ID   RSSA_PINFU              Reviewed;         301 AA.
AC   A3RLT6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=40S ribosomal protein SA {ECO:0000255|HAMAP-Rule:MF_03015};
OS   Pinctada fucata (Akoya pearl oyster) (Pinctada imbricata fucata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=50426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Fu Y., Xie L., Zhang R.;
RT   "Cloning and characterization of 67kD laminin receptor in Pinctada
RT   fucata.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- 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       (28S, 5.8S and 5S). Interacts with ribosomal protein S21.
CC       {ECO:0000255|HAMAP-Rule:MF_03015}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03015}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03015}.
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DR   EMBL; EF427937; ABO10190.1; -; mRNA.
DR   AlphaFoldDB; A3RLT6; -.
DR   SMR; A3RLT6; -.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
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; PS00962; RIBOSOMAL_S2_1; 1.
DR   PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03015"
FT   CHAIN           2..301
FT                   /note="40S ribosomal protein SA"
FT                   /id="PRO_0000371594"
FT   REGION          256..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   301 AA;  33520 MW;  6C2E9E0902E28805 CRC64;
     MSGGLDVLAL KEEDITKFLA CSTHLGATNV DFQMEQYVYK RKPDGVYIIN LRRTWEKLLL
     AARAIAAIEN PADVCVISAR PYGQRAVLKF ASATGATPIA GRFTPGTFTN QIQAAFREPR
     LLVVTDPRID HQPVTEASYV NIPVIALCNT DSPLRYVDVA IPCNNKSVHS VGLMWWLLAR
     EVLRLRGTIS RDHPWEVMVD LYFYRDPEEA EKEEQTVVEK PAVKSDEVQD QWATTDIAIQ
     PPQQEVSDWA AESIPVAPPG QPFMPPPAKD WSASTTEDWS AASGPAPQSA LNGRWHLRNW
     G