ID RL4A_YEAST Reviewed; 362 AA. AC P10664; D6VQ32; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 02-SEP-2026, entry version 216. DE RecName: Full=Large ribosomal subunit protein uL4A {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L4-A {ECO:0000303|PubMed:9559554}; DE AltName: Full=L2; DE AltName: Full=RP2; DE AltName: Full=YL2; GN Name=RPL4A {ECO:0000303|PubMed:9559554}; Synonyms=RPL2, RPL2A; GN OrderedLocusNames=YBR031W; ORFNames=YBR0315; 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]. RX PubMed=2834365; DOI=10.1016/s0021-9258(18)68770-8; RA Presutti C., Lucioli A., Bozzoni I.; RT "Ribosomal protein L2 in Saccharomyces cerevisiae is homologous to RT ribosomal protein L1 in Xenopus laevis. Isolation and characterization of RT the genes."; RL J. Biol. Chem. 263:6188-6192(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8091864; DOI=10.1002/yea.320100010; RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.; RT "The complete sequence of a 33 kb fragment on the right arm of chromosome RT II from Saccharomyces cerevisiae reveals 16 open reading frames, including RT ten new open reading frames, five previously identified genes and a RT homologue of the SCO1 gene."; RL Yeast 10:S75-S80(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [4] 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 [5] RP FUNCTION IN L2 MRNA REGULATION. RX PubMed=2065661; DOI=10.1002/j.1460-2075.1991.tb07757.x; RA Presutti C., Ciafre S.-A., Bozzoni I.; RT "The ribosomal protein L2 in S. cerevisiae controls the level of RT accumulation of its own mRNA."; RL EMBO J. 10:2215-2221(1991). RN [6] RP PROTEIN SEQUENCE OF 2-21, AND ACETYLATION AT SER-2 BY NATA. RX PubMed=1544921; DOI=10.1016/s0021-9258(18)42785-8; RA Takakura H., Tsunasawa S., Miyagi M., Warner J.R.; RT "NH2-terminal acetylation of ribosomal proteins of Saccharomyces RT cerevisiae."; RL J. Biol. Chem. 267:5442-5445(1992). 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 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 [10] RP SUBUNIT, INTERACTION WITH ACL4 AND KAP104, DOMAIN, SUBCELLULAR LOCATION, RP AND MUTAGENESIS OF ARG-95; ARG-98; ILE-289; ILE-290; ILE-295; LYS-314; RP LYS-315; LYS-319; LYS-332 AND PHE-334. RX PubMed=25936803; DOI=10.1016/j.molcel.2015.03.029; RA Stelter P., Huber F.M., Kunze R., Flemming D., Hoelz A., Hurt E.; RT "Coordinated ribosomal L4 protein assembly into the pre-ribosome is RT regulated by its eukaryote-specific extension."; RL Mol. Cell 58:854-862(2015). RN [11] RP METHYLATION AT ARG-95. RX PubMed=26046779; DOI=10.1002/pmic.201500032; RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O., RA Pears C., Schofield C.J., Kessler B.M.; RT "Expanding the yeast