RSSA_MOUSE
ID RSSA_MOUSE Reviewed; 295 AA.
AC P14206; Q58E74; Q8BHL0; Q8BNL2; Q91V31; Q9CY13;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 202.
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 kDa oncofetal antigen;
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};
DE AltName: Full=OFA/iLRP;
GN Name=Rpsa; Synonyms=Lamr1, P40-8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2531008; DOI=10.1021/bi00444a047;
RA Rao C.N., Castronovo V., Schmitt M.C., Wewer U.M., Claysmith A.P.,
RA Liotta L.A., Sobel M.E.;
RT "Evidence for a precursor of the high-affinity metastasis-associated murine
RT laminin receptor.";
RL Biochemistry 28:7476-7486(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3357791; DOI=10.1093/nar/16.5.2349;
RA Makrides S., Chitpatima S.T., Bandyopadhyay R., Brawerman G.;
RT "Nucleotide sequence for a major messenger RNA for a 40 kilodalton
RT polypeptide that is under translational control in mouse tumor cells.";
RL Nucleic Acids Res. 16:2349-2349(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Fibrosarcoma;
RX PubMed=10697612;
RA Coggin J.H. Jr., Barsoum A.L., Rohrer J.W.;
RT "37 kilodalton oncofetal antigen protein and immature laminin receptor
RT protein are identical, universal T-cell inducing immunogens on primary
RT rodent and human cancers.";
RL Anticancer Res. 19:5535-5542(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CAST/EiJ, and SJL/J;
RA Lee I.Y., Baxter D.H., Qin S., Hood L.E.;
RT "Genomic sequence analysis of laminin receptor loci in mice.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Liver, Muellerian duct, Pancreas, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Brain, Colon, Eye, Kidney, Mammary gland, Mammary tumor, and
RC Pancreas;
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 [7]
RP PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA Kanor S., Quadroni M., Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 18-40; 43-50; 90-100 AND 155-163, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8954992; DOI=10.1006/bbrc.1996.1899;
RA Sato M., Kinoshita K., Kaneda Y., Saeki Y., Iwamatsu A., Tanaka K.;
RT "Analysis of nuclear localization of laminin binding protein precursor p40
RT (LBP/p40).";
RL Biochem. Biophys. Res. Commun. 229:896-901(1996).
RN [9]
RP PROTEIN SEQUENCE OF 64-80; 90-117 AND 129-155, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [10]
RP FUNCTION AS LAMININ RECEPTOR, AND SUBCELLULAR LOCATION.
RX PubMed=6301485; DOI=10.1016/0006-291x(83)91370-0;
RA Rao N.C., Barsky S.H., Terranova V.P., Liotta L.A.;
RT "Isolation of a tumor cell laminin receptor.";
RL Biochem. Biophys. Res. Commun. 111:804-808(1983).
RN [11]
RP FUNCTION, AND INTERACTION WITH LAMININ-1.
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 [12]
RP FUNCTION, AND INTERACTION WITH LAMININ-1.
RX PubMed=6302102; DOI=10.1083/jcb.96.5.1475;
RA Malinoff H.L., Wicha M.S.;
RT "Isolation of a cell surface receptor protein for laminin from murine
RT fibrosarcoma cells.";
RL J. Cell Biol. 96:1475-1479(1983).
RN [13]
RP FUNCTION IN RIBOSOME, AND SUBCELLULAR LOCATION.
RX PubMed=1374897; DOI=10.1073/pnas.89.10.4368;
RA Auth D., Brawerman G.;
RT "A 33-kDa polypeptide with homology to the laminin receptor: component of
RT translation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4368-4372(1992).
RN [14]
RP INTERACTION WITH PRNP, AND SUBCELLULAR LOCATION.
RX PubMed=11689427; DOI=10.1093/emboj/20.21.5863;
RA Gauczynski S., Peyrin J.-M., Haik S., Leucht C., Hundt C., Rieger R.,
RA Krasemann S., Deslys J.-P., Dormont D., Lasmezas C.I., Weiss S.;
RT "The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for
RT the cellular prion protein.";
RL EMBO J. 20:5863-5875(2001).
