RMP1_YEAST
ID RMP1_YEAST Reviewed; 201 AA.
AC Q12530; D6VYD9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ribonuclease MRP protein subunit RMP1;
DE AltName: Full=RNA-processing protein RMP1;
DE AltName: Full=RNase MRP 23.6 kDa subunit;
GN Name=RMP1 {ECO:0000312|SGD:S000004135}; OrderedLocusNames=YLR145W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1] {ECO:0000312|EMBL:AAB82379.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4] {ECO:0000305}
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY, AND
RP MUTAGENESIS OF CYS-103.
RX PubMed=15637077; DOI=10.1074/jbc.m409568200;
RA Salinas K., Wierzbicki S., Zhou L., Schmitt M.E.;
RT "Characterization and purification of Saccharomyces cerevisiae RNase MRP
RT reveals a new unique protein component.";
RL J. Biol. Chem. 280:11352-11360(2005).
CC -!- FUNCTION: Functions as part of ribonuclease MRP (RNase MRP), which is
CC involved in rRNA processing in mitochondria.
CC {ECO:0000269|PubMed:15637077}.
CC -!- SUBUNIT: Component of RNase MRP complex which consists of an RNA moiety
CC and at least 10 protein subunits including POP1, POP3, POP4, POP5,
CC POP6, POP7, POP8, RMP1, RPP1 and SNM1, many of which are shared with
CC the RNase P complex. {ECO:0000269|PubMed:15637077}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U53879; AAB82379.1; -; Genomic_DNA.
DR EMBL; Z73317; CAA97717.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09455.1; -; Genomic_DNA.
DR PIR; S64994; S64994.
DR RefSeq; NP_013246.1; NM_001182032.1.
DR PDB; 6W6V; EM; 3.00 A; L=1-201.
DR PDB; 7C79; EM; 2.50 A; L=1-201.
DR PDB; 7C7A; EM; 2.80 A; L=1-201.
DR PDBsum; 6W6V; -.
DR PDBsum; 7C79; -.
DR PDBsum; 7C7A; -.
DR AlphaFoldDB; Q12530; -.
DR SMR; Q12530; -.
DR BioGRID; 31414; 181.
DR ComplexPortal; CPX-3284; Nucleolar ribonuclease MRP complex.
DR DIP; DIP-4813N; -.
DR IntAct; Q12530; 9.
DR MINT; Q12530; -.
DR STRING; 4932.YLR145W; -.
DR MaxQB; Q12530; -.
DR PaxDb; Q12530; -.
DR PRIDE; Q12530; -.
DR EnsemblFungi; YLR145W_mRNA; YLR145W; YLR145W.
DR GeneID; 850837; -.
DR KEGG; sce:YLR145W; -.
DR SGD; S000004135; RMP1.
DR VEuPathDB; FungiDB:YLR145W; -.
DR eggNOG; ENOG502S2QW; Eukaryota.
DR HOGENOM; CLU_031977_1_1_1; -.
DR InParanoid; Q12530; -.
DR OMA; HRRTKWW; -.
DR BioCyc; YEAST:G3O-32282-MON; -.
DR PRO; PR:Q12530; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12530; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000172; C:ribonuclease MRP complex; IDA:SGD.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IDA:ComplexPortal.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IDA:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Membrane; Nucleus; Reference proteome;
KW rRNA processing; Transmembrane; Transmembrane helix.
FT CHAIN 1..201
FT /note="Ribonuclease MRP protein subunit RMP1"
FT /id="PRO_0000270572"
FT TRANSMEM 86..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 103
FT /note="C->R: In RMP1-6; temperature-sensitive phenotype.
FT Defective in 5.8S rRNA processing."
FT /evidence="ECO:0000269|PubMed:15637077"
FT HELIX 4..25
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:7C7A"
FT HELIX 33..57
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7C7A"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 81..95
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 100..130
FT /evidence="ECO:0007829|PDB:7C79"
SQ SEQUENCE 201 AA; 23619 MW; EDE608D76402BBBC CRC64;
MDEMDNVIRS LEQEYRLILL LNHRNKNQHR AASWYGSFNE MKRNCGQIIT LFSSRRLQAK
RLKDVEWVKL HRLLQRALFR QLKRWYWQFN GVIALGQFVT LGCTLVTLLA NVRALYMRLW
EINETEFIRC GCLIKNLPRT KAKSVVNDVE ELGEIIDEDI GNNVQENELV ITSIPKPLTE
NCKKKKKRKK KNKSAIDGIF G
