ID LEM3_YEAST Reviewed; 414 AA. AC P42838; D6W0M3; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 190. DE RecName: Full=Phospholipid-transporting ATPase accessory subunit LEM3 {ECO:0000305}; DE AltName: Full=Alkylphosphocholine resistance protein LEM3; DE AltName: Full=Brefeldin-A sensitivity protein 3; DE AltName: Full=Ro-sensitive 3; GN Name=LEM3 {ECO:0000303|PubMed:12842877}; GN Synonyms=BRE3, ROS3 {ECO:0000303|PubMed:12133835}; GN OrderedLocusNames=YNL323W; ORFNames=N0333; 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=S288c / FY1676; RX PubMed=7645347; DOI=10.1002/yea.320110606; RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.; RT "Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV RT identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames."; RL Yeast 11:567-572(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(1997). RN [3] 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 [4] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12133835; DOI=10.1074/jbc.m205564200; RA Kato U., Emoto K., Fredriksson C., Nakamura H., Ohta A., Kobayashi T., RA Murakami-Murofushi K., Kobayashi T., Umeda M.; RT "A novel membrane protein, Ros3p, is required for phospholipid RT translocation across the plasma membrane in Saccharomyces cerevisiae."; RL J. Biol. Chem. 277:37855-37862(2002). RN [5] RP FUNCTION. RX PubMed=12842877; DOI=10.1074/jbc.m305263200; RA Hanson P.K., Malone L., Birchmore J.L., Nichols J.W.; RT "Lem3p is essential for the uptake and potency of alkylphosphocholine RT drugs, edelfosine and miltefosine."; RL J. Biol. Chem. 278:36041-36050(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [9] RP INTERACTION WITH DNF1. RX PubMed=19411703; DOI=10.1074/jbc.m109.013722; RA Lenoir G., Williamson P., Puts C.F., Holthuis J.C.; RT "Cdc50p plays a vital role in the ATPase reaction cycle of the putative RT aminophospholipid transporter Drs2p."; RL J. Biol. Chem. 284:17956-17967(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY RP 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 [11] 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 [12] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DNF1, INTERACTION WITH DNF1, RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, DISULFIDE BOND, AND MUTAGENESIS RP OF ALA-65; ALA-83; CYS-110; CYS-159; CYS-216; CYS-231; SER-237; GLY-375 AND RP ALA-404. RX PubMed=22791719; DOI=10.1074/jbc.m112.371088; RA Puts C.F., Panatala R., Hennrich H., Tsareva A., Williamson P., RA Holthuis J.C.; RT "Mapping functional interactions in a heterodimeric phospholipid pump."; RL J. Biol. Chem. 287:30529-30540(2012). RN [13] {ECO:0007744|PDB:7KY5, ECO:0007744|PDB:7KY7, ECO:0007744|PDB:7KY8, ECO:0007744|PDB:7KY9, ECO:0007744|PDB:7KYA, ECO:0007744|PDB:7KYB, ECO:0007744|PDB:7KYC} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH DNF1, RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DNF1 AND DNF2, INTERACTION WITH RP DNF1 AND DNF2, GLYCOSYLATION AT ASN-240; ASN-256; ASN-298 AND ASN-332, RP DISULFIDE BONDS, AND MUTAGENESIS OF ARG-51. RX PubMed=33320091; DOI=10.7554/elife.62163; RA Bai L., You Q., Jain B.K., Duan H.D., Kovach A., Graham T.R., Li H.; RT "Transport mechanism of P4 ATPase phosphatidylcholine flippases."; RL Elife 9:e62163-e62163(2020). RN [14] {ECO:0007744|PDB:7DRX, ECO:0007744|PDB:7DSH, ECO:0007744|PDB:7DSI, ECO:0007744|PDB:7F7F, ECO:0007744|PDB:7WHV, ECO:0007744|PDB:7WHW} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH DNF1, RP IDENTIFICATION IN A COMPLEX WITH DNF1, INTERACTION WITH DNF1, AND DISULFIDE RP BONDS. RX PubMed=35294892; DOI=10.1016/j.celrep.2022.110518; RA Xu J., He Y., Wu X., Li L.; RT "Conformational changes of a phosphatidylcholine flippase in lipid RT membranes."; RL Cell Rep. 38:110518-110518(2022). CC -!