FYV4_YEAST
ID FYV4_YEAST Reviewed; 130 AA.
AC P38783; D3DL08;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein FYV4, mitochondrial;
DE AltName: Full=Function required for yeast viability protein 4;
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS41 {ECO:0000303|PubMed:28154081};
DE Flags: Precursor;
GN Name=FYV4; OrderedLocusNames=YHR059W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(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 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 [4]
RP FUNCTION.
RX PubMed=12663529; DOI=10.1093/genetics/163.3.875;
RA Page N., Gerard-Vincent M., Menard P., Beaulieu M., Azuma M.,
RA Dijkgraaf G.J.P., Li H., Marcoux J., Nguyen T., Dowse T., Sdicu A.-M.,
RA Bussey H.;
RT "A Saccharomyces cerevisiae genome-wide mutant screen for altered
RT sensitivity to K1 killer toxin.";
RL Genetics 163:875-894(2003).
RN [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=16552446; DOI=10.1371/journal.pgen.0020035;
RA Gatbonton T., Imbesi M., Nelson M., Akey J.M., Ruderfer D.M., Kruglyak L.,
RA Simon J.A., Bedalov A.;
RT "Telomere length as a quantitative trait: genome-wide survey and genetic
RT mapping of telomere length-control genes in yeast.";
RL PLoS Genet. 2:304-315(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). mS41 is involved in
CC telomere length regulation and required for survival upon exposure to
CC K1 killer toxin (PubMed:12663529, PubMed:16552446).
CC {ECO:0000269|PubMed:12663529, ECO:0000269|PubMed:16552446,
CC ECO:0000305|PubMed:25609543, 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 Note=Mitoribosomes are tethered to the mitochondrial inner membrane and
CC spatially aligned with the membrane insertion machinery through two
CC distinct membrane contact sites, formed by the 21S rRNA expansion
CC segment 96-ES1 and the inner membrane protein MBA1.
CC {ECO:0000269|PubMed:25609543}.
CC -!- MISCELLANEOUS: Present with 2630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS41 family. {ECO:0000305}.
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DR EMBL; U00061; AAB68381.1; -; Genomic_DNA.
DR EMBL; AY558280; AAS56606.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06752.1; -; Genomic_DNA.
DR PIR; S46702; S46702.
DR RefSeq; NP_011926.1; NM_001179189.1.
DR PDB; 5MRC; EM; 3.25 A; 22=30-128.
DR PDB; 5MRE; EM; 3.75 A; 22=30-128.
DR PDB; 5MRF; EM; 4.97 A; 22=30-128.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P38783; -.
DR SMR; P38783; -.
DR BioGRID; 36491; 121.
DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR DIP; DIP-4906N; -.
DR IntAct; P38783; 7.
DR MINT; P38783; -.
DR STRING; 4932.YHR059W; -.
DR MaxQB; P38783; -.
DR PaxDb; P38783; -.
DR PRIDE; P38783; -.
DR EnsemblFungi; YHR059W_mRNA; YHR059W; YHR059W.
DR GeneID; 856456; -.
DR KEGG; sce:YHR059W; -.
DR SGD; S000001101; FYV4.
DR VEuPathDB; FungiDB:YHR059W; -.
DR eggNOG; ENOG502SCMV; Eukaryota.
DR HOGENOM; CLU_126121_2_0_1; -.
DR InParanoid; P38783; -.
DR OMA; FENKWEN; -.
DR BioCyc; YEAST:G3O-31112-MON; -.
DR PRO; PR:P38783; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38783; protein.
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; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR InterPro; IPR039603; Fyv4.
DR InterPro; IPR019083; IGR_protein_motif.
DR PANTHER; PTHR28235; PTHR28235; 1.
DR Pfam; PF09597; IGR; 1.
DR SMART; SM01238; IGR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..130
FT /note="Protein FYV4, mitochondrial"
FT /id="PRO_0000202897"
SQ SEQUENCE 130 AA; 15292 MW; 1662DB8385D067B9 CRC64;
MIPSRISHKF PLFLRSSLAA PKAAYRFSST IPKPSDQVPD VDAFLNKIGR NCNELKDTFE
NNWNNLFQWD SKILKEKGVN IQQRKYILKQ VHNYRNNRPI HEIKLGKKSF FGGERKRKAF
TAKWKAENKQ
