ID   RSSA_TRIGR              Reviewed;         316 AA.
AC   P38980;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=40S ribosomal protein SA {ECO:0000255|HAMAP-Rule:MF_03015};
OS   Tripneustes gratilla (Hawaian sea urchin) (Echinus gratilla).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Temnopleuroida; Toxopneustidae; Tripneustes.
OX   NCBI_TaxID=7673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7738101; DOI=10.1242/jcs.108.1.245;
RA   Rosenthal E.T., Wordeman L.;
RT   "A protein similar to the 67 kDa laminin binding protein and p40 is
RT   probably a component of the translational machinery in Urechis caupo
RT   oocytes and embryos.";
RL   J. Cell Sci. 108:245-256(1995).
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.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03015}.
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DR   EMBL; U02371; AAA90977.1; -; mRNA.
DR   AlphaFoldDB; P38980; -.
DR   SMR; P38980; -.
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   CHAIN           1..316
FT                   /note="40S ribosomal protein SA"
FT                   /id="PRO_0000134363"
FT   REGION          209..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   316 AA;  34525 MW;  4047265A61FB013C CRC64;
     MSGGLDCLAL KEDDVQKFLA SGAHIGSSNL DYQMTQYVYK RKPDGTYIIN LRRTWEKLLM
     AARIIVAIEN PADVCVISSR PYGQRAVLKF GAHTGATPIA GRYTPGTFTN QIQAAFREPR
     ILIVTDPRSD HQPVTEASYV NIPVIALCNT DSPLRYVDIA IPCNNKSIHS IGLMWWMLSR
     EVLRLRGAIS RDVTWEIMCD LYFFRDPEEA EKEEQEARDR ATAVKEEPAQ PYAEQWSDPV
     AVPPAGQPVA EVTDWAADSV KAPVAGIGTY GGPSEDWAVA DAPAAPAAPT PAAPSQEFTA
     TDDWGGAASN DWAISS