RSSA_XENLA
ID RSSA_XENLA Reviewed; 306 AA.
AC Q3ZM03;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CLEAVAGE BY ST3.
RC TISSUE=Small intestine;
RX PubMed=15780176; DOI=10.1038/sj.cr.7290280;
RA Amano T., Kwak O., Fu L., Marshak A., Shi Y.-B.;
RT "The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two
RT distinct sites between the transmembrane domain and laminin binding
RT sequence within the extracellular domain.";
RL Cell Res. 15:150-159(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=16059908; DOI=10.1002/dvdy.20511;
RA Amano T., Fu L., Marshak A., Kwak O., Shi Y.-B.;
RT "Spatio-temporal regulation and cleavage by matrix metalloproteinase
RT stromelysin-3 implicate a role for laminin receptor in intestinal
RT remodeling during Xenopus laevis metamorphosis.";
RL Dev. Dyn. 234:190-200(2005).
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 -!- DEVELOPMENTAL STAGE: Expressed in the intestinal epithelium of
CC premetamorphic tadpoles. During intestinal metamorphosis, down-
CC regulated in the apoptotic epithelium and concurrently up-regulated in
CC the connective tissue but with little expression in the developing
CC adult epithelium. Toward the end of metamorphosis, expressed in adult
CC epithelial cells as they differentiate. {ECO:0000269|PubMed:16059908}.
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.
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; AY730625; AAW62261.1; -; mRNA.
DR EMBL; BC123144; AAI23145.1; -; mRNA.
DR RefSeq; NP_001089106.1; NM_001095637.1.
DR RefSeq; XP_018112404.1; XM_018256915.1.
DR RefSeq; XP_018112405.1; XM_018256916.1.
DR AlphaFoldDB; Q3ZM03; -.
DR SMR; Q3ZM03; -.
DR BioGRID; 591817; 2.
DR IntAct; Q3ZM03; 1.
DR DNASU; 733335; -.
DR GeneID; 733335; -.
DR KEGG; xla:733335; -.
DR CTD; 733335; -.
DR Xenbase; XB-GENE-17333214; rpsa.L.
DR OMA; QCHLGAK; -.
DR OrthoDB; 1129610at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 733335; Expressed in internal ear and 19 other tissues.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
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; 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 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 1: Evidence at protein 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..306
FT /note="40S ribosomal protein SA"
FT /id="PRO_0000371573"
FT REPEAT 230..232
FT /note="[DE]-W-[ST] 1"
FT REPEAT 245..247
FT /note="[DE]-W-[ST] 2"
FT REPEAT 276..278
FT /note="[DE]-W-[ST] 3"
FT REPEAT 286..288
FT /note="[DE]-W-[ST] 4"
FT REPEAT 304..306
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..306
FT /note="Laminin-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT REGION 247..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..306
FT /note="Polar residues"
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 306 AA; 34058 MW; 701FD3C9F1A6461B CRC64;
MSGGLDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL
AARAIVAIEN PADVCVISSR NTGQRAVLKF ASASGATPIA GRFTPGTFTN QIQAAFREPR
LLVVTDPRAD HQPITEASYV NIPTIALCNT DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR
EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK ATTKEEFQGE WTAPVAEFPQ
AEVADWSEGV QVPSVPIQQF TAERTDVPPA PKPTEDWSTQ PASTDDWSAA PTAQASEWTG
TTTEWS
