RMP1_SCHPO
ID RMP1_SCHPO Reviewed; 211 AA.
AC Q9UT91;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ribonuclease MRP protein subunit rmp1;
DE AltName: Full=RNA-processing protein rmp1;
GN ORFNames=SPAC323.08;
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-156, 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: Functions as part of ribonuclease MRP (RNase MRP), which is
CC involved in rRNA processing in mitochondria. {ECO:0000250}.
CC -!- SUBUNIT: Component of RNase MRP complex which consists of an RNA moiety
CC and at least 10 protein subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB53411.1; -; Genomic_DNA.
DR PIR; T38645; T38645.
DR RefSeq; NP_594378.1; NM_001019799.2.
DR AlphaFoldDB; Q9UT91; -.
DR SMR; Q9UT91; -.
DR BioGRID; 279521; 11.
DR STRING; 4896.SPAC323.08.1; -.
DR iPTMnet; Q9UT91; -.
DR MaxQB; Q9UT91; -.
DR PaxDb; Q9UT91; -.
DR PRIDE; Q9UT91; -.
DR EnsemblFungi; SPAC323.08.1; SPAC323.08.1:pep; SPAC323.08.
DR GeneID; 2543088; -.
DR KEGG; spo:SPAC323.08; -.
DR PomBase; SPAC323.08; -.
DR VEuPathDB; FungiDB:SPAC323.08; -.
DR eggNOG; ENOG502S2QW; Eukaryota.
DR HOGENOM; CLU_031977_1_0_1; -.
DR InParanoid; Q9UT91; -.
DR OMA; HRRTKWW; -.
DR PRO; PR:Q9UT91; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000172; C:ribonuclease MRP complex; EXP:PomBase.
DR GO; GO:0042134; F:rRNA primary transcript binding; IBA:GO_Central.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IDA:PomBase.
DR GO; GO:1905267; P:endonucleolytic cleavage involved in tRNA processing; IDA:PomBase.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0006379; P:mRNA cleavage; ISO:PomBase.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IBA:GO_Central.
PE 1: Evidence at protein level;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; rRNA processing;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..211
FT /note="Ribonuclease MRP protein subunit rmp1"
FT /id="PRO_0000372385"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 178..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 211 AA; 24202 MW; 3F71AC02366B81C6 CRC64;
MQELQYDVVL LQKIVYRNRN QHRLSVWWRH VRMLLRRLKQ SLDGNEKAKI AILEQLPKSY
FYFTNLIAHG QYPALGLVLL GILARVWFVM GGIEYEAKIQ SEIVFSQKEQ KKLELQSQDD
IDTGTVVARD ELLATEPISL SINPASTSYE KLTVSSPNSF LKNQDESLFL SSSPITVSQG
TKRKSKNSNS TVKKKKKRAR KGRDEIDDIF G
