RSSA_CHLAE
ID RSSA_CHLAE Reviewed; 295 AA.
AC Q2L9X0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 76.
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 Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Zhu X., Zhang Q., Huang P.;
RT "Cloning of African green monkey laminin receptor 1 cDNA.";
RL Submitted (DEC-2005) 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. Also acts
CC as a receptor for several other ligands, including the pathogenic prion
CC protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate
CC of PPP1CA. {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. The mature dimeric form interacts with PPP1R16B
CC (via its fourth ankyrin repeat). Interacts with PPP1CA only in the
CC presence of PPP1R16B. {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 Colocalizes with PPP1R16B in the cell membrane (By similarity).
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; DQ343296; ABC69238.1; -; mRNA.
DR AlphaFoldDB; Q2L9X0; -.
DR SMR; Q2L9X0; -.
DR PRIDE; Q2L9X0; -.
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; ISS:UniProtKB.
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; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Receptor; Repeat; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT CHAIN 2..295
FT /note="40S ribosomal protein SA"
FT /id="PRO_0000271750"
FT REPEAT 230..232
FT /note="[DE]-W-[ST] 1"
FT REPEAT 247..249
FT /note="[DE]-W-[ST] 2"
FT REPEAT 266..268
FT /note="[DE]-W-[ST] 3"
FT REPEAT 275..277
FT /note="[DE]-W-[ST] 4"
FT REPEAT 293..295
FT /note="[DE]-W-[ST] 5"
FT REGION 54..113
FT /note="Interaction with PPP1R16B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
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..295
FT /note="Laminin-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT REGION 266..295
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:0000250|UniProtKB:P08865, ECO:0000255|HAMAP-
FT Rule:MF_03016"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08865"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08865"
FT MOD_RES 89
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14206"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08865"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08865"
SQ SEQUENCE 295 AA; 32868 MW; C68DDAA6B759E79E CRC64;
MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL
AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA GRFTPGTFTN QIQAAFREPR
LLVVTDPRAD HQPLTEASYV NLPTIALCNT DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR
EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA
TQPEVADWSE GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTEWS
