RNPS1_SCHPO
ID RNPS1_SCHPO Reviewed; 243 AA.
AC Q1MTR2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=RNA-binding protein with serine-rich domain 1 homolog;
GN ORFNames=SPBC13G1.14c;
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 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: Putative component of the spliceosome which enhances the
CC formation of the ATP-dependent A complex of the spliceosome. may
CC participate in mRNA 3'-end cleavage. Also mediates increase of mRNA
CC abundance and translational efficiency (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the active spliceosome. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; CU329671; CAA20103.2; -; Genomic_DNA.
DR RefSeq; NP_596549.2; NM_001022470.2.
DR AlphaFoldDB; Q1MTR2; -.
DR SMR; Q1MTR2; -.
DR BioGRID; 276249; 2.
DR STRING; 4896.SPBC13G1.14c.1; -.
DR MaxQB; Q1MTR2; -.
DR PaxDb; Q1MTR2; -.
DR EnsemblFungi; SPBC13G1.14c.1; SPBC13G1.14c.1:pep; SPBC13G1.14c.
DR GeneID; 2539695; -.
DR KEGG; spo:SPBC13G1.14c; -.
DR PomBase; SPBC13G1.14c; -.
DR VEuPathDB; FungiDB:SPBC13G1.14c; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_112579_0_0_1; -.
DR InParanoid; Q1MTR2; -.
DR OMA; MANKDES; -.
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 Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q1MTR2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0061574; C:ASAP complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; ISS:PomBase.
DR GO; GO:0003723; F:RNA binding; ISM:PomBase.
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 CDD; cd12365; RRM_RNPS1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034201; RNPS1_RRM.
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 3: Inferred from homology;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..243
FT /note="RNA-binding protein with serine-rich domain 1
FT homolog"
FT /id="PRO_0000372694"
FT DOMAIN 99..177
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 48..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 243 AA; 28369 MW; 53E9DE7D5DE55D32 CRC64;
MLISTFVFLL YEVTALSTAI HVTKSYTHTR TGTSFFMYQK EAFYRGRSST RQFNNTRSPS
GRSASRSSNF SHRSSSRDSF SSNRSYSSSL SRSPEEPLRT ILVENLTRNV TKEHIAEIFG
IYGLIDHIFM PIYKKSELNK GYCYIEYVYH DQAANAVDKM NNAELDGEEL FVSIKRFPFE
SLHKNHKHYE NSYRPSRSQN NSHYNDKSFH RSRYSRARSR SPGSNISEYS DQSPPYHSYR
HRP
