COX24_YEAST
ID COX24_YEAST Reviewed; 111 AA.
AC P32344; D6VYK5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Mitochondrial mRNA-processing protein COX24;
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS38 {ECO:0000303|PubMed:28154081};
GN Name=QRI5; Synonyms=COX24; OrderedLocusNames=YLR204W;
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 [GENOMIC DNA].
RX PubMed=1523888; DOI=10.1002/yea.320080707;
RA Simon M., della Seta F., Sor F., Faye G.;
RT "Analysis of the MSS51 region on chromosome XII of Saccharomyces
RT cerevisiae.";
RL Yeast 8:559-567(1992).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
RX PubMed=6297789; DOI=10.1016/0092-8674(83)90498-1;
RA Faye G., Simon M.;
RT "Analysis of a yeast nuclear gene involved in the maturation of
RT mitochondrial pre-messenger RNA of the cytochrome oxidase subunit I.";
RL Cell 32:77-87(1983).
RN [6]
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16339141; DOI=10.1074/jbc.m510778200;
RA Barros M.H., Myers A.M., Van Driesche S., Tzagoloff A.;
RT "COX24 codes for a mitochondrial protein required for processing of the
RT COX1 transcript.";
RL J. Biol. Chem. 281:3743-3751(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=25609543; DOI=10.1038/ncomms7019;
RA Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.;
RT "Organization of the mitochondrial translation machinery studied in situ by
RT cryoelectron tomography.";
RL Nat. Commun. 6:6019-6019(2015).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), AND SUBUNIT.
RX PubMed=28154081; DOI=10.1126/science.aal2415;
RA Desai N., Brown A., Amunts A., Ramakrishnan V.;
RT "The structure of the yeast mitochondrial ribosome.";
RL Science 355:528-531(2017).
CC -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC mitochondrial genome-encoded proteins, including at least some of the
CC essential transmembrane subunits of the mitochondrial respiratory
CC chain. The mitoribosomes are attached to the mitochondrial inner
CC membrane and translation products are cotranslationally integrated into
CC the membrane (PubMed:25609543, PubMed:28154081). mS38 is also involved
CC in the splicing of the COX1 mRNA (PubMed:16339141).
CC {ECO:0000269|PubMed:16339141, ECO:0000305|PubMed:25609543,
CC ECO:0000305|PubMed:28154081}.
CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S)
CC and a large (54S) subunit. The 37S small subunit contains a 15S
CC ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large
CC subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins.
CC {ECO:0000269|PubMed:28154081}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC Mitochondrion inner membrane {ECO:0000269|PubMed:16339141}; Peripheral
CC membrane protein {ECO:0000269|PubMed:16339141}; Matrix side
CC {ECO:0000269|PubMed:16339141}. Note=Mitoribosomes are tethered to the
CC mitochondrial inner membrane and spatially aligned with the membrane
CC insertion machinery through two distinct membrane contact sites, formed
CC by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein
CC MBA1. {ECO:0000269|PubMed:25609543}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS38 family. {ECO:0000305}.
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DR EMBL; J01487; AAA66925.1; -; Genomic_DNA.
DR EMBL; S43721; AAB23217.1; -; Genomic_DNA.
DR EMBL; AY693193; AAT93212.1; -; Genomic_DNA.
DR EMBL; U14913; AAB67429.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09521.1; -; Genomic_DNA.
DR PIR; S25343; S25343.
DR RefSeq; NP_013305.1; NM_001182091.1.
DR PDB; 5MRC; EM; 3.25 A; 11=78-111.
DR PDB; 5MRE; EM; 3.75 A; 11=78-111.
DR PDB; 5MRF; EM; 4.97 A; 11=78-111.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P32344; -.
DR BioGRID; 31472; 138.
DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR DIP; DIP-7605N; -.
DR IntAct; P32344; 73.
DR STRING; 4932.YLR204W; -.
DR PaxDb; P32344; -.
DR EnsemblFungi; YLR204W_mRNA; YLR204W; YLR204W.
DR GeneID; 850901; -.
DR KEGG; sce:YLR204W; -.
DR SGD; S000004194; QRI5.
DR VEuPathDB; FungiDB:YLR204W; -.
DR HOGENOM; CLU_145590_0_0_1; -.
DR OMA; AINTTMP; -.
DR BioCyc; YEAST:G3O-32323-MON; -.
DR PRO; PR:P32344; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32344; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR GO; GO:0006397; P:mRNA processing; IMP:SGD.
DR InterPro; IPR013177; COX24_C.
DR Pfam; PF08213; DUF1713; 1.
DR SMART; SM01155; DUF1713; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW mRNA processing; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..111
FT /note="Mitochondrial mRNA-processing protein COX24"
FT /id="PRO_0000097136"
FT REGION 82..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..104
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 111 AA; 12772 MW; 5B25627D5B4C833D CRC64;
MLGRALRPGW LGITRTVVKK PSCGSYFNRT FQTAINTTMP PMQEGMLSTM MMMTATATRI
TGTVSEPLNG SNIVMQLDSV MRKRKKKMKK HKLRKRRKRE KAERRKLSQG R