RN [15]
RP INTERACTION WITH MDK, AND SUBCELLULAR LOCATION.
RX PubMed=11597123; DOI=10.1006/excr.2001.5341;
RA Salama R.H.M., Muramatsu H., Zou K., Inui T., Kimura T., Muramatsu T.;
RT "Midkine binds to 37-kDa laminin binding protein precursor, leading to
RT nuclear transport of the complex.";
RL Exp. Cell Res. 270:13-20(2001).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=18339329; DOI=10.1016/j.bbadis.2008.02.003;
RA Nikles D., Vana K., Gauczynski S., Knetsch H., Ludewigs H., Weiss S.;
RT "Subcellular localization of prion proteins and the 37 kDa/67 kDa laminin
RT receptor fused to fluorescent proteins.";
RL Biochim. Biophys. Acta 1782:335-340(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 (By similarity). Enables malignant tumor cells to penetrate
CC laminin tissue and vessel barriers. Activates precursor thymic anti-
CC OFA/iLRP specific cytotoxic T-cell. May induce CD8 T-suppressor cells
CC secreting IL-10. {ECO:0000255|HAMAP-Rule:MF_03016,
CC ECO:0000269|PubMed:10697612, ECO:0000269|PubMed:1374897,
CC ECO:0000269|PubMed:16453457, ECO:0000269|PubMed:6301485,
CC ECO:0000269|PubMed:6302102}.
CC -!- SUBUNIT: Monomer (37LRP) and homodimer (67LR) (By similarity).
CC Component of the small ribosomal subunit. Mature ribosomes consist of a
CC small (40S) and a large (60S) subunit. The 40S subunit contains about
CC 33 different proteins and 1 molecule of RNA (18S). The 60S subunit
CC contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S
CC and 5S). Interacts with RPS21 (By similarity). Interacts with several
CC laminins including at least LAMB1. Interacts with MDK. Interacts with
CC PRNP. The mature dimeric form interacts with PPP1R16B (via its fourth
CC ankyrin repeat). Interacts with PPP1CA only in the presence of PPP1R16B
CC (By similarity). {ECO:0000255|HAMAP-Rule:MF_03016}.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus. 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). 37LRP
CC shuttles to the nucleus upon midkine (MDK) binding. {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 -!- 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; J02870; AAA39413.1; -; mRNA.
DR EMBL; X06406; CAA29696.1; -; mRNA.
DR EMBL; AF140348; AAD26866.1; -; mRNA.
DR EMBL; DQ360291; ABC95972.1; -; Genomic_DNA.
DR EMBL; DQ360292; ABC95977.1; -; Genomic_DNA.
DR EMBL; AK010423; BAB26926.1; -; mRNA.
DR EMBL; AK010985; BAB27306.1; -; mRNA.
DR EMBL; AK011041; BAB27353.1; -; mRNA.
DR EMBL; AK011043; BAB27355.1; -; mRNA.
DR EMBL; AK075778; BAC35952.1; -; mRNA.
DR EMBL; AK075790; BAC35960.1; -; mRNA.
DR EMBL; AK082935; BAC38701.1; -; mRNA.
DR EMBL; AK088954; BAC40671.1; -; mRNA.
DR EMBL; AK134224; BAE22057.1; -; mRNA.
DR EMBL; AK135488; BAE22550.1; -; mRNA.
DR EMBL; AK160551; BAE35867.1; -; mRNA.
DR EMBL; AK160625; BAE35924.1; -; mRNA.
DR EMBL; AK165219; BAE38083.1; -; mRNA.
DR EMBL; AK166697; BAE38953.1; -; mRNA.
DR EMBL; AK166874; BAE39085.1; -; mRNA.
DR EMBL; AK167132; BAE39278.1; -; mRNA.
DR EMBL; BC003829; AAH03829.1; -; mRNA.
