ID COX1_YEAST Reviewed; 534 AA. AC P00401; A0A0A7NYF6; Q9ZZX6; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-APR-2003, sequence version 2. DT 27-MAR-2024, entry version 191. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=7.1.1.9 {ECO:0000269|PubMed:30598554}; DE AltName: Full=Cytochrome c oxidase polypeptide I; GN Name=COX1; Synonyms=OXI3; OrderedLocusNames=Q0045; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OG Mitochondrion. 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 24657 / D273-10B; RX PubMed=6254986; DOI=10.1016/s0021-9258(19)70224-5; RA Bonitz S.G., Coruzzi G., Thalenfeld B.E., Tzagoloff A., Macino G.; RT "Assembly of the mitochondrial membrane system. Structure and nucleotide RT sequence of the gene coding for subunit 1 of yeast cytochrome oxidase."; RL J. Biol. Chem. 255:11927-11941(1980). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=9872396; DOI=10.1016/s0014-5793(98)01467-7; RA Foury F., Roganti T., Lecrenier N., Purnelle B.; RT "The complete sequence of the mitochondrial genome of Saccharomyces RT cerevisiae."; RL FEBS Lett. 440:325-331(1998). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 96604 / S288c / FY1679; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. RC STRAIN=ATCC 24657 / D273-10B; RX PubMed=2664712; DOI=10.1093/nar/17.12.4886; RA Seraphin B., Simon M., Jacq C., Faye G.; RT "Sequence of the yeast mitochondrial OX13/OL12 promoter region."; RL Nucleic Acids Res. 17:4886-4886(1989). RN [5] RP COMPOSITION OF THE CYTOCHROME C OXIDASE COMPLEX. RX PubMed=1331058; DOI=10.1016/s0021-9258(18)41697-3; RA Taanman J.-W., Capaldi R.A.; RT "Purification of yeast cytochrome c oxidase with a subunit composition RT resembling the mammalian enzyme."; RL J. Biol. Chem. 267:22481-22485(1992). RN [6] RP COMPOSITION OF THE CYTOCHROME C OXIDASE COMPLEX, AND BLOCKED N-TERMINUS. RX PubMed=7851399; DOI=10.1111/j.1432-1033.1995.tb20388.x; RA Geier B.M., Schagger H., Ortwein C., Link T.A., Hagen W.R., Brandt U., RA Von Jagow G.; RT "Kinetic properties and ligand binding of the eleven-subunit cytochrome-c RT oxidase from Saccharomyces cerevisiae isolated with a novel large-scale RT purification method."; RL Eur. J. Biochem. 227:296-302(1995). RN [7] RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX. RX PubMed=10775262; DOI=10.1093/emboj/19.8.1777; RA Schaegger H., Pfeiffer K.; RT "Supercomplexes in the respiratory chains of yeast and mammalian RT mitochondria."; RL EMBO J. 19:1777-1783(2000). RN [8] RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX. RX PubMed=10764779; DOI=10.1074/jbc.m001901200; RA Cruciat C.M., Brunner S., Baumann F., Neupert W., Stuart R.A.; RT "The cytochrome bc1 and cytochrome c oxidase complexes associate to form a RT single supracomplex in yeast mitochondria."; RL J. Biol. Chem. 275:18093-18098(2000). RN [9] RP STRUCTURE BY ELECTRON MICROSCOPY (3.23 ANGSTROMS) IN COMPLEX WITH COPPER RP AND HEME. RX PubMed=30598556; DOI=10.1038/s41594-018-0169-7; RA Rathore S., Berndtsson J., Marin-Buera L., Conrad J., Carroni M., RA Brzezinski P., Ott M.; RT "Cryo-EM structure of the yeast respiratory supercomplex."; RL Nat. Struct. Mol. Biol. 26:50-57(2019). RN [10] RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS) IN COMPLEX WITH COPPER; RP MAGNESIUM; CALCIUM AND HEME, COVALENT BOND, FUNCTION, AND CATALYTIC RP ACTIVITY. RX PubMed=30598554; DOI=10.1038/s41594-018-0172-z; RA Hartley A.M., Lukoyanova N., Zhang Y., Cabrera-Orefice A., Arnold S., RA Meunier B., Pinotsis N., Marechal A.; RT "Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome RT bc1."; RL Nat. Struct. Mol. Biol. 26:78-83(2019). CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the CC active site in COX1, a binuclear center (BNC) formed by heme A3 and CC copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules CC using 4 electrons from cytochrome c in the IMS and 4 protons from the CC mitochondrial matrix (Probable). COX1 is a catalytic core subunit CC containing heme A and the active site BNC with heme A3 and the copper CC atom CU(B) (PubMed:30598554). {ECO:0000269|PubMed:30598554, CC ECO:0000305|PubMed:30598554}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000269|PubMed:30598554}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000269|PubMed:30598554}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:30598556}; CC Note=Binds 2 heme A groups non-covalently per subunit. CC {ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:30598556}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Note=Binds a copper B center. {ECO:0000269|PubMed:30598554, CC ECO:0000269|PubMed:30598556}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a CC multisubunit enzyme composed of 12 subunits. The complex is composed of CC a catalytic core of 3 subunits COX1, COX2 and COX3, encoded in the CC mitochondrial DNA, and 9 supernumerary subunits COX4, COX5A (or COX5B), CC COX6, COX7, COX8, COX9, COX12, COX13 and COX26, which are encoded in CC the nuclear genome (PubMed:7851399, PubMed:30598556, PubMed:30598554). CC The complex exists as a monomer or a dimer and forms supercomplexes CC (SCs) in the inner mitochondrial membrane with a dimer of ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII), resulting in 2 different assemblies (supercomplexes III(2)IV and CC III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556, CC PubMed:30598554). {ECO:0000269|PubMed:10764779, CC ECO:0000269|PubMed:10775262, ECO:0000269|PubMed:30598554, CC ECO:0000269|PubMed:30598556, ECO:0000269|PubMed:7851399}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:30598554}; Multi-pass membrane protein CC {ECO:0000269|PubMed:30598554}. CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7851399}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase 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; V00694; CAA24070.1; -; Genomic_DNA. DR EMBL; KP263414; AIZ98881.1; -; Genomic_DNA. DR EMBL; X14910; CAA33036.1; -; Genomic_DNA. DR PIR; A00468; ODBY1. DR PIR; S78640; S78640. DR RefSeq; NP_009305.1; NC_001224.1. DR PDB; 6GIQ; EM; 3.23 A; a=1-534. DR PDB; 6HU9; EM; 3.35 A; a/m=1-534. DR PDB; 6T0B; EM; 2.80 A; a/n=1-534. DR PDB; 6T15; EM; 3.29 A; a=1-534. DR PDB; 6YMX; EM; 3.17 A; a=5-534. DR PDB; 6YMY; EM; 3.41 A; a=5-534. DR PDB; 7Z10; EM; 3.87 A; a=1-534. DR PDB; 8DH6; EM; 2.94 A; a=1-534. DR PDB; 8E7S; EM; 3.20 A; K/k=1-534. DR PDB; 8EC0; EM; 3.30 A; K=1-534. DR PDBsum; 6GIQ; -. DR PDBsum; 6HU9; -. DR PDBsum; 6T0B; -. DR PDBsum; 6T15; -. DR PDBsum; 6YMX; -. DR PDBsum; 6YMY; -. DR PDBsum; 7Z10; -. DR PDBsum; 8DH6; -. DR PDBsum; 8E7S; -. DR PDBsum; 8EC0; -. DR AlphaFoldDB; P00401; -. DR EMDB; EMD-0004; -. DR EMDB; EMD-10318; -. DR EMDB; EMD-10334; -. DR EMDB; EMD-10335; -. DR EMDB; EMD-10340; -. DR EMDB; EMD-10375; -. DR EMDB; EMD-10376; -. DR EMDB; EMD-10847; -. DR EMDB; EMD-10848; -. DR EMDB; EMD-14436; -. DR EMDB; EMD-27430; -. DR SMR; P00401; -. DR BioGRID; 34790; 73. DR ComplexPortal; CPX-1721; Mitochondrial respiratory chain complex IV, COX5A variant. DR ComplexPortal; CPX-1722; Mitochondrial respiratory chain complex IV, COX5B variant. DR IntAct; P00401; 6. DR MINT; P00401; -. DR STRING; 4932.Q0045; -. DR TCDB; 3.D.4.8.1; the proton-translocating cytochrome oxidase (cox) superfamily. DR MaxQB; P00401; -. DR PaxDb; 4932-Q0045; -. DR PeptideAtlas; P00401; -. DR EnsemblFungi; Q0045_mRNA; Q0045; Q0045. DR GeneID; 854598; -. DR KEGG; sce:Q0045; -. DR AGR; SGD:S000007260; -. DR SGD; S000007260; COX1. DR VEuPathDB; FungiDB:Q0045; -. DR eggNOG; KOG4769; Eukaryota. DR GeneTree; ENSGT00390000001518; -. DR HOGENOM; CLU_011899_7_3_1; -. DR InParanoid; P00401; -. DR OMA; WAMMSIG; -. DR OrthoDB; 5387269at2759; -. DR BioCyc; MetaCyc:Q0045-MONOMER; -. DR BioCyc; YEAST:Q0045-MONOMER; -. DR UniPathway; UPA00705; -. DR BioGRID-ORCS; 854598; 0 hits in 10 CRISPR screens. DR PRO; PR:P00401; -. DR Proteomes; UP000002311; Mitochondrion. DR RNAct; P00401; Protein. DR GO; GO:0031966; C:mitochondrial membrane; IDA:ComplexPortal. DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009060; P:aerobic respiration; IMP:SGD. DR GO; GO:0045333; P:cellular respiration; IDA:ComplexPortal. DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IDA:SGD. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR033944; Cyt_c_oxase_su1_dom. DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 1: Evidence at protein level; KW 3D-structure; Copper; Electron transport; Heme; Iron; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Reference proteome; Respiratory chain; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..534 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000183432" FT TOPO_DOM 1..14 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 15..39 FT /note="Helical; Name=1" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 40..54 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 55..88 FT /note="Helical; Name=2" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 89..97 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 98..118 FT /note="Helical; Name=3" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 119..142 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 143..171 FT /note="Helical; Name=4" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 172..183 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 184..215 FT /note="Helical; Name=5" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 216..228 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 229..263 FT /note="Helical; Name=6" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 264..269 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 270..295 FT /note="Helical; Name=7" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 296..298 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 299..327 FT /note="Helical; Name=8" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 328..335 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 336..358 FT /note="Helical; Name=9" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 359..370 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 371..400 FT /note="Helical; Name=10" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 401..406 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 407..431 FT /note="Helical; Name=11" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 432..449 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:30598554" FT TRANSMEM 450..474 FT /note="Helical; Name=12" FT /evidence="ECO:0000269|PubMed:30598554" FT TOPO_DOM 475..534 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000269|PubMed:30598554" FT BINDING 39 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT BINDING 42 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT BINDING 44 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT BINDING 62 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_note="low-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT BINDING 241 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT BINDING 245 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 290 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT BINDING 291 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT BINDING 368 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with COX2" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT BINDING 369 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with COX2" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT BINDING 376 FT /ligand="heme a3" FT /ligand_id="ChEBI:CHEBI:83282" FT /ligand_note="high-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:30598554" FT BINDING 378 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_note="low-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT BINDING 441 