RSSA_TAEGU
ID RSSA_TAEGU Reviewed; 296 AA.
AC B5FXT6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=17018643; DOI=10.1073/pnas.0607098103;
RA Wada K., Howard J.T., McConnell P., Whitney O., Lints T., Rivas M.V.,
RA Horita H., Patterson M.A., White S.A., Scharff C., Haesler S., Zhao S.,
RA Sakaguchi H., Hagiwara M., Shiraki T., Hirozane-Kishikawa T., Skene P.,
RA Hayashizaki Y., Carninci P., Jarvis E.D.;
RT "A molecular neuroethological approach for identifying and characterizing a
RT cascade of behaviorally regulated genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15212-15217(2006).
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; DQ213582; ACH43847.1; -; mRNA.
DR EMBL; DQ213584; ACH43849.1; -; mRNA.
DR EMBL; DQ213585; ACH43850.1; -; mRNA.
DR RefSeq; NP_001232377.1; NM_001245448.2.
DR AlphaFoldDB; B5FXT6; -.
DR SMR; B5FXT6; -.
DR STRING; 59729.ENSTGUP00000004739; -.
DR Ensembl; ENSTGUT00000035475; ENSTGUP00000033926; ENSTGUG00000004584.
DR GeneID; 100190067; -.
DR KEGG; tgu:100190067; -.
DR CTD; 3921; -.
DR GeneTree; ENSGT00950000183099; -.
DR HOGENOM; CLU_058171_1_0_1; -.
DR InParanoid; B5FXT6; -.
DR OMA; ENKMKRY; -.
DR OrthoDB; 1129610at2759; -.
DR TreeFam; TF300100; -.
DR Proteomes; UP000007754; Chromosome 2.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
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; 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 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..296
FT /note="40S ribosomal protein SA"
FT /id="PRO_0000371568"
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; 32991 MW; 3486A86EE964E5CD 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 TATEWS
