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Database: UniProt
Entry: G1TFE8
LinkDB: G1TFE8
Original site: G1TFE8 
ID   RS26_RABIT              Reviewed;         115 AA.
AC   G1TFE8;
DT   27-MAR-2024, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Small ribosomal subunit protein eS26;
DE   AltName: Full=40S ribosomal protein S26 {ECO:0000255|RuleBase:RU363128};
GN   Name=RPS26;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke;
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0007744|PDB:4KZX, ECO:0007744|PDB:4KZY}
RP   X-RAY CRYSTALLOGRAPHY (7.01 ANGSTROMS) OF 40S RIBOSOME, FUNCTION, SUBUNIT,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=23873042; DOI=10.1038/nature12355;
RA   Lomakin I.B., Steitz T.A.;
RT   "The initiation of mammalian protein synthesis and mRNA scanning
RT   mechanism.";
RL   Nature 500:307-311(2013).
RN   [3]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=26245381; DOI=10.1038/nature14896;
RA   Brown A., Shao S., Murray J., Hegde R.S., Ramakrishnan V.;
RT   "Structural basis for stop codon recognition in eukaryotes.";
RL   Nature 524:493-496(2015).
RN   [4] {ECO:0007744|PDB:4D5L, ECO:0007744|PDB:4D61}
RP   STRUCTURE BY ELECTRON MICROSCOPY (9.00 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=25601755; DOI=10.1016/j.molcel.2014.12.016;
RA   Muhs M., Hilal T., Mielke T., Skabkin M.A., Sanbonmatsu K.Y., Pestova T.V.,
RA   Spahn C.M.;
RT   "Cryo-EM of ribosomal 80S complexes with termination factors reveals the
RT   translocated cricket paralysis virus IRES.";
RL   Mol. Cell 57:422-432(2015).
RN   [5] {ECO:0007744|PDB:6D90}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF RIBOSOME, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=29856316; DOI=10.7554/elife.34062;
RA   Pisareva V.P., Pisarev A.V., Fernandez I.S.;
RT   "Dual tRNA mimicry in the Cricket paralysis virus IRES uncovers an
RT   unexpected similarity with the Hepatitis C Virus IRES.";
RL   Elife 7:0-0(2018).
RN   [6] {ECO:0007744|PDB:6P5I, ECO:0007744|PDB:6P5J}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF RIBOSOME, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=31609474; DOI=10.15252/embj.2019102226;
RA   Acosta-Reyes F., Neupane R., Frank J., Fernandez I.S.;
RT   "The Israeli acute paralysis virus IRES captures host ribosomes by
RT   mimicking a ribosomal state with hybrid tRNAs.";
RL   EMBO J. 38:e102226-e102226(2019).
RN   [7] {ECO:0007744|PDB:6W2S, ECO:0007744|PDB:6W2T}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF RIBOSOME, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=32286223; DOI=10.7554/elife.54575;
RA   Neupane R., Pisareva V.P., Rodriguez C.F., Pisarev A.V., Fernandez I.S.;
RT   "A complex IRES at the 5'-UTR of a viral mRNA assembles a functional 48S
RT   complex via an uAUG intermediate.";
RL   Elife 9:0-0(2020).
RN   [8] {ECO:0007744|PDB:7SYO, ECO:0007744|PDB:7SYP}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF RIBOSOME, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=35822879; DOI=10.15252/embj.2022110581;
RA   Brown Z.P., Abaeva I.S., De S., Hellen C.U.T., Pestova T.V., Frank J.;
RT   "Molecular architecture of 40S translation initiation complexes on the
RT   hepatitis C virus IRES.";
RL   EMBO J. 41:e110581-e110581(2022).
RN   [9] {ECO:0007744|PDB:7UCJ, ECO:0007744|PDB:7UCK}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF 2-102 OF RIBOSOME,
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=35679869; DOI=10.1016/j.molcel.2022.05.016;
RA   Arango D., Sturgill D., Yang R., Kanai T., Bauer P., Roy J., Wang Z.,
RA   Hosogane M., Schiffers S., Oberdoerffer S.;
RT   "Direct epitranscriptomic regulation of mammalian translation initiation
RT   through N4-acetylcytidine.";
RL   Mol. Cell 82:2797-2814(2022).
