SLAAYTVSKE GIEWGSKNMD INSDEAIGYE
PSMAEKCQLL LSDRIQGFFL VPEEGVWNYN FNGASFSPKM TYSLKLDVPL PFFALEHRPT
HVISYTELET NDRLEEDMPD AFA
