RS21_SCHPO
ID RS21_SCHPO Reviewed; 87 AA.
AC P05764; O94496;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=40S ribosomal protein S21;
DE AltName: Full=S28;
GN Name=rps21; ORFNames=SPBC18E5.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=3910104; DOI=10.1021/bi00346a058;
RA Itoh T., Otaka E., Matsui K.A.;
RT "Primary structures of ribosomal protein YS25 from Saccharomyces cerevisiae
RT and its counterparts from Schizosaccharomyces pombe and rat liver.";
RL Biochemistry 24:7418-7423(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, INTERACTION WITH RPS0A AND RPS0B, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=14623272; DOI=10.1016/j.bbrc.2003.10.086;
RA Sato M., Kong C.J., Yoshida H., Nakamura T., Wada A., Shimoda C.,
RA Kaneda Y.;
RT "Ribosomal proteins S0 and S21 are involved in the stability of 18S rRNA in
RT fission yeast, Schizosaccharomyces pombe.";
RL Biochem. Biophys. Res. Commun. 311:942-947(2003).
CC -!- FUNCTION: Required for the processing of the 20S rRNA-precursor to
CC mature 18S rRNA in a late step of the maturation of 40S ribosomal
CC subunits. Has a physiological role leading to 18S rRNA stability.
CC {ECO:0000269|PubMed:14623272}.
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 (25S, 5.8S and 5S). Interacts with rps0a and rps0b, strongest
CC interaction is with rps0b. {ECO:0000269|PubMed:14623272}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14623272}.
CC -!- DISRUPTION PHENOTYPE: Deficiency of 40S ribosomal subunit formation,
CC this is likely to be caused by insufficient 18S rRNA stability.
CC {ECO:0000269|PubMed:14623272}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA22666.1; -; Genomic_DNA.
DR PIR; B23862; B23862.
DR PIR; T39757; T39757.
DR RefSeq; NP_595852.1; NM_001021756.2.
DR AlphaFoldDB; P05764; -.
DR SMR; P05764; -.
DR BioGRID; 277325; 7.
DR STRING; 4896.SPBC18E5.06.1; -.
DR iPTMnet; P05764; -.
DR SwissPalm; P05764; -.
DR MaxQB; P05764; -.
DR PaxDb; P05764; -.
DR PRIDE; P05764; -.
DR EnsemblFungi; SPBC18E5.06.1; SPBC18E5.06.1:pep; SPBC18E5.06.
DR GeneID; 2540806; -.
DR KEGG; spo:SPBC18E5.06; -.
DR PomBase; SPBC18E5.06; rps21.
DR VEuPathDB; FungiDB:SPBC18E5.06; -.
DR eggNOG; KOG3486; Eukaryota.
DR HOGENOM; CLU_167122_2_0_1; -.
DR InParanoid; P05764; -.
DR OMA; ALCGYIR; -.
DR PhylomeDB; P05764; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SPO-72649; Translation initiation complex formation.
DR Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SPO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SPO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P05764; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002182; P:cytoplasmic translational elongation; NAS:PomBase.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000461; P:endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:PomBase.
DR Gene3D; 3.30.1230.20; -; 1.
DR InterPro; IPR001931; Ribosomal_S21e.
DR InterPro; IPR018279; Ribosomal_S21e_CS.
DR InterPro; IPR038579; Ribosomal_S21e_sf.
DR PANTHER; PTHR10442; PTHR10442; 1.
DR Pfam; PF01249; Ribosomal_S21e; 1.
DR PIRSF; PIRSF002148; Ribosomal_S21e; 1.
DR PROSITE; PS00996; RIBOSOMAL_S21E; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; rRNA processing.
FT CHAIN 1..87
FT /note="40S ribosomal protein S21"
FT /id="PRO_0000194760"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:3910104"
FT CONFLICT 37
FT /note="C -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="A -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="C -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="T -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="E -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 87 AA; 9617 MW; 970F7B10DC348B6A CRC64;
MENEAGQLVD LYVPRKCSAT NRIIQAKDHA SVQINVCAVD AEGRQIPGEK TTYAISGFVR
SKGESDDCIN RLTTQDGLLE GVWSYQR
