RS2_DICDI
ID RS2_DICDI Reviewed; 265 AA.
AC P27685; Q54BC7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=40S ribosomal protein S2;
DE AltName: Full=Protein LLRep3;
DE AltName: Full=Ribosomal protein S4;
GN Name=rps2; Synonyms=rp29; ORFNames=DDB_G0293742;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX2;
RX PubMed=1861979; DOI=10.1093/nar/19.14.3867;
RA Proffitt J.A., Jagger P.S., Wilson G.A., Donovan J.T.J., Widdowson D.C.C.,
RA Hames B.D.;
RT "A developmentally regulated gene encodes the dictyostelium homolog of
RT yeast ribosomal protein S4 and mammalian LLRep3 proteins.";
RL Nucleic Acids Res. 19:3867-3873(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 2-16; 133-146 AND 199-214, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Ura S., Insall R.H.;
RL Submitted (JUL-2009) to UniProtKB.
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 -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
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DR EMBL; X56297; CAA39744.1; -; mRNA.
DR EMBL; AAFI02000219; EAL60548.1; -; Genomic_DNA.
DR PIR; S22297; S22297.
DR RefSeq; XP_628967.1; XM_628965.1.
DR AlphaFoldDB; P27685; -.
DR SMR; P27685; -.
DR STRING; 44689.DDB0215391; -.
DR PaxDb; P27685; -.
DR PRIDE; P27685; -.
DR EnsemblProtists; EAL60548; EAL60548; DDB_G0293742.
DR GeneID; 8629395; -.
DR KEGG; ddi:DDB_G0293742; -.
DR dictyBase; DDB_G0293742; rps2.
DR eggNOG; KOG0877; Eukaryota.
DR HOGENOM; CLU_065898_0_2_1; -.
DR InParanoid; P27685; -.
DR OMA; DLKNWVP; -.
DR PhylomeDB; P27685; -.
DR Reactome; R-DDI-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DDI-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-DDI-3214858; RMTs methylate histone arginines.
DR Reactome; R-DDI-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-DDI-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DDI-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DDI-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DDI-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-DDI-8876725; Protein methylation.
DR Reactome; R-DDI-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DDI-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P27685; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
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 Acetylation; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..265
FT /note="40S ribosomal protein S2"
FT /id="PRO_0000131678"
FT DOMAIN 89..152
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3"
SQ SEQUENCE 265 AA; 28717 MW; 7BF5C5066ABC271C CRC64;
MADTTTAAQA DQKPTRAFGA GRPQRGAGGA PQRGGPRPQR GGQGETKSWT PVTKLGRLVA
LGLVENIHEI YLFSLPIKEY QIIDKFLNLK DEVMKIVPVQ KQTRAGQRTR FKAFVVVGDH
NGHVGLGVKC AKEVATAISG AIVAAKLSVI PVRRGYWGNK LGAPHTVPTK VTGKCGSVAV
RLVPAPRGTG IVAARVPKKL LQYAGVDDVY TSSRGKTRTM GNFVMATFFA ITKTFAYLTP
DLWREVKLIK TPYQEHSAKL SEKQQ