CC   -!- FUNCTION: Component of the small ribosomal subunit (PubMed:23873042,
CC       PubMed:26245381, PubMed:25601755). The ribosome is a large
CC       ribonucleoprotein complex responsible for the synthesis of proteins in
CC       the cell (PubMed:23873042, PubMed:26245381, PubMed:25601755).
CC       {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755,
CC       ECO:0000269|PubMed:26245381}.
CC   -!- SUBUNIT: Component of the 40S small ribosomal subunit.
CC       {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755,
CC       ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:29856316,
CC       ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:32286223,
CC       ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35822879}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P62854}. Cytoplasm {ECO:0000269|PubMed:23873042,
CC       ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381,
CC       ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:31609474,
CC       ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:35679869,
CC       ECO:0000269|PubMed:35822879}. Rough endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P49171}. Note=Detected on cytosolic polysomes
CC       (By similarity). Detected in ribosomes that are associated with the
CC       rough endoplasmic reticulum (By similarity).
CC       {ECO:0000250|UniProtKB:P49171, ECO:0000250|UniProtKB:P62854}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS26 family.
CC       {ECO:0000305}.
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DR   EMBL; AAGW02026493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_002717359.1; XM_002717313.3.
DR   PDB; 4D5L; EM; 9.00 A; a=1-115.
DR   PDB; 4D61; EM; 9.00 A; a=1-115.
DR   PDB; 4KZX; X-ray; 7.81 A; a=1-115.
DR   PDB; 4KZY; X-ray; 7.01 A; a=1-115.
DR   PDB; 4KZZ; X-ray; 7.03 A; a=1-115.
DR   PDB; 5K0Y; EM; 5.80 A; k=2-100.
DR   PDB; 6D90; EM; 3.20 A; bb=1-115.
DR   PDB; 6P4G; EM; 3.10 A; b=1-115.
DR   PDB; 6P4H; EM; 3.20 A; b=1-115.
DR   PDB; 6P5I; EM; 3.10 A; b=1-115.
DR   PDB; 6P5J; EM; 3.10 A; b=1-115.
DR   PDB; 6P5K; EM; 3.10 A; b=1-115.
DR   PDB; 6P5N; EM; 3.20 A; b=1-115.
DR   PDB; 6W2S; EM; 3.00 A; b=1-115.
DR   PDB; 6W2T; EM; 3.36 A; b=1-115.
DR   PDB; 6YAL; EM; 3.00 A; b=1-115.
DR   PDB; 6YAM; EM; 3.60 A; b=1-115.
DR   PDB; 6YAN; EM; 3.48 A; b=2-100.
DR   PDB; 7JQB; EM; 2.70 A; b=1-115.
DR   PDB; 7JQC; EM; 3.30 A; b=1-115.
DR   PDB; 7MDZ; EM; 3.20 A; aa=1-115.
DR   PDB; 7SYG; EM; 4.30 A; b=2-102.
DR   PDB; 7SYH; EM; 4.60 A; b=2-102.
DR   PDB; 7SYI; EM; 4.50 A; b=2-102.
DR   PDB; 7SYJ; EM; 4.80 A; b=2-102.
DR   PDB; 7SYK; EM; 4.20 A; b=2-102.
DR   PDB; 7SYL; EM; 4.50 A; b=2-102.
DR   PDB; 7SYM; EM; 4.80 A; b=2-102.
DR   PDB; 7SYN; EM; 4.00 A; b=2-102.
DR   PDB; 7SYO; EM; 4.60 A; b=2-102.
DR   PDB; 7SYP; EM; 4.00 A; b=2-102.
DR   PDB; 7SYQ; EM; 3.80 A; b=2-102.
DR   PDB; 7SYR; EM; 3.60 A; b=2-102.
DR   PDB; 7SYS; EM; 3.50 A; b=2-102.
DR   PDB; 7SYT; EM; 4.40 A; b=2-102.
DR   PDB; 7SYU; EM; 4.60 A; b=2-102.
