SPP2_SCHPO
ID SPP2_SCHPO Reviewed; 381 AA.
AC O43031; Q9US93;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 3.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Pre-mRNA-splicing factor cwf28;
DE AltName: Full=Complexed with cdc5 protein 28;
GN Name=cwf28; ORFNames=SPBC3B9.02c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 140-321, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
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 [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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; SER-275 AND
RP SER-277, AND 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 spliceosome maturation and the first step of pre-
CC mRNA splicing. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SPP2 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17782.1; -; Genomic_DNA.
DR EMBL; AB027944; BAA87248.1; -; Genomic_DNA.
DR PIR; T40341; T40341.
DR RefSeq; NP_596659.1; NM_001022581.2.
DR AlphaFoldDB; O43031; -.
DR BioGRID; 276832; 89.
DR IntAct; O43031; 1.
DR STRING; 4896.SPBC3B9.02c.1; -.
DR iPTMnet; O43031; -.
DR MaxQB; O43031; -.
DR PaxDb; O43031; -.
DR PRIDE; O43031; -.
DR EnsemblFungi; SPBC3B9.02c.1; SPBC3B9.02c.1:pep; SPBC3B9.02c.
DR GeneID; 2540302; -.
DR KEGG; spo:SPBC3B9.02c; -.
DR PomBase; SPBC3B9.02c; cwf28.
DR VEuPathDB; FungiDB:SPBC3B9.02c; -.
DR eggNOG; ENOG502RZY8; Eukaryota.
DR HOGENOM; CLU_756852_0_0_1; -.
DR InParanoid; O43031; -.
DR OMA; TEGVYMP; -.
DR PhylomeDB; O43031; -.
DR PRO; PR:O43031; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; ISO:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISO:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR InterPro; IPR045166; Spp2-like.
DR InterPro; IPR026822; Spp2/MOS2_G-patch.
DR PANTHER; PTHR15818; PTHR15818; 1.
DR Pfam; PF12656; G-patch_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT CHAIN 1..381
FT /note="Pre-mRNA-splicing factor cwf28"
FT /id="PRO_0000218527"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..157
FT /evidence="ECO:0000255"
FT COMPBIAS 262..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 381 AA; 44215 MW; E1542538B667549F CRC64;
MKRKAVLEAF SDSEDEDEKK LKGPQLITGF SAEEGVHYQN ETIQRIHEKK RAPKIIHIAS
DENWMEKRKA RFKKKETEVH EKPSQLPDSG LNYGLNIRVA SSSAADNEIV DWKANNSNEK
AQNKIATNKE STDILPEEVQ LVLNDLNDDV KSANSANLQP ITTNVVNEKD AYRKDIDELP
EPSNMKDYSE IPVEEFGAAM LRGMGWNGQL SSKDAFDVNQ RPTFLGMGAK PVDSELTELD
IWKNPKKTMF LPVKPLESNS ALNSQNEHTE VQKKSNSIDN LTPSSELFRK RSRDNNLSRE
SSVSSKHLDY NSRNYNKRDR DPDRTKYREY HSERRKQHRT DRYSDDYYQG RSYSYKKRSH
RSDRYTEREN PDRSYRSTRT L
