RSSA_CHICK
ID RSSA_CHICK Reviewed; 296 AA.
AC P50890;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 {ECO:0000255|HAMAP-Rule:MF_03016}; Synonyms=LAMR1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=White leghorn; TISSUE=Spleen;
RX PubMed=8985115; DOI=10.1089/dna.1996.15.1009;
RA Clausse N., Jackers P., Jares P., Joris B., Sobel M.E., Castronovo V.;
RT "Identification of the active gene coding for the metastasis-associated
RT 37LRP/p40 multifunctional protein.";
RL DNA Cell Biol. 15:1009-1023(1996).
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. Nucleus {ECO:0000255|HAMAP-Rule:MF_03016}. Note=67LR is
CC found at the surface of the plasma membrane, with its C-terminal
CC laminin-binding domain accessible to extracellular ligands. 37LRP is
CC found at the cell surface, in the cytoplasm and in the nucleus.
CC {ECO:0000255|HAMAP-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 -!- MISCELLANEOUS: It is thought that in vertebrates 37/67 kDa laminin
CC receptor acquired a dual function during evolution. It developed from
CC the ribosomal protein SA, playing an essential role in the protein
CC biosynthesis lacking any laminin binding activity, to a cell surface
CC receptor with laminin binding activity.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000255|HAMAP-Rule:MF_03016}.
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DR EMBL; X94368; CAA64147.1; -; Genomic_DNA.
DR RefSeq; NP_001007824.1; NM_001007823.1.
DR AlphaFoldDB; P50890; -.
DR SMR; P50890; -.
DR BioGRID; 675476; 2.
DR IntAct; P50890; 1.
DR STRING; 9031.ENSGALP00000019469; -.
DR PaxDb; P50890; -.
DR Ensembl; ENSGALT00000082200; ENSGALP00000056649; ENSGALG00000035079.
DR GeneID; 395181; -.
DR KEGG; gga:395181; -.
DR CTD; 388524; -.
DR VEuPathDB; HostDB:geneid_395181; -.
DR eggNOG; KOG0830; Eukaryota.
DR GeneTree; ENSGT00950000183099; -.
DR HOGENOM; CLU_058171_1_0_1; -.
DR InParanoid; P50890; -.
DR OMA; ENKMKRY; -.
DR OrthoDB; 1129610at2759; -.
DR PhylomeDB; P50890; -.
DR TreeFam; TF300100; -.
DR Reactome; R-GGA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-GGA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-GGA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-GGA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P50890; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000035079; Expressed in colon and 12 other tissues.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
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; ISS:UniProtKB.
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 3: Inferred from homology;
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..296
FT /note="40S ribosomal protein SA"
FT /id="PRO_0000134361"
FT REPEAT 230..232
FT /note="[DE]-W-[ST] 1"
FT REPEAT 248..250
FT /note="[DE]-W-[ST] 2"
FT REPEAT 267..269
FT /note="[DE]-W-[ST] 3"
FT REPEAT 276..278
FT /note="[DE]-W-[ST] 4"
FT REPEAT 294..296
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 243..296
FT /note="Laminin-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT REGION 267..296
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 296 AA; 33021 MW; 3486A86EF514E5CD CRC64;
MSGGLDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL
AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA GRFTPGTFTN QIQAAFREPR
LLVVTDPRAD HQPLTEASYV NIPTIALCNT DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR
EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK AVTKEEFQTE WTAPAPEFTA
PPQPEVADWS EGVQVPSVPI QQFPTEDWSA QPATEDWSAA PTAQATEWVG TTTEWS
