SCE3_SCHPO
ID SCE3_SCHPO Reviewed; 388 AA.
AC O14369;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable RNA-binding protein sce3;
GN Name=sce3; ORFNames=SPBC18H10.04c;
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].
RX PubMed=9254700; DOI=10.1093/nar/25.17.3433;
RA Schmidt S., Hofmann K., Simanis V.;
RT "Sce3, a suppressor of the Schizosaccharomyces pombe septation mutant
RT cdc11, encodes a putative RNA-binding protein.";
RL Nucleic Acids Res. 25:3433-3439(1997).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-50; SER-60; THR-61;
RP SER-64; SER-67; SER-71; SER-197; SER-250; SER-251; SER-252 AND SER-347, 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 -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR EMBL; AJ000318; CAA03989.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA18401.1; -; Genomic_DNA.
DR PIR; T45516; T45516.
DR RefSeq; NP_595728.1; NM_001021626.2.
DR AlphaFoldDB; O14369; -.
DR SMR; O14369; -.
DR BioGRID; 277056; 63.
DR STRING; 4896.SPBC18H10.04c.1; -.
DR iPTMnet; O14369; -.
DR SwissPalm; O14369; -.
DR MaxQB; O14369; -.
DR PaxDb; O14369; -.
DR PRIDE; O14369; -.
DR EnsemblFungi; SPBC18H10.04c.1; SPBC18H10.04c.1:pep; SPBC18H10.04c.
DR GeneID; 2540528; -.
DR KEGG; spo:SPBC18H10.04c; -.
DR PomBase; SPBC18H10.04c; sce3.
DR VEuPathDB; FungiDB:SPBC18H10.04c; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_712052_0_0_1; -.
DR InParanoid; O14369; -.
DR OMA; VARGSNF; -.
DR PhylomeDB; O14369; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-72649; Translation initiation complex formation.
DR Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:O14369; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR GO; GO:0034057; F:RNA strand-exchange activity; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:PomBase.
DR GO; GO:0097010; P:eukaryotic translation initiation factor 4F complex assembly; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..388
FT /note="Probable RNA-binding protein sce3"
FT /id="PRO_0000081900"
FT DOMAIN 94..169
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 18..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 388 AA; 42514 MW; A72E7E2578853AD7 CRC64;
MGPKKSTKMS LNAFLGDESF GSTNWADDID DLPALPQDRT TSTYRATPSS ADAGYNAPSS
TFESVRSPPE SRREGGMGSG YQRDAIPIPS EPPFTAHVGN LSFDLTENDL GDFFGEGVTS
IRLVIDPLTE RSRGFGYVEF ETADTLSAAL ALSGEDLMGR PVRITVAEPR RSFAREERST
GDWVRRGPLP PAEPAESPFG KRRTNSGRFR DPARDPSDRV REEPREWVRR GPLPPRESSE
RPRLNLKPRS SSNVNTEATP SATTTTSSKP KRDPFGGAKP VDNTSVLQRV EEKLAKRTQS
FRREDNANRE RSTSRKPSAD KAEKTDKTDA IAEKVSDIRL GDGEKKSSET DSEVAATKTP
ATEDAPATNA GEAEEEEGWT KIGKGRKH
