ID   RS2_CRIGR               Reviewed;         202 AA.
AC   P46791;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=40S ribosomal protein S2;
DE   Flags: Fragment;
GN   Name=RPS2;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RA   Harpold M.M., Evans R.M., Salditt-Georgieff M., Darnell J.E. Jr.;
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Interacts with zinc finger protein ZNF277 (via zinc-finger
CC       domains); the interaction is direct; the interaction is extra-
CC       ribosomal. Interaction with ZNF277 competes with the binding of RPS2 to
CC       protein arginine methyltransferase PRMT3.
CC       {ECO:0000250|UniProtKB:P15880}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P15880}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:P15880}. Note=Probably
CC       localized to nucleolus and cytoplasm in complex with ZNF277.
CC       {ECO:0000250|UniProtKB:P15880}.
CC   -!- PTM: Asymmetric arginine dimethylation by PRMT3 occurs at multiple
CC       sites in the Arg/Gly-rich region. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000305}.
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DR   EMBL; L22552; AAA36999.1; -; mRNA.
DR   PIR; I48117; I48117.
DR   AlphaFoldDB; P46791; -.
DR   SMR; P46791; -.
DR   STRING; 10029.NP_001230972.1; -.
DR   eggNOG; KOG0877; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           <1..>202
FT                   /note="40S ribosomal protein S2"
FT                   /id="PRO_0000131672"
FT   DOMAIN          42..105
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT   MOD_RES         192
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P15880"
FT   NON_TER         1
FT   NON_TER         202
SQ   SEQUENCE   202 AA;  22047 MW;  1E4EC4C2AAA1918D CRC64;
     IPVTKLGRLV KDMKIKSLEE IYLFSLPIKE SEIIDFFLGA SLKDEVLKIM PVQKQTRAGQ
     RTRFKAFVAI GDYNGHVGLG VKCSKEVATA IRGAIILAKL SIVPVRRGYW GNKIGKPHTV
     PCKVTGRCGS VLVRLIPAPR GTGIVSAPVP KKLLMMAGID DCYTSARGCT ATLGNFAKAT
     FDAISKTYSY LTPDLWKETV FT