ID RSSA_HUMAN Reviewed; 295 AA. AC P08865; P11085; P12030; Q16471; Q6IPD1; Q6IPD2; Q6NSD1; Q6NXQ8; Q86VC0; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 02-SEP-2026, entry version 256. DE RecName: Full=Small ribosomal subunit protein uS2 {ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000303|PubMed:24524803}; 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=40S ribosomal protein SA; 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=Colon carcinoma laminin-binding protein; 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=Multidrug resistance-associated protein MGr1-Ag; DE AltName: Full=NEM/1CHD4; GN Name=RPSA {ECO:0000255|HAMAP-Rule:MF_03016}; Synonyms=LAMBR, LAMR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2970639; DOI=10.1073/pnas.85.17.6394; RA Yow H., Wong J.M., Chen H.S., Lee C., Steele G.D. Jr., Chen L.B.; RT "Increased mRNA expression of a laminin-binding protein in human colon RT carcinoma: complete sequence of a full-length cDNA encoding the protein."; RL Proc. Natl. Acad. Sci. U.S.A. 85:6394-6398(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2543954; DOI=10.1093/nar/17.10.3829; RA van den Ouweland A.M.W., van Duijnhoven H.L.P., Deichmann K.A., RA van Groningen J.J.M., de Leij L., van de Ven W.J.M.; RT "Characteristics of a multicopy gene family predominantly consisting of RT processed pseudogenes."; RL Nucleic Acids Res. 17:3829-3843(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung; RX PubMed=1534510; DOI=10.1016/0304-3835(92)90096-e; RA Satoh K., Narumi K., Sakai T., Abe T., Kikuchi T., Matsushima K., RA Sindoh S., Motomiya M.; RT "Cloning of 67-kDa laminin receptor cDNA and gene expression in normal and RT malignant cell lines of the human lung."; RL Cancer Lett. 62:199-203(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8760291; RA Jackers P., Minoletti F., Belotti D., Clausse N., Sozzi G., Sobel M.E., RA Castronovo V.; RT "Isolation from a multigene family of the active human gene of the RT metastasis-associated multifunctional protein 37LRP/p40 at chromosome RT 3p21.3."; RL Oncogene 13:495-503(1996). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Shi Y., Zhai H., Wang X., Wu H., Ning X., Han Y., Zhang D., Xiao B., Wu K., RA Fan D.; RT "Multidrug resistance associated protein MGr1-Ag is identical to human 67- RT KDa laminin receptor precursor."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-117. RC TISSUE=Bone marrow, Brain, Cervix, Hippocampus, Liver, Lung, Lymph, RC Placenta, Prostate, Skin, and Urinary bladder; 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 [8] RP PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V., Potts A., Barblan J., Quadroni M.; RL Submitted (JUL-2004) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-295. RA Siyanova E.Y., Lukashev V.A., Blinov V.M., Troyanovskii S.M.; RT "Determination and analysis of the primary sequence of human laminin- RT binding protein."; RL Dokl. Biochem. 313:227-231(1990). RN [10] RP PROTEIN SEQUENCE OF 16-26 AND 90-99. RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x; RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., RA Thiede B., Wittmann-Liebold B., Otto A.; RT "Characterization of the human small-ribosomal-subunit proteins by N- RT terminal and internal sequencing, and mass spectrometry."; RL Eur. J. Biochem. 239:144-149(1996). RN [11] RP PROTEIN SEQUENCE OF 43-52; 64-80; 103-117; 129-155 AND 192-205, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-209. RC TISSUE=Blood; RX PubMed=8586453; RA Selvamurugan N., Eliceiri G.L.; RT "The gene for human E2 small nucleolar RNA resides in an intron of a RT laminin-binding protein gene."; RL Genomics 30:400-401(1995). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 161-295, AND PROTEIN SEQUENCE OF 177-184. RX PubMed=2429301; DOI=10.1073/pnas.83.19.7137; RA Wewer U.M., Liotta L.A., Jaye M., Ricca G.A., Drohan W.N., Claysmith A.P., RA Rao C.N., Wirth P., Coligan J.E., Albrechtsen R., Mudryj M., Sobel M.E.; RT "Altered levels of laminin receptor mRNA in various human carcinoma cells RT that have different abilities to bind laminin."; RL Proc. Natl. Acad. Sci. U.S.A. 83:7137-7141(1986). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-295. RX PubMed=9582194; DOI=10.1101/gr.8.5.509; RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., RA Tanaka T., Page D.C.; RT "A map of 75 human ribosomal protein genes."; RL Genome Res. 8:509-523(1998). RN [15] RP FUNCTION, AND INTERACTION WITH LAMININ-1. RX PubMed=6300843; DOI=10.1073/pnas.80.2.444; RA Terranova V.P., Rao C.N., Kalebic T., Margulies I.M., Liotta L.A.; RT "Laminin receptor on human breast carcinoma cells."; RL Proc. Natl. Acad. Sci. U.S.A. 80:444-448(1983). RN [16] RP DOMAINS, AND INTERACTION WITH LAMININ-1. RX PubMed=1834645; DOI=10.1016/s0021-9258(18)54943-7; RA Castronovo V., Taraboletti G., Sobel M.E.; RT "Functional domains of the 67-kDa laminin receptor precursor."; RL J. Biol. Chem. 266:20440-20446(1991). RN [17] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SINDBIS VIRUS E2 RP ENVELOPE GLYCOPROTEIN. RX PubMed=1385835; DOI=10.1128/jvi.66.8.4992-5001.1992; RA Wang K.-S., Kuhn R.J., Strauss E.G., Ou S., Strauss J.H.; RT "High-affinity laminin receptor is a receptor for Sindbis virus in RT mammalian cells."; RL J. Virol. 66:4992-5001(1992). RN [18] RP INTERACTION WITH LAMININ-1. RX PubMed=8433567; DOI=10.1038/ki.1993.7; RA Cioce V., Margulies I.M.K., Sobel M.E., Castronovo V.; RT "Interaction between the 67 kilodalton metastasis-associated laminin RT receptor and laminin."; RL Kidney Int. 43:30-37(1993). RN [19] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH VENEZUELAN EQUINE RP ENCEPHALITIS VIRUS E2 GLYCOPROTEIN. RX PubMed=8764073; DOI=10.1128/jvi.70.8.5592-5599.1996; RA Ludwig G.V., Kondig J.P., Smith J.F.; RT "A putative receptor for Venezuelan equine encephalitis virus from mosquito RT cells."; RL J. Virol. 70:5592-5599(1996). RN [20] RP INTERACTION WITH PRNP. RX PubMed=9396609; DOI=10.1038/nm1297-1383; RA Rieger R., Edenhofer F., Lasmezas C.I., Weiss S.; RT "The human 37-kDa laminin receptor precursor interacts with the prion RT protein in eukaryotic cells."; RL Nat. Med. 3:1383-1388(1997). RN [21] RP ACYLATION. RX PubMed=9581863; RX DOI=10.1002/(sici)1097-4644(19980601)69:3<244::aid-jcb2>3.0.co;2-r; RA Buto S., Tagliabue E., Ardini E., Magnifico A., Ghirelli C., RA van den Brule F., Castronovo V., Colnaghi M.I., Sobel M.E., Menard S.; RT "Formation of the 67-kDa laminin receptor by acylation of the precursor."; RL J. Cell. Biochem. 69:244-251(1998). RN [22] RP INTERACTION WITH LAMININ-5. RX PubMed=9718729; DOI=10.1093/oxfordjournals.molbev.a026000; RA Ardini E., Pesole G., Tagliabue E., Magnifico A., Castronovo V., RA Sobel M.E., Colnaghi M.I., Menard S.; RT "The 67-kDa laminin receptor originated from a ribosomal protein that RT acquired a dual function during evolution."; RL Mol. Biol. Evol. 15:1017-1025(1998). RN [23] RP INTERACTION WITH RPS21. RX PubMed=10079194; DOI=10.1006/bbrc.1999.0343; RA Sato M., Saeki Y., Tanaka K., Kaneda Y.; RT "Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: RT analysis using a yeast two-hybrid system."; RL Biochem. Biophys. Res. Commun. 256:385-390(1999). RN [24] RP INTERACTION WITH LAMB1. RX PubMed=10772861; DOI=10.1006/jmbi.2000.3680; RA Kazmin D.A., Hoyt T.R., Taubner L., Teintze M., Starkey J.R.; RT "Phage display mapping for peptide 11 sensitive sequences binding to RT laminin-1."; RL J. Mol. Biol. 298:431-445(2000). RN [25] RP PRION-BINDING, SUBCELLULAR LOCATION, AND SUBUNIT. 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 [26] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [27] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH DENGUE VIRUS ENVELOPE RP PROTEIN E. RX PubMed=15507651; DOI=10.1128/jvi.78.22.12647-12656.2004; RA Thepparit C., Smith D.R.; RT "Serotype-specific entry of dengue virus into liver cells: identification RT of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a RT dengue virus serotype 1 receptor."; RL J. Virol. 78:12647-12656(2004). RN [28] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH RP PPP1R16B AND PPP1CA. RX PubMed=16263087; DOI=10.1016/j.bbrc.2005.10.089; RA Kim K., Li L., Kozlowski K., Suh H.S., Cao W., Ballermann B.J.; RT "The protein phosphatase-1 targeting subunit TIMAP regulates LAMR1 RT phosphorylation."; RL Biochem. Biophys. Res. Commun. 338:1327-1334(2005). RN [29] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=15516338; DOI=10.1074/jbc.m410176200; RA Kim K.J., Chung J.W., Kim K.S.; RT "67-kDa laminin receptor promotes internalization of cytotoxic necrotizing RT factor 1-expressing Escherichia coli K1 into human brain microvascular RT endothelial cells."; RL J. Biol. Chem. 280:1360-1368(2005). RN [30] 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 [31] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENO-ASSOCIATED VIRUS RP CAPSID PROTEINS. RX PubMed=16973587; DOI=10.1128/jvi.00878-06; RA Akache B., Grimm D., Pandey K., Yant S.R., Xu H., Kay M.A.; RT "The 37/67-kilodalton laminin receptor is a receptor for adeno-associated RT virus serotypes 8, 2, 3, and 9."; RL J. Virol. 80:9831-9836(2006). RN [32] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [33] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [34] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [35] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [36] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND THR-97, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [37] RP INVOLVEMENT IN ICAS, VARIANTS ICAS ASN-54; PHE-58; GLY-180; TRP-180 AND RP CYS-186, CHARACTERIZATION OF VARIANTS ICAS ASN-54; PHE-58; GLY-180; TRP-180 RP AND CYS-186, AND VARIANTS VAL-185; GLY-257 AND THR-278. RX PubMed=23579497; DOI=10.1126/science.1234864; RA Bolze A., Mahlaoui N., Byun M., Turner B., Trede N., Ellis S.R., RA Abhyankar A., Itan Y., Patin E., Brebner S., Sackstein P., Puel A., RA Picard C., Abel L., Quintana-Murci L., Faust S.N., Williams A.P., RA Baretto R., Duddridge M., Kini U., Pollard A.J., Gaud C., Frange P., RA Orbach D., Emile J.F., Stephan J.L., Sorensen R., Plebani A., RA Hammarstrom L., Conley M.E., Selleri L., Casanova J.L.; RT "Ribosomal protein SA haploinsufficiency in humans with isolated congenital RT asplenia."; RL Science 340:976-978(2013). RN [38] RP NOMENCLATURE. RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002; RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R., RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A., RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V., RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J., RA Williamson J.R., Wilson D., Yonath A., Yusupov M.; RT "A new system for naming ribosomal proteins."; RL Curr. Opin. Struct. Biol. 24:165-169(2014). RN [39] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [40] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [41] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-89, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [42] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 9-205. RX PubMed=18063583; DOI=10.1074/jbc.c700206200; RA Jamieson K.V., Wu J., Hubbard S.R., Meruelo D.; RT "Crystal structure of the human laminin receptor precursor."; RL J. Biol. Chem. 283:3002-3005(2008). 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. Acts as a CC PPP1R16B-dependent substrate of PPP1CA. {ECO:0000255|HAMAP- CC Rule:MF_03016, ECO:0000269|PubMed:16263087, CC ECO:0000269|PubMed:6300843}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the Adeno- CC associated viruses 2,3,8 and 9. {ECO:0000269|PubMed:16973587}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the Dengue CC virus. {ECO:0000269|PubMed:15507651}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the Sindbis CC virus. {ECO:0000269|PubMed:1385835}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the Venezuelan CC equine encephalitis virus. {ECO:0000269|PubMed:1385835}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the pathogenic CC prion protein. {ECO:0000269|PubMed:11689427, CC ECO:0000269|PubMed:9396609}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for bacteria. CC {ECO:0000269|PubMed:15516338}. 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 (By similarity). The mature dimeric form interacts CC with PPP1R16B (via its fourth ankyrin repeat). Interacts with PPP1CA CC only in the presence of PPP1R16B. {ECO:0000255|HAMAP-Rule:MF_03016, CC ECO:0000269|PubMed:10079194, ECO:0000269|PubMed:10772861, CC ECO:0000269|PubMed:11689427, ECO:0000269|PubMed:15507651, CC ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:1834645, CC ECO:0000269|PubMed:6300843, ECO:0000269|PubMed:8433567, CC ECO:0000269|PubMed:9396609, ECO:0000269|PubMed:9718729}. CC -!- SUBUNIT: (Microbial infection) 67LR interacts with capsid protein of CC Adeno-associated virus 2,3,8 and 9. {ECO:0000269|PubMed:16973587}. CC -!- SUBUNIT: (Microbial infection) 67LR interacts with envelope protein of CC dengue virus. {ECO:0000269|PubMed:15507651}. CC -!- SUBUNIT: (Microbial infection) 6s7LR interacts with E2 glycoprotein of CC Sindbis and Venezuelan equine encephalitis virus (PubMed:1385835, CC PubMed:8764073). {ECO:0000269|PubMed:1385835, CC ECO:0000269|PubMed:8764073}. CC -!- INTERACTION: CC P08865; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-354112, EBI-10961312; CC P08865; P02489: CRYAA; NbExp=3; IntAct=EBI-354112, EBI-6875961; CC P08865; Q9UQC2: GAB2; NbExp=3; IntAct=EBI-354112, EBI-975200; CC P08865; P04792: HSPB1; NbExp=4; IntAct=EBI-354112, EBI-352682; CC P08865; Q15046: KARS1; NbExp=9; IntAct=EBI-354112, EBI-356367; CC P08865; Q9Y2W7: KCNIP3; NbExp=3; IntAct=EBI-354112, EBI-751501; CC P08865; O60333-2: KIF1B; NbExp=3; IntAct=EBI-354112, EBI-10975473; CC P08865; O60260-5: PRKN; NbExp=3; IntAct=EBI-354112, EBI-21251460; CC P08865; P63220: RPS21; NbExp=4; IntAct=EBI-354112, EBI-714051; CC P08865; P00441: SOD1; NbExp=3; IntAct=EBI-354112, EBI-990792; CC P08865; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-354112, EBI-717399; CC P08865; O76024: WFS1; NbExp=3; IntAct=EBI-354112, EBI-720609; CC -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. 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 (By similarity). CC Colocalizes with PPP1R16B in the cell membrane. {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 (PubMed:9581863). {ECO:0000255|HAMAP- CC Rule:MF_03016, ECO:0000269|PubMed:9581863}. 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 -!- DISEASE: Asplenia, isolated congenital (ICAS) [MIM:271400]: A rare CC primary immunodeficiency and life-threatening condition, often CC presenting with pneumococcal sepsis. Most affected individuals die of CC severe bacterial infections in early childhood. Isolated asplenia is CC distinct from asplenia associated with other complex visceral defects, CC notably heterotaxy syndromes such as Ivemark syndrome. CC {ECO:0000269|PubMed:23579497}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J03799; AAA36161.1; -; mRNA. DR EMBL; X15005; CAA33112.1; -; mRNA. DR EMBL; S37431; AAB22299.1; -; mRNA. DR EMBL; U43901; AAC50652.1; -; Genomic_DNA. DR EMBL; AF503367; AAM33304.1; -; mRNA. DR EMBL; BT007219; AAP35883.1; -; mRNA. DR EMBL; BC005391; AAH05391.1; -; mRNA. DR EMBL; BC008867; AAH08867.1; -; mRNA. DR EMBL; BC010418; AAH10418.1; -; mRNA. DR EMBL; BC013827; AAH13827.1; -; mRNA. DR EMBL; BC034537; AAH34537.1; -; mRNA. DR EMBL; BC050688; AAH50688.1; -; mRNA. DR EMBL; BC053370; AAH53370.1; -; mRNA. DR EMBL; BC062714; AAH62714.1; -; mRNA. DR EMBL; BC066941; AAH66941.1; -; mRNA. DR EMBL; BC068062; AAH68062.1; -; mRNA. DR EMBL; BC070263; AAH70263.1; -; mRNA. DR EMBL; BC071693; AAH71693.1; -; mRNA. DR EMBL; BC071968; AAH71968.1; -; mRNA. DR EMBL; BC071969; AAH71969.1; -; mRNA. DR EMBL; BC071970; AAH71970.1; -; mRNA. DR EMBL; BC073863; AAH73863.1; -; mRNA. DR EMBL; BC107567; AAI07568.1; -; mRNA. DR EMBL; X61156; CAA43469.1; -; mRNA. DR EMBL; U36484; AAC50313.1; -; Genomic_DNA. DR EMBL; M14199; AAA36165.1; -; mRNA. DR EMBL; AB007146; BAA25812.1; -; Genomic_DNA. DR CCDS; CCDS2686.1; -. DR PIR; A31233; A31233. DR RefSeq; NP_001291217.1; NM_001304288.2. DR RefSeq; NP_002286.2; NM_002295.6. DR PDB; 22TU; EM; 3.00 A; SA=1-295. DR PDB; 3BCH; X-ray; 2.15 A; A=2-220. DR PDB; 4UG0; EM; -; SA=1-295. DR PDB; 4V5Z; EM; 8.70 A; Ab=1-295. DR PDB; 4V6X; EM; 5.00 A; AA=1-295. DR PDB; 5A2Q; EM; 3.90 A; A=1-295. DR PDB; 5AJ0; EM; 3.50 A; BA=1-295. DR PDB; 5FLX; EM; 3.90 A; A=1-295. DR PDB; 5LKS; EM; 3.60 A; SA=1-295. DR PDB; 5OA3; EM; 4.30 A; A=1-295. DR PDB; 5T2C; EM; 3.60 A; Ao=1-295. DR PDB; 5VYC; X-ray; 6.00 A; A1/A2/A3/A4/A5/A6=1-295. DR PDB; 6FEC; EM; 6.30 A; f=2-209. DR PDB; 6G18; EM; 3.60 A; A=1-295. DR PDB; 6G4S; EM; 4.00 A; A=1-295. DR PDB; 6G51; EM; 4.10 A; A=1-295. DR PDB; 6G53; EM; 4.50 A; A=1-295. DR PDB; 6G5H; EM; 3.60 A; A=1-295. DR PDB; 6G5I; EM; 3.50 A; A=1-295. DR PDB; 6IP5; EM; 3.90 A; 2n=1-295. DR PDB; 6IP6; EM; 4.50 A; 2n=1-295. DR PDB; 6IP8; EM; 3.90 A; 2n=1-295. DR PDB; 6OLE; EM; 3.10 A; SA=3-223. DR PDB; 6OLF; EM; 3.90 A; SA=3-223. DR PDB; 6OLG; EM; 3.40 A; BA=5-219. DR PDB; 6OLI; EM; 3.50 A; SA=3-223. DR PDB; 6OLZ; EM; 3.90 A; BA=5-219. DR PDB; 6OM0; EM; 3.10 A; SA=3-223. DR PDB; 6OM7; EM; 3.70 A; SA=3-223. DR PDB; 6QZP; EM; 2.90 A; SA=3-223. DR PDB; 6XA1; EM; 2.80 A; SA=2-217. DR PDB; 6Y0G; EM; 3.20 A; SA=1-295. DR PDB; 6Y2L; EM; 3.00 A; SA=1-295. DR PDB; 6Y57; EM; 3.50 A; SA=1-295. DR PDB; 6YBD; EM; 3.30 A; N=1-295. DR PDB; 6YBW; EM; 3.10 A; N=1-295. DR PDB; 6Z6L; EM; 3.00 A; SA=1-295. DR PDB; 6Z6M; EM; 3.10 A; SA=1-295. DR PDB; 6Z6N; EM; 2.90 A; SA=1-295. DR PDB; 6ZLW; EM; 2.60 A; B=1-295. DR PDB; 6ZM7; EM; 2.70 A; SA=1-295. DR PDB; 6ZME; EM; 3.00 A; SA=1-295. DR PDB; 6ZMI; EM; 2.60 A; SA=1-295. DR PDB; 6ZMO; EM; 3.10 A; SA=1-295. DR PDB; 6ZMT; EM; 3.00 A; B=1-295. DR PDB; 6ZMW; EM; 3.70 A; N=1-295. DR PDB; 6ZN5; EM; 3.20 A; B=2-207. DR PDB; 6ZOJ; EM; 2.80 A; A=1-295. DR PDB; 6ZOK; EM; 2.80 A; A=1-295. DR PDB; 6ZON; EM; 3.00 A; a=1-295. DR PDB; 6ZP4; EM; 2.90 A; a=1-295. DR PDB; 6ZUO; EM; 3.10 A; A=1-295. DR PDB; 6ZV6; EM; 2.90 A; A=1-295. DR PDB; 6ZVH; EM; 2.90 A; A=3-223. DR PDB; 6ZVJ; EM; 3.80 A; a=2-217. DR PDB; 6ZXD; EM; 3.20 A; A=1-295. DR PDB; 6ZXE; EM; 3.00 A; A=1-295. DR PDB; 6ZXF; EM; 3.70 A; A=1-295. DR PDB; 6ZXG; EM; 2.60 A; A=1-295. DR PDB; 6ZXH; EM; 2.70 A; A=1-295. DR PDB; 7A09; EM; 3.50 A; a=1-295. DR PDB; 7K5I; EM; 2.90 A; A=1-295. DR PDB; 7QP6; EM; 4.70 A; N=1-295. DR PDB; 7QP7; EM; 3.70 A; N=1-295. DR PDB; 7QVP; EM; 3.00 A; RA/SA=1-295. DR PDB; 7R4X; EM; 2.15 A; A=1-295. DR PDB; 7TQL; EM; 3.40 A; B/C=2-207. DR PDB; 7WTV; EM; 3.50 A; A=1-295. DR PDB; 7WTW; EM; 3.20 A; A=1-295. DR PDB; 7WTX; EM; 3.10 A; A=1-295. DR PDB; 7WTZ; EM; 3.00 A; A=1-295. DR PDB; 7WU0; EM; 3.30 A; A=1-295. DR PDB; 7XNX; EM; 2.70 A; SA=1-295. DR PDB; 7XNY; EM; 2.50 A; SA=1-295. DR PDB; 8G5Y; EM; 2.29 A; SA=1-295. DR PDB; 8G5Z; EM; 2.64 A; SA=2-223. DR PDB; 8G60; EM; 2.54 A; SA=1-295. DR PDB; 8G61; EM; 2.94 A; SA=1-295. DR PDB; 8G6J; EM; 2.80 A; SA=1-295. DR PDB; 8GLP; EM; 1.67 A; SA=1-295. DR PDB; 8IFD; EM; 2.59 A; 2n=1-295. DR PDB; 8IFE; EM; 2.57 A; 2n=1-295. DR PDB; 8JDJ; EM; 2.50 A; x=1-295. DR PDB; 8JDK; EM; 2.26 A; x=1-295. DR PDB; 8JDL; EM; 2.42 A; x=1-295. DR PDB; 8JDM; EM; 2.67 A; x=1-295. DR PDB; 8K2C; EM; 2.40 A; SA=1-295. DR PDB; 8OZ0; EM; 3.50 A; Q=1-295. DR PDB; 8PJ1; EM; 3.40 A; N=1-295. DR PDB; 8PJ2; EM; 3.40 A; N=1-295. DR PDB; 8PJ3; EM; 3.70 A; N=1-295. DR PDB; 8PJ4; EM; 3.20 A; N=1-295. DR PDB; 8PJ5; EM; 2.90 A; N=1-295. DR PDB; 8PJ6; EM; 2.90 A; N=1-295. DR PDB; 8PPK; EM; 2.98 A; A=1-295. DR PDB; 8PPL; EM; 2.65 A; AA=1-295. DR PDB; 8QOI; EM; 1.90 A; SA=1-295. DR PDB; 8RG0; EM; 3.40 A; N=1-295. DR PDB; 8T4S; EM; 2.60 A; A=1-295. DR PDB; 8UKB; EM; 3.05 A; SA=3-223. DR PDB; 8XP2; EM; 3.20 A; SA=1-295. DR PDB; 8XP3; EM; 3.40 A; SA=1-295. DR PDB; 8XSX; EM; 2.40 A; SA=1-295. DR PDB; 8XSY; EM; 3.00 A; SA=1-295. DR PDB; 8XSZ; EM; 3.20 A; SA=1-295. DR PDB; 8XXL; EM; 2.90 A; SA=1-295. DR PDB; 8XXM; EM; 3.20 A; SA=1-295. DR PDB; 8XXN; EM; 3.60 A; SA=1-295. DR PDB; 8Y0W; EM; 3.40 A; SA=1-295. DR PDB; 8Y0X; EM; 3.30 A; SA=1-295. DR PDB; 8YOO; EM; 2.00 A; SA=1-295. DR PDB; 8YOP; EM; 2.20 A; SA=1-295. DR PDB; 8ZDB; EM; 3.60 A; A=1-295. DR PDB; 8ZDC; EM; 3.80 A; A=1-295. DR PDB; 8ZDD; EM; 3.70 A; A=1-295. DR PDB; 9B0P; EM; 2.82 A; SA=3-223. DR PDB; 9B0Q; EM; 3.20 A; SA/sA=3-223. DR PDB; 9B0S; EM; 3.80 A; SA/sA=3-223. DR PDB; 9BKD; EM; 2.60 A; N=1-295. DR PDB; 9BLN; EM; 3.90 A; N=1-295. DR PDB; 9C3H; EM; 2.00 A; SA=2-295. DR PDB; 9ED0; EM; 2.80 A; A=1-295. DR PDB; 9FQZ; EM; 2.85 A; SA=1-295. DR PDB; 9G8M; EM; 3.30 A; SA=1-295. DR PDB; 9G8O; EM; 3.40 A; SA=1-295. DR PDB; 9I14; EM; 3.34 A; SA=1-295. DR PDB; 9I2D; EM; 2.19 A; SA=1-295. DR PDB; 9I2E; EM; 2.95 A; SA=1-295. DR PDB; 9KKF; EM; 3.30 A; SA=1-295. DR PDB; 9KMT; EM; 2.81 A; A=1-295. DR PDB; 9KMU; EM; 2.87 A; A=1-295. DR PDB; 9KMV; EM; 2.65 A; A=1-295. DR PDB; 9KMW; EM; 2.73 A; A=1-295. DR PDB; 9KMX; EM; 2.89 A; A=1-295. DR PDB; 9KMY; EM; 2.70 A; A=1-295. DR PDB; 9KMZ; EM; 2.78 A; A=1-295. DR PDB; 9KN0; EM; 2.65 A; A=1-295. DR PDB; 9KN5; EM; 3.20 A; SA=1-295. DR PDB; 9KN6; EM; 3.30 A; SA=1-295. DR PDB; 9KRP; EM; 3.20 A; SA=1-295. DR PDB; 9KZU; EM; 3.00 A; SA=1-295. DR PDB; 9KZX; EM; 3.30 A; SA=1-295. DR PDB; 9M0P; EM; 2.78 A; SA=1-295. DR PDB; 9O3W; EM; 1.90 A; SA=2-295. DR PDB; 9O3Y; EM; 2.20 A; SA=2-295. DR PDB; 9P6Z; EM; 2.97 A; SA=3-223. DR PDB; 9P72; EM; 2.80 A; SA=3-223. DR PDB; 9P73; EM; 2.66 A; SA=3-223. DR PDB; 9P76; EM; 2.83 A; SA=3-223. DR PDB; 9P78; EM; 2.90 A; SA=3-223. DR PDB; 9P79; EM; 3.10 A; SA=3-223. DR PDB; 9P7A; EM; 2.81 A; SA=3-223. DR PDB; 9P7C; EM; 2.78 A; SA=3-223. DR PDB; 9P7D; EM; 2.57 A; SA=3-223. DR PDB; 9P7E; EM; 2.59 A; SA=3-223. DR PDB; 9P7F; EM; 3.56 A; SA=3-223. DR PDB; 9P7G; EM; 3.54 A; SA=3-223. DR PDB; 9P7H; EM; 3.68 A; SA=3-223. DR PDB; 9P7I; EM; 3.69 A; SA=3-223. DR PDB; 9P7J; EM; 3.91 A; SA=3-223. DR PDB; 9P7K; EM; 2.80 A; SA=3-223. DR PDB; 9P7L; EM; 2.92 A; SA=3-223. DR PDB; 9P7N; EM; 2.83 A; SA=3-223. DR PDB; 9P7O; EM; 2.65 A; SA=3-223. DR PDB; 9P7W; EM; 2.93 A; SA=3-223. DR PDB; 9P7X; EM; 2.83 A; SA=3-223. DR PDB; 9P7Y; EM; 2.75 A; SA=3-223. DR PDB; 9P8B; EM; 2.48 A; SA=3-223. DR PDB; 9P8C; EM; 3.11 A; SA=3-223. DR PDB; 9P8H; EM; 2.98 A; SA=3-223. DR PDB; 9P8I; EM; 3.89 A; SA=3-223. DR PDB; 9P9H; EM; 2.84 A; SA=3-223. DR PDB; 9P9I; EM; 2.77 A; SA=3-223. DR PDB; 9PA7; EM; 2.67 A; SA=3-223. DR PDB; 9PBE; EM; 2.19 A; SA=3-223. DR PDB; 9PKG; EM; 3.26 A; SA=3-223. DR PDB; 9QLO; EM; 2.47 A; SA=1-295. DR PDB; 9QLP; EM; 2.75 A; SA=1-295. DR PDB; 9QLQ; EM; 2.57 A; SA=1-295. DR PDB; 9RPV; EM; 2.35 A; RA=2-295, SA=1-295. DR PDB; 9S3B; EM; 2.38 A; SA=1-295. DR PDB; 9S3C; EM; 2.42 A; SA=1-295. DR PDB; 9S3D; EM; 2.32 A; SA=1-295. DR PDB; 9SPF; EM; 2.40 A; SA=2-295. DR PDB; 9SPI; EM; 2.40 A; SA=1-295. DR PDB; 9SYR; EM; 3.55 A; St=2-295. DR AlphaFoldDB; P08865; -. DR EMDB; EMD-10668; -. DR EMDB; EMD-10674; -. DR EMDB; EMD-10690; -. DR EMDB; EMD-10769; -. DR EMDB; EMD-10775; -. DR EMDB; EMD-11098; -. DR EMDB; EMD-11099; -. DR EMDB; EMD-11100; -. DR EMDB; EMD-11276; -. DR EMDB; EMD-11288; -. DR EMDB; EMD-11289; -. DR EMDB; EMD-11292; -. DR EMDB; EMD-11299; -. DR EMDB; EMD-11301; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11310; -. DR EMDB; EMD-11320; -. DR EMDB; EMD-11321; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11440; -. DR EMDB; EMD-11441; -. DR EMDB; EMD-11456; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11517; -. DR EMDB; EMD-11518; -. DR EMDB; EMD-11519; -. DR EMDB; EMD-11520; -. DR EMDB; EMD-11521; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-14181; -. DR EMDB; EMD-14317; -. DR EMDB; EMD-17297; -. DR EMDB; EMD-17696; -. DR EMDB; EMD-17697; -. DR EMDB; EMD-17698; -. DR EMDB; EMD-17699; -. DR EMDB; EMD-17700; -. DR EMDB; EMD-17701; -. DR EMDB; EMD-17804; -. DR EMDB; EMD-17805; -. DR EMDB; EMD-18539; -. DR EMDB; EMD-19128; -. DR EMDB; EMD-22681; -. DR EMDB; EMD-26067; -. DR EMDB; EMD-29757; -. DR EMDB; EMD-29758; -. DR EMDB; EMD-29759; -. DR EMDB; EMD-29760; -. DR EMDB; EMD-29771; -. DR EMDB; EMD-32802; -. DR EMDB; EMD-32803; -. DR EMDB; EMD-32804; -. DR EMDB; EMD-32806; -. DR EMDB; EMD-32807; -. DR EMDB; EMD-33329; -. DR EMDB; EMD-33330; -. DR EMDB; EMD-35413; -. DR EMDB; EMD-35414; -. DR EMDB; EMD-36178; -. DR EMDB; EMD-36179; -. DR EMDB; EMD-36180; -. DR EMDB; EMD-36181; -. DR EMDB; EMD-36838; -. DR EMDB; EMD-3770; -. DR EMDB; EMD-38548; -. DR EMDB; EMD-38549; -. DR EMDB; EMD-38629; -. DR EMDB; EMD-38630; -. DR EMDB; EMD-38631; -. DR EMDB; EMD-38752; -. DR EMDB; EMD-38753; -. DR EMDB; EMD-38754; -. DR EMDB; EMD-3883; -. DR EMDB; EMD-39455; -. DR EMDB; EMD-39456; -. DR EMDB; EMD-39956; -. DR EMDB; EMD-39957; -. DR EMDB; EMD-39958; -. DR EMDB; EMD-40205; -. DR EMDB; EMD-4070; -. DR EMDB; EMD-41039; -. DR EMDB; EMD-42297; -. DR EMDB; EMD-42351; -. DR EMDB; EMD-4242; -. DR EMDB; EMD-4337; -. DR EMDB; EMD-4348; -. DR EMDB; EMD-4350; -. DR EMDB; EMD-4351; -. DR EMDB; EMD-4352; -. DR EMDB; EMD-4353; -. DR EMDB; EMD-44014; -. DR EMDB; EMD-44049; -. DR EMDB; EMD-44050; -. DR EMDB; EMD-44052; -. DR EMDB; EMD-44641; -. DR EMDB; EMD-44671; -. DR EMDB; EMD-45170; -. DR EMDB; EMD-47929; -. DR EMDB; EMD-50673; -. DR EMDB; EMD-51132; -. DR EMDB; EMD-51134; -. DR EMDB; EMD-52565; -. DR EMDB; EMD-52581; -. DR EMDB; EMD-52582; -. DR EMDB; EMD-53230; -. DR EMDB; EMD-53231; -. DR EMDB; EMD-53232; -. DR EMDB; EMD-54172; -. DR EMDB; EMD-54528; -. DR EMDB; EMD-54529; -. DR EMDB; EMD-54530; -. DR EMDB; EMD-55083; -. DR EMDB; EMD-55091; -. DR EMDB; EMD-55351; -. DR EMDB; EMD-62386; -. DR EMDB; EMD-62444; -. DR EMDB; EMD-62445; -. DR EMDB; EMD-62446; -. DR EMDB; EMD-62447; -. DR EMDB; EMD-62448; -. DR EMDB; EMD-62449; -. DR EMDB; EMD-62450; -. DR EMDB; EMD-62451; -. DR EMDB; EMD-62453; -. DR EMDB; EMD-62454; -. DR EMDB; EMD-62535; -. DR EMDB; EMD-62671; -. DR EMDB; EMD-62679; -. DR EMDB; EMD-63560; -. DR EMDB; EMD-68666; -. DR EMDB; EMD-70084; -. DR EMDB; EMD-70086; -. DR EMDB; EMD-71329; -. DR EMDB; EMD-71331; -. DR EMDB; EMD-71332; -. DR EMDB; EMD-71333; -. DR EMDB; EMD-71334; -. DR EMDB; EMD-71335; -. DR EMDB; EMD-71336; -. DR EMDB; EMD-71337; -. DR EMDB; EMD-71338; -. DR EMDB; EMD-71339; -. DR EMDB; EMD-71340; -. DR EMDB; EMD-71341; -. DR EMDB; EMD-71342; -. DR EMDB; EMD-71343; -. DR EMDB; EMD-71344; -. DR EMDB; EMD-71345; -. DR EMDB; EMD-71346; -. DR EMDB; EMD-71348; -. DR EMDB; EMD-71349; -. DR EMDB; EMD-71355; -. DR EMDB; EMD-71356; -. DR EMDB; EMD-71357; -. DR EMDB; EMD-71371; -. DR EMDB; EMD-71372; -. DR EMDB; EMD-71377; -. DR EMDB; EMD-71378; -. DR EMDB; EMD-71411; -. DR EMDB; EMD-71412; -. DR EMDB; EMD-71435; -. DR EMDB; EMD-71477; -. DR EMDB; EMD-71696; -. DR EMDB; EMD-9701; -. DR EMDB; EMD-9702; -. DR EMDB; EMD-9703; -. DR SMR; P08865; -. DR BioGRID; 110115; 562. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P08865; -. DR DIP; DIP-32878N; -. DR FunCoup; P08865; 2463. DR IntAct; P08865; 260. DR MINT; P08865; -. DR NDEx; IQUERY-CP-RPSA; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000389351; -. DR BindingDB; P08865; -. DR ChEMBL; CHEMBL6119; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB01421; Paromomycin. DR DrugBank; DB04985; Tigapotide. DR GlyGen; P08865; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P08865; -. DR MetOSite; P08865; -. DR PhosphoSitePlus; P08865; -. DR SwissPalm; P08865; -. DR BioMuta; RPSA; -. DR DMDM; 125969; -. DR jPOST; P08865; -. DR MassIVE; P08865; -. DR PaxDb; 9606-ENSP00000389351; -. DR PeptideAtlas; P08865; -. DR PRIDE; P08865; -. DR ProteomicsDB; 52170; -. DR Pumba; P08865; -. DR TopDownProteomics; P08865; -. DR Antibodypedia; 4030; 444 antibodies from 40 providers. DR DNASU; 3921; -. DR Ensembl; ENST00000301821.11; ENSP00000346067.4; ENSG00000168028.16. DR Ensembl; ENST00000458478.6; ENSP00000410848.2; ENSG00000168028.16. DR Ensembl; ENST00000697729.1; ENSP00000513423.1; ENSG00000168028.16. DR Ensembl; ENST00000697730.1; ENSP00000513424.1; ENSG00000168028.16. DR Ensembl; ENST00000697731.1; ENSP00000513425.1; ENSG00000168028.16. DR Ensembl; ENST00000869093.1; ENSP00000539152.1; ENSG00000168028.16. DR Ensembl; ENST00000869094.1; ENSP00000539153.1; ENSG00000168028.16. DR Ensembl; ENST00000922533.1; ENSP00000592592.1; ENSG00000168028.16. DR Ensembl; ENST00000922542.1; ENSP00000592601.1; ENSG00000168028.16. DR Ensembl; ENST00000922543.1; ENSP00000592602.1; ENSG00000168028.16. DR Ensembl; ENST00000922544.1; ENSP00000592603.1; ENSG00000168028.16. DR GeneID; 3921; -. DR KEGG; hsa:3921; -. DR MANE-Select; ENST00000301821.11; ENSP00000346067.4; NM_002295.6; NP_002286.2. DR UCSC; uc003cjp.4; human. DR AGR; HGNC:6502; -. DR ClinPGx; PA30287; -. DR CTD; 3921; -. DR DisGeNET; 3921; -. DR GeneCards; RPSA; -. DR HGNC; HGNC:6502; RPSA. DR HPA; ENSG00000168028; Low tissue specificity. DR MalaCards; RPSA; -. DR MIM; 150370; gene. DR MIM; 271400; phenotype. DR OpenTargets; ENSG00000168028; -. DR Orphanet; 101351; Familial isolated congenital asplenia. DR VEuPathDB; HostDB:ENSG00000168028; -. DR eggNOG; KOG0830; Eukaryota. DR GeneTree; ENSGT00950000183099; -. DR InParanoid; P08865; -. DR OrthoDB; 9517787at2759; -. DR PAN-GO; P08865; 4 GO annotations based on evolutionary models. DR PhylomeDB; P08865; -. DR PathwayCommons; P08865; -. DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-HSA-156902; Peptide chain elongation. DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane. DR Reactome; R-HSA-192823; Viral mRNA Translation. DR Reactome; R-HSA-2408557; Selenocysteine synthesis. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR Reactome; R-HSA-72649; Translation initiation complex formation. DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits. DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex. DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition. DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit. DR Reactome; R-HSA-72764; Eukaryotic Translation Termination. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency. DR Reactome; R-HSA-9735869; SARS-CoV-1 modulates host translation machinery. DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery. DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR Reactome; R-HSA-9918485; Dengue Virus Attachment and Entry. DR Reactome; R-HSA-9954714; PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA. DR Reactome; R-HSA-9954716; ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA. DR SignaLink; P08865; -. DR SIGNOR; P08865; -. DR Agora; ENSG00000168028; -. DR BioGRID-ORCS; 3921; 783 hits in 1166 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; RPSA; human. DR EvolutionaryTrace; P08865; -. DR GeneWiki; Ribosomal_protein_SA; -. DR GenomeRNAi; 3921; -. DR Pharos; P08865; Tbio. DR PRO; PR:P08865; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P08865; protein. DR Bgee; ENSG00000168028; Expressed in primordial germ cell in gonad and 110 other cell types or tissues. DR ExpressionAtlas; P08865; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProt. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:UniProt. DR GO; GO:0043236; F:laminin binding; IEA:UniProtKB-UniRule. DR GO; GO:0005055; F:laminin receptor activity; IEA:UniProtKB-UniRule. DR GO; GO:0043022; F:ribosome binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase. DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProt. 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; IC:UniProtKB. DR CDD; cd01425; RPS2; 1. DR FunFam; 3.40.50.10490:FF:000012; 40S ribosomal protein SA; 1. DR Gene3D; 3.40.50.10490; Glucose-6-phosphate isomerase like protein, domain 1; 1. DR HAMAP; MF_03015; Ribosomal_S2_euk; 1. DR HAMAP; MF_03016; Ribosomal_S2_laminin_receptor; 1. DR InterPro; IPR001865; Ribosomal_uS2. DR InterPro; IPR032281; Ribosomal_uS2_C. DR InterPro; IPR018130; Ribosomal_uS2_CS. DR InterPro; IPR027498; Ribosomal_uS2_euk. DR InterPro; IPR005707; Ribosomal_uS2_euk_arc. DR InterPro; IPR023591; Ribosomal_uS2_flav_dom_sf. DR InterPro; IPR027504; Ribosomal_uS2_vert. DR NCBIfam; TIGR01012; uS2_euk_arch; 1. DR PANTHER; PTHR11489; 40S RIBOSOMAL PROTEIN SA; 1. DR Pfam; PF16122; 40S_SA_C; 1. DR Pfam; PF00318; Ribosomal_S2; 2. DR PRINTS; PR00395; RIBOSOMALS2. DR SUPFAM; SSF52313; Ribosomal protein S2; 1. DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1. DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1. DR PDBsum; 22TU; -. DR PDBsum; 3BCH; -. DR PDBsum; 4UG0; -. DR PDBsum; 4V5Z; -. DR PDBsum; 4V6X; -. DR PDBsum; 5A2Q; -. DR PDBsum; 5AJ0; -. DR PDBsum; 5FLX; -. DR PDBsum; 5LKS; -. DR PDBsum; 5OA3; -. DR PDBsum; 5T2C; -. DR PDBsum; 5VYC; -. DR PDBsum; 6FEC; -. DR PDBsum; 6G18; -. DR PDBsum; 6G4S; -. DR PDBsum; 6G51; -. DR PDBsum; 6G53; -. DR PDBsum; 6G5H; -. DR PDBsum; 6G5I; -. DR PDBsum; 6IP5; -. DR PDBsum; 6IP6; -. DR PDBsum; 6IP8; -. DR PDBsum; 6OLE; -. DR PDBsum; 6OLF; -. DR PDBsum; 6OLG; -. DR PDBsum; 6OLI; -. DR PDBsum; 6OLZ; -. DR PDBsum; 6OM0; -. DR PDBsum; 6OM7; -. DR PDBsum; 6QZP; -. DR PDBsum; 6XA1; -. DR PDBsum; 6Y0G; -. DR PDBsum; 6Y2L; -. DR PDBsum; 6Y57; -. DR PDBsum; 6YBD; -. DR PDBsum; 6YBW; -. DR PDBsum; 6Z6L; -. DR PDBsum; 6Z6M; -. DR PDBsum; 6Z6N; -. DR PDBsum; 6ZLW; -. DR PDBsum; 6ZM7; -. DR PDBsum; 6ZME; -. DR PDBsum; 6ZMI; -. DR PDBsum; 6ZMO; -. DR PDBsum; 6ZMT; -. DR PDBsum; 6ZMW; -. DR PDBsum; 6ZN5; -. DR PDBsum; 6ZOJ; -. DR PDBsum; 6ZOK; -. DR PDBsum; 6ZON; -. DR PDBsum; 6ZP4; -. DR PDBsum; 6ZUO; -. DR PDBsum; 6ZV6; -. DR PDBsum; 6ZVH; -. DR PDBsum; 6ZVJ; -. DR PDBsum; 6ZXD; -. DR PDBsum; 6ZXE; -. DR PDBsum; 6ZXF; -. DR PDBsum; 6ZXG; -. DR PDBsum; 6ZXH; -. DR PDBsum; 7A09; -. DR PDBsum; 7K5I; -. DR PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 7QVP; -. DR PDBsum; 7R4X; -. DR PDBsum; 7TQL; -. DR PDBsum; 7WTV; -. DR PDBsum; 7WTW; -. DR PDBsum; 7WTX; -. DR PDBsum; 7WTZ; -. DR PDBsum; 7WU0; -. DR PDBsum; 7XNX; -. DR PDBsum; 7XNY; -. DR PDBsum; 8G5Y; -. DR PDBsum; 8G5Z; -. DR PDBsum; 8G60; -. DR PDBsum; 8G61; -. DR PDBsum; 8G6J; -. DR PDBsum; 8GLP; -. DR PDBsum; 8IFD; -. DR PDBsum; 8IFE; -. DR PDBsum; 8JDJ; -. DR PDBsum; 8JDK; -. DR PDBsum; 8JDL; -. DR PDBsum; 8JDM; -. DR PDBsum; 8K2C; -. DR PDBsum; 8OZ0; -. DR PDBsum; 8PJ1; -. DR PDBsum; 8PJ2; -. DR PDBsum; 8PJ3; -. DR PDBsum; 8PJ4; -. DR PDBsum; 8PJ5; -. DR PDBsum; 8PJ6; -. DR PDBsum; 8PPK; -. DR PDBsum; 8PPL; -. DR PDBsum; 8QOI; -. DR PDBsum; 8RG0; -. DR PDBsum; 8T4S; -. DR PDBsum; 8UKB; -. DR PDBsum; 8XP2; -. DR PDBsum; 8XP3; -. DR PDBsum; 8XSX; -. DR PDBsum; 8XSY; -. DR PDBsum; 8XSZ; -. DR PDBsum; 8XXL; -. DR PDBsum; 8XXM; -. DR PDBsum; 8XXN; -. DR PDBsum; 8Y0W; -. DR PDBsum; 8Y0X; -. DR PDBsum; 8YOO; -. DR PDBsum; 8YOP; -. DR PDBsum; 8ZDB; -. DR PDBsum; 8ZDC; -. DR PDBsum; 8ZDD; -. DR PDBsum; 9B0P; -. DR PDBsum; 9B0Q; -. DR PDBsum; 9B0S; -. DR PDBsum; 9BKD; -. DR PDBsum; 9BLN; -. DR PDBsum; 9C3H; -. DR PDBsum; 9ED0; -. DR PDBsum; 9FQZ; -. DR PDBsum; 9G8M; -. DR PDBsum; 9G8O; -. DR PDBsum; 9I14; -. DR PDBsum; 9I2D; -. DR PDBsum; 9I2E; -. DR PDBsum; 9KKF; -. DR PDBsum; 9KMT; -. DR PDBsum; 9KMU; -. DR PDBsum; 9KMV; -. DR PDBsum; 9KMW; -. DR PDBsum; 9KMX; -. DR PDBsum; 9KMY; -. DR PDBsum; 9KMZ; -. DR PDBsum; 9KN0; -. DR PDBsum; 9KN5; -. DR PDBsum; 9KN6; -. DR PDBsum; 9KRP; -. DR PDBsum; 9KZU; -. DR PDBsum; 9KZX; -. DR PDBsum; 9M0P; -. DR PDBsum; 9O3W; -. DR PDBsum; 9O3Y; -. DR PDBsum; 9P6Z; -. DR PDBsum; 9P72; -. DR PDBsum; 9P73; -. DR PDBsum; 9P76; -. DR PDBsum; 9P78; -. DR PDBsum; 9P79; -. DR PDBsum; 9P7A; -. DR PDBsum; 9P7C; -. DR PDBsum; 9P7D; -. DR PDBsum; 9P7E; -. DR PDBsum; 9P7F; -. DR PDBsum; 9P7G; -. DR PDBsum; 9P7H; -. DR PDBsum; 9P7I; -. DR PDBsum; 9P7J; -. DR PDBsum; 9P7K; -. DR PDBsum; 9P7L; -. DR PDBsum; 9P7N; -. DR PDBsum; 9P7O; -. DR PDBsum; 9P7W; -. DR PDBsum; 9P7X; -. DR PDBsum; 9P7Y; -. DR PDBsum; 9P8B; -. DR PDBsum; 9P8C; -. DR PDBsum; 9P8H; -. DR PDBsum; 9P8I; -. DR PDBsum; 9P9H; -. DR PDBsum; 9P9I; -. DR PDBsum; 9PA7; -. DR PDBsum; 9PBE; -. DR PDBsum; 9PKG; -. DR PDBsum; 9QLO; -. DR PDBsum; 9QLP; -. DR PDBsum; 9QLQ; -. DR PDBsum; 9RPV; -. DR PDBsum; 9S3B; -. DR PDBsum; 9S3C; -. DR PDBsum; 9S3D; -. DR PDBsum; 9SPF; -. DR PDBsum; 9SPI; -. DR PDBsum; 9SYR; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell membrane; Cytoplasm; KW Direct protein sequencing; Disease variant; KW Host cell receptor for virus entry; Host-virus interaction; KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; KW Proteomics identification; Receptor; Reference proteome; Repeat; KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016, FT ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712" FT CHAIN 2..295 FT /note="Small ribosomal subunit protein uS2" FT /id="PRO_0000134358" 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:0000269|PubMed:16263087" FT REGION 161..180 FT /note="Laminin-binding" FT REGION 205..229 FT /note="Laminin-binding" FT REGION 242..295 FT /note="Laminin-binding" 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.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712" FT MOD_RES 43 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 52 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" 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:0007744|PubMed:23186163" FT CROSSLNK 89 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 54 FT /note="T -> N (in ICAS; reduced protein levels; FT dbSNP:rs397514762)" FT /evidence="ECO:0000269|PubMed:23579497" FT /id="VAR_075092" FT VARIANT 58 FT /note="L -> F (in ICAS; reduced protein levels; FT dbSNP:rs397514763)" FT /evidence="ECO:0000269|PubMed:23579497" FT /id="VAR_075093" FT VARIANT 117 FT /note="R -> W (in dbSNP:rs17856150)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_025522" FT VARIANT 180 FT /note="R -> G (in ICAS; reduced protein levels; FT dbSNP:rs397514760)" FT /evidence="ECO:0000269|PubMed:23579497" FT /id="VAR_075094" FT VARIANT 180 FT /note="R -> W (in ICAS; reduced protein levels; FT dbSNP:rs397514760)" FT /evidence="ECO:0000269|PubMed:23579497" FT /id="VAR_075095" FT VARIANT 185 FT /note="M -> V (in dbSNP:rs1214087389)" FT /evidence="ECO:0000269|PubMed:23579497" FT /id="VAR_075096" FT VARIANT 186 FT /note="R -> C (in ICAS; reduced protein levels; FT dbSNP:rs397514761)" FT /evidence="ECO:0000269|PubMed:23579497" FT /id="VAR_075097" FT VARIANT 257 FT /note="V -> G (in dbSNP:rs369708612)" FT /evidence="ECO:0000269|PubMed:23579497" FT /id="VAR_075098" FT VARIANT 278 FT /note="A -> T (in dbSNP:rs143085301)" FT /evidence="ECO:0000269|PubMed:23579497" FT /id="VAR_075099" FT CONFLICT 60 FT /note="L -> V (in Ref. 9; CAA43469)" FT /evidence="ECO:0000305" FT CONFLICT 84 FT /note="Q -> QVCGTV (in Ref. 2; CAA33112)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="A -> T (in Ref. 7; AAH50688)" FT /evidence="ECO:0000305" FT CONFLICT 135 FT /note="T -> S (in Ref. 7; AAH70263)" FT /evidence="ECO:0000305" FT CONFLICT 211 FT /note="E -> G (in Ref. 3; AAB22299)" FT /evidence="ECO:0000305" FT CONFLICT 214 FT /note="E -> G (in Ref. 7; AAH66941)" FT /evidence="ECO:0000305" FT CONFLICT 228 FT /note="Q -> L (in Ref. 3; AAB22299)" FT /evidence="ECO:0000305" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:8YOO" FT HELIX 12..21 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 22..24 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:8IFE" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:9C3H" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 38..41 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 43..45 FT /evidence="ECO:0007829|PDB:6ZLW" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 51..66 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:8YOP" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 74..77 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:9C3H" FT HELIX 84..94 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:8QOI" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 105..109 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:8JDK" FT STRAND 120..125 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 127..130 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 131..137 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 138..141 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:8IFD" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:8K2C" FT HELIX 168..186 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 199..202 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 203..206 FT /evidence="ECO:0007829|PDB:9B0P" FT HELIX 207..222 FT /evidence="ECO:0007829|PDB:8GLP" SQ 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 //