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40S ribosomal protein SA (37 kDa laminin receptor precursor) (37LRP) (37 kDa oncofetal antigen) (37/67 kDa laminin receptor) (LRP/LR) (67 kDa laminin receptor) (67LR) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40) (OFA/iLRP)

 RSSA_MOUSE              Reviewed;         295 AA.
P14206; Q58E74; Q8BHL0; Q8BNL2; Q91V31; Q9CY13;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 4.
28-MAR-2018, entry version 175.
RecName: Full=40S ribosomal protein SA {ECO:0000255|HAMAP-Rule:MF_03016};
AltName: Full=37 kDa laminin receptor precursor {ECO:0000255|HAMAP-Rule:MF_03016};
Short=37LRP {ECO:0000255|HAMAP-Rule:MF_03016};
AltName: Full=37 kDa oncofetal antigen;
AltName: Full=37/67 kDa laminin receptor {ECO:0000255|HAMAP-Rule:MF_03016};
Short=LRP/LR {ECO:0000255|HAMAP-Rule:MF_03016};
AltName: Full=67 kDa laminin receptor {ECO:0000255|HAMAP-Rule:MF_03016};
Short=67LR {ECO:0000255|HAMAP-Rule:MF_03016};
AltName: Full=Laminin receptor 1 {ECO:0000255|HAMAP-Rule:MF_03016};
Short=LamR {ECO:0000255|HAMAP-Rule:MF_03016};
AltName: Full=Laminin-binding protein precursor p40 {ECO:0000255|HAMAP-Rule:MF_03016};
Short=LBP/p40 {ECO:0000255|HAMAP-Rule:MF_03016};
AltName: Full=OFA/iLRP;
Name=Rpsa; Synonyms=Lamr1, P40-8;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2531008; DOI=10.1021/bi00444a047;
Rao C.N., Castronovo V., Schmitt M.C., Wewer U.M., Claysmith A.P.,
Liotta L.A., Sobel M.E.;
"Evidence for a precursor of the high-affinity metastasis-associated
murine laminin receptor.";
Biochemistry 28:7476-7486(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3357791; DOI=10.1093/nar/16.5.2349;
Makrides S., Chitpatima S.T., Bandyopadhyay R., Brawerman G.;
"Nucleotide sequence for a major messenger RNA for a 40 kilodalton
polypeptide that is under translational control in mouse tumor
cells.";
Nucleic Acids Res. 16:2349-2349(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=BALB/cJ; TISSUE=Fibrosarcoma;
PubMed=10697612;
Coggin J.H. Jr., Barsoum A.L., Rohrer J.W.;
"37 kilodalton oncofetal antigen protein and immature laminin receptor
protein are identical, universal T-cell inducing immunogens on primary
rodent and human cancers.";
Anticancer Res. 19:5535-5542(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CAST/EiJ, and SJL/J;
Lee I.Y., Baxter D.H., Qin S., Hood L.E.;
"Genomic sequence analysis of laminin receptor loci in mice.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Liver, Muellerian duct, Pancreas, Spleen, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, Czech II, and FVB/N;
TISSUE=Brain, Colon, Eye, Kidney, Mammary gland, Mammary tumor, and
Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
Kanor S., Quadroni M., Bienvenut W.V.;
Submitted (MAR-2006) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 18-40; 43-50; 90-100 AND 155-163, AND SUBCELLULAR
LOCATION.
PubMed=8954992; DOI=10.1006/bbrc.1996.1899;
Sato M., Kinoshita K., Kaneda Y., Saeki Y., Iwamatsu A., Tanaka K.;
"Analysis of nuclear localization of laminin binding protein precursor
p40 (LBP/p40).";
Biochem. Biophys. Res. Commun. 229:896-901(1996).
[9]
PROTEIN SEQUENCE OF 64-80; 90-117 AND 129-155, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[10]
FUNCTION AS LAMININ RECEPTOR, AND SUBCELLULAR LOCATION.
PubMed=6301485; DOI=10.1016/0006-291X(83)91370-0;
Rao N.C., Barsky S.H., Terranova V.P., Liotta L.A.;
"Isolation of a tumor cell laminin receptor.";
Biochem. Biophys. Res. Commun. 111:804-808(1983).
[11]
FUNCTION, AND INTERACTION WITH LAMININ-1.
