RSSA1_SCHPO
ID RSSA1_SCHPO Reviewed; 292 AA.
AC Q9Y7L8;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 156.
DE RecName: Full=40S ribosomal protein S0-A {ECO:0000255|HAMAP-Rule:MF_03015};
GN Name=rps001; Synonyms=rps0a, rpsa1; ORFNames=SPBC685.06;
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 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 [2]
RP FUNCTION, INTERACTION WITH RPS21, AND 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).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Required for the assembly and/or stability of the 40S
CC ribosomal subunit. Required for the processing of the 20S rRNA-
CC precursor to mature 18S rRNA in a late step of the maturation of 40S
CC ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_03015,
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 rps21. {ECO:0000255|HAMAP-
CC Rule:MF_03015, ECO:0000269|PubMed:14623272}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03015,
CC ECO:0000269|PubMed:16823372}.
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 -!- MISCELLANEOUS: There are two genes for S0 in S.pombe.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000255|HAMAP-Rule:MF_03015}.
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DR EMBL; CU329671; CAB39363.1; -; Genomic_DNA.
DR PIR; T40637; T40637.
DR RefSeq; NP_596140.1; NM_001022058.2.
DR AlphaFoldDB; Q9Y7L8; -.
DR SMR; Q9Y7L8; -.
DR BioGRID; 277659; 38.
DR STRING; 4896.SPBC685.06.1; -.
DR iPTMnet; Q9Y7L8; -.
DR MaxQB; Q9Y7L8; -.
DR PaxDb; Q9Y7L8; -.
DR PRIDE; Q9Y7L8; -.
DR EnsemblFungi; SPBC685.06.1; SPBC685.06.1:pep; SPBC685.06.
DR GeneID; 2541144; -.
DR KEGG; spo:SPBC685.06; -.
DR PomBase; SPBC685.06; rps001.
DR VEuPathDB; FungiDB:SPBC685.06; -.
DR eggNOG; KOG0830; Eukaryota.
DR HOGENOM; CLU_058171_1_0_1; -.
DR InParanoid; Q9Y7L8; -.
DR OMA; QQKTKDM; -.
DR PhylomeDB; Q9Y7L8; -.
DR PRO; PR:Q9Y7L8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:PomBase.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR InterPro; IPR032281; 40S_SA_C.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR027498; Ribosomal_S2_euk.
DR InterPro; IPR005707; Ribosomal_S2_euk/arc.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR11489; PTHR11489; 1.
DR Pfam; PF16122; 40S_SA_C; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..292
FT /note="40S ribosomal protein S0-A"
FT /id="PRO_0000134368"
FT REGION 265..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 292 AA; 31760 MW; CE0DB640C7D20FEF CRC64;
MAQVGRPNIL NATDEDIKQL LAANCHIGSK NLEVRMDNYV WKRRSDGVHI LNLGKTWEKL
VLAARVIATI ENPADVCVVS TRTYGHRAVL KFAAHTGATA IAGRFTPGNF TNYITRTYRE
PRLIVVTDPR ADAQAIKEAS FVNIPVIALC DTDSILNHVD IAIPTNNKGR KSIGLIWYLL
AREVLRVRGT LSRSAPWDVM PDLYFYRDPE EVEREEEAKK AAAAAAEEAQ VEEAVAAAEF
EITDSAAGSV DPNVLAAATA GQVGENTWEG AGDWNTTGAA QTSDWTAAAE AQ
