RS17A_YEAST
ID RS17A_YEAST Reviewed; 136 AA.
AC P02407; D6VZF0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=40S ribosomal protein S17-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP51A;
DE AltName: Full=Small ribosomal subunit protein eS17-A {ECO:0000303|PubMed:24524803};
GN Name=RPS17A {ECO:0000303|PubMed:9559554}; Synonyms=RP51A;
GN OrderedLocusNames=YML024W;
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].
RC STRAIN=RY26;
RX PubMed=6308621; DOI=10.1073/pnas.80.14.4403;
RA Teem J.L., Rosbash M.;
RT "Expression of a beta-galactosidase gene containing the ribosomal protein
RT 51 intron is sensitive to the rna2 mutation of yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4403-4407(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 NOMENCLATURE, AND SUBUNIT.
RX PubMed=9559554;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA Planta R.J., Mager W.H.;
RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL Yeast 14:471-477(1998).
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 NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=21109664; DOI=10.1126/science.1194294;
RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT "Crystal structure of the eukaryotic ribosome.";
RL Science 330:1203-1209(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22096102; DOI=10.1126/science.1212642;
RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. {ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC different proteins (encoded by 57 genes). The large 60S subunit
CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- MISCELLANEOUS: Present with 30900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS17 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS17 family.
CC {ECO:0000305}.
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DR EMBL; J01349; AAA88733.1; -; Genomic_DNA.
DR EMBL; Z46659; CAA86631.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09874.1; -; Genomic_DNA.
DR PIR; A02784; R5BY51.
DR RefSeq; NP_013688.1; NM_001182382.1.
DR PDB; 3J6X; EM; 6.10 A; 17=1-136.
DR PDB; 3J6Y; EM; 6.10 A; 17=1-136.
DR PDB; 3J77; EM; 6.20 A; 17=1-136.
DR PDB; 3J78; EM; 6.30 A; 17=1-136.
DR PDB; 4U3M; X-ray; 3.00 A; C7/c7=1-136.
DR PDB; 4U3N; X-ray; 3.20 A; C7/c7=1-136.
DR PDB; 4U3U; X-ray; 2.90 A; C7/c7=1-136.
DR PDB; 4U4N; X-ray; 3.10 A; C7/c7=1-136.
DR PDB; 4U4O; X-ray; 3.60 A; C7/c7=1-136.
DR PDB; 4U4Q; X-ray; 3.00 A; C7/c7=1-136.
DR PDB; 4U4R; X-ray; 2.80 A; C7/c7=1-136.
DR PDB; 4U4U; X-ray; 3.00 A; C7/c7=1-136.
DR PDB; 4U4Y; X-ray; 3.20 A; C7/c7=1-136.
DR PDB; 4U4Z; X-ray; 3.10 A; C7/c7=1-136.
DR PDB; 4U50; X-ray; 3.20 A; C7/c7=1-136.
DR PDB; 4U51; X-ray; 3.20 A; C7/c7=1-136.
DR PDB; 4U52; X-ray; 3.00 A; C7/c7=1-136.
DR PDB; 4U53; X-ray; 3.30 A; C7/c7=1-136.
DR PDB; 4U55; X-ray; 3.20 A; C7/c7=1-136.
DR PDB; 4U56; X-ray; 3.45 A; C7/c7=1-136.
DR PDB; 4U6F; X-ray; 3.10 A; C7/c7=1-136.
DR PDB; 4V6I; EM; 8.80 A; AQ=1-136.
DR PDB; 4V7R; X-ray; 4.00 A; AK/CK=1-136.
DR PDB; 4V88; X-ray; 3.00 A; AR/CR=1-136.
DR PDB; 4V8Y; EM; 4.30 A; AR=1-136.
DR PDB; 4V8Z; EM; 6.60 A; AR=1-136.
DR PDB; 4V92; EM; 3.70 A; R=2-125.
DR PDB; 5DAT; X-ray; 3.15 A; C7/c7=1-136.
DR PDB; 5DC3; X-ray; 3.25 A; C7/c7=1-136.
DR PDB; 5DGE; X-ray; 3.45 A; C7/c7=1-136.
DR PDB; 5DGF; X-ray; 3.30 A; C7/c7=1-136.
DR PDB; 5DGV; X-ray; 3.10 A; C7/c7=1-136.
DR PDB; 5FCI; X-ray; 3.40 A; C7/c7=1-136.
DR PDB; 5FCJ; X-ray; 3.10 A; C7/c7=1-136.
DR PDB; 5I4L; X-ray; 3.10 A; C7/c7=1-136.