PubMed=16453457;
Lesot H., Kuehl U., von der Mark K.;
"Isolation of a laminin-binding protein from muscle cell membranes.";
EMBO J. 2:861-865(1983).
[12]
FUNCTION, AND INTERACTION WITH LAMININ-1.
PubMed=6302102; DOI=10.1083/jcb.96.5.1475;
Malinoff H.L., Wicha M.S.;
"Isolation of a cell surface receptor protein for laminin from murine
fibrosarcoma cells.";
J. Cell Biol. 96:1475-1479(1983).
[13]
FUNCTION IN RIBOSOME, AND SUBCELLULAR LOCATION.
PubMed=1374897; DOI=10.1073/pnas.89.10.4368;
Auth D., Brawerman G.;
"A 33-kDa polypeptide with homology to the laminin receptor: component
of translation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 89:4368-4372(1992).
[14]
INTERACTION WITH PRNP, AND SUBCELLULAR LOCATION.
PubMed=11689427; DOI=10.1093/emboj/20.21.5863;
Gauczynski S., Peyrin J.-M., Haik S., Leucht C., Hundt C., Rieger R.,
Krasemann S., Deslys J.-P., Dormont D., Lasmezas C.I., Weiss S.;
"The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor
for the cellular prion protein.";
EMBO J. 20:5863-5875(2001).
[15]
INTERACTION WITH MDK, AND SUBCELLULAR LOCATION.
PubMed=11597123; DOI=10.1006/excr.2001.5341;
Salama R.H.M., Muramatsu H., Zou K., Inui T., Kimura T., Muramatsu T.;
"Midkine binds to 37-kDa laminin binding protein precursor, leading to
nuclear transport of the complex.";
Exp. Cell Res. 270:13-20(2001).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[17]
SUBCELLULAR LOCATION.
PubMed=18339329; DOI=10.1016/j.bbadis.2008.02.003;
Nikles D., Vana K., Gauczynski S., Knetsch H., Ludewigs H., Weiss S.;
"Subcellular localization of prion proteins and the 37 kDa/67 kDa
laminin receptor fused to fluorescent proteins.";
Biochim. Biophys. Acta 1782:335-340(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Required for the assembly and/or stability of the 40S
ribosomal subunit. Required for the processing of the 20S rRNA-
precursor to mature 18S rRNA in a late step of the maturation of
40S ribosomal subunits. Also functions as a cell surface receptor
for laminin. Plays a role in cell adhesion to the basement
membrane and in the consequent activation of signaling
transduction pathways. May play a role in cell fate determination
and tissue morphogenesis. Also acts as a receptor for several
other ligands, including the pathogenic prion protein, viruses,
and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA (By
similarity). Enables malignant tumor cells to penetrate laminin
tissue and vessel barriers. Activates precursor thymic anti-
OFA/iLRP specific cytotoxic T-cell. May induce CD8 T-suppressor
cells secreting IL-10. {ECO:0000255|HAMAP-Rule:MF_03016,
ECO:0000269|PubMed:10697612, ECO:0000269|PubMed:1374897,
ECO:0000269|PubMed:16453457, ECO:0000269|PubMed:6301485,
ECO:0000269|PubMed:6302102}.
-!- SUBUNIT: Monomer (37LRP) and homodimer (67LR) (By similarity).
Component of the small ribosomal subunit. Mature ribosomes consist
of a small (40S) and a large (60S) subunit. The 40S subunit
contains about 33 different proteins and 1 molecule of RNA (18S).
The 60S subunit contains about 49 different proteins and 3
molecules of RNA (28S, 5.8S and 5S). Interacts with RPS21 (By
similarity). Interacts with several laminins including at least
LAMB1. Interacts with MDK. Interacts with PRNP. The mature dimeric
form interacts with PPP1R16B (via its fourth ankyrin repeat).
Interacts with PPP1CA only in the presence of PPP1R16B (By
similarity). {ECO:0000255|HAMAP-Rule:MF_03016}.
-!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus. Note=67LR
is found at the surface of the plasma membrane, with its C-
terminal laminin-binding domain accessible to extracellular
ligands. 37LRP is found at the cell surface, in the cytoplasm and
in the nucleus. Colocalizes with PPP1R16B in the cell membrane (By
similarity). 37LRP shuttles to the nucleus upon midkine (MDK)
binding. {ECO:0000255|HAMAP-Rule:MF_03016}.