- FUNCTION: Accessory component of a P4-ATPase flippase complex which CC catalyzes the hydrolysis of ATP coupled to the transport of CC glucosylceramide, phosphatidylcholine, phosphatidylethanolamine, and CC small amounts of phosphatidylserine from the lumenal to the cytosolic CC leaflet of the cell membrane and ensures the maintenance of asymmetric CC distribution of phospholipids (PubMed:12133835, PubMed:12842877, CC PubMed:22791719). Contributes to substrate binding and specificity of CC the P4-ATPase catalytic subunit (PubMed:33320091). CC {ECO:0000269|PubMed:12133835, ECO:0000269|PubMed:12842877, CC ECO:0000269|PubMed:22791719, ECO:0000269|PubMed:33320091}. CC -!- SUBUNIT: Component of a flippase complex consisting of DNF1 or DNF2 and CC LEM3 (PubMed:22791719, PubMed:33320091, PubMed:35294892). Interacts CC with DNF1; the interaction is direct and required for their mutual CC export from the endoplasmic reticulum (PubMed:22791719, CC PubMed:33320091, PubMed:35294892, PubMed:19411703). Interacts with CC DNF2; the interaction is direct and required for their mutual export CC from the endoplasmic reticulum (PubMed:22791719, PubMed:33320091). CC {ECO:0000269|PubMed:19411703, ECO:0000269|PubMed:22791719, CC ECO:0000269|PubMed:33320091, ECO:0000269|PubMed:35294892}. CC -!- INTERACTION: CC P42838; P32660: DNF1; NbExp=8; IntAct=EBI-28396, EBI-3121; CC P42838; Q12675: DNF2; NbExp=2; IntAct=EBI-28396, EBI-3114; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12133835, CC ECO:0000305|PubMed:22791719}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- DISRUPTION PHENOTYPE: Resistance to miltefosine (cytotoxic CC phosphatidylcholine analog) and sensitive to duramycin CC (phosphatidylethanolamine-binding cytoxin). CC {ECO:0000269|PubMed:22791719}. CC -!- MISCELLANEOUS: Present with 2460 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {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; Z46259; CAA86374.1; -; Genomic_DNA. DR EMBL; Z71599; CAA96254.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10239.1; -; Genomic_DNA. DR PIR; S55865; S55865. DR RefSeq; NP_014076.1; NM_001183161.1. DR PDB; 7DRX; EM; 2.90 A; B=1-414. DR PDB; 7DSH; EM; 3.67 A; B=1-414. DR PDB; 7DSI; EM; 3.21 A; B=1-414. DR PDB; 7F7F; EM; 3.81 A; B=1-414. DR PDB; 7KY5; EM; 3.98 A; B=1-414. DR PDB; 7KY7; EM; 3.08 A; B=1-414. DR PDB; 7KY8; EM; 3.85 A; B=1-414. DR PDB; 7KY9; EM; 4.05 A; B=1-414. DR PDB; 7KYA; EM; 3.50 A; B=1-414. DR PDB; 7KYB; EM; 3.20 A; B=1-414. DR PDB; 7KYC; EM; 2.80 A; B=1-414. DR PDB; 7WHV; EM; 2.80 A; B=1-414. DR PDB; 7WHW; EM; 3.10 A; B=1-414. DR PDBsum; 7DRX; -. DR PDBsum; 7DSH; -. DR PDBsum; 7DSI; -. DR PDBsum; 7F7F; -. DR PDBsum; 7KY5; -. DR PDBsum; 7KY7; -. DR PDBsum; 7KY8; -. DR PDBsum; 7KY9; -. DR PDBsum; 7KYA; -. DR PDBsum; 7KYB; -. DR PDBsum; 7KYC; -. DR PDBsum; 7WHV; -. DR PDBsum; 7WHW; -. DR AlphaFoldDB; P42838; -. DR EMDB; EMD-23068; -. DR EMDB; EMD-23069; -. DR EMDB; EMD-23070; -. DR EMDB; EMD-23071; -. DR EMDB; EMD-23072; -. DR EMDB; EMD-23073; -. DR EMDB; EMD-23074; -. DR EMDB; EMD-23075; -. DR EMDB; EMD-30829; -. DR EMDB; EMD-30834; -. DR EMDB; EMD-31487; -. DR EMDB; EMD-32512; -. DR EMDB; EMD-32513; -. DR SMR; P42838; -. DR BioGRID; 35517; 262. DR ComplexPortal; CPX-1021; DNF1-LEM3 P4-ATPase complex. DR ComplexPortal; CPX-1022; DNF2-LEM3 P4-ATPase complex. DR DIP; DIP-4598N; -. DR IntAct; P42838; 17. DR MINT; P42838; -. DR STRING; 4932.YNL323W; -. DR TCDB; 8.A.27.1.1; the cdc50 p-type atpase lipid flippase subunit (cdc50) family. DR GlyCosmos; P42838; 6 sites, No reported glycans. DR