DR   PDB; 7SYV; EM; 3.90 A; b=2-102.
DR   PDB; 7SYW; EM; 3.70 A; b=2-102.
DR   PDB; 7SYX; EM; 3.70 A; b=2-102.
DR   PDB; 7TOQ; EM; 3.10 A; AS26=2-102.
DR   PDB; 7TOR; EM; 2.90 A; AS26=2-102.
DR   PDB; 7UCJ; EM; 3.10 A; Aa=2-102.
DR   PDB; 7UCK; EM; 2.80 A; Aa=2-102.
DR   PDBsum; 4D5L; -.
DR   PDBsum; 4D61; -.
DR   PDBsum; 4KZX; -.
DR   PDBsum; 4KZY; -.
DR   PDBsum; 4KZZ; -.
DR   PDBsum; 5K0Y; -.
DR   PDBsum; 6D90; -.
DR   PDBsum; 6P4G; -.
DR   PDBsum; 6P4H; -.
DR   PDBsum; 6P5I; -.
DR   PDBsum; 6P5J; -.
DR   PDBsum; 6P5K; -.
DR   PDBsum; 6P5N; -.
DR   PDBsum; 6W2S; -.
DR   PDBsum; 6W2T; -.
DR   PDBsum; 6YAL; -.
DR   PDBsum; 6YAM; -.
DR   PDBsum; 6YAN; -.
DR   PDBsum; 7JQB; -.
DR   PDBsum; 7JQC; -.
DR   PDBsum; 7MDZ; -.
DR   PDBsum; 7SYG; -.
DR   PDBsum; 7SYH; -.
DR   PDBsum; 7SYI; -.
DR   PDBsum; 7SYJ; -.
DR   PDBsum; 7SYK; -.
DR   PDBsum; 7SYL; -.
DR   PDBsum; 7SYM; -.
DR   PDBsum; 7SYN; -.
DR   PDBsum; 7SYO; -.
DR   PDBsum; 7SYP; -.
DR   PDBsum; 7SYQ; -.
DR   PDBsum; 7SYR; -.
DR   PDBsum; 7SYS; -.
DR   PDBsum; 7SYT; -.
DR   PDBsum; 7SYU; -.
DR   PDBsum; 7SYV; -.
DR   PDBsum; 7SYW; -.
DR   PDBsum; 7SYX; -.
DR   PDBsum; 7TOQ; -.
DR   PDBsum; 7TOR; -.
DR   PDBsum; 7UCJ; -.
DR   PDBsum; 7UCK; -.
DR   AlphaFoldDB; G1TFE8; -.
DR   IntAct; G1TFE8; 1.
DR   STRING; 9986.ENSOCUP00000015638; -.
DR   PaxDb; 9986-ENSOCUP00000015638; -.
DR   Ensembl; ENSOCUT00000013552.2; ENSOCUP00000015638.1; ENSOCUG00000028015.1.
DR   GeneID; 100346996; -.
DR   eggNOG; KOG1768; Eukaryota.
DR   HOGENOM; CLU_129451_0_1_1; -.
DR   InParanoid; G1TFE8; -.
DR   OrthoDB; 329at2759; -.
DR   TreeFam; TF300234; -.
DR   Proteomes; UP000001811; Chromosome 16.
DR   Bgee; ENSOCUG00000028015; Expressed in uterus and 17 other cell types or tissues.
DR   PROSITE; PS00733; RIBOSOMAL_S26E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endoplasmic reticulum; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62854"
FT   CHAIN           2..115
FT                   /note="Small ribosomal subunit protein eS26"
FT                   /id="PRO_0000460076"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:26245381"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:26245381"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:26245381"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:26245381"
FT   MOD_RES         54
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62854"
SQ   SEQUENCE   115 AA;  12931 MW;  B71DE8998E01CD03 CRC64;
     MTKKRRNNGR AKKGRGHVQP IRCTNCACCV PKDKAIKKFV IRNIVEAAAV RDISEVSVFD
     AYVLPKLYVK LHYCVSCAIH SKVVRNRSRE ARKDRTPPPR FRPAGAAPPP PPKPM
//
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