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40S ribosomal protein SA (37 kDa laminin receptor precursor) (37LRP) (37/67 kDa laminin receptor) (LRP/LR) (67 kDa laminin receptor) (67LR) (Colon carcinoma laminin-binding protein) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40) (Multidrug resistance-associated protein MGr1-Ag) (NEM/1CHD4) (Small ribosomal subunit protein uS2)

 RSSA_HUMAN              Reviewed;         295 AA.
P08865; P11085; P12030; Q16471; Q6IPD1; Q6IPD2; Q6NSD1; Q6NXQ8;
Q86VC0;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
30-AUG-2017, entry version 200.
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=37/67 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=Colon carcinoma laminin-binding protein;
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=Multidrug resistance-associated protein MGr1-Ag;
AltName: Full=NEM/1CHD4;
AltName: Full=Small ribosomal subunit protein uS2 {ECO:0000303|PubMed:24524803};
Name=RPSA {ECO:0000255|HAMAP-Rule:MF_03016}; Synonyms=LAMBR, LAMR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2970639; DOI=10.1073/pnas.85.17.6394;
Yow H., Wong J.M., Chen H.S., Lee C., Steele G.D. Jr., Chen L.B.;
"Increased mRNA expression of a laminin-binding protein in human colon
carcinoma: complete sequence of a full-length cDNA encoding the
protein.";
Proc. Natl. Acad. Sci. U.S.A. 85:6394-6398(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2543954; DOI=10.1093/nar/17.10.3829;
van den Ouweland A.M.W., van Duijnhoven H.L.P., Deichmann K.A.,
van Groningen J.J.M., de Leij L., van de Ven W.J.M.;
"Characteristics of a multicopy gene family predominantly consisting
of processed pseudogenes.";
Nucleic Acids Res. 17:3829-3843(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=1534510; DOI=10.1016/0304-3835(92)90096-E;
Satoh K., Narumi K., Sakai T., Abe T., Kikuchi T., Matsushima K.,
Sindoh S., Motomiya M.;
"Cloning of 67-kDa laminin receptor cDNA and gene expression in normal
and malignant cell lines of the human lung.";
Cancer Lett. 62:199-203(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8760291;
Jackers P., Minoletti F., Belotti D., Clausse N., Sozzi G.,
Sobel M.E., Castronovo V.;
"Isolation from a multigene family of the active human gene of the
metastasis-associated multifunctional protein 37LRP/p40 at chromosome
3p21.3.";
Oncogene 13:495-503(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Shi Y., Zhai H., Wang X., Wu H., Ning X., Han Y., Zhang D., Xiao B.,
Wu K., Fan D.;
"Multidrug resistance associated protein MGr1-Ag is identical to human
67-KDa laminin receptor precursor.";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-117.
TISSUE=Bone marrow, Brain, Cervix, Hippocampus, Liver, Lung, Lymph,
Placenta, Prostate, Skin, and Urinary bladder;
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).
[8]
PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V., Potts A., Barblan J., Quadroni M.;
Submitted (JUL-2004) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-295.
Siyanova E.Y., Lukashev V.A., Blinov V.M., Troyanovskii S.M.;
"Determination and analysis of the primary sequence of human laminin-
binding protein.";
Dokl. Biochem. 313:227-231(1990).
[10]
PROTEIN SEQUENCE OF 16-26 AND 90-99.
PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
"Characterization of the human small-ribosomal-subunit proteins by N-
terminal and internal sequencing, and mass spectrometry.";
Eur. J. Biochem. 239:144-149(1996).
[11]
PROTEIN SEQUENCE OF 43-52; 64-80; 103-117; 129-155 AND 192-205, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-209.
TISSUE=Blood;
PubMed=8586453;
Selvamurugan N., Eliceiri G.L.;
"The gene for human E2 small nucleolar RNA resides in an intron of a
laminin-binding protein gene.";
Genomics 30:400-401(1995).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 161-295, AND PROTEIN SEQUENCE OF
177-184.
