RS2_SCHPO
ID RS2_SCHPO Reviewed; 253 AA.
AC O74892;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=40S ribosomal protein S2;
GN Name=rps2; ORFNames=SPCC576.08c;
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).
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. Plays a role in the assembly and function of the 40S ribosomal
CC subunit. Mutations in this protein affects the control of translational
CC fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and
CC ribosome assembly. {ECO:0000250|UniProtKB:P25443}.
CC -!- INTERACTION:
CC O74892; O13648: rmt3; NbExp=2; IntAct=EBI-367715, EBI-367706;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA21187.1; -; Genomic_DNA.
DR PIR; T41418; T41418.
DR RefSeq; NP_588435.1; NM_001023426.2.
DR AlphaFoldDB; O74892; -.
DR SMR; O74892; -.
DR BioGRID; 275639; 12.
DR IntAct; O74892; 2.
DR STRING; 4896.SPCC576.08c.1; -.
DR iPTMnet; O74892; -.
DR MaxQB; O74892; -.
DR PaxDb; O74892; -.
DR PRIDE; O74892; -.
DR EnsemblFungi; SPCC576.08c.1; SPCC576.08c.1:pep; SPCC576.08c.
DR GeneID; 2539067; -.
DR KEGG; spo:SPCC576.08c; -.
DR PomBase; SPCC576.08c; rps2.
DR VEuPathDB; FungiDB:SPCC576.08c; -.
DR eggNOG; KOG0877; Eukaryota.
DR HOGENOM; CLU_065898_0_2_1; -.
DR InParanoid; O74892; -.
DR OMA; DLKNWVP; -.
DR PhylomeDB; O74892; -.
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-3214858; RMTs methylate histone arginines.
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-8876725; Protein methylation.
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:O74892; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:PomBase.
DR GO; GO:0032040; C:small-subunit processome; ISO:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:PomBase.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01020; uS5_euk_arch; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..253
FT /note="40S ribosomal protein S2"
FT /id="PRO_0000131683"
FT DOMAIN 75..138
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 27637 MW; 0F932A14F40597F6 CRC64;
MAESAPRGFG RGGRGGRGRG RGRRGAKRDE EKEWVPVTKL GRLVKAGKIK SIEEIYLYSL
PIKEYQIVDY FLPRLNDEVM KVVPVQKQTR AGQRTRFKAF VVIGDSDGHV GLGIKCAKEV
ATAIRGAIIM GKLSIMPIRR GYWGTALGDP HTVPVKVSGK CGSVTVRLVP APRGAGLVAA
PVTKRFLQLA GIEDCYTQSR GSTKTLGNFV KAAFAAASLT YGILTPNLWA ERPFGQTPIE
EYADILMQTE KKY