protein arginine methylome."; RL Proteomics 15:3232-3243(2015). RN [12] RP 3D-STRUCTURE MODELING OF 5-260, 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 [13] 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 [14] 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 (PubMed:22096102). uL4 participates in the regulation of the CC accumulation of its own mRNA (PubMed:2065661). CC {ECO:0000269|PubMed:2065661, 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). uL4 is associated with the polypeptide CC exit tunnel (PubMed:22096102, PubMed:9559554). uL4 interacts with its CC chaperone ACL4 and the nuclear import receptor KAP104 CC (PubMed:25936803). {ECO:0000269|PubMed:22096102, CC ECO:0000269|PubMed:25936803, ECO:0000305|PubMed:9559554}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:22096102, ECO:0000269|PubMed:25936803}. Nucleus CC {ECO:0000269|PubMed:25936803}. CC -!- DOMAIN: The eukaryote-specific C-terminal extension harbors a nuclear CC import signal and delivers the ACL4-uL4/RPL4 complex to the pre- CC ribosome, triggering uL4 release from ACL4 and incorporation into the CC 60S ribosomal subunit. {ECO:0000269|PubMed:25936803}. CC -!- PTM: N-terminally acetylated by acetyltransferase NatA. CC {ECO:0000269|PubMed:1544921}. CC -!- MISCELLANEOUS: There are 2 genes for uL4 in yeast. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 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; X76078; CAA53687.1; -; Genomic_DNA. DR EMBL; J03195; AAA34974.1; -; Genomic_DNA. DR EMBL; Z35900; CAA84973.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07152.1; -; Genomic_DNA. DR PIR; S45887; S45887. DR RefSeq; NP_009587.1; NM_001178379.1. DR PDB; 3J6X; EM; 6.10 A; L4=1-362. DR PDB; 3J6Y; EM; 6.10 A; L4=1-362. DR PDB; 3J77; EM; 6.20 A; L4=1-362. DR PDB; 3J78; EM; 6.30 A; L4=1-362. DR PDB; 3JCT; EM; 3.08 A; C=1-362. DR PDB; 4U3M; X-ray; 3.00 A; L4/l4=2-362. DR PDB; 4U3N; X-ray; 3.20 A; L4/l4=2-362. DR PDB; 4U3U; X-ray; 2.90 A; L4/l4=2-362. DR PDB; 4U4N; X-ray; 3.10 A; L4/l4=2-362. DR PDB; 4U4O; X-ray; 3.60 A; L4/l4=2-362. DR PDB; 4U4Q; X-ray; 3.00 A; L4/l4=2-362. DR PDB; 4U4R; X-ray; 2.80 A; L4/l4=2-362. DR PDB; 4U4U; X-ray; 3.00 A; L4/l4=2-362. DR PDB; 4U4Y; X-ray; 3.20 A; L4/l4=2-362. DR PDB; 4U4Z; X-ray; 3.10 A; L4/l4=2-362. DR PDB; 4U50; X-ray; 3.20 A; L4/l4=2-362. DR PDB; 4U51; X-ray; 3.20 A; L4/l4=2-362. DR PDB; 4U52; X-ray; 3.00 A; L4/l4=2-362. DR PDB; 4U53; X-ray; 3.30 A; L4/l4=2-362. DR PDB; 4U55; X-ray; 3.20 A; L4/l4=2-362. DR PDB; 4U56; X-ray; 3.45 A; L4/l4=2-362. DR PDB; 4U6F; X-ray; 3.10 A; L4/l4=2-362. DR PDB; 4V5Z; EM; 8.70 A; Bc=2-332. DR PDB; 4V6I; EM; 8.80 A; BD=1-362. DR PDB; 4V7F; EM; 8.70 A; D=1-362. DR PDB; 4V7R; X-ray; 4.00 A; BD/DD=1-362. DR PDB; 4V88; X-ray; 3.00 A; BC/DC=1-362. DR PDB; 4V8T; EM; 8.10 A; C=1-362. DR PDB; 4V8Y; EM; 4.30 A; BC=2-362. DR PDB; 4V8Z; EM; 6.60 A; BC=2-362. DR PDB; 4V91; EM; 3.70 A; C=1-362. DR PDB; 5APN; EM; 3.91 A; C=1-362. DR PDB; 5APO; EM; 3.41 A; C=1-362. DR PDB; 5DAT; X-ray; 3.15 A; L4/l4=2-362. DR PDB; 5DC3; X-ray; 3.25 A; L4/l4=2-362. DR PDB; 5DGE; X-ray; 3.45 A; L4/l4=2-362. DR PDB; 5DGF; X-ray; 3.30 A; L4/l4=2-362. DR PDB; 5DGV; X-ray; 3.10 A; L4/l4=2-362. DR PDB; 5FCI; X-ray; 3.40 A; L4/l4=2-362. DR PDB; 5FCJ; X-ray; 3.10 A; L4/l4=2-362. DR PDB; 5GAK; EM; 3.88 A; G=1-362. DR PDB; 5H4P; EM; 3.07 A; C=2-362. DR PDB; 5I4L; X-ray; 3.10 A; L4/l4=2-362. DR PDB; 5JCS; EM; 9.50 A; C=1-362. DR PDB; 5JUO; EM; 4.00 A; H=1-362. DR PDB; 5JUP; EM; 3.50 A; H=1-362. DR PDB; 5JUS; EM; 4.20 A; H=1-362. DR PDB; 5JUT; EM; 4.00 A; H=1-362. DR PDB; 5JUU; EM; 4.00 A; H=1-362. DR PDB; 5LYB; X-ray; 3.25 A; L4/l4=2-362. DR PDB; 5M1J; EM; 3.30 A; C5=2-362. DR PDB; 5MC6; EM; 3.80 A; BE=1-362. DR PDB; 5MEI; X-ray; 3.50 A; CF/l=2-362. DR PDB; 5NDG; X-ray; 3.70 A; L4/l4=2-362. DR PDB; 5NDV; X-ray; 3.30 A; L4/l4=2-362. DR PDB; 5NDW; X-ray; 3.70 A; L4/l4=2-362. DR PDB; 5OBM; X-ray; 3.40 A; L4/l4=2-362. DR PDB; 5ON6; X-ray; 3.10 A; CF/l=2-362. DR PDB; 5T62; EM; 3.30 A; F=1-362. DR PDB; 5T6R; EM; 4.50 A; F=1-362. DR PDB; 5TBW; X-ray; 3.00 A; CF/l=2-362. DR PDB; 5TGA; X-ray; 3.30 A; L4/l4=2-362. DR PDB; 5TGM; X-ray; 3.50 A; L4/l4=2-362. DR PDB; 5Z3G; EM; 3.65 A; G=1-362. DR PDB; 6C0F; EM; 3.70 A; C=1-362. DR PDB; 6CB1; EM; 4.60 A; C=1-362. DR PDB; 6ELZ; EM; 3.30 A; C=1-362. DR PDB; 6EM1; EM; 3.60 A; C=1-362. DR PDB; 6EM3; EM; 3.20 A; C=1-362. DR PDB; 6EM4; EM; 4.10 A; C=1-362. DR PDB; 6EM5; EM; 4.30 A; C=1-362. DR PDB; 6FT6; EM; 3.90 A; C=1-362. DR PDB; 6GQ1; EM; 4.40 A; C=2-362. DR PDB; 6GQB; EM; 3.90 A; C=2-362. DR PDB; 6GQV; EM; 4.00 A; C=2-362. DR PDB; 6HD7; EM; 3.40 A; G=1-362. DR PDB; 6HHQ; X-ray; 3.10 A; CF/l=1-362. DR PDB; 6I7O; EM; 5.30 A; BE/YE=2-362. DR PDB; 6M62; EM; 3.20 A; C=1-362. DR PDB; 6N8J; EM; 3.50 A; C=1-362. DR PDB; 6N8K; EM; 3.60 A; C=1-362. DR PDB; 6N8L; EM; 3.60 A; C=1-362. DR PDB; 6N8M; EM; 3.50 A; F=1-362. DR PDB; 6N8N; EM; 3.80 A; F=1-362. DR PDB; 6N8O; EM; 3.50 A; F=1-362. DR PDB; 6OIG; EM; 3.80 A; C=2-362. DR PDB; 6Q8Y; EM; 3.10 A; BE=2-362. DR PDB; 6QIK; EM; 3.10 A; D=1-362. DR PDB; 6QT0; EM; 3.40 A; D=1-362. DR PDB; 6QTZ; EM; 3.50 A; D=1-362. DR PDB; 6R84; EM; 3.60 A; G=2-362. DR PDB; 6R86; EM; 3.40 A; G=2-362. DR PDB; 6R87; EM; 3.40 A; G=2-362. DR PDB; 6RI5; EM; 3.30 A; D=1-362. DR PDB; 6RZZ; EM; 3.20 A; D=1-362. DR PDB; 6S05; EM; 3.90 A; D=1-362. DR PDB; 6S47; EM; 3.28 A; AF=2-362. DR PDB; 6SNT; EM; 2.80 A; j=1-362. DR PDB; 6SV4; EM; 3.30 A; BE/YE/ZE=1-362. DR PDB; 6T4Q; EM; 2.60 A; LC=2-362. DR PDB; 6T7I; EM; 3.20 A; LC=1-362. DR PDB; 6T7T; EM; 3.10 A; LC=2-362. DR PDB; 6T83; EM; 4.00 A; Cy/Fa=1-362. DR PDB; 6TB3; EM; 2.80 A; BE=2-362. DR PDB; 6TNU; EM; 3.10 A; BE=2-362. DR PDB; 6WOO; EM; 2.90 A; C=3-361. DR PDB; 6YLG; EM; 3.00 A; C=1-362. DR PDB; 6YLH; EM; 3.10 A; C=1-362. DR PDB; 6YLX; EM; 3.90 A; C=1-362. DR PDB; 6YLY; EM; 3.80 A; C=1-362. DR PDB; 6Z6J; EM; 3.40 A; LC=1-362. DR PDB; 6Z6K; EM; 3.40 A; LC=1-362. DR PDB; 7AZY; EM; 2.88 A; p=1-362. DR PDB; 7B7D; EM; 3.30 A; LF=2-362. DR PDB; 7BT6; EM; 3.12 A; C=1-362. DR PDB; 7BTB; EM; 3.22 A; C=1-362. DR PDB; 7MPI; EM; 3.05 A; AC=2-362. DR PDB; 7MPJ; EM; 2.70 A; AC=2-362. DR PDB; 7N8B; EM; 3.05 A; AC=2-362. DR PDB; 7NAC; EM; 3.04 A; C=1-362. DR PDB; 7NRC; EM; 3.90 A; LF=2-362. DR PDB; 7NRD; EM; 4.36 A; LF=2-362. DR PDB; 7OF1; EM; 3.10 A; C=1-362. DR PDB; 7OH3; EM; 3.40 A; C=1-362. DR PDB; 7OHP; EM; 3.90 A; C=1-362. DR PDB; 7OHQ; EM; 3.10 A; C=1-362. DR PDB; 7OHR; EM; 4.72 A; C=1-362. DR PDB; 7OHS; EM; 4.38 A; C=1-362. DR PDB; 7OHT; EM; 4.70 A; C=1-362. DR PDB; 7OHU; EM; 3.70 A; C=1-362. DR PDB; 7OHV; EM; 3.90 A; C=1-362. DR PDB; 7OHW; EM; 3.50 A; C=1-362. DR PDB; 7OHX; EM; 3.30 A; C=1-362. DR PDB; 7OHY; EM; 3.90 A; C=1-362. DR PDB; 7R7A; EM; 3.04 A; C=1-362. DR PDB; 7U0H; EM; 2.76 A; C=1-362. DR PDB; 7UG6; EM; 2.90 A; C=1-362. DR PDB; 7UOO; EM; 2.34 A; C=1-362. DR PDB; 7UQB; EM; 2.43 A; C=1-362. DR PDB; 7UQZ; EM; 2.44 A; C=1-362. DR PDB; 7V08; EM; 2.36 A; C=1-362. DR PDB; 7Z34; EM; 3.80 A; C=1-362. DR PDB; 7ZPQ; EM; 3.47 A; BC=2-362. DR PDB; 7ZRS; EM; 4.80 A; BC=2-362. DR PDB; 7ZS5; EM; 3.20 A; BE=2-362. DR PDB; 7ZUW; EM; 4.30 A; BC=2-362. DR PDB; 7ZUX; EM; 2.50 A; EC=2-362. DR PDB; 7ZW0; EM; 2.40 A; LG=1-362. DR PDB; 8AAF; EM; 2.50 A; l=1-362. DR PDB; 8AGT; EM; 2.60 A; l=1-362. DR PDB; 8AGU; EM; 2.70 A; l=1-362. DR PDB; 8AGV; EM; 2.60 A; l=1-362. DR PDB; 8AGW; EM; 2.60 A; l=1-362. DR PDB; 8AGX; EM; 2.40 A; l=1-362. DR PDB; 8AGZ; EM; 2.60 A; l=1-362. DR PDB; 8BIP; EM; 3.10 A; LC=2-362. DR PDB; 8BJQ; EM; 3.80 A; LC=2-362. DR PDB; 8BN3; EM; 2.40 A; L4=2-362. DR PDB; 8BQD; EM; 3.90 A; BE=2-362. DR PDB; 8BQX; EM; 3.80 A; BE=2-362. DR PDB; 8CCS; EM; 1.97 A; GG=1-362. DR PDB; 8CDL; EM; 2.72 A; GG=1-362. DR PDB; 8CDR; EM; 2.04 A; GG=1-362. DR PDB; 8CEH; EM; 2.05 A; GG=1-362. DR PDB; 8CF5; EM; 2.71 A; GG=1-362. DR PDB; 8CG8; EM; 2.57 A; GG=1-362. DR PDB; 8CGN; EM; 2.28 A; GG=1-362. DR PDB; 8CIV; EM; 2.47 A; GG=1-362. DR PDB; 8CKU; EM; 3.11 A; GG=1-362. DR PDB; 8CMJ; EM; 3.79 A; GG=1-362. DR PDB; 8E5T; EM; 4.00 A; C=1-362. DR PDB; 8HFR; EM; 2.64 A; DO=1-362. DR PDB; 8K2D; EM; 3.20 A; LC=1-362. DR PDB; 8K82; EM; 3.00 A; LC=1-362. DR PDB; 8P4V; X-ray; 3.16 A; CF/l=1-362. DR PDB; 8P85; X-ray; 2.90 A; CF/l=1-362. DR PDB; 8P8M; EM; 2.66 A; LH=1-362. DR PDB; 8P8N; EM; 2.15 A; LH=1-362. DR PDB; 8P8U; EM; 2.23 A; LH=1-362. DR PDB; 8P9A; X-ray; 2.90 A; CF/l=1-362. DR PDB; 8PFR; EM; 2.15 A; LH=1-362. DR PDB; 8PNN; X-ray; 2.90 A; CF/l=1-362. DR PDB; 8T2X; EM; 2.46 A; AC=1-362. DR PDB; 8T2Y; EM; 2.20 A; AC=1-362. DR PDB; 8T2Z; EM; 2.40 A; AC=1-362. DR PDB; 8T30; EM; 2.88 A; AC=1-362. DR PDB; 8T3A; EM; 2.86 A; AC=1-362. DR PDB; 8T3B; EM; 3.08 A; AC=1-362. DR PDB; 8T3C; EM; 3.86 A; AC=1-362. DR PDB; 8T3D; EM; 2.95 A; AC=1-362. DR PDB; 8T3E; EM; 3.04 A; AC=1-362. DR PDB; 8T3F; EM; 3.09 A; AC=1-362. DR PDB; 8UT0; EM; 3.22 A; LF=2-362. DR PDB; 8UTI; EM; 3.13 A; LF=2-362. DR PDB; 8V83; EM; 2.53 A; C=1-362. DR PDB; 8V84; EM; 2.70 A; C=1-362. DR PDB; 8V87; EM; 2.66 A; C=1-362. DR PDB; 8XU8; EM; 3.40 A; F=2-362. DR PDB; 8Y0U; EM; 3.59 A; LC=1-362. DR PDB; 8YLD; EM; 3.90 A; F=2-362. DR PDB; 8YLR; EM; 3.90 A; F=2-362. DR PDB; 8Z70; EM; 3.20 A; F=2-362. DR PDB; 8Z71; EM; 3.60 A; F=2-362. DR PDB; 8ZGR; EM; 2.70 A; LF=2-362. DR PDB; 8ZGY; EM; 2.80 A; LF=2-362. DR PDB; 8ZH3; EM; 2.70 A; LF=2-362. DR PDB; 8ZHB; EM; 2.60 A; LF=2-362. DR PDB; 8ZHC; EM; 2.30 A; LF=2-362. DR PDB; 9F58; EM; 3.10 A; 3=1-362. DR PDB; 9F9S; EM; 2.90 A; Ly/My=1-362. DR PDB; 9OFV; EM; 3.16 A; l=1-362. DR PDB; 9QJC; EM; 3.20 A; C=1-362. DR PDB; 9R9O; EM; 2.90 A; LC=1-362. DR PDB; 9R9P; EM; 3.00 A; LC=1-362. DR AlphaFoldDB; P10664; -. 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-10841; -. DR EMDB; EMD-10842; -. 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-12866; -. DR EMDB; EMD-12892; -. DR EMDB; EMD-12904; -. DR EMDB; EMD-12905; -. DR EMDB; EMD-12906; -. DR EMDB; EMD-12907; -. DR EMDB; EMD-12908; -. DR EMDB; EMD-12909; -. DR EMDB; EMD-12910; -. DR EMDB; EMD-12911; -. DR EMDB; EMD-12912; -. DR EMDB; EMD-12913; -. DR EMDB; EMD-14471; -. DR EMDB; EMD-14926; -. DR EMDB; EMD-14979; -. DR EMDB; EMD-14990; -. DR EMDB; EMD-15296; -. DR EMDB; EMD-15423; -. DR EMDB; EMD-15425; -. DR EMDB; EMD-15426; -. DR EMDB; EMD-15427; -. DR EMDB; EMD-15428; -. 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-24269; -. DR EMDB; EMD-24296; -. DR EMDB; EMD-26259; -. DR EMDB; EMD-26485; -. DR EMDB; EMD-26651; -. DR EMDB; EMD-26686; -. DR EMDB; EMD-26703; -. DR EMDB; EMD-26941; -. DR EMDB; EMD-27919; -. 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-42540; -. DR EMDB; EMD-43017; -. DR EMDB; EMD-4302; -. DR EMDB; EMD-43021; -. DR EMDB; EMD-43027; -. 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-53201; -. 