GlyGen; P42838; 6 sites. DR iPTMnet; P42838; -. DR MaxQB; P42838; -. DR PaxDb; 4932-YNL323W; -. DR PeptideAtlas; P42838; -. DR EnsemblFungi; YNL323W_mRNA; YNL323W; YNL323W. DR GeneID; 855393; -. DR KEGG; sce:YNL323W; -. DR AGR; SGD:S000005267; -. DR SGD; S000005267; LEM3. DR VEuPathDB; FungiDB:YNL323W; -. DR eggNOG; KOG2952; Eukaryota. DR GeneTree; ENSGT00390000004660; -. DR HOGENOM; CLU_025025_0_1_1; -. DR InParanoid; P42838; -. DR OMA; REDATNF; -. DR OrthoDB; 196427at2759; -. DR BioCyc; YEAST:G3O-33308-MONOMER; -. DR BioGRID-ORCS; 855393; 1 hit in 10 CRISPR screens. DR PRO; PR:P42838; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P42838; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:SGD. DR GO; GO:0005886; C:plasma membrane; IDA:SGD. DR GO; GO:0140331; P:aminophospholipid translocation; IEA:GOC. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:SGD. DR GO; GO:0045332; P:phospholipid translocation; IDA:UniProtKB. DR GO; GO:0044088; P:regulation of vacuole organization; IGI:SGD. DR InterPro; IPR005045; CDC50/LEM3_fam. DR PANTHER; PTHR10926:SF20; ALKYLPHOSPHOCHOLINE RESISTANCE PROTEIN LEM3; 1. DR PANTHER; PTHR10926; CELL CYCLE CONTROL PROTEIN 50; 1. DR Pfam; PF03381; CDC50; 1. DR PIRSF; PIRSF015840; DUF284_TM_euk; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Membrane; KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..414 FT /note="Phospholipid-transporting ATPase accessory subunit FT LEM3" FT /id="PRO_0000207671" FT TOPO_DOM 1..74 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 75..95 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 96..372 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 373..393 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 394..414 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REGION 1..50 FT /note="Required for localization to the plasma membrane" FT /evidence="ECO:0000269|PubMed:33320091" FT REGION 20..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 400..414 FT /note="Required for localization to the plasma membrane" FT /evidence="ECO:0000269|PubMed:33320091" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT CARBOHYD 113 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 240 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:33320091" FT CARBOHYD 256 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:33320091, FT ECO:0007744|PDB:7KY5" FT CARBOHYD 279 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 298 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:33320091" FT CARBOHYD 332 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:33320091" FT DISULFID 110..159 FT /evidence="ECO:0000269|PubMed:33320091, FT ECO:0000269|PubMed:35294892, ECO:0000305|PubMed:22791719, FT ECO:0007744|PDB:7DRX, ECO:0007744|PDB:7DSH, FT ECO:0007744|PDB:7DSI, ECO:0007744|PDB:7F7F, FT ECO:0007744|PDB:7KY5, ECO:0007744|PDB:7KY7, FT ECO:0007744|PDB:7KY8, ECO:0007744|PDB:7KY9, FT ECO:0007744|PDB:7KYA, ECO:0007744|PDB:7KYB, FT ECO:0007744|PDB:7KYC, ECO:0007744|PDB:7WHV, FT ECO:0007744|PDB:7WHW" FT DISULFID 216..231 FT /evidence="ECO:0007744|PDB:7DRX, ECO:0007744|PDB:7DSH, FT ECO:0007744|PDB:7DSI, ECO:0007744|PDB:7F7F, FT ECO:0007744|PDB:7KY5, ECO:0007744|PDB:7KY7, FT ECO:0007744|PDB:7KY8, ECO:0007744|PDB:7KY9, FT ECO:0007744|PDB:7KYA, ECO:0007744|PDB:7KYB, FT ECO:0007744|PDB:7KYC, ECO:0007744|PDB:7WHV, FT ECO:0007744|PDB:7WHW" FT MUTAGEN 51 FT /note="R->A: Increases glucosylceramide transport activity FT of DNF1 and DNF2, but not their phosphatidylethanolamine or FT phosphatidylcholine transport activity." FT /evidence="ECO:0000269|PubMed:33320091" FT MUTAGEN 65 FT /note="A->V: Mildly reduces interaction with DNF1." FT /evidence="ECO:0000269|PubMed:22791719" FT MUTAGEN 83 FT /note="A->T: Reduces interaction with DNF1." FT /evidence="ECO:0000269|PubMed:22791719" FT MUTAGEN 110 FT /note="C->A: Strongly reduces interaction with DNF1. Mildly FT resistant to miltefosine. Decreases protein level. Normal FT protein level; when associated with C-159." FT /evidence="ECO:0000269|PubMed:22791719" FT MUTAGEN 159 FT /note="C->A: Strongly reduces interaction with DNF1. Mildly FT resistant to miltefosine. Decreases protein level. Normal FT protein level; when associated with C-110." FT /evidence="ECO:0000269|PubMed:22791719" FT MUTAGEN 216 FT /note="C->A: Decreases DNF1 activity. Reduces interaction FT with DNF1. Resistant to miltefosine. Sensitive to FT duramycin." FT /evidence="ECO:0000269|PubMed:22791719" FT MUTAGEN 231 FT /note="C->A: Mildly decreases DNF1 activity. Reduces FT interaction with DNF1. Resistant to miltefosine." FT /evidence="ECO:0000269|PubMed:22791719" FT MUTAGEN 237 FT /note="S->L: Strongly reduces interaction with DNF1." FT /evidence="ECO:0000269|PubMed:22791719" FT MUTAGEN 375 FT /note="G->E: Reduces interaction with DNF1." FT /evidence="ECO:0000269|PubMed:22791719" FT MUTAGEN 404 FT /note="A->V: Strongly reduces interaction with DNF1." FT /evidence="ECO:0000269|PubMed:22791719" FT HELIX 37..43 FT /evidence="ECO:0007829|PDB:7KYC" FT TURN 57..61 FT /evidence="ECO:0007829|PDB:7KYC" FT HELIX 72..98 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 102..106 FT /evidence="ECO:0007829|PDB:7KYC" FT TURN 108..113 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 125..129 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:7WHW" FT STRAND 141..145 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:7DSI" FT STRAND 157..167 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 173..181 FT /evidence="ECO:0007829|PDB:7KYC" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:7KYC" FT HELIX 195..198 FT /evidence="ECO:0007829|PDB:7KYC" FT HELIX 205..209 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:7DRX" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 227..230 FT /evidence="ECO:0007829|PDB:7KYC" FT HELIX 233..236 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 245..251 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 260..265 FT /evidence="ECO:0007829|PDB:7KYC" FT HELIX 267..271 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 280..284 FT /evidence="ECO:0007829|PDB:7KYC" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:7KYC" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:7DRX" FT TURN 299..301 FT /evidence="ECO:0007829|PDB:7KYC" FT TURN 305..307 FT /evidence="ECO:0007829|PDB:7KYC" FT HELIX 309..314 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 319..332 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 337..345 FT /evidence="ECO:0007829|PDB:7KYC" FT HELIX 351..353 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 356..362 FT /evidence="ECO:0007829|PDB:7KYC" FT STRAND 366..369 FT /evidence="ECO:0007829|PDB:7KY7" FT HELIX 373..399 FT /evidence="ECO:0007829|PDB:7KYC" FT HELIX 406..408 FT /evidence="ECO:0007829|PDB:7KY7" FT HELIX 410..413 FT /evidence="ECO:0007829|PDB:7KYC" SQ SEQUENCE 414 AA; 47438 MW; 55BDA1F32251B4E6 CRC64; MVNFDLGQVG EVFRRKDKGA IVSGDNPEEE EDVDASEFEE DEVKPVRTKN RRPKEDAFTQ QRLAAINPVL TPRTVLPLYL LIAVVFVIVG GCILAQNSKV DEVTIYYQDC MTNATSSWSD IPSEHWQFVF HKYKTYNTAP QWRFVDDESD DFTKQRGTCQ IRFTTPSDMK NNVYLNYVLE KFAANHRRYV LSFSEDQIRG EDASYETVHD ATGINCKPLS KNADGKIYYP CGLIANSMFN DTFPLQLTNV GDTSNNYSLT NKGINWESDK KRYKKTKYNY TQIAPPPYWE KMYPDGYNET NIPDIQDWEE FQNWMRPGAF DKITKLIRIN KNDTLPAGEY QLDIGLHWPV LEFNGKKGIY LTHGSHLGGR NPFLGIVYLI GGCICAAMAL ILLTFWLFGG RKIADASSLS WNMK //