ID   G1TN72_RABIT            Unreviewed;       264 AA.
AC   G1TN72;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Small ribosomal subunit protein eS1 {ECO:0000256|HAMAP-Rule:MF_03122};
GN   Name=RPS3A {ECO:0000256|HAMAP-Rule:MF_03122};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000018441.1, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000018441.1, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
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:0007829|PDB:4KZX, ECO:0007829|PDB:4KZY}
RP   X-RAY CRYSTALLOGRAPHY (7.01 ANGSTROMS).
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] {ECO:0007829|PDB:5K0Y}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.80 ANGSTROMS) OF 19-233.
RX   PubMed=27373335; DOI=10.1016/j.molcel.2016.05.033;
RA   Simonetti A., Brito Querido J., Myasnikov A.G., Mancera-Martinez E.,
RA   Renaud A., Kuhn L., Hashem Y.;
RT   "eIF3 Peripheral Subunits Rearrangement after mRNA Binding and Start-Codon
RT   Recognition.";
RL   Mol. Cell 63:206-217(2016).
RN   [4] {ECO:0007829|PDB:6YAN}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.48 ANGSTROMS) OF 19-233.
RX   PubMed=32268096; DOI=10.1016/j.celrep.2020.03.061;
RA   Simonetti A., Guca E., Bochler A., Kuhn L., Hashem Y.;
RT   "Structural Insights into the Mammalian Late-Stage Initiation Complexes.";
RL   Cell Rep. 31:107497-107497(2020).
RN   [5] {ECO:0007829|PDB:6YAL, ECO:0007829|PDB:6YAM}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS).
RA   Simonetti A., Guca E., Bochler A., Kuhn L., Hashem Y.;
RT   "Structural insights into the mammalian late-stage initiation complexes.";
RL   Submitted (MAR-2020) to the PDB data bank.
RN   [6] {ECO:0000313|Ensembl:ENSOCUP00000018441.1}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000018441.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May play a role during erythropoiesis through regulation of
CC       transcription factor DDIT3. {ECO:0000256|HAMAP-Rule:MF_03122}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC       consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC       contains about 33 different proteins and 1 molecule of RNA (18S). The
CC       60S subunit contains about 49 different proteins and 3 molecules of RNA
CC       (28S, 5.8S and 5S). Identified in a IGF2BP1-dependent mRNP granule
CC       complex containing untranslated mRNAs. Binds with high affinity to
CC       IPO4. Interacts with DDIT3. {ECO:0000256|HAMAP-Rule:MF_03122}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03122}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03122}. Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}. Note=Localized in cytoplasmic mRNP
CC       granules containing untranslated mRNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_03122}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_03122, ECO:0000256|RuleBase:RU000668}.
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DR   PDB; 4KZX; X-ray; 7.81 A; B=1-264.
DR   PDB; 4KZY; X-ray; 7.01 A; B=1-264.
DR   PDB; 4KZZ; X-ray; 7.03 A; B=1-264.
DR   PDB; 5K0Y; EM; 5.80 A; i=19-233.
DR   PDB; 6YAL; EM; 3.00 A; D=1-264.
DR   PDB; 6YAM; EM; 3.60 A; D=1-264.
DR   PDB; 6YAN; EM; 3.48 A; D=19-233.
DR   PDBsum; 4KZX; -.
DR   PDBsum; 4KZY; -.
DR   PDBsum; 4KZZ; -.
DR   PDBsum; 5K0Y; -.
DR   PDBsum; 6YAL; -.
DR   PDBsum; 6YAM; -.
DR   PDBsum; 6YAN; -.
DR   AlphaFoldDB; G1TN72; -.
DR   SMR; G1TN72; -.
DR   STRING; 9986.ENSOCUP00000018441; -.
DR   PaxDb; 9986-ENSOCUP00000018441; -.
DR   Ensembl; ENSOCUT00000031254.1; ENSOCUP00000018441.1; ENSOCUG00000024968.1.
DR   eggNOG; KOG1628; Eukaryota.
DR   GeneTree; ENSGT00390000018433; -.
DR   HOGENOM; CLU_062507_0_1_1; -.
DR   InParanoid; G1TN72; -.
DR   OMA; MVKKWQX; -.
DR   TreeFam; TF300037; -.
DR   Proteomes; UP000001811; Unplaced.
DR   Bgee; ENSOCUG00000024968; Expressed in blood and 16 other cell types or tissues.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03122; Ribosomal_S3Ae_euk; 1.
DR   InterPro; IPR001593; Ribosomal_eS1.
DR   InterPro; IPR018281; Ribosomal_eS1_CS.
DR   InterPro; IPR027500; Ribosomal_eS1_euk.
DR   PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR   PANTHER; PTHR11830:SF28; 40S RIBOSOMAL PROTEIN S3A; 1.
DR   Pfam; PF01015; Ribosomal_S3Ae; 1.
DR   SMART; SM01397; Ribosomal_S3Ae; 1.
DR   PROSITE; PS01191; RIBOSOMAL_S3AE; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4KZX, ECO:0007829|PDB:4KZY};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03122};
KW   Differentiation {ECO:0000256|HAMAP-Rule:MF_03122};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03122};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_03122};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_03122}.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03122"
FT   REGION          232..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  29873 MW;  B812224E085F63CB CRC64;
     MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD
     GLKGRVFEVS LADLQNDEVA FRKFKLITED VQGKNCLTNF HGMDLTRDKM CSMVKKWQTM
     IEAHVDVKTT DGYLLHLFCV GFTKKCNNQI RKTSYAQHQQ VRQIRKKMME IMTREVQTND
     LKEVVNKLIP DSIGKDIEKA CQSIYPLHDV FVRKVKMLKK PKFELGKLME LHGEGSSSGK
     ATGDETGAKV ERADGYEPPV QESV
//