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-6878; -. DR EMDB; EMD-70444; -. DR EMDB; EMD-7324; -. DR EMDB; EMD-8362; -. DR EMDB; EMD-8368; -. DR SMR; P10664; -. DR BioGRID; 32733; 407. DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit. DR DIP; DIP-8314N; -. DR FunCoup; P10664; 1704. DR IntAct; P10664; 309. DR MINT; P10664; -. DR STRING; 4932.YBR031W; -. DR CarbonylDB; P10664; -. DR iPTMnet; P10664; -. DR PaxDb; 4932-YBR031W; -. DR PeptideAtlas; P10664; -. DR TopDownProteomics; P10664; -. DR EnsemblFungi; YBR031W_mRNA; YBR031W; YBR031W. DR GeneID; 852319; -. DR KEGG; sce:YBR031W; -. DR AGR; SGD:S000000235; -. DR SGD; S000000235; RPL4A. DR VEuPathDB; FungiDB:YBR031W; -. DR eggNOG; KOG1475; Eukaryota. DR HOGENOM; CLU_026535_4_0_1; -. DR InParanoid; P10664; -. DR OMA; ALYGTWR; -. DR OrthoDB; 10259785at2759; -. DR BioCyc; YEAST:G3O-29009-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 PRO; PR:P10664; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P10664; 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:0003735; F:structural constituent of ribosome; IC:SGD. DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD. DR FunFam; 3.40.1370.10:FF:000002; 60S ribosomal protein L4; 1. DR Gene3D; 3.40.1370.10; -; 1. DR InterPro; IPR025755; Ribos_uL4_C_dom. DR InterPro; IPR002136; Ribosomal_uL4. DR InterPro; IPR023574; Ribosomal_uL4_dom_sf. DR InterPro; IPR045240; Ribosomal_uL4_euk_arc. DR InterPro; IPR013000; Ribosomal_uL4_euk_arc_CS. DR PANTHER; PTHR19431; 60S RIBOSOMAL PROTEIN L4; 1. DR Pfam; PF14374; Ribos_L4_asso_C; 1. DR Pfam; PF00573; Ribosomal_L4; 1. DR SUPFAM; SSF52166; Ribosomal protein L4; 1. DR PROSITE; PS00939; RIBOSOMAL_L1E; 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; 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; 5Z3G; -. DR PDBsum; 6C0F; -. DR PDBsum; 6CB1; -. DR PDBsum; 6ELZ; -. DR PDBsum; 6EM1; -. DR PDBsum; 6EM3; -. DR PDBsum; 6EM4; -. DR PDBsum; 6EM5; -. 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; 6YLX; -. DR PDBsum; 6YLY; -. 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; 7NAC; -. DR PDBsum; 7NRC; -. DR PDBsum; 7NRD; -. DR PDBsum; 7OF1; -. DR PDBsum; 7OH3; -. DR PDBsum; 7OHP; -. DR PDBsum; 7OHQ; -. DR PDBsum; 7OHR; -. DR PDBsum; 7OHS; -. DR PDBsum; 7OHT; -. DR PDBsum; 7OHU; -. DR PDBsum; 7OHV; -. DR PDBsum; 7OHW; -. DR PDBsum; 7OHX; -. DR PDBsum; 7OHY; -. DR PDBsum; 7R7A; -. DR PDBsum; 7U0H; -. 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; 8E5T; -. 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; 8V83; -. DR PDBsum; 8V84; -. DR PDBsum; 8V87; -. 