RNC1_SCHPO
ID RNC1_SCHPO Reviewed; 398 AA.
AC O74919;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=RNA-binding protein rnc1;
DE AltName: Full=RNA-binding protein that suppresses calcineurin deletion 1;
GN Name=rnc1 {ECO:0000312|EMBL:CAA21234.1}; ORFNames=SPCC757.09c;
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] {ECO:0000312|EMBL:CAA21234.1}
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] {ECO:0000305}
RP FUNCTION, PHOSPHORYLATION AT THR-50, AND MUTAGENESIS OF THR-50; GLY-110;
RP GLY-195 AND GLY-337.
RX PubMed=12931193; DOI=10.1038/nature01907;
RA Sugiura R., Kita A., Shimizu Y., Shuntoh H., Sio S.O., Kuno T.;
RT "Feedback regulation of MAPK signalling by an RNA-binding protein.";
RL Nature 424:961-965(2003).
RN [3] {ECO:0000305}
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: Binds and stabilizes pmp1 mRNA and hence acts as a negative
CC regulator of pmk1 signaling. Overexpression suppresses the Cl(-)
CC sensitivity of calcineurin deletion. {ECO:0000269|PubMed:12931193}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- PTM: Phosphorylated by pmk1. Phosphorylation causes enhancement of the
CC RNA-binding activity. {ECO:0000269|PubMed:12931193}.
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DR EMBL; CU329672; CAA21234.1; -; Genomic_DNA.
DR PIR; T41600; T41600.
DR RefSeq; NP_587684.1; NM_001022679.2.
DR AlphaFoldDB; O74919; -.
DR SMR; O74919; -.
DR BioGRID; 275997; 160.
DR IntAct; O74919; 1.
DR STRING; 4896.SPCC757.09c.1; -.
DR iPTMnet; O74919; -.
DR MaxQB; O74919; -.
DR PaxDb; O74919; -.
DR PRIDE; O74919; -.
DR EnsemblFungi; SPCC757.09c.1; SPCC757.09c.1:pep; SPCC757.09c.
DR GeneID; 2539434; -.
DR KEGG; spo:SPCC757.09c; -.
DR PomBase; SPCC757.09c; rnc1.
DR VEuPathDB; FungiDB:SPCC757.09c; -.
DR eggNOG; KOG2190; Eukaryota.
DR HOGENOM; CLU_022670_4_2_1; -.
DR InParanoid; O74919; -.
DR OMA; SIAKEPH; -.
DR PhylomeDB; O74919; -.
DR PRO; PR:O74919; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:PomBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IPI:PomBase.
DR GO; GO:0003729; F:mRNA binding; IPI:PomBase.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; EXP:PomBase.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IMP:PomBase.
DR GO; GO:1903138; P:negative regulation of cell wall integrity MAPK cascade; IMP:PomBase.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IDA:PomBase.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..398
FT /note="RNA-binding protein rnc1"
FT /id="PRO_0000334490"
FT DOMAIN 93..157
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 178..243
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 320..385
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 40..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12931193"
FT MUTAGEN 50
FT /note="T->A: Fails to suppress the Cl(-) sensitivity of
FT calcineurin deletion. No longer phosphorylated."
FT /evidence="ECO:0000269|PubMed:12931193"
FT MUTAGEN 50
FT /note="T->D,E: Potently suppresses the Cl(-) sensitivity of
FT calcineurin deletion compared with wild type."
FT /evidence="ECO:0000269|PubMed:12931193"
FT MUTAGEN 110
FT /note="G->D: Barely detectable binding to pmp1 mRNA. Fails
FT to suppress the Cl(-) sensitivity of calcineurin deletion."
FT /evidence="ECO:0000269|PubMed:12931193"
FT MUTAGEN 195
FT /note="G->D: Barely detectable binding to pmp1 mRNA. Fails
FT to suppress the Cl(-) sensitivity of calcineurin deletion."
FT /evidence="ECO:0000269|PubMed:12931193"
FT MUTAGEN 337
FT /note="G->D: Barely detectable binding to pmp1 mRNA. Fails
FT to suppress the Cl(-) sensitivity of calcineurin deletion."
FT /evidence="ECO:0000269|PubMed:12931193"
SQ SEQUENCE 398 AA; 43377 MW; E76CA18E1612492C CRC64;
MAYNHFSIPK NIEEKENSFF DVTFQDEPDE TTSTATGIAK VSIPTPKPST PLSTLTNGST
IQQSMTNQPE PTSQVPPISA KPPMDDATYA TQQLTLRALL STREAGIIIG KAGKNVAELR
STTNVKAGVT KAVPNVHDRV LTISGPLENV VRAYRFIIDI FAKNSTNPDG TPSDANTPRK
LRLLIAHSLM GSIIGRNGLR IKLIQDKCSC RMIASKDMLP QSTERTVEIH GTVDNLHAAI
WEIGKCLIDD WERGAGTVFY NPVSRLTQPL PSLASTASPQ QVSPPAAPST TSGEAIPENF
VSYGAQVFPA TQMPFLQQPK VTQNISIPAD MVGCIIGRGG SKISEIRRTS GSKISIAKEP
HDETGERMFT ITGTHEENEK ALFLLYQQLE MEKDRRSH
