RMD9L_YEAST
ID RMD9L_YEAST Reviewed; 731 AA.
AC P38330; D6VQN4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=RNA-binding protein RMD9-like, mitochondrial {ECO:0000250|UniProtKB:P53140};
DE Flags: Precursor;
GN OrderedLocusNames=YBR238C; ORFNames=YBR1608;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: May be involved in the processing or stability of
CC mitochondrial mRNAs. {ECO:0000250|UniProtKB:P53140}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P53140}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P53140}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53140}; Matrix side
CC {ECO:0000250|UniProtKB:P53140}.
CC -!- PTM: Phosphorylated. Phosphorylation promotes binding to RNA.
CC {ECO:0000250|UniProtKB:P53140}.
CC -!- MISCELLANEOUS: Present with 2080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RMD9 family. {ECO:0000305}.
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DR EMBL; Z36107; CAA85201.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07354.1; -; Genomic_DNA.
DR PIR; S46115; S46115.
DR RefSeq; NP_009797.1; NM_001178586.1.
DR AlphaFoldDB; P38330; -.
DR SMR; P38330; -.
DR BioGRID; 32933; 401.
DR DIP; DIP-4848N; -.
DR IntAct; P38330; 17.
DR STRING; 4932.YBR238C; -.
DR iPTMnet; P38330; -.
DR MaxQB; P38330; -.
DR PaxDb; P38330; -.
DR PRIDE; P38330; -.
DR EnsemblFungi; YBR238C_mRNA; YBR238C; YBR238C.
DR GeneID; 852540; -.
DR KEGG; sce:YBR238C; -.
DR SGD; S000000442; YBR238C.
DR VEuPathDB; FungiDB:YBR238C; -.
DR eggNOG; ENOG502QUSW; Eukaryota.
DR GeneTree; ENSGT00940000176413; -.
DR HOGENOM; CLU_019840_0_0_1; -.
DR InParanoid; P38330; -.
DR OMA; EMKYGYL; -.
DR BioCyc; YEAST:G3O-29169-MON; -.
DR PRO; PR:P38330; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38330; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0009060; P:aerobic respiration; IGI:SGD.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..731
FT /note="RNA-binding protein RMD9-like, mitochondrial"
FT /id="PRO_0000202521"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..119
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 731 AA; 83761 MW; 4A6800D8476F3DE2 CRC64;
MIRLAQQTQV LKGKPPNQFV PHPTKNSLTH PMKFNGTIAM EHHEHNYAIP YTPATFNNPA
LATYQVSPAN HFVPHFGGNI GANNNNHLAQ NNSNNSNNHH NNNRNHHHNN NRNHHQNNHN
HSKYNNSNQG NSISPDSPWF HKVCAFEDCV SQTLYMSQTP RRQNMKHHSE HPNSNANPLF
WDSIGRAMGL YHDLLTTPEL NSDRVSKLVH LLHNGLRANR NQLTRMNKKP DYDSQSFHKE
MTNYLCKSLR EISEDVLNGK VELNEYGAMH LITAFKELLL FEEAVDIWKA AINGQNTYTS
NIFLNPRVVG VILPILYDNG VSYPEIQALY EKSSSMINYF HPNLSVGMIR ASLSASENDM
ALKLFQKLCQ ESTEMKYGYL IETHLSFIGE CKDLNVAQTF FDKALNDEMP YKIDLQVSYV
KSFLRNIWSQ TRDFNHIYQI WYKSSLHYGR NVNHGISSSL NDTFFDIFFE NYAVDKMQGF
QTLQNIIQTY NNIKHIDEPF FNIILAKCTV WHDRSILEYI DKSYEAYHIP KTIVAYRILL
KSMGSVDDAS NAEILQRWMD LIRKSDEIGQ RFIANADWAA LRDATVTWTQ NDRDSKKSNM
NSTQISRTAT PSPSLTPMDT PAPEHLFNNP QNPMDFYSHP ALQAATASGA FDEFAAEAAS
SSIPVDGRMV LYLKIVKRYS PYCRDSRQLA RLTTGTAVKY SVLQEVLNQF QTLIVNDIPI
PELHNLKPTC V
