ID RL5_YEAST Reviewed; 297 AA. AC P26321; D6W3N6; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 4. DT 02-SEP-2026, entry version 222. DE RecName: Full=Large ribosomal subunit protein uL18 {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L5 {ECO:0000303|PubMed:9559554}; DE AltName: Full=L1; DE AltName: Full=L1a; DE AltName: Full=Ribosomal 5S RNA-binding protein; DE AltName: Full=YL3; GN Name=RPL5 {ECO:0000303|PubMed:9559554}; Synonyms=RPL1, RPL1A; GN OrderedLocusNames=YPL131W; ORFNames=LPI14W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=2007570; DOI=10.1016/s0021-9258(18)38092-x; RA Tang B., Nazar R.N.; RT "Structure of the yeast ribosomal 5 S RNA-binding protein YL3."; RL J. Biol. Chem. 266:6120-6123(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1325447; DOI=10.1016/s0021-9258(19)37105-4; RA Tang B., Nazar R.N.; RT "Unbalanced regulation of the ribosomal 5 S RNA-binding protein in RT Saccharomyces cerevisiae expressing mutant 5 S rRNAs."; RL J. Biol. Chem. 267:17738-17742(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8474444; DOI=10.1128/mcb.13.5.2835-2845.1993; RA Deshmukh M.P., Tsay Y.F., Paulovich A.G., Woolford J.L. Jr.; RT "Yeast ribosomal protein L1 is required for the stability of newly RT synthesized 5S rRNA and the assembly of 60S ribosomal subunits."; RL Mol. Cell. Biol. 13:2835-2845(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; DOI=10.1038/387s103; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [5] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [6] RP PROTEIN SEQUENCE OF 2-31 AND 219-253. RX PubMed=393511; DOI=10.1111/j.1432-1033.1979.tb04274.x; RA Nazar R.N., Yaguchi M., Willick G.E., Rollin C.F., Roy C.; RT "The 5-S RNA binding protein from yeast (Saccharomyces cerevisiae) RT ribosomes. Evolution of the eukaryotic 5-S RNA binding protein."; RL Eur. J. Biochem. 102:573-582(1979). RN [7] RP NOMENCLATURE, AND SUBUNIT. RX PubMed=9559554; RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u; RA Planta R.J., Mager W.H.; RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."; RL Yeast 14:471-477(1998). RN [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-176 AND SER-235, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [14] RP INTERACTION WITH RPL11A; RPL11B AND SYO1, AND SUBCELLULAR LOCATION. RX PubMed=23118189; DOI=10.1126/science.1226960; RA Kressler D., Bange G., Ogawa Y., Stjepanovic G., Bradatsch B., Pratte D., RA Amlacher S., Strauss D., Yoneda Y., Katahira J., Sinning I., Hurt E.; RT "Synchronizing nuclear import of ribosomal proteins with ribosome RT assembly."; RL Science 338:666-671(2012). RN [15] 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 [16] RP SUBUNIT. RX PubMed=37291423; DOI=10.1038/s41594-023-01006-7; RA Castillo Duque de Estrada N.M., Thoms M., Flemming D., Hammaren H.M., RA Buschauer R., Ameismeier M., Bassler J., Beck M., Beckmann R., Hurt E.; RT "Structure of nascent 5S RNPs at the crossroad between ribosome assembly RT and MDM2-p53 pathways."; RL Nat. Struct. Mol. Biol. 30:1119-1131(2023). RN [17] RP 3D-STRUCTURE MODELING OF 11-232, AND ELECTRON MICROSCOPY. RX PubMed=11701127; DOI=10.1016/s0092-8674(01)00539-6; RA Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., RA Frank J.; RT "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA- RT ribosome and subunit-subunit interactions."; RL Cell 107:373-386(2001). RN [18] RP 3D-STRUCTURE MODELING OF 11-232, AND ELECTRON MICROSCOPY. RX PubMed=14976550; DOI=10.1038/sj.emboj.7600102; RA Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., RA Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.; RT "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome RT facilitate tRNA translocation."; RL EMBO J. 23:1008-1019(2004). RN [19] RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME. RX PubMed=21109664; DOI=10.1126/science.1194294; RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.; RT "Crystal structure of the eukaryotic ribosome."; RL Science 330:1203-1209(2010). RN [20] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=22096102; DOI=10.1126/science.1212642; RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G., RA Yusupov M.; RT "The structure of the eukaryotic ribosome at 3.0 A resolution."; RL Science 334:1524-1529(2011). CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex CC responsible for the synthesis of proteins in the cell. The small CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) CC molecules. The large subunit (LSU) contains the ribosomal catalytic CC site termed the peptidyl transferase center (PTC), which catalyzes the CC formation of peptide bonds, thereby polymerizing the amino acids CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides CC leave the ribosome through a tunnel in the LSU and interact with CC protein factors that function in enzymatic processing, targeting, and CC the membrane insertion of nascent chains at the exit of the ribosomal CC tunnel. {ECO:0000305|PubMed:22096102}. CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU). Mature yeast CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 CC different proteins (encoded by 57 genes). The large 60S subunit CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different CC proteins (encoded by 81 genes) (PubMed:22096102, PubMed:9559554). CC Component of a hexameric 5S RNP precursor complex, composed of 5S RNA, CC RRS1, RPF2, RPL5, RPL11A/RPL11B and SYO1; this complex acts as a CC precursor for ribosome assembly (PubMed:37291423). RPL5/uL18 forms a CC heterotrimeric complex with SYO1 and RPL11A/RPL11B/uL5. Interaction of CC this complex with KAP104 allows the nuclear import of the heterotrimer CC (PubMed:23118189). {ECO:0000269|PubMed:22096102, CC ECO:0000269|PubMed:23118189, ECO:0000269|PubMed:37291423, CC ECO:0000305|PubMed:9559554}. CC -!- INTERACTION: CC P26321; Q02892: NOG1; NbExp=2; IntAct=EBI-15398, EBI-12105; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus CC {ECO:0000269|PubMed:23118189}. Note=The SYO1-uL5-uL18 complex is CC transported into the nucleus by KAP104. {ECO:0000269|PubMed:23118189}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family. CC {ECO:0000305}. 