ID   COX3_BOVIN              Reviewed;         261 AA.
AC   P00415; Q576A5; Q8SE13;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 2.
DT   24-JAN-2024, entry version 165.
DE   RecName: Full=Cytochrome c oxidase subunit 3;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide III;
GN   Name=MT-CO3; Synonyms=COIII, COXIII, MTCO3;
OS   Bos taurus (Bovine).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136}; TISSUE=Heart;
RX   PubMed=7120390; DOI=10.1016/0022-2836(82)90137-1;
RA   Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F.,
RA   Young I.G.;
RT   "Complete sequence of bovine mitochondrial DNA. Conserved features of the
RT   mammalian mitochondrial genome.";
RL   J. Mol. Biol. 156:683-717(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=65, 66, D, and F;
RA   Wettstein P.J.;
RT   "Bos taurus mitochondrial protein coding regions.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RA   Hiendleder S., Wolf E.;
RT   "Complete sequence of a new Bos taurus mitochondrial genome.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SUBUNIT.
RX   PubMed=26698328; DOI=10.1074/jbc.m115.680553;
RA   Shinzawa-Itoh K., Shimomura H., Yanagisawa S., Shimada S., Takahashi R.,
RA   Oosaki M., Ogura T., Tsukihara T.;
RT   "Purification of active respiratory supercomplex from bovine heart
RT   mitochondria enables functional studies.";
RL   J. Biol. Chem. 291:4178-4184(2