COX1_YEAST
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 03-AUG-2022, entry version 184.
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}.
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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 PDBsum; 6GIQ; -.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR PDBsum; 6YMX; -.
DR PDBsum; 6YMY; -.
DR AlphaFoldDB; P00401; -.
DR SMR; P00401; -.
DR BioGRID; 34790; 61.
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; P00401; -.
DR PRIDE; P00401; -.
DR EnsemblFungi; Q0045_mRNA; Q0045; Q0045.
DR GeneID; 854598; -.
DR KEGG; sce:Q0045; -.
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 BioCyc; MetaCyc:Q0045-MON; -.
DR BioCyc; YEAST:Q0045-MON; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:P00401; -.
DR Proteomes; UP000002311; Mitochondrion.
DR RNAct; P00401; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; -; 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; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 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:6YMX"
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:6HU9"
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