DR EMBL; BC037195; AAH37195.1; -; mRNA.
DR EMBL; BC055886; AAH55886.1; -; mRNA.
DR EMBL; BC081461; AAH81461.1; -; mRNA.
DR EMBL; BC084677; AAH84677.1; -; mRNA.
DR EMBL; BC092041; AAH92041.1; -; mRNA.
DR EMBL; BC094902; AAH94902.1; -; mRNA.
DR EMBL; BC099601; AAH99601.1; -; mRNA.
DR EMBL; BC110285; AAI10286.1; -; mRNA.
DR CCDS; CCDS23623.1; -.
DR PIR; A29395; A29395.
DR RefSeq; NP_035159.3; NM_011029.4.
DR PDB; 7CPU; EM; 2.82 A; SA=1-295.
DR PDB; 7CPV; EM; 3.03 A; SA=1-295.
DR PDB; 7LS1; EM; 3.30 A; o2=1-295.
DR PDB; 7LS2; EM; 3.10 A; o2=1-295.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P14206; -.
DR SMR; P14206; -.
DR BioGRID; 201107; 92.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR DIP; DIP-38089N; -.
DR IntAct; P14206; 16.
DR MINT; P14206; -.
DR STRING; 10090.ENSMUSP00000035105; -.
DR ChEMBL; CHEMBL1075301; -.
DR iPTMnet; P14206; -.
DR PhosphoSitePlus; P14206; -.
DR SwissPalm; P14206; -.
DR REPRODUCTION-2DPAGE; IPI00123604; -.
DR REPRODUCTION-2DPAGE; P14206; -.
DR SWISS-2DPAGE; P14206; -.
DR CPTAC; non-CPTAC-4059; -.
DR EPD; P14206; -.
DR jPOST; P14206; -.
DR MaxQB; P14206; -.
DR PaxDb; P14206; -.
DR PeptideAtlas; P14206; -.
DR PRIDE; P14206; -.
DR ProteomicsDB; 260999; -.
DR DNASU; 16785; -.
DR Ensembl; ENSMUST00000035105; ENSMUSP00000035105; ENSMUSG00000032518.
DR Ensembl; ENSMUST00000217317; ENSMUSP00000148933; ENSMUSG00000032518.
DR GeneID; 16785; -.
DR KEGG; mmu:16785; -.
DR UCSC; uc009scd.2; mouse.
DR CTD; 3921; -.
DR MGI; MGI:105381; Rpsa.
DR VEuPathDB; HostDB:ENSMUSG00000032518; -.
DR eggNOG; KOG0830; Eukaryota.
DR GeneTree; ENSGT00950000183099; -.
DR HOGENOM; CLU_058171_1_0_1; -.
DR InParanoid; P14206; -.
DR OMA; ENKMKRY; -.
DR OrthoDB; 1129610at2759; -.
DR PhylomeDB; P14206; -.
DR TreeFam; TF300100; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 16785; 23 hits in 72 CRISPR screens.
DR ChiTaRS; Rpsa; mouse.
DR PRO; PR:P14206; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P14206; protein.
DR Bgee; ENSMUSG00000032518; Expressed in ventricular zone and 75 other tissues.
DR ExpressionAtlas; P14206; baseline and differential.
DR Genevisible; P14206; MM.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0043236; F:laminin binding; IDA:MGI.
DR GO; GO:0005055; F:laminin receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016,
FT ECO:0000269|Ref.7"
FT CHAIN 2..295
FT /note="40S ribosomal protein SA"
FT /id="PRO_0000134359"
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|Ref.7"
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:0007744|PubMed:23806337"
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 18
FT /note="F -> L (in Ref. 1; AAA39413)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="N -> H (in Ref. 5; BAB27355)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="R -> A (in Ref. 1; AAA39413)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="P -> T (in Ref. 6; AAH92041)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="S -> Y (in Ref. 5; BAC38701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 32838 MW; C698CFA6B759FD2E 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
AQPEVADWSE GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTEWS
