RR14C_SCHPO
ID RR14C_SCHPO Reviewed; 233 AA.
AC O43082;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Ribosomal RNA-processing protein 14-C;
DE AltName: Full=Ribosome biogenesis protein rrp14-C;
GN Name=rrp14c; ORFNames=SPBC947.07;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, 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 ribosome biogenesis and cell polarity. Required
CC for the synthesis of both 40S and 60S ribosomal subunits and may also
CC play some direct role in correct positioning of the mitotic spindle
CC during mitosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the 90S and 60S pre-ribosomal particles.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SURF6 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17035.1; -; Genomic_DNA.
DR PIR; T40775; T40775.
DR RefSeq; NP_595269.1; NM_001021176.2.
DR AlphaFoldDB; O43082; -.
DR SMR; O43082; -.
DR STRING; 4896.SPBC947.07.1; -.
DR iPTMnet; O43082; -.
DR MaxQB; O43082; -.
DR PaxDb; O43082; -.
DR PRIDE; O43082; -.
DR EnsemblFungi; SPBC947.07.1; SPBC947.07.1:pep; SPBC947.07.
DR GeneID; 2541261; -.
DR KEGG; spo:SPBC947.07; -.
DR PomBase; SPBC947.07; -.
DR VEuPathDB; FungiDB:SPBC947.07; -.
DR eggNOG; KOG2885; Eukaryota.
DR HOGENOM; CLU_1143100_0_0_1; -.
DR InParanoid; O43082; -.
DR OMA; HTFEELH; -.
DR PhylomeDB; O43082; -.
DR PRO; PR:O43082; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:PomBase.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR029190; Rrp14/SURF6_C.
DR InterPro; IPR007019; SURF6.
DR PANTHER; PTHR14369; PTHR14369; 1.
DR Pfam; PF04935; SURF6; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; rRNA processing.
FT CHAIN 1..233
FT /note="Ribosomal RNA-processing protein 14-C"
FT /id="PRO_0000356272"
FT REGION 47..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..65
FT /evidence="ECO:0000255"
FT COILED 122..223
FT /evidence="ECO:0000255"
FT COMPBIAS 47..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..233
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 233 AA; 27125 MW; 5148EC3FF992EA1C CRC64;
METTEGKNDL RAKLAEKIQT FRSQRKATEK VDRALLLQRR KEKAKARAEA KKLAKKESKA
KQESKVAAYD TGNSSDNIAD EENDNHKSTI TYGTLIVGDD KFSNGKLKVA GKKRGPTDVF
GALKHLEAKK RRIESMDEEK RRKIEESDKW HRVLLQAEGK KLKDNEQLLK KSIRRKEKEK
KKSSDAWKER KDNEKKAMLM RQQRREENLK KRRESKKSKK GKAPKKKKPS KKK
