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   27-MAR-2024, entry version 142.
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   EMDB; EMD-21564; -.
DR   EMDB; EMD-30296; -.
DR   EMDB; EMD-30297; -.
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; 4932-YLR145W; -.
DR   PeptideAtlas; Q12530; -.
DR   EnsemblFungi; YLR145W_mRNA; YLR145W; YLR145W.
DR   GeneID; 850837; -.
DR   KEGG; sce:YLR145W; -.
DR   AGR; SGD:S000004135; -.
DR   SGD; S000004135; RMP1.
DR   VEuPathDB; FungiDB:YLR145W; -.
DR   eggNOG; ENOG502S2QW; Eukaryota.
DR   HOGENOM; CLU_031977_1_1_1; -.
DR   InParanoid; Q12530; -.
DR   OMA; VIPRCYI; -.
DR   OrthoDB; 1404540at2759; -.
DR   BioCyc; YEAST:G3O-32282-MONOMER; -.
DR   BioGRID-ORCS; 850837; 5 hits in 10 CRISPR screens.
DR   PRO; PR:Q12530; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q12530; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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, RNase MRP-dependent; IDA:SGD.
DR   CDD; cd22573; RMP1_RBD; 1.
DR   InterPro; IPR047205; RMP1.
DR   InterPro; IPR047204; RMP1_RBD.
DR   PANTHER; PTHR37792; RIBONUCLEASE MRP PROTEIN SUBUNIT RMP1; 1.
DR   PANTHER; PTHR37792:SF1; RIBONUCLEASE MRP PROTEIN SUBUNIT RMP1; 1.
DR   Pfam; PF20945; RMP1; 1.
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
//