PubMed=2429301; DOI=10.1073/pnas.83.19.7137;
Wewer U.M., Liotta L.A., Jaye M., Ricca G.A., Drohan W.N.,
Claysmith A.P., Rao C.N., Wirth P., Coligan J.E., Albrechtsen R.,
Mudryj M., Sobel M.E.;
"Altered levels of laminin receptor mRNA in various human carcinoma
cells that have different abilities to bind laminin.";
Proc. Natl. Acad. Sci. U.S.A. 83:7137-7141(1986).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-295.
PubMed=9582194;
Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
Hudson T.J., Tanaka T., Page D.C.;
"A map of 75 human ribosomal protein genes.";
Genome Res. 8:509-523(1998).
[15]
FUNCTION, AND INTERACTION WITH LAMININ-1.
PubMed=6300843; DOI=10.1073/pnas.80.2.444;
Terranova V.P., Rao C.N., Kalebic T., Margulies I.M., Liotta L.A.;
"Laminin receptor on human breast carcinoma cells.";
Proc. Natl. Acad. Sci. U.S.A. 80:444-448(1983).
[16]
DOMAINS, AND INTERACTION WITH LAMININ-1.
PubMed=1834645;
Castronovo V., Taraboletti G., Sobel M.E.;
"Functional domains of the 67-kDa laminin receptor precursor.";
J. Biol. Chem. 266:20440-20446(1991).
[17]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SINDBIS VIRUS E2
ENVELOPE GLYCOPROTEIN.
PubMed=1385835;
Wang K.-S., Kuhn R.J., Strauss E.G., Ou S., Strauss J.H.;
"High-affinity laminin receptor is a receptor for Sindbis virus in
mammalian cells.";
J. Virol. 66:4992-5001(1992).
[18]
INTERACTION WITH LAMININ-1.
PubMed=8433567; DOI=10.1038/ki.1993.7;
Cioce V., Margulies I.M.K., Sobel M.E., Castronovo V.;
"Interaction between the 67 kilodalton metastasis-associated laminin
receptor and laminin.";
Kidney Int. 43:30-37(1993).
[19]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH VENEZUELAN EQUINE
ENCEPHALITIS VIRUS E2 GLYCOPROTEIN.
PubMed=8764073;
Ludwig G.V., Kondig J.P., Smith J.F.;
"A putative receptor for Venezuelan equine encephalitis virus from
mosquito cells.";
J. Virol. 70:5592-5599(1996).
[20]
INTERACTION WITH PRNP.
PubMed=9396609; DOI=10.1038/nm1297-1383;
Rieger R., Edenhofer F., Lasmezas C.I., Weiss S.;
"The human 37-kDa laminin receptor precursor interacts with the prion
protein in eukaryotic cells.";
Nat. Med. 3:1383-1388(1997).
[21]
ACYLATION.
PubMed=9581863;
DOI=10.1002/(SICI)1097-4644(19980601)69:3<244::AID-JCB2>3.0.CO;2-R;
Buto S., Tagliabue E., Ardini E., Magnifico A., Ghirelli C.,
van den Brule F., Castronovo V., Colnaghi M.I., Sobel M.E., Menard S.;
"Formation of the 67-kDa laminin receptor by acylation of the
precursor.";
J. Cell. Biochem. 69:244-251(1998).
[22]
INTERACTION WITH LAMININ-5.
PubMed=9718729; DOI=10.1093/oxfordjournals.molbev.a026000;
Ardini E., Pesole G., Tagliabue E., Magnifico A., Castronovo V.,
Sobel M.E., Colnaghi M.I., Menard S.;
"The 67-kDa laminin receptor originated from a ribosomal protein that
acquired a dual function during evolution.";
Mol. Biol. Evol. 15:1017-1025(1998).
[23]
INTERACTION WITH RPS21.
PubMed=10079194; DOI=10.1006/bbrc.1999.0343;
Sato M., Saeki Y., Tanaka K., Kaneda Y.;
"Ribosome-associated protein LBP/p40 binds to S21 protein of 40S
ribosome: analysis using a yeast two-hybrid system.";
Biochem. Biophys. Res. Commun. 256:385-390(1999).
[24]
INTERACTION WITH LAMB1.
PubMed=10772861; DOI=10.1006/jmbi.2000.3680;
Kazmin D.A., Hoyt T.R., Taubner L., Teintze M., Starkey J.R.;
"Phage display mapping for peptide 11 sensitive sequences binding to
laminin-1.";
J. Mol. Biol. 298:431-445(2000).
[25]
PRION-BINDING, SUBCELLULAR LOCATION, AND SUBUNIT.
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).
[26]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH DENGUE VIRUS
ENVELOPE PROTEIN E.
PubMed=15507651; DOI=10.1128/JVI.78.22.12647-12656.2004;
Thepparit C., Smith D.R.;
"Serotype-specific entry of dengue virus into liver cells:
identification of the 37-kilodalton/67-kilodalton high-affinity
laminin receptor as a dengue virus serotype 1 receptor.";
J. Virol. 78:12647-12656(2004).
[27]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
PPP1R16B AND PPP1CA.
PubMed=16263087; DOI=10.1016/j.bbrc.2005.10.089;
Kim K., Li L., Kozlowski K., Suh H.S., Cao W., Ballermann B.J.;
"The protein phosphatase-1 targeting subunit TIMAP regulates LAMR1
phosphorylation.";
Biochem. Biophys. Res. Commun. 338:1327-1334(2005).
[28]
FUNCTION (MICROBIAL INFECTION).
PubMed=15516338; DOI=10.1074/jbc.M410176200;
Kim K.J., Chung J.W., Kim K.S.;
"67-kDa laminin receptor promotes internalization of cytotoxic
necrotizing factor 1-expressing Escherichia coli K1 into human brain
microvascular endothelial cells.";
J. Biol. Chem. 280:1360-1368(2005).
[29]
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).
[30]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENO-ASSOCIATED
VIRUS CAPSID PROTEINS.
PubMed=16973587; DOI=10.1128/JVI.00878-06;
Akache B., Grimm D., Pandey K., Yant S.R., Xu H., Kay M.A.;
"The 37/67-kilodalton laminin receptor is a receptor for adeno-
associated virus serotypes 8, 2, 3, and 9.";
J. Virol. 80:9831-9836(2006).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND THR-97, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
INVOLVEMENT IN ICAS, VARIANTS ICAS ASN-54; PHE-58; GLY-180; TRP-180
AND CYS-186, CHARACTERIZATION OF VARIANTS ICAS ASN-54; PHE-58;
GLY-180; TRP-180 AND CYS-186, AND VARIANTS VAL-185; GLY-257 AND
THR-278.
PubMed=23579497; DOI=10.1126/science.1234864;
Bolze A., Mahlaoui N., Byun M., Turner B., Trede N., Ellis S.R.,
Abhyankar A., Itan Y., Patin E., Brebner S., Sackstein P., Puel A.,
Picard C., Abel L., Quintana-Murci L., Faust S.N., Williams A.P.,
Baretto R., Duddridge M., Kini U., Pollard A.J., Gaud C., Frange P.,
Orbach D., Emile J.F., Stephan J.L., Sorensen R., Plebani A.,
Hammarstrom L., Conley M.E., Selleri L., Casanova J.L.;
"Ribosomal protein SA haploinsufficiency in humans with isolated
congenital asplenia.";
Science 340:976-978(2013).
[37]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-89, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[41]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 9-205.
PubMed=18063583; DOI=10.1074/jbc.C700206200;
Jamieson K.V., Wu J., Hubbard S.R., Meruelo D.;
"Crystal structure of the human laminin receptor precursor.";
J. Biol. Chem. 283:3002-3005(2008).
-!- 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. Acts as a PPP1R16B-dependent substrate
of PPP1CA. {ECO:0000255|HAMAP-Rule:MF_03016,
ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:6300843}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for the adeno-
associated viruses 2,3,8 and 9, dengue virus, Sindbis virus and
Venezuelan equine encephalitis virus (PubMed:1385835,
PubMed:15507651, PubMed:16973587). Also acts as a receptor for
pathogenic prion protein and bacteria (PubMed:9396609,
PubMed:11689427, PubMed:15516338). {ECO:0000269|PubMed:11689427,
ECO:0000269|PubMed:1385835, ECO:0000269|PubMed:15507651,
ECO:0000269|PubMed:15516338, ECO:0000269|PubMed:16973587,
ECO:0000269|PubMed:9396609}.
-!- SUBUNIT: Monomer (37LRP) and homodimer (67LR). 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. Interacts with several
laminins including at least LAMB1. Interacts with MDK (By
similarity). The mature dimeric form interacts with PPP1R16B (via
its fourth ankyrin repeat). Interacts with PPP1CA only in the
presence of PPP1R16B. {ECO:0000255|HAMAP-Rule:MF_03016,
ECO:0000269|PubMed:10079194, ECO:0000269|PubMed:10772861,
ECO:0000269|PubMed:11689427, ECO:0000269|PubMed:15507651,
ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:1834645,
ECO:0000269|PubMed:6300843, ECO:0000269|PubMed:8433567,
ECO:0000269|PubMed:9396609, ECO:0000269|PubMed:9718729}.
-!- SUBUNIT: (Microbial infection) 67LR interacts with capsid protein
of Adeno-associated virus 2,3,8 and 9.
{ECO:0000269|PubMed:16973587}.
-!- SUBUNIT: (Microbial infection) 67LR interacts with envelope
protein of dengue virus. {ECO:0000269|PubMed:15507651}.
-!- SUBUNIT: (Microbial infection) 6s7LR interacts with E2
glycoprotein of Sindbis and Venezuelan equine encephalitis virus
(PubMed:8764073, PubMed:1385835). {ECO:0000269|PubMed:1385835,
ECO:0000269|PubMed:8764073}.
-!- INTERACTION:
Q15046:KARS; NbExp=5; IntAct=EBI-354112, EBI-356367;
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-354112, EBI-717399;
-!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus
{ECO:0000255|HAMAP-Rule:MF_03016}. 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 (By
similarity). Colocalizes with PPP1R16B in the cell membrane.
{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 (PubMed:9581863).
{ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000269|PubMed:9581863}.
-!- 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}.
-!- DISEASE: Asplenia, isolated congenital (ICAS) [MIM:271400]: A rare
primary immunodeficiency and life-threatening condition, often
presenting with pneumococcal sepsis. Most affected individuals die
of severe bacterial infections in early childhood. Isolated
asplenia is distinct from asplenia associated with other complex
visceral defects, notably heterotaxy syndromes such as Ivemark
syndrome. {ECO:0000269|PubMed:23579497}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- 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; J03799; AAA36161.1; -; mRNA.
EMBL; X15005; CAA33112.1; -; mRNA.
EMBL; S37431; AAB22299.1; -; mRNA.
EMBL; U43901; AAC50652.1; -; Genomic_DNA.
EMBL; AF503367; AAM33304.1; -; mRNA.
EMBL; BT007219; AAP35883.1; -; mRNA.
EMBL; BC005391; AAH05391.1; -; mRNA.
EMBL; BC008867; AAH08867.1; -; mRNA.
EMBL; BC010418; AAH10418.1; -; mRNA.
EMBL; BC013827; AAH13827.1; -; mRNA.
EMBL; BC034537; AAH34537.1; -; mRNA.
EMBL; BC050688; AAH50688.1; -; mRNA.
EMBL; BC053370; AAH53370.1; -; mRNA.
EMBL; BC062714; AAH62714.1; -; mRNA.
EMBL; BC066941; AAH66941.1; -; mRNA.
EMBL; BC068062; AAH68062.1; -; mRNA.
EMBL; BC070263; AAH70263.1; -; mRNA.
EMBL; BC071693; AAH71693.1; -; mRNA.
EMBL; BC071968; AAH71968.1; -; mRNA.
EMBL; BC071969; AAH71969.1; -; mRNA.
EMBL; BC071970; AAH71970.1; -; mRNA.
EMBL; BC073863; AAH73863.1; -; mRNA.
EMBL; BC107567; AAI07568.1; -; mRNA.
EMBL; X61156; CAA43469.1; -; mRNA.
EMBL; U36484; AAC50313.1; -; Genomic_DNA.
EMBL; M14199; AAA36165.1; -; mRNA.
EMBL; AB007146; BAA25812.1; -; Genomic_DNA.
CCDS; CCDS2686.1; -.
PIR; A31233; A31233.
RefSeq; NP_001291217.1; NM_001304288.1.
RefSeq; NP_002286.2; NM_002295.5.
UniGene; Hs.449909; -.
PDB; 3BCH; X-ray; 2.15 A; A=2-220.
PDB; 4UG0; EM; -; SA=1-295.
PDB; 4V6X; EM; 5.00 A; AA=1-295.
PDB; 5A2Q; EM; 3.90 A; A=1-295.
PDB; 5AJ0; EM; 3.50 A; BA=1-295.
PDB; 5FLX; EM; 3.90 A; A=1-295.
PDB; 5LKS; EM; 3.60 A; SA=1-295.
PDB; 5T2C; EM; 3.60 A; Ao=1-295.
PDBsum; 3BCH; -.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5A2Q; -.
PDBsum; 5AJ0; -.
PDBsum; 5FLX; -.
PDBsum; 5LKS; -.
PDBsum; 5T2C; -.
ProteinModelPortal; P08865; -.
SMR; P08865; -.
BioGrid; 110115; 221.
DIP; DIP-32878N; -.
IntAct; P08865; 42.
MINT; MINT-1402850; -.
STRING; 9606.ENSP00000346067; -.
ChEMBL; CHEMBL6119; -.
DrugBank; DB04985; PCK3145.
iPTMnet; P08865; -.
PhosphoSitePlus; P08865; -.
SwissPalm; P08865; -.
BioMuta; RPSA; -.
DMDM; 125969; -.
EPD; P08865; -.
MaxQB; P08865; -.
PaxDb; P08865; -.
PeptideAtlas; P08865; -.
PRIDE; P08865; -.
TopDownProteomics; P08865; -.
DNASU; 3921; -.
Ensembl; ENST00000301821; ENSP00000346067; ENSG00000168028.
GeneID; 3921; -.
KEGG; hsa:3921; -.
UCSC; uc003cjp.4; human.
CTD; 3921; -.
DisGeNET; 3921; -.
GeneCards; RPSA; -.
HGNC; HGNC:6502; RPSA.
HPA; CAB009561; -.
MalaCards; RPSA; -.
MIM; 150370; gene.
MIM; 271400; phenotype.
neXtProt; NX_P08865; -.
OpenTargets; ENSG00000168028; -.
Orphanet; 101351; Familial isolated congenital asplenia.
PharmGKB; PA30287; -.
eggNOG; KOG0830; Eukaryota.
eggNOG; COG0052; LUCA.
GeneTree; ENSGT00390000015036; -.
HOVERGEN; HBG054466; -.
InParanoid; P08865; -.
KO; K02998; -.
PhylomeDB; P08865; -.
TreeFam; TF300100; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-2408557; Selenocysteine synthesis.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; RPSA; human.
EvolutionaryTrace; P08865; -.
GeneWiki; Ribosomal_protein_SA; -.
GenomeRNAi; 3921; -.
PRO; PR:P08865; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000168028; -.
ExpressionAtlas; P08865; baseline and differential.
Genevisible; P08865; HS.
GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005055; F:laminin receptor activity; IEA:InterPro.
GO; GO:0043022; F:ribosome binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
GO; GO:0006407; P:rRNA export from nucleus; IBA:GO_Central.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
GO; GO:0006412; P:translation; IBA:GO_Central.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
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.
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;
3D-structure; Acetylation; Cell membrane; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation;
Host cell receptor for virus entry; Host-virus interaction;
Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Ribonucleoprotein;
Ribosomal protein; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000255|HAMAP-Rule:MF_03016,
ECO:0000269|Ref.8}.
CHAIN 2 295 40S ribosomal protein SA.
/FTId=PRO_0000134358.