DR PDB; 5JUO; EM; 4.00 A; OB=1-136.
DR PDB; 5JUP; EM; 3.50 A; OB=1-136.
DR PDB; 5JUS; EM; 4.20 A; OB=1-136.
DR PDB; 5JUT; EM; 4.00 A; OB=1-136.
DR PDB; 5JUU; EM; 4.00 A; OB=1-136.
DR PDB; 5LYB; X-ray; 3.25 A; C7/c7=2-126.
DR PDB; 5MEI; X-ray; 3.50 A; c7=2-122.
DR PDB; 5NDG; X-ray; 3.70 A; C7/c7=1-136.
DR PDB; 5NDV; X-ray; 3.30 A; C7/c7=1-136.
DR PDB; 5NDW; X-ray; 3.70 A; C7/c7=1-136.
DR PDB; 5OBM; X-ray; 3.40 A; C7/c7=1-136.
DR PDB; 5ON6; X-ray; 3.10 A; S/c7=2-126.
DR PDB; 5TBW; X-ray; 3.00 A; S=2-126, c7=2-122.
DR PDB; 6EML; EM; 3.60 A; C=1-136.
DR PDB; 6FAI; EM; 3.40 A; R=1-136.
DR PDB; 6HHQ; X-ray; 3.10 A; S/c7=1-136.
DR PDB; 6I7O; EM; 5.30 A; G/Gb=2-126.
DR PDB; 6Q8Y; EM; 3.10 A; G=2-126.
DR PDB; 6RBD; EM; 3.47 A; R=1-136.
DR PDB; 6RBE; EM; 3.80 A; R=1-136.
DR PDB; 6S47; EM; 3.28 A; BS=2-136.
DR PDB; 6T4Q; EM; 2.60 A; SR=2-126.
DR PDB; 6WDR; EM; 3.70 A; R=2-126.
DR PDB; 6Y7C; EM; 3.80 A; R=1-136.
DR PDB; 6Z6J; EM; 3.40 A; SR=1-136.
DR PDB; 6Z6K; EM; 3.40 A; SR=1-136.
DR PDB; 6ZCE; EM; 5.30 A; S=1-136.
DR PDB; 6ZU9; EM; 6.20 A; I=1-136.
DR PDB; 6ZVI; EM; 3.00 A; z=2-126.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6WDR; -.
DR PDBsum; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR AlphaFoldDB; P02407; -.
DR SMR; P02407; -.
DR BioGRID; 35145; 614.
DR IntAct; P02407; 65.
DR MINT; P02407; -.
DR STRING; 4932.YML024W; -.
DR iPTMnet; P02407; -.
DR MaxQB; P02407; -.
DR PaxDb; P02407; -.
DR PRIDE; P02407; -.
DR EnsemblFungi; YML024W_mRNA; YML024W; YML024W.
DR GeneID; 854984; -.
DR KEGG; sce:YML024W; -.
DR SGD; S000004486; RPS17A.
DR VEuPathDB; FungiDB:YML024W; -.
DR eggNOG; KOG0187; Eukaryota.
DR GeneTree; ENSGT00390000006548; -.
DR HOGENOM; CLU_112958_0_1_1; -.
DR InParanoid; P02407; -.
DR OMA; GMAFRGP; -.
DR BioCyc; YEAST:G3O-32626-MON; -.
DR PRO; PR:P02407; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P02407; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; NAS:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:SGD.
DR Gene3D; 1.10.60.20; -; 1.
DR HAMAP; MF_00511; Ribosomal_S17e; 1.
DR InterPro; IPR001210; Ribosomal_S17e.
DR InterPro; IPR018273; Ribosomal_S17e_CS.
DR InterPro; IPR036401; RPS17e-like_sf.
DR PANTHER; PTHR10732; PTHR10732; 1.
DR Pfam; PF00833; Ribosomal_S17e; 1.
DR SUPFAM; SSF116820; SSF116820; 1.
DR PROSITE; PS00712; RIBOSOMAL_S17E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..136
FT /note="40S ribosomal protein S17-A"
FT /id="PRO_0000141546"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6RBD"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6FAI"
SQ SEQUENCE 136 AA; 15788 MW; 956E5382870EA289 CRC64;
MGRVRTKTVK RASKALIERY YPKLTLDFQT NKRLCDEIAT IQSKRLRNKI AGYTTHLMKR
IQKGPVRGIS FKLQEEERER KDQYVPEVSA LDLSRSNGVL NVDNQTSDLV KSLGLKLPLS
VINVSAQRDR RYRKRV