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; M65056; AAA35234.1; -; Genomic_DNA. DR EMBL; M94864; AAA35236.1; -; Genomic_DNA. DR EMBL; L01796; AAA34979.1; -; Genomic_DNA. DR EMBL; U43703; AAB68228.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11302.1; -; Genomic_DNA. DR PIR; S42144; S42144. DR RefSeq; NP_015194.1; NM_001183945.1. DR PDB; 3J6X; EM; 6.10 A; L5=1-297. DR PDB; 3J6Y; EM; 6.10 A; L5=1-297. DR PDB; 3J77; EM; 6.20 A; L5=1-297. DR PDB; 3J78; EM; 6.30 A; L5=1-297. DR PDB; 3JCT; EM; 3.08 A; D=1-297. DR PDB; 4U3M; X-ray; 3.00 A; L5/l5=2-297. DR PDB; 4U3N; X-ray; 3.20 A; L5/l5=2-297. DR PDB; 4U3U; X-ray; 2.90 A; L5/l5=2-297. DR PDB; 4U4N; X-ray; 3.10 A; L5/l5=2-297. DR PDB; 4U4O; X-ray; 3.60 A; L5/l5=2-297. DR PDB; 4U4Q; X-ray; 3.00 A; L5/l5=2-297. DR PDB; 4U4R; X-ray; 2.80 A; L5/l5=2-297. DR PDB; 4U4U; X-ray; 3.00 A; L5/l5=2-297. DR PDB; 4U4Y; X-ray; 3.20 A; L5/l5=2-297. DR PDB; 4U4Z; X-ray; 3.10 A; L5/l5=2-297. DR PDB; 4U50; X-ray; 3.20 A; L5/l5=2-297. DR PDB; 4U51; X-ray; 3.20 A; L5/l5=2-297. DR PDB; 4U52; X-ray; 3.00 A; L5/l5=2-297. DR PDB; 4U53; X-ray; 3.30 A; L5/l5=2-297. DR PDB; 4U55; X-ray; 3.20 A; L5/l5=2-297. DR PDB; 4U56; X-ray; 3.45 A; L5/l5=2-297. DR PDB; 4U6F; X-ray; 3.10 A; L5/l5=2-297. DR PDB; 4V4B; EM; 11.70 A; BE=11-232. DR PDB; 4V5Z; EM; 8.70 A; Bn=1-297. DR PDB; 4V6I; EM; 8.80 A; BQ=1-297. DR PDB; 4V7F; EM; 8.70 A; P=1-297. DR PDB; 4V7R; X-ray; 4.00 A; BE/DE=1-297. DR PDB; 4V88; X-ray; 3.00 A; BD/DD=1-297. DR PDB; 4V8T; EM; 8.10 A; D=1-297. DR PDB; 4V8Y; EM; 4.30 A; BD=2-297. DR PDB; 4V8Z; EM; 6.60 A; BD=2-297. DR PDB; 4V91; EM; 3.70 A; D=1-297. DR PDB; 5APN; EM; 3.91 A; D=1-297. DR PDB; 5APO; EM; 3.41 A; D=1-297. DR PDB; 5DAT; X-ray; 3.15 A; L5/l5=2-297. DR PDB; 5DC3; X-ray; 3.25 A; L5/l5=2-297. DR PDB; 5DGE; X-ray; 3.45 A; L5/l5=2-297. DR PDB; 5DGF; X-ray; 3.30 A; L5/l5=2-297. DR PDB; 5DGV; X-ray; 3.10 A; L5/l5=2-297. DR PDB; 5FCI; X-ray; 3.40 A; L5/l5=2-297. DR PDB; 5FCJ; X-ray; 3.10 A; L5/l5=2-297. DR PDB; 5GAK; EM; 3.88 A; H=1-297. DR PDB; 5H4P; EM; 3.07 A; D=1-297. DR PDB; 5I4L; X-ray; 3.10 A; L5/l5=2-297. DR PDB; 5JCS; EM; 9.50 A; D=1-297. DR PDB; 5JUO; EM; 4.00 A; I=1-297. DR PDB; 5JUP; EM; 3.50 A; I=1-297. DR PDB; 5JUS; EM; 4.20 A; I=1-297. DR PDB; 5JUT; EM; 4.00 A; I=1-297. DR PDB; 5JUU; EM; 4.00 A; I=1-297. DR PDB; 5LYB; X-ray; 3.25 A; L5/l5=2-297. DR PDB; 5M1J; EM; 3.30 A; D5=2-297. DR PDB; 5MC6; EM; 3.80 A; BI=1-297. DR PDB; 5MEI; X-ray; 3.50 A; CG/m=2-297. DR PDB; 5NDG; X-ray; 3.70 A; L5/l5=2-297. DR PDB; 5NDV; X-ray; 3.30 A; L5/l5=2-297. DR PDB; 5NDW; X-ray; 3.70 A; L5/l5=2-297. DR PDB; 5OBM; X-ray; 3.40 A; L5/l5=2-297. DR PDB; 5ON6; X-ray; 3.10 A; CG/m=2-297. DR PDB; 5T62; EM; 3.30 A; G=1-297. DR PDB; 5T6R; EM; 4.50 A; G=1-297. DR PDB; 5TBW; X-ray; 3.00 A; CG/m=2-297. DR PDB; 5TGA; X-ray; 3.30 A; L5/l5=2-297. DR PDB; 5TGM; X-ray; 3.50 A; L5/l5=2-297. DR PDB; 6FT6; EM; 3.90 A; D=1-297. DR PDB; 6GQ1; EM; 4.40 A; D=2-297. DR PDB; 6GQB; EM; 3.90 A; D=2-297. DR PDB; 6GQV; EM; 4.00 A; D=2-297. DR PDB; 6HD7; EM; 3.40 A; H=1-297. DR PDB; 6HHQ; X-ray; 3.10 A; CG/m=1-297. DR PDB; 6I7O; EM; 5.30 A; BI/YI=4-297. DR PDB; 6M62; EM; 3.20 A; D=1-297. DR PDB; 6N8J; EM; 3.50 A; D=1-297. DR PDB; 6N8K; EM; 3.60 A; D=1-297. DR PDB; 6N8L; EM; 3.60 A; D=1-297. DR PDB; 6N8M; EM; 3.50 A; G=1-297. DR PDB; 6N8N; EM; 3.80 A; G=1-297. DR PDB; 6N8O; EM; 3.50 A; G=1-297. DR PDB; 6OIG; EM; 3.80 A; D=2-297. DR PDB; 6Q8Y; EM; 3.10 A; BI=2-297. DR PDB; 6QIK; EM; 3.10 A; P=1-297. DR PDB; 6QT0; EM; 3.40 A; P=1-297. DR PDB; 6QTZ; EM; 3.50 A; P=1-297. DR PDB; 6R84; EM; 3.60 A; H=2-297. DR PDB; 6R86; EM; 3.40 A; H=2-297. DR PDB; 6R87; EM; 3.40 A; H=2-297. DR PDB; 6RI5; EM; 3.30 A; P=1-297. DR PDB; 6RZZ; EM; 3.20 A; P=1-297. DR PDB; 6S05; EM; 3.90 A; P=1-297. DR PDB; 6S47; EM; 3.28 A; AG=2-297. DR PDB; 6SNT; EM; 2.80 A; k=1-297. DR PDB; 6SV4; EM; 3.30 A; BI/YI/ZI=1-297. DR PDB; 6T4Q; EM; 2.60 A; LD=4-297. DR PDB; 6T7I; EM; 3.20 A; LD=1-297. DR PDB; 6T7T; EM; 3.10 A; LD=4-297. DR PDB; 6T83; EM; 4.00 A; Dy/Ga=1-297. DR PDB; 6TB3; EM; 2.80 A; BI=4-297. DR PDB; 6TNU; EM; 3.10 A; BI=4-297. DR PDB; 6WOO; EM; 2.90 A; D=3-297. DR PDB; 6YLG; EM; 3.00 A; D=1-297. DR PDB; 6YLH; EM; 3.10 A; D=1-297. DR PDB; 6Z6J; EM; 3.40 A; LD=1-297. DR PDB; 6Z6K; EM; 3.40 A; LD=1-297. DR PDB; 7AZY; EM; 2.88 A; t=1-297. DR PDB; 7B7D; EM; 3.30 A; LG=4-297. DR PDB; 7BT6; EM; 3.12 A; D=1-297. DR PDB; 7BTB; EM; 3.22 A; D=1-297. DR PDB; 7MPI; EM; 3.05 A; AD=6-297. DR PDB; 7MPJ; EM; 2.70 A; AD=6-297. DR PDB; 7N8B; EM; 3.05 A; AD=6-297. DR PDB; 7NRC; EM; 3.90 A; LG=4-297. DR PDB; 7NRD; EM; 4.36 A; LG=4-297. DR PDB; 7OH3; EM; 3.40 A; D=1-297. DR PDB; 7OHQ; EM; 3.10 A; D=1-297. DR PDB; 7OHT; EM; 4.70 A; D=1-297. DR PDB; 7UG6; EM; 2.90 A; D=1-297. DR PDB; 7UOO; EM; 2.34 A; D=1-297. DR PDB; 7UQB; EM; 2.43 A; D=1-297. DR PDB; 7UQZ; EM; 2.44 A; D=1-297. DR PDB; 7V08; EM; 2.36 A; D=1-297. DR PDB; 7Z34; EM; 3.80 A; D=1-297. DR PDB; 7ZPQ; EM; 3.47 A; BD=4-297. DR PDB; 7ZRS; EM; 4.80 A; BD=4-297. DR PDB; 7ZS5; EM; 3.20 A; BF=2-297. DR PDB; 7ZUW; EM; 4.30 A; BD=4-297. DR PDB; 7ZUX; EM; 2.50 A; ED=4-297. DR PDB; 7ZW0; EM; 2.40 A; LH=1-297. DR PDB; 8AAF; EM; 2.50 A; m=1-297. DR PDB; 8AGT; EM; 2.60 A; m=1-297. DR PDB; 8AGU; EM; 2.70 A; m=1-297. DR PDB; 8AGV; EM; 2.60 A; m=1-297. DR PDB; 8AGW; EM; 2.60 A; m=1-297. DR PDB; 8AGX; EM; 2.40 A; m=1-297. DR PDB; 8AGZ; EM; 2.60 A; m=1-297. DR PDB; 8BIP; EM; 3.10 A; LD=4-297. DR PDB; 8BJQ; EM; 3.80 A; LD=4-297. DR PDB; 8BN3; EM; 2.40 A; L5=2-296. DR PDB; 8BQD; EM; 3.90 A; BI=4-297. DR PDB; 8BQX; EM; 3.80 A; BI=4-297. DR PDB; 8CCS; EM; 1.97 A; HH=1-297. DR PDB; 8CDL; EM; 2.72 A; HH=1-297. DR PDB; 8CDR; EM; 2.04 A; HH=1-297. DR PDB; 8CEH; EM; 2.05 A; HH=1-297. DR PDB; 8CF5; EM; 2.71 A; HH=1-297. DR PDB; 8CG8; EM; 2.57 A; HH=1-297. DR PDB; 8CGN; EM; 2.28 A; HH=1-297. DR PDB; 8CIV; EM; 2.47 A; HH=1-297. DR PDB; 8CKU; EM; 3.11 A; HH=1-297. DR PDB; 8CMJ; EM; 3.79 A; HH=1-297. DR PDB; 8HFR; EM; 2.64 A; Ez=1-297. DR PDB; 8K2D; EM; 3.20 A; LD=1-297. DR PDB; 8K82; EM; 3.00 A; LD=1-297. DR PDB; 8P4V; X-ray; 3.16 A; CG/m=1-297. DR PDB; 8P85; X-ray; 2.90 A; CG/m=1-297. DR PDB; 8P8M; EM; 2.66 A; LI=1-297. DR PDB; 8P8N; EM; 2.15 A; LI=1-297. DR PDB; 8P8U; EM; 2.23 A; LI=1-297. DR PDB; 8P9A; X-ray; 2.90 A; CG/m=1-297. DR PDB; 8PFR; EM; 2.15 A; LI=1-297. DR PDB; 8PNN; X-ray; 2.90 A; CG/m=1-297. DR PDB; 8T2X; EM; 2.46 A; AD=1-297. DR PDB; 8T2Y; EM; 2.20 A; AD=1-297. DR PDB; 8T2Z; EM; 2.40 A; AD=1-297. DR PDB; 8T30; EM; 2.88 A; AD=1-297. DR PDB; 8T3A; EM; 2.86 A; AD=1-297. DR PDB; 8T3B; EM; 3.08 A; AD=1-297. DR PDB; 8T3C; EM; 3.86 A; AD=1-297. DR PDB; 8T3D; EM; 2.95 A; AD=1-297. DR PDB; 8T3E; EM; 3.04 A; AD=1-297. DR PDB; 8T3F; EM; 3.09 A; AD=1-297. DR PDB; 8UT0; EM; 3.22 A; LG=4-297. DR PDB; 8UTI; EM; 3.13 A; LG=4-297. DR PDB; 8XU8; EM; 3.40 A; G=4-297. DR PDB; 8Y0U; EM; 3.59 A; LD=1-297. DR PDB; 8YLD; EM; 3.90 A; G=4-297. DR PDB; 8YLR; EM; 3.90 A; G=4-297. DR PDB; 8Z70; EM; 3.20 A; G=4-297. DR PDB; 8Z71; EM; 3.60 A; G=4-297. DR PDB; 8ZGR; EM; 2.70 A; LG=4-297. DR PDB; 8ZGY; EM; 2.80 A; LG=4-297. DR PDB; 8ZH3; EM; 2.70 A; LG=4-297. DR PDB; 8ZHB; EM; 2.60 A; LG=4-297. DR PDB; 8ZHC; EM; 2.30 A; LG=4-297. DR PDB; 9F58; EM; 3.10 A; e=1-297. DR PDB; 9F9S; EM; 2.90 A; Lz/Mz=1-297. DR PDB; 9OFV; EM; 3.16 A; m=1-297. DR PDB; 9R9O; EM; 2.90 A; LD=1-297. DR PDB; 9R9P; EM; 3.00 A; LD=1-297. DR AlphaFoldDB; P26321; -. DR EMDB; EMD-0047; -. DR EMDB; EMD-0048; -. DR EMDB; EMD-0049; -. DR EMDB; EMD-0202; -. DR EMDB; EMD-0369; -. DR EMDB; EMD-0370; -. DR EMDB; EMD-0371; -. DR EMDB; EMD-0372; -. DR EMDB; EMD-0373; -. DR EMDB; EMD-0374; -. DR EMDB; EMD-10068; -. DR EMDB; EMD-10071; -. DR EMDB; EMD-10098; -. DR EMDB; EMD-10262; -. DR EMDB; EMD-10315; -. DR EMDB; EMD-10377; -. DR EMDB; EMD-10396; -. DR EMDB; EMD-10397; -. DR EMDB; EMD-10398; -. DR EMDB; EMD-10431; -. DR EMDB; EMD-10537; -. DR EMDB; EMD-10838; -. DR EMDB; EMD-10839; -. DR EMDB; EMD-11096; -. DR EMDB; EMD-11097; -. DR EMDB; EMD-11951; -. DR EMDB; EMD-12081; -. DR EMDB; EMD-12534; -. DR EMDB; EMD-12535; -. DR EMDB; EMD-12892; -. DR EMDB; EMD-12905; -. DR EMDB; EMD-12908; -. DR EMDB; EMD-14471; -. DR EMDB; EMD-14926; -. DR EMDB; EMD-14979; -. DR EMDB; EMD-14990; -. DR EMDB; EMD-15423; -. DR EMDB; EMD-15427; -. DR EMDB; EMD-16086; -. DR EMDB; EMD-16090; -. DR EMDB; EMD-16191; -. DR EMDB; EMD-16563; -. DR EMDB; EMD-16591; -. DR EMDB; EMD-16594; -. DR EMDB; EMD-16609; -. DR EMDB; EMD-16616; -. DR EMDB; EMD-16634; -. DR EMDB; EMD-16648; -. DR EMDB; EMD-16684; -. DR EMDB; EMD-16702; -. DR EMDB; EMD-16729; -. DR EMDB; EMD-17549; -. DR EMDB; EMD-17550; -. DR EMDB; EMD-17552; -. DR EMDB; EMD-17653; -. DR EMDB; EMD-20077; -. DR EMDB; EMD-21859; -. DR EMDB; EMD-23934; -. DR EMDB; EMD-23935; -. DR EMDB; EMD-24235; -. DR EMDB; EMD-26485; -. DR EMDB; EMD-26651; -. DR EMDB; EMD-26686; -. DR EMDB; EMD-26703; -. DR EMDB; EMD-26941; -. DR EMDB; EMD-30108; -. DR EMDB; EMD-30170; -. DR EMDB; EMD-30174; -. DR EMDB; EMD-3461; -. DR EMDB; EMD-34725; -. DR EMDB; EMD-36839; -. DR EMDB; EMD-36945; -. DR EMDB; EMD-38660; -. DR EMDB; EMD-4140; -. DR EMDB; EMD-42525; -. DR EMDB; EMD-4302; -. DR EMDB; EMD-4427; -. DR EMDB; EMD-4474; -. DR EMDB; EMD-4560; -. DR EMDB; EMD-4630; -. DR EMDB; EMD-4636; -. DR EMDB; EMD-4751; -. DR EMDB; EMD-4752; -. DR EMDB; EMD-4753; -. DR EMDB; EMD-4884; -. DR EMDB; EMD-50188; -. DR EMDB; EMD-50259; -. DR EMDB; EMD-53860; -. DR EMDB; EMD-53861; -. DR EMDB; EMD-60088; -. DR EMDB; EMD-60091; -. DR EMDB; EMD-60094; -. DR EMDB; EMD-60097; -. DR EMDB; EMD-60098; -. DR EMDB; EMD-70444; -. DR EMDB; EMD-8362; -. DR EMDB; EMD-8368; -. DR SMR; P26321; -. DR BioGRID; 36050; 380. DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit. DR DIP; DIP-1790N; -. DR FunCoup; P26321; 1606. DR IntAct; P26321; 268. DR MINT; P26321; -. DR STRING; 4932.YPL131W; -. DR CarbonylDB; P26321; -. DR iPTMnet; P26321; -. DR PaxDb; 4932-YPL131W; -. DR PeptideAtlas; P26321; -. DR EnsemblFungi; YPL131W_mRNA; YPL131W; YPL131W. DR GeneID; 855972; -. DR KEGG; sce:YPL131W; -. DR AGR; SGD:S000006052; -. DR SGD; S000006052; RPL5. DR VEuPathDB; FungiDB:YPL131W; -. DR eggNOG; KOG0875; Eukaryota. DR HOGENOM; CLU_056222_1_0_1; -. DR InParanoid; P26321; -. DR OMA; IYEAQVE; -. DR OrthoDB; 1618453at2759; -. DR BioCyc; YEAST:G3O-34030-MONOMER; -. DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane. DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits. DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit. DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR Reactome; R-SCE-9954709; Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide. DR Reactome; R-SCE-9954714; PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA. DR BioGRID-ORCS; 855972; 10 hits in 10 CRISPR screens. DR PRO; PR:P26321; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; P26321; protein. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0008097; F:5S rRNA binding; IDA:SGD. DR GO; GO:0003735; F:structural constituent of ribosome; IC:SGD. DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal. DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD. DR CDD; cd00432; Ribosomal_L18_L5e; 1. DR FunFam; 3.30.420.100:FF:000002; 60S ribosomal protein L5; 1. DR Gene3D; 3.30.420.100; -; 1. DR HAMAP; MF_01337_A; Ribosomal_uL18_A; 1. DR InterPro; IPR005485; Rbsml_uL18_euk_arc. DR InterPro; IPR057268; Ribosomal_L18. DR InterPro; IPR025607; Ribosomal_uL18_C_euk. DR PANTHER; PTHR23410:SF12; LARGE RIBOSOMAL SUBUNIT PROTEIN UL18; 1. DR PANTHER; PTHR23410; RIBOSOMAL PROTEIN L5-RELATED; 1. DR Pfam; PF14204; Ribosomal_L18_c; 1. DR Pfam; PF17144; Ribosomal_L5e; 1. DR PRINTS; PR00058; RIBOSOMALL5. DR SUPFAM; SSF53137; Translational machinery components; 1. DR PDBsum; 3J6X; -. DR PDBsum; 3J6Y; -. DR PDBsum; 3J77; -. DR PDBsum; 3J78; -. DR PDBsum; 3JCT; -. DR PDBsum; 4U3M; -. DR PDBsum; 4U3N; -. DR PDBsum; 4U3U; -. DR PDBsum; 4U4N; -. DR PDBsum; 4U4O; -. DR PDBsum; 4U4Q; -. DR PDBsum; 4U4R; -. DR PDBsum; 4U4U; -. DR PDBsum; 4U4Y; -. DR PDBsum; 4U4Z; -. DR PDBsum; 4U50; -. DR PDBsum; 4U51; -. DR PDBsum; 4U52; -. DR PDBsum; 4U53; -. DR PDBsum; 4U55; -. DR PDBsum; 4U56; -. DR PDBsum; 4U6F; -. DR PDBsum; 4V4B; -. DR PDBsum; 4V5Z; -. DR PDBsum; 4V6I; -. DR PDBsum; 4V7F; -. DR PDBsum; 4V7R; -. DR PDBsum; 4V88; -. DR PDBsum; 4V8T; -. DR PDBsum; 4V8Y; -. DR PDBsum; 4V8Z; -. DR PDBsum; 4V91; -. DR PDBsum; 5APN; -. DR PDBsum; 5APO; -. DR PDBsum; 5DAT; -. DR PDBsum; 5DC3; -. DR PDBsum; 5DGE; -. DR PDBsum; 5DGF; -. DR PDBsum; 5DGV; -. DR PDBsum; 5FCI; -. DR PDBsum; 5FCJ; -. DR PDBsum; 5GAK; -. DR PDBsum; 5H4P; -. DR PDBsum; 5I4L; -. DR PDBsum; 5JCS; -. DR PDBsum; 5JUO; -. DR PDBsum; 5JUP; -. DR PDBsum; 5JUS; -. DR PDBsum; 5JUT; -. DR PDBsum; 5JUU; -. DR PDBsum; 5LYB; -. DR PDBsum; 5M1J; -. DR PDBsum; 5MC6; -. DR PDBsum; 5MEI; -. DR PDBsum; 5NDG; -. DR PDBsum; 5NDV; -. DR PDBsum; 5NDW; -. DR PDBsum; 5OBM; -. DR PDBsum; 5ON6; -. DR PDBsum; 5T62; -. DR PDBsum; 5T6R; -. DR PDBsum; 5TBW; -. DR PDBsum; 5TGA; -. DR PDBsum; 5TGM; -. DR PDBsum; 6FT6; -. DR PDBsum; 6GQ1; -. DR PDBsum; 6GQB; -. DR PDBsum; 6GQV; -. DR PDBsum; 6HD7; -. DR PDBsum; 6HHQ; -. DR PDBsum; 6I7O; -. DR PDBsum; 6M62; -. DR PDBsum; 6N8J; -. DR PDBsum; 6N8K; -. DR PDBsum; 6N8L; -. DR PDBsum; 6N8M; -. DR PDBsum; 6N8N; -. DR PDBsum; 6N8O; -. DR PDBsum; 6OIG; -. DR PDBsum; 6Q8Y; -. DR PDBsum; 6QIK; -. DR PDBsum; 6QT0; -. DR PDBsum; 6QTZ; -. DR PDBsum; 6R84; -. DR PDBsum; 6R86; -. DR PDBsum; 6R87; -. DR PDBsum; 6RI5; -. DR PDBsum; 6RZZ; -. DR PDBsum; 6S05; -. DR PDBsum; 6S47; -. DR PDBsum; 6SNT; -. DR PDBsum; 6SV4; -. DR PDBsum; 6T4Q; -. DR PDBsum; 6T7I; -. DR PDBsum; 6T7T; -. DR PDBsum; 6T83; -. DR PDBsum; 6TB3; -. DR PDBsum; 6TNU; -. DR PDBsum; 6WOO; -. DR PDBsum; 6YLG; -. DR PDBsum; 6YLH; -. DR PDBsum; 6Z6J; -. DR PDBsum; 6Z6K; -. DR PDBsum; 7AZY; -. DR PDBsum; 7B7D; -. DR PDBsum; 7BT6; -. DR PDBsum; 7BTB; -. DR PDBsum; 7MPI; -. DR PDBsum; 7MPJ; -. DR PDBsum; 7N8B; -. DR PDBsum; 7NRC; -. DR PDBsum; 7NRD; -. DR PDBsum; 7OH3; -. DR PDBsum; 7OHQ; -. DR PDBsum; 7OHT; -. DR PDBsum; 7UG6; -. DR PDBsum; 7UOO; -. DR PDBsum; 7UQB; -. DR PDBsum; 7UQZ; -. DR PDBsum; 7V08; -. DR PDBsum; 7Z34; -. DR PDBsum; 7ZPQ; -. DR PDBsum; 7ZRS; -. DR PDBsum; 7ZS5; -. DR PDBsum; 7ZUW; -. DR PDBsum; 7ZUX; -. DR PDBsum; 7ZW0; -. DR PDBsum; 8AAF; -. DR PDBsum; 8AGT; -. DR PDBsum; 8AGU; -. DR PDBsum; 8AGV; -. DR PDBsum; 8AGW; -. DR PDBsum; 8AGX; -. DR PDBsum; 8AGZ; -. DR PDBsum; 8BIP; -. DR PDBsum; 8BJQ; -. DR PDBsum; 8BN3; -. DR PDBsum; 8BQD; -. DR PDBsum; 8BQX; -. DR PDBsum; 8CCS; -. DR PDBsum; 8CDL; -. DR PDBsum; 8CDR; -. DR PDBsum; 8CEH; -. DR PDBsum; 8CF5; -. DR PDBsum; 8CG8; -. DR PDBsum; 8CGN; -. DR PDBsum; 8CIV; -. DR PDBsum; 8CKU; -. DR PDBsum; 8CMJ; -. DR PDBsum; 8HFR; -. DR PDBsum; 8K2D; -. DR PDBsum; 8K82; -. DR PDBsum; 8P4V; -. DR PDBsum; 8P85; -. DR PDBsum; 8P8M; -. DR PDBsum; 8P8N; -. DR PDBsum; 8P8U; -. DR PDBsum; 8P9A; -. DR PDBsum; 8PFR; -. DR PDBsum; 8PNN; -. DR PDBsum; 8T2X; -. DR PDBsum; 8T2Y; -. DR PDBsum; 8T2Z; -. DR PDBsum; 8T30; -. DR PDBsum; 8T3A; -. DR PDBsum; 8T3B; -. DR PDBsum; 8T3C; -. DR PDBsum; 8T3D; -. DR PDBsum; 8T3E; -. DR PDBsum; 8T3F; -. DR PDBsum; 8UT0; -. DR PDBsum; 8UTI; -. DR PDBsum; 8XU8; -. DR PDBsum; 8Y0U; -. DR PDBsum; 8YLD; -. DR PDBsum; 8YLR; -. DR PDBsum; 8Z70; -. DR PDBsum; 8Z71; -. DR PDBsum; 8ZGR; -. DR PDBsum; 8ZGY; -. DR PDBsum; 8ZH3; -. DR PDBsum; 8ZHB; -. DR PDBsum; 8ZHC; -. DR PDBsum; 9F58; -. DR PDBsum; 9F9S; -. DR PDBsum; 9OFV; -. DR PDBsum; 9R9O; -. DR PDBsum; 9R9P; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond; KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:393511" FT CHAIN 2..297 FT /note="Large ribosomal subunit protein uL18" FT /id="PRO_0000131454" FT MOD_RES 167 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 176 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 235 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT CROSSLNK 164 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CONFLICT 18 FT /note="T -> Y (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 112 FT /note="K -> R (in Ref. 1; AAA35234 and 2; AAA35236)" FT /evidence="ECO:0000305" FT STRAND 4..7 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 10..15 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 18..20 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:8CCS" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:7UG6" FT HELIX 30..37 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:8CDR" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 50..56 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 59..66 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:7BT6" FT STRAND 73..79 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 80..86 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:6T4Q" FT HELIX 95..113 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 123..126 FT /evidence="ECO:0007829|PDB:5APO" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:5APO" FT HELIX 131..135 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:8BN3" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:7ZW0" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:6M62" FT HELIX 158..168 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:8PFR" FT STRAND 180..184 FT /evidence="ECO:0007829|PDB:4U4U" FT STRAND 185..189 FT /evidence="ECO:0007829|PDB:8P8N" FT HELIX 192..199 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 202..213 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 216..221 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 224..228 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 236..249 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 262..271 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 274..278 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 279..291 FT /evidence="ECO:0007829|PDB:8CCS" FT TURN 294..296 FT /evidence="ECO:0007829|PDB:8PFR" SQ SEQUENCE 297 AA; 33715 MW; 14E3B2931C3CAE2B CRC64; MAFQKDAKSS AYSSRFQTPF RRRREGKTDY YQRKRLVTQH KAKYNTPKYR LVVRFTNKDI ICQIISSTIT GDVVLAAAYS HELPRYGITH GLTNWAAAYA TGLLIARRTL QKLGLDETYK GVEEVEGEYE LTEAVEDGPR PFKVFLDIGL QRTTTGARVF GALKGASDGG LYVPHSENRF PGWDFETEEI DPELLRSYIF GGHVSQYMEE LADDDEERFS ELFKGYLADD IDADSLEDIY TSAHEAIRAD PAFKPTEKKF TKEQYAAESK KYRQTKLSKE ERAARVAAKI AALAGQQ //