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:0000269|PubMed:16263087}.
REGION 161 180 Laminin-binding.
REGION 205 229 Laminin-binding.
REGION 242 295 Laminin-binding.
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:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000255|HAMAP-Rule:MF_03016,
ECO:0000269|Ref.8}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 52 52 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 89 89 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P14206}.
MOD_RES 97 97 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 89 89 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VARIANT 54 54 T -> N (in ICAS; reduced protein levels;
dbSNP:rs397514762).
{ECO:0000269|PubMed:23579497}.
/FTId=VAR_075092.
VARIANT 58 58 L -> F (in ICAS; reduced protein levels;
dbSNP:rs397514763).
{ECO:0000269|PubMed:23579497}.
/FTId=VAR_075093.
VARIANT 117 117 R -> W (in dbSNP:rs17856150).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_025522.
VARIANT 180 180 R -> G (in ICAS; reduced protein levels;
dbSNP:rs397514760).
{ECO:0000269|PubMed:23579497}.
/FTId=VAR_075094.
VARIANT 180 180 R -> W (in ICAS; reduced protein levels;
dbSNP:rs397514760).
{ECO:0000269|PubMed:23579497}.
/FTId=VAR_075095.
VARIANT 185 185 M -> V. {ECO:0000269|PubMed:23579497}.
/FTId=VAR_075096.
VARIANT 186 186 R -> C (in ICAS; reduced protein levels;
dbSNP:rs397514761).
{ECO:0000269|PubMed:23579497}.
/FTId=VAR_075097.
VARIANT 257 257 V -> G (in dbSNP:rs369708612).
{ECO:0000269|PubMed:23579497}.
/FTId=VAR_075098.
VARIANT 278 278 A -> T (in dbSNP:rs143085301).
{ECO:0000269|PubMed:23579497}.
/FTId=VAR_075099.
CONFLICT 60 60 L -> V (in Ref. 9; CAA43469).
{ECO:0000305}.
CONFLICT 84 84 Q -> QVCGTV (in Ref. 2; CAA33112).
{ECO:0000305}.
CONFLICT 115 115 A -> T (in Ref. 7; AAH50688).
{ECO:0000305}.
CONFLICT 135 135 T -> S (in Ref. 7; AAH70263).
{ECO:0000305}.
CONFLICT 211 211 E -> G (in Ref. 3; AAB22299).
{ECO:0000305}.
CONFLICT 214 214 E -> G (in Ref. 7; AAH66941).
{ECO:0000305}.
CONFLICT 228 228 Q -> L (in Ref. 3; AAB22299).
{ECO:0000305}.
HELIX 12 21 {ECO:0000244|PDB:3BCH}.
TURN 22 24 {ECO:0000244|PDB:3BCH}.
HELIX 32 37 {ECO:0000244|PDB:3BCH}.
STRAND 38 41 {ECO:0000244|PDB:3BCH}.
STRAND 47 49 {ECO:0000244|PDB:3BCH}.
HELIX 51 66 {ECO:0000244|PDB:3BCH}.
HELIX 71 73 {ECO:0000244|PDB:3BCH}.
STRAND 74 78 {ECO:0000244|PDB:3BCH}.
HELIX 81 94 {ECO:0000244|PDB:3BCH}.
STRAND 97 101 {ECO:0000244|PDB:3BCH}.
TURN 105 109 {ECO:0000244|PDB:3BCH}.
STRAND 120 125 {ECO:0000244|PDB:3BCH}.
TURN 127 130 {ECO:0000244|PDB:3BCH}.
HELIX 131 139 {ECO:0000244|PDB:3BCH}.
STRAND 144 148 {ECO:0000244|PDB:3BCH}.
STRAND 158 163 {ECO:0000244|PDB:3BCH}.
HELIX 168 185 {ECO:0000244|PDB:3BCH}.
STRAND 191 193 {ECO:0000244|PDB:3BCH}.
HELIX 199 202 {ECO:0000244|PDB:3BCH}.
SEQUENCE 295 AA; 32854 MW; C68DDB16B759E79E 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 TTDWS


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