RSSA_URECA
ID RSSA_URECA Reviewed; 317 AA.
AC P38981;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=40S ribosomal protein SA {ECO:0000255|HAMAP-Rule:MF_03015};
DE AltName: Full=Laminin-binding protein p40;
DE Short=LBP/p40;
OS Urechis caupo (Innkeeper worm) (Spoonworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Echiura; Xenopneusta; Urechidae; Urechis.
OX NCBI_TaxID=6431;
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 {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; U02370; AAA90978.1; -; mRNA.
DR AlphaFoldDB; P38981; -.
DR SMR; P38981; -.
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; 1.
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..317
FT /note="40S ribosomal protein SA"
FT /id="PRO_0000134364"
FT REGION 277..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 34247 MW; 1A7403BBBA9C4CD7 CRC64;
MSGSIDTLAL KEEDVTKFLA CASHLGANNV DFQMEQYVYK RRPDGTSIIN VRKTWEKVLL
AARAIAAIEN PADICVISAR PYGQRAVLKF AHYTGATPIA GRFTPGTFTN QIQTAFREPR
LLVVTDPYTD HQPVTEASYV NIPVIALTNT DSPLKYVDIA IPCNNKSIHS VGLMWWMLAR
EVLRLRGTIS REVPWEVMVD LFFYRDPEEA EKEAQAEQAA AEKDKAPKEE FTADQAFTAP
GTEVSDWASE VPVAPVPILA GGVDAATTED WSVPAQSDWT APAANPANAA AAGAPAPAPA
AATTTESWGG SGAENWG