RPA14_SCHPO
ID RPA14_SCHPO Reviewed; 147 AA.
AC Q9P7P1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=DNA-directed RNA polymerase I subunit rpa14;
DE Short=RNA polymerase I subunit A14;
DE AltName: Full=DNA-directed RNA polymerase I 17 kDa polypeptide;
DE AltName: Full=Nucleolar protein ker1;
GN Name=ker1; ORFNames=SPBC1718.03;
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 [MRNA], FUNCTION, INTERACTION WITH RPA43,
RP IDENTIFICATION IN THE RNA POL I COMPLEX, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=15647272; DOI=10.1074/jbc.m411150200;
RA Imazawa Y., Hisatake K., Mitsuzawa H., Matsumoto M., Tsukui T.,
RA Nakagawa K., Nakadai T., Shimada M., Ishihama A., Nogi Y.;
RT "The fission yeast protein Ker1p is an ortholog of RNA polymerase I subunit
RT A14 in Saccharomyces cerevisiae and is required for stable association of
RT Rrn3p and RPA21 in RNA polymerase I.";
RL J. Biol. Chem. 280:11467-11474(2005).
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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase I which synthesizes ribosomal RNA
CC precursors. A14 seems to play a role in the stability of Pol I subunit
CC A43 and association of rrn3 to Pol I. {ECO:0000269|PubMed:15647272}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of 14 subunits. Part of a Pol I subcomplex consisting of the subunits
CC A14 and A43. Interacts with rpa43. {ECO:0000269|PubMed:15647272}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15647272}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15647272}.
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DR EMBL; AB079137; BAB91320.1; -; mRNA.
DR EMBL; CU329671; CAB75993.1; -; Genomic_DNA.
DR PIR; T50331; T50331.
DR RefSeq; NP_596449.1; NM_001022368.2.
DR PDB; 7AOC; EM; 3.84 A; D=1-147.
DR PDB; 7AOD; EM; 4.50 A; D/P=1-147.
DR PDB; 7AOE; EM; 3.90 A; D=1-147.
DR PDBsum; 7AOC; -.
DR PDBsum; 7AOD; -.
DR PDBsum; 7AOE; -.
DR AlphaFoldDB; Q9P7P1; -.
DR SMR; Q9P7P1; -.
DR BioGRID; 276230; 9.
DR STRING; 4896.SPBC1718.03.1; -.
DR MaxQB; Q9P7P1; -.
DR PaxDb; Q9P7P1; -.
DR EnsemblFungi; SPBC1718.03.1; SPBC1718.03.1:pep; SPBC1718.03.
DR GeneID; 2539675; -.
DR KEGG; spo:SPBC1718.03; -.
DR PomBase; SPBC1718.03; ker1.
DR VEuPathDB; FungiDB:SPBC1718.03; -.
DR HOGENOM; CLU_1787937_0_0_1; -.
DR OMA; NFLEGYV; -.
DR PRO; PR:Q9P7P1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:PomBase.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IGI:PomBase.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription.
FT CHAIN 1..147
FT /note="DNA-directed RNA polymerase I subunit rpa14"
FT /id="PRO_0000073961"
FT REGION 71..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 147 AA; 16976 MW; CE29FCA8638BEF02 CRC64;
MATECPPKMI LRKSEKLDKD ASSKFLNRYI QTIERFQDEK SGSESVLSQL NRVLMYLKGE
EIPLISLNLP VQGPPTEELI IPPEEMLETK EEESLKHARE ENDDLHLDKE TKKRLKKEKK
KAARREKEEA RKAKADTTQG VGEKEQS
