RSSA_RAT
ID RSSA_RAT Reviewed; 295 AA.
AC P38983; B6ZB78;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8119397; DOI=10.1016/0014-5793(94)80188-6;
RA Tohgo A., Takasawa S., Munakata H., Yonekura H., Hayashi N., Okamoto H.;
RT "Structural determination and characterization of a 40 kDa protein isolated
RT from rat 40 S ribosomal subunit.";
RL FEBS Lett. 340:133-138(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Ning Z., Luo M.;
RT "Cloning and analysis of laminin receptor gene in SD rat.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-11; 43-52; 90-102 AND 156-166, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15548204; DOI=10.1111/j.1460-9568.2004.03728.x;
RA Baloui H., von Boxberg Y., Vinh J., Weiss S., Rossier J., Nothias F.,
RA Stettler O.;
RT "Cellular prion protein/laminin receptor: distribution in adult central
RT nervous system and characterization of an isoform associated with a subtype
RT of cortical neurons.";
RL Eur. J. Neurosci. 20:2605-2616(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-17; 64-80; 90-102; 121-128 AND 156-166, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fibroblast;
RA Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL Submitted (JUN-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 199-295.
RC STRAIN=Holtzman; TISSUE=Intestinal epithelium;
RX PubMed=8076763; DOI=10.1016/0016-5085(94)90125-2;
RA Rao M., Manishen W.J., Maheshwari Y., Sykes D.E., Siyanova E.Y.,
RA Tyner A.L., Weiser M.M.;
RT "Laminin receptor expression in rat intestine and liver during development
RT and differentiation.";
RL Gastroenterology 107:764-772(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 226-295.
RA Burns F.R., Rajnavolgy E., Yamashita K., Li X., Shen N., Heber-Katz E.;
RL Submitted (SEP-1989) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION IN SMALL RIBOSOMAL SUBUNIT.
RX PubMed=925037; DOI=10.1016/s0021-9258(17)38346-1;
RA Collatz E., Ulbrich N., Tsurugi K., Lightfoot H.N., MacKinlay W., Lin A.,
RA Wool I.G.;
RT "Isolation of eukaryotic ribosomal proteins. Purification and
RT characterization of the 40 S ribosomal subunit proteins Sa, Sc, S3a, S3b,
RT S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18, S19, S20, S21, S26,
RT S27', and S29.";
RL J. Biol. Chem. 252:9071-9080(1977).
RN [9]
RP FUNCTION.
RX PubMed=16453457; DOI=10.1002/j.1460-2075.1983.tb01514.x;
RA Lesot H., Kuehl U., von der Mark K.;
RT "Isolation of a laminin-binding protein from muscle cell membranes.";
RL EMBO J. 2:861-865(1983).
RN [10]
RP MASS SPECTROMETRY.
RX PubMed=8910435; DOI=10.1074/jbc.271.45.28189;
RA Louie D.F., Resing K.A., Lewis T.S., Ahn N.G.;
RT "Mass spectrometric analysis of 40 S ribosomal proteins from Rat-1
RT fibroblasts.";
RL J. Biol. Chem. 271:28189-28198(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. 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 ECO:0000269|PubMed:16453457}.
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 ECO:0000269|PubMed:15548204}. Cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03016, ECO:0000269|PubMed:15548204}. 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. Colocalizes with PPP1R16B
CC in the cell membrane (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_03016}.
CC -!- TISSUE SPECIFICITY: Expressed in most neurons and in a subset of glial
CC cells. The overall distribution of LR correlates with that reported for
CC laminin-1 but also with brain regions classically associated with
CC prion-related neurodegeneration. {ECO:0000269|PubMed:15548204}.
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 -!- MASS SPECTROMETRY: Mass=32734.1; Mass_error=1.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8910435};
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; D25224; BAA04953.1; -; mRNA.
DR EMBL; FJ386454; ACJ13448.1; -; mRNA.
DR EMBL; BC060578; AAH60578.1; -; mRNA.
DR EMBL; U04942; AAB60453.1; -; mRNA.
DR EMBL; M27798; AAA41509.1; -; mRNA.
DR PIR; S42405; S42405.
DR RefSeq; NP_058834.1; NM_017138.2.
DR AlphaFoldDB; P38983; -.
DR SMR; P38983; -.
DR BioGRID; 247913; 6.
DR IntAct; P38983; 4.
DR MINT; P38983; -.
DR STRING; 10116.ENSRNOP00000025224; -.
DR iPTMnet; P38983; -.
DR PhosphoSitePlus; P38983; -.
DR jPOST; P38983; -.
DR PaxDb; P38983; -.
DR PRIDE; P38983; -.
DR DNASU; 29236; -.
DR GeneID; 29236; -.
DR KEGG; rno:29236; -.
DR UCSC; RGD:71026; rat.
DR CTD; 3921; -.
DR RGD; 71026; Rpsa.
DR VEuPathDB; HostDB:ENSRNOG00000018645; -.
DR eggNOG; KOG0830; Eukaryota.
DR HOGENOM; CLU_058171_1_0_1; -.
DR InParanoid; P38983; -.
DR OMA; ENKMKRY; -.
DR OrthoDB; 1129610at2759; -.
DR PhylomeDB; P38983; -.
DR TreeFam; TF300100; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-72649; Translation initiation complex formation.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-RNO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P38983; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000018645; Expressed in spleen and 19 other tissues.
DR Genevisible; P38983; RN.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0043236; F:laminin binding; ISO:RGD.
DR GO; GO:0005055; F:laminin receptor activity; TAS:RGD.
DR GO; GO:0043022; F:ribosome binding; ISO:RGD.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR GO; GO:0005198; F:structural molecule activity; IC:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:RGD.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:RGD.
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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016,
FT ECO:0000269|PubMed:15548204, ECO:0000269|Ref.5"
FT CHAIN 2..295
FT /note="40S ribosomal protein SA"
FT /id="PRO_0000134360"
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:0000255|HAMAP-Rule:MF_03016,
FT ECO:0000269|PubMed:15548204, ECO:0000269|Ref.5"
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"
FT CONFLICT 177
FT /note="M -> V (in Ref. 2; ACJ13448)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="E -> G (in Ref. 2; ACJ13448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 32824 MW; D7DDD887DBDD340C CRC64;
MSGGLDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL
AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA GRFTPGTFTN QIQAAFREPR
LLVVTDPRAD HQPLTEASYV NLPTIALCNT DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR
EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA
AQPEVADWSE GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTEWS