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; 9QJC; -. DR PDBsum; 9R9O; -. DR PDBsum; 9R9P; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Methylation; Nucleus; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1544921" FT CHAIN 2..362 FT /note="Large ribosomal subunit protein uL4A" FT /id="PRO_0000129367" FT REGION 277..362 FT /note="C-terminal-extended nuclear localization signal" FT /evidence="ECO:0000269|PubMed:25936803" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:1544921" FT MOD_RES 95 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:26046779" FT MUTAGEN 95 FT /note="R->E: Leads to a slower growth at higher FT temperatures but allows RPL4 assembly into the 60S subunit; FT when associated with E-98." FT /evidence="ECO:0000269|PubMed:25936803" FT MUTAGEN 98 FT /note="R->E: Leads to a slower growth at higher FT temperatures but allows RPL4 assembly into the 60S subunit; FT when associated with E-95." FT /evidence="ECO:0000269|PubMed:25936803" FT MUTAGEN 289 FT /note="I->A: Leads to an inefficient release from ACL4 with FT a delayed assembly into the 60S subunit; when associated FT with A-290 and A-295." FT /evidence="ECO:0000269|PubMed:25936803" FT MUTAGEN 290 FT /note="I->A: Leads to an inefficient release from ACL4 with FT a delayed assembly into the 60S subunit; when associated FT with A-289 and A-295." FT /evidence="ECO:0000269|PubMed:25936803" FT MUTAGEN 295 FT /note="I->A: Leads to an inefficient release from ACL4 with FT a delayed assembly into the 60S subunit; when associated FT with A-289 and A-290." FT /evidence="ECO:0000269|PubMed:25936803" FT MUTAGEN 314 FT /note="K->A: Significantly diminished nuclear localization; FT when associated with A-315 and A-319." FT /evidence="ECO:0000269|PubMed:25936803" FT MUTAGEN 315 FT /note="K->A: Significantly diminished nuclear localization; FT when associated with A-314 and A-319." FT /evidence="ECO:0000269|PubMed:25936803" FT MUTAGEN 319 FT /note="K->A: Significantly diminished nuclear localization; FT when associated with A-314 and A-315." FT /evidence="ECO:0000269|PubMed:25936803" FT MUTAGEN 332 FT /note="K->E: Leads to an inefficient release from ACL4 with FT a delayed assembly into the 60S subunit; when associated FT with A-334." FT /evidence="ECO:0000269|PubMed:25936803" FT MUTAGEN 334 FT /note="F->A: Leads to an inefficient release from ACL4 with FT a delayed assembly into the 60S subunit; when associated FT with e-332." FT /evidence="ECO:0000269|PubMed:25936803" FT CONFLICT 38 FT /note="V -> L (in Ref. 1; AAA34974)" FT /evidence="ECO:0000305" FT CONFLICT 144 FT /note="K -> T (in Ref. 1; AAA34974)" FT /evidence="ECO:0000305" FT CONFLICT 157 FT /note="E -> D (in Ref. 1; AAA34974)" FT /evidence="ECO:0000305" FT CONFLICT 224 FT /note="G -> S (in Ref. 1; AAA34974)" FT /evidence="ECO:0000305" FT CONFLICT 241 FT /note="G -> S (in Ref. 1; AAA34974)" FT /evidence="ECO:0000305" FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:8P8N" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 25..27 FT /evidence="ECO:0007829|PDB:8P8U" FT HELIX 32..42 FT /evidence="ECO:0007829|PDB:8CCS" FT TURN 43..46 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:8T2Z" FT TURN 54..57 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:7UQB" FT STRAND 67..71 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 81..84 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 90..94 FT /evidence="ECO:0007829|PDB:7ZUX" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:4U52" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:5FCI" FT HELIX 115..129 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 132..137 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:6T4Q" FT STRAND 147..152 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 154..158 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 162..172 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 175..180 FT /evidence="ECO:0007829|PDB:8CCS" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 191..194 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 206..211 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 215..219 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:8P8U" FT STRAND 226..229 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 230..232 FT /evidence="ECO:0007829|PDB:8P8N" FT HELIX 235..238 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 252..262 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 270..273 FT /evidence="ECO:0007829|PDB:7OHQ" FT HELIX 276..279 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 280..282 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 286..291 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 293..298 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 307..309 FT /evidence="ECO:0007829|PDB:8P8N" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:8CCS" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:8P8N" FT HELIX 321..326 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 330..337 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 339..341 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 342..346 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:8ZHC" FT HELIX 353..360 FT /evidence="ECO:0007829|PDB:8CCS" SQ SEQUENCE 362 AA; 39092 MW; 37D0942A10AAE89F CRC64; MSRPQVTVHS LTGEATANAL PLPAVFSAPI RPDIVHTVFT SVNKNKRQAY AVSEKAGHQT SAESWGTGRA VARIPRVGGG GTGRSGQGAF GNMCRGGRMF APTKTWRKWN VKVNHNEKRY ATASAIAATA VASLVLARGH RVEKIPEIPL VVSTDLESIQ KTKEAVAALK AVGAHSDLLK VLKSKKLRAG KGKYRNRRWT QRRGPLVVYA EDNGIVKALR NVPGVETANV ASLNLLQLAP GAHLGRFVIW TEAAFTKLDQ VWGSETVASS KVGYTLPSHI ISTSDVTRII NSSEIQSAIR PAGQATQKRT HVLKKNPLKN KQVLLRLNPY AKVFAAEKLG SKKAEKTGTK PAAVFTETLK HD //