RSSA_DANRE
ID RSSA_DANRE Reviewed; 308 AA.
AC Q803F6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=40S ribosomal protein SA {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=37 kDa laminin receptor precursor {ECO:0000255|HAMAP-Rule:MF_03016};
DE Short=37LRP {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=37/67 kDa laminin receptor {ECO:0000255|HAMAP-Rule:MF_03016};
DE Short=LRP/LR {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=67 kDa laminin receptor {ECO:0000255|HAMAP-Rule:MF_03016};
DE Short=67LR {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=Laminin receptor 1 {ECO:0000255|HAMAP-Rule:MF_03016};
DE Short=LamR {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=Laminin-binding protein precursor p40 {ECO:0000255|HAMAP-Rule:MF_03016};
DE Short=LBP/p40 {ECO:0000255|HAMAP-Rule:MF_03016};
GN Name=rpsa; Synonyms=lamr1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2003) 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. Also functions as a cell surface receptor for
CC laminin. Plays a role in cell adhesion to the basement membrane and in
CC the consequent activation of signaling transduction pathways. May play
CC a role in cell fate determination and tissue morphogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_03016}.
CC -!- SUBUNIT: Monomer (37LRP) and homodimer (67LR). Component of the small
CC ribosomal subunit. Mature ribosomes consist of a small (40S) and a
CC large (60S) subunit. The 40S subunit contains about 33 different
CC proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49
CC different proteins and 3 molecules of RNA (28S, 5.8S and 5S). Interacts
CC with rps21. Interacts with several laminins including at least lamb1.
CC Interacts with mdk. {ECO:0000255|HAMAP-Rule:MF_03016}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_03016}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03016}. Nucleus
CC {ECO:0000255|HAMAP-Rule:MF_03016}. Note=67LR is found at the surface of
CC the plasma membrane, with its C-terminal laminin-binding domain
CC accessible to extracellular ligands. 37LRP is found at the cell
CC surface, in the cytoplasm and in the nucleus. {ECO:0000255|HAMAP-
CC Rule:MF_03016}.
CC -!- PTM: Acylated. Acylation may be a prerequisite for conversion of the
CC monomeric 37 kDa laminin receptor precursor (37LRP) to the mature
CC dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for
CC membrane association. {ECO:0000255|HAMAP-Rule:MF_03016}.
CC -!- PTM: Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by
CC stromelysin-3 may be a mechanism to alter cell-extracellular matrix
CC interactions. {ECO:0000255|HAMAP-Rule:MF_03016}.
CC -!- MISCELLANEOUS: This protein appears to have acquired a second function
CC as a laminin receptor specifically in the vertebrate lineage.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000255|HAMAP-Rule:MF_03016}.
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DR EMBL; AY391434; AAQ91246.1; -; mRNA.
DR EMBL; BC044504; AAH44504.1; -; mRNA.
DR EMBL; BC062859; AAH62859.1; -; mRNA.
DR RefSeq; NP_957346.1; NM_201052.1.
DR AlphaFoldDB; Q803F6; -.
DR SMR; Q803F6; -.
DR IntAct; Q803F6; 1.
DR MINT; Q803F6; -.
DR STRING; 7955.ENSDARP00000123183; -.
DR PaxDb; Q803F6; -.
DR PRIDE; Q803F6; -.
DR Ensembl; ENSDART00000135945; ENSDARP00000123183; ENSDARG00000019181.
DR Ensembl; ENSDART00000189664; ENSDARP00000155439; ENSDARG00000019181.
DR GeneID; 394027; -.
DR KEGG; dre:394027; -.
DR CTD; 3921; -.
DR ZFIN; ZDB-GENE-040426-811; rpsa.
DR eggNOG; KOG0830; Eukaryota.
DR GeneTree; ENSGT00950000183099; -.
DR HOGENOM; CLU_058171_1_0_1; -.
DR InParanoid; Q803F6; -.
DR OMA; ENKMKRY; -.
DR OrthoDB; 1129610at2759; -.
DR PhylomeDB; Q803F6; -.
DR TreeFam; TF300100; -.
DR Reactome; R-DRE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DRE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-DRE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-DRE-72649; Translation initiation complex formation.
DR Reactome; R-DRE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DRE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DRE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DRE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-DRE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DRE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q803F6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000019181; Expressed in presomitic mesoderm and 27 other tissues.
DR ExpressionAtlas; Q803F6; baseline and differential.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043236; F:laminin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005055; F:laminin receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR HAMAP; MF_03016; Ribosomal_S2_laminin_receptor; 1.
DR InterPro; IPR027504; 40S_ribosomal_SA.
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 Acetylation; Cell membrane; Cytoplasm; Membrane; Nucleus; Receptor;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT CHAIN 2..308
FT /note="40S ribosomal protein SA"
FT /id="PRO_0000371569"
FT REPEAT 230..232
FT /note="[DE]-W-[ST] 1"
FT REPEAT 245..247
FT /note="[DE]-W-[ST] 2"
FT REPEAT 279..281
FT /note="[DE]-W-[ST] 3"
FT REPEAT 288..290
FT /note="[DE]-W-[ST] 4"
FT REPEAT 306..308
FT /note="[DE]-W-[ST] 5"
FT REGION 161..180
FT /note="Laminin-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT REGION 205..229
FT /note="Laminin-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT REGION 242..308
FT /note="Laminin-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT REGION 262..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 115..116
FT /note="Cleavage; by ST3; site 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT SITE 133..134
FT /note="Cleavage; by ST3; site 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
SQ SEQUENCE 308 AA; 34012 MW; 430C6E3DC7DE162C CRC64;
MSGGLDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYVYK RKSDGVYIIN LKKTWEKLLL
AARAIVAIEN PADVCVISSR NTGQRAVLKF ASATGSTTFA GRFTPGTFTN QIQAAFREPR
LLIVTDPRAD HQPLTEASYV NIPTIALCNT DSPLRYVDIA IPCNNKGPHS VGLMWWMLAR
EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK AVGKEEFQGE WTAPVPDFNQ
PEVADWSEGV QVPSVPIQQF PAGIEAPGKP APAEVYAEDW SAQPATEDWS AAPTAQAGDW
GGATADWS