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:30598554, FT ECO:0000269|PubMed:30598556" FT CROSSLNK 241..245 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000269|PubMed:30598554" FT CONFLICT 57 FT /note="Missing (in Ref. 1; CAA24070)" FT /evidence="ECO:0000305" FT CONFLICT 69 FT /note="F -> CT (in Ref. 1; CAA24070)" FT /evidence="ECO:0000305" FT CONFLICT 224 FT /note="S -> A (in Ref. 1; CAA24070)" FT /evidence="ECO:0000305" FT CONFLICT 328 FT /note="H -> Y (in Ref. 1; CAA24070)" FT /evidence="ECO:0000305" FT CONFLICT 378 FT /note="H -> Y (in Ref. 1; CAA24070)" FT /evidence="ECO:0000305" FT CONFLICT 479..485 FT /note="Missing (in Ref. 1; CAA24070)" FT /evidence="ECO:0000305" FT CONFLICT 492 FT /note="N -> A (in Ref. 1; CAA24070)" FT /evidence="ECO:0000305" FT CONFLICT 496..510 FT /note="Missing (in Ref. 1; CAA24070)" FT /evidence="ECO:0000305" FT HELIX 2..5 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 11..39 FT /evidence="ECO:0007829|PDB:6T0B" FT STRAND 41..44 FT /evidence="ECO:0007829|PDB:6T0B" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:8DH6" FT HELIX 52..67 FT /evidence="ECO:0007829|PDB:6T0B" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 71..75 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 78..87 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 96..118 FT /evidence="ECO:0007829|PDB:6T0B" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:6T0B" FT TURN 126..129 FT /evidence="ECO:0007829|PDB:6YMX" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:6T0B" FT TURN 136..138 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 143..171 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:8DH6" FT HELIX 186..215 FT /evidence="ECO:0007829|PDB:6T0B" FT TURN 223..226 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 231..246 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 249..263 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 270..283 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 288..291 FT /evidence="ECO:0007829|PDB:6T0B" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 301..307 FT /evidence="ECO:0007829|PDB:6T0B" FT TURN 308..312 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 313..327 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 336..359 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 361..364 FT /evidence="ECO:0007829|PDB:6T0B" FT TURN 365..369 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 371..378 FT /evidence="ECO:0007829|PDB:6T0B" FT TURN 379..384 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 385..400 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 407..425 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 427..433 FT /evidence="ECO:0007829|PDB:6T0B" FT STRAND 437..439 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 445..447 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 449..484 FT /evidence="ECO:0007829|PDB:6T0B" FT STRAND 485..488 FT /evidence="ECO:0007829|PDB:6T0B" FT STRAND 493..495 FT /evidence="ECO:0007829|PDB:6GIQ" FT STRAND 497..499 FT /evidence="ECO:0007829|PDB:6T0B" FT HELIX 503..506 FT /evidence="ECO:0007829|PDB:6T0B" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:6GIQ" FT HELIX 514..516 FT /evidence="ECO:0007829|PDB:6T0B" FT STRAND 524..526 FT /evidence="ECO:0007829|PDB:6YMY" SQ SEQUENCE 534 AA; 58798 MW; 5D555084C127E8B1 CRC64; MVQRWLYSTN AKDIAVLYFM LAIFSGMAGT AMSLIIRLEL AAPGSQYLHG NSQLFNVLVV GHAVLMIFFL VMPALIGGFG NYLLPLMIGA TDTAFPRINN IAFWVLPMGL VCLVTSTLVE SGAGTGWTVY PPLSSIQAHS GPSVDLAIFA LHLTSISSLL GAINFIVTTL NMRTNGMTMH KLPLFVWSIF ITAFLLLLSL PVLSAGITML LLDRNFNTSF FEVSGGGDPI LYEHLFWFFG HPEVYILIIP GFGIISHVVS TYSKKPVFGE ISMVYAMASI GLLGFLVWSH HMYIVGLDAD TRAYFTSATM IIAIPTGIKI FSWLATIHGG SIRLATPMLY AIAFLFLFTM GGLTGVALAN ASLDVAFHDT YYVVGHFHYV LSMGAIFSLF AGYYYWSPQI LGLNYNEKLA QIQFWLIFIG ANVIFFPMHF LGINGMPRRI PDYPDAFAGW NYVASIGSFI ATLSLFLFIY ILYDQLVNGL NNKVNNKSVI YNKAPDFVES NTIFNLNTVK SSSIEFLLTS PPAVHSFNTP AVQS //