-!- PTM: Acylated. Acylation may be a prerequisite for conversion of
the monomeric 37 kDa laminin receptor precursor (37LRP) to the
mature dimeric 67 kDa laminin receptor (67LR), and may provide a
mechanism for membrane association. {ECO:0000255|HAMAP-
Rule:MF_03016}.
-!- PTM: Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage
by stromelysin-3 may be a mechanism to alter cell-extracellular
matrix interactions. {ECO:0000255|HAMAP-Rule:MF_03016}.
-!- MISCELLANEOUS: This protein appears to have acquired a second
function as a laminin receptor specifically in the vertebrate
lineage.
-!- MISCELLANEOUS: It is thought that in vertebrates 37/67 kDa laminin
receptor acquired a dual function during evolution. It developed
from the ribosomal protein SA, playing an essential role in the
protein biosynthesis lacking any laminin binding activity, to a
cell surface receptor with laminin binding activity.
-!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
{ECO:0000255|HAMAP-Rule:MF_03016}.
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EMBL; J02870; AAA39413.1; -; mRNA.
EMBL; X06406; CAA29696.1; -; mRNA.
EMBL; AF140348; AAD26866.1; -; mRNA.
EMBL; DQ360291; ABC95972.1; -; Genomic_DNA.
EMBL; DQ360292; ABC95977.1; -; Genomic_DNA.
EMBL; AK010423; BAB26926.1; -; mRNA.
EMBL; AK010985; BAB27306.1; -; mRNA.
EMBL; AK011041; BAB27353.1; -; mRNA.
EMBL; AK011043; BAB27355.1; -; mRNA.
EMBL; AK075778; BAC35952.1; -; mRNA.
EMBL; AK075790; BAC35960.1; -; mRNA.
EMBL; AK082935; BAC38701.1; -; mRNA.
EMBL; AK088954; BAC40671.1; -; mRNA.
EMBL; AK134224; BAE22057.1; -; mRNA.
EMBL; AK135488; BAE22550.1; -; mRNA.
EMBL; AK160551; BAE35867.1; -; mRNA.
EMBL; AK160625; BAE35924.1; -; mRNA.
EMBL; AK165219; BAE38083.1; -; mRNA.
EMBL; AK166697; BAE38953.1; -; mRNA.
EMBL; AK166874; BAE39085.1; -; mRNA.
EMBL; AK167132; BAE39278.1; -; mRNA.
EMBL; BC003829; AAH03829.1; -; mRNA.
EMBL; BC037195; AAH37195.1; -; mRNA.
EMBL; BC055886; AAH55886.1; -; mRNA.
EMBL; BC081461; AAH81461.1; -; mRNA.
EMBL; BC084677; AAH84677.1; -; mRNA.
EMBL; BC092041; AAH92041.1; -; mRNA.
EMBL; BC094902; AAH94902.1; -; mRNA.
EMBL; BC099601; AAH99601.1; -; mRNA.
EMBL; BC110285; AAI10286.1; -; mRNA.
CCDS; CCDS23623.1; -.
PIR; A29395; A29395.
RefSeq; NP_035159.3; NM_011029.4.
UniGene; Mm.311972; -.
UniGene; Mm.391708; -.
UniGene; Mm.4071; -.
ProteinModelPortal; P14206; -.
SMR; P14206; -.
BioGrid; 201107; 5.
DIP; DIP-38089N; -.
IntAct; P14206; 14.
MINT; P14206; -.
STRING; 10090.ENSMUSP00000035105; -.
ChEMBL; CHEMBL1075301; -.
iPTMnet; P14206; -.
PhosphoSitePlus; P14206; -.
SwissPalm; P14206; -.
REPRODUCTION-2DPAGE; IPI00123604; -.
REPRODUCTION-2DPAGE; P14206; -.
SWISS-2DPAGE; P14206; -.
EPD; P14206; -.
MaxQB; P14206; -.
PaxDb; P14206; -.
PeptideAtlas; P14206; -.
PRIDE; P14206; -.
Ensembl; ENSMUST00000035105; ENSMUSP00000035105; ENSMUSG00000032518.
Ensembl; ENSMUST00000217317; ENSMUSP00000148933; ENSMUSG00000032518.
GeneID; 16785; -.
KEGG; mmu:16785; -.
UCSC; uc009scd.2; mouse.
CTD; 3921; -.
MGI; MGI:105381; Rpsa.
eggNOG; KOG0830; Eukaryota.
eggNOG; COG0052; LUCA.
GeneTree; ENSGT00390000015036; -.
HOGENOM; HOG000232073; -.
HOVERGEN; HBG054466; -.
InParanoid; P14206; -.
KO; K02998; -.
OMA; QQKTKDM; -.
OrthoDB; EOG091G0J0Q; -.
PhylomeDB; P14206; -.
TreeFam; TF300100; -.
Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-MMU-72649; Translation initiation complex formation.
Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; Rpsa; mouse.
PRO; PR:P14206; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032518; -.
CleanEx; MM_RPSA; -.
ExpressionAtlas; P14206; baseline and differential.
Genevisible; P14206; MM.
GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0015935; C:small ribosomal subunit; IDA:MGI.
GO; GO:0043236; F:laminin binding; IDA:MGI.
GO; GO:0005055; F:laminin receptor activity; IEA:InterPro.
GO; GO:0043022; F:ribosome binding; ISO:MGI.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
GO; GO:0000461; P:endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
GO; GO:0006407; P:rRNA export from nucleus; IBA:GO_Central.
GO; GO:0006412; P:translation; IBA:GO_Central.
CDD; cd01425; RPS2; 1.
HAMAP; MF_03015; Ribosomal_S2_euk; 1.
HAMAP; MF_03016; Ribosomal_S2_laminin_receptor; 1.
InterPro; IPR027504; 40S_ribosomal_SA.
InterPro; IPR032281; 40S_SA_C.
InterPro; IPR001865; Ribosomal_S2.
InterPro; IPR018130; Ribosomal_S2_CS.
InterPro; IPR027498; Ribosomal_S2_euk.
InterPro; IPR005707; Ribosomal_S2_euk/arc.
InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
PANTHER; PTHR11489; PTHR11489; 1.
Pfam; PF16122; 40S_SA_C; 1.
Pfam; PF00318; Ribosomal_S2; 2.
PRINTS; PR00395; RIBOSOMALS2.
SUPFAM; SSF52313; SSF52313; 1.
TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Membrane; Nucleus;
Phosphoprotein; Receptor; Reference proteome; Repeat;
Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000255|HAMAP-
Rule:MF_03016, ECO:0000269|Ref.7}.
CHAIN 2 295 40S ribosomal protein SA.
/FTId=PRO_0000134359.
REPEAT 230 232 [DE]-W-[ST] 1.
REPEAT 247 249 [DE]-W-[ST] 2.
REPEAT 266 268 [DE]-W-[ST] 3.
REPEAT 275 277 [DE]-W-[ST] 4.
REPEAT 293 295 [DE]-W-[ST] 5.
REGION 54 113 Interaction with PPP1R16B.
{ECO:0000255|HAMAP-Rule:MF_03016}.
REGION 161 180 Laminin-binding. {ECO:0000255|HAMAP-
Rule:MF_03016}.
REGION 205 229 Laminin-binding. {ECO:0000255|HAMAP-
Rule:MF_03016}.
REGION 242 295 Laminin-binding. {ECO:0000255|HAMAP-
Rule:MF_03016}.
SITE 115 116 Cleavage; by ST3; site 1.
{ECO:0000255|HAMAP-Rule:MF_03016}.
SITE 133 134 Cleavage; by ST3; site 2.
{ECO:0000255|HAMAP-Rule:MF_03016}.
MOD_RES 2 2 N-acetylserine. {ECO:0000255|HAMAP-
Rule:MF_03016, ECO:0000269|Ref.7}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:P08865}.
MOD_RES 52 52 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08865}.
MOD_RES 89 89 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 97 97 Phosphothreonine.
{ECO:0000250|UniProtKB:P08865}.
CROSSLNK 89 89 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08865}.
CONFLICT 18 18 F -> L (in Ref. 1; AAA39413).
{ECO:0000305}.
CONFLICT 29 29 N -> H (in Ref. 5; BAB27355).
{ECO:0000305}.
CONFLICT 155 155 R -> A (in Ref. 1; AAA39413).
{ECO:0000305}.
CONFLICT 243 243 P -> T (in Ref. 6; AAH92041).
{ECO:0000305}.
CONFLICT 249 249 S -> Y (in Ref. 5; BAC38701).
{ECO:0000305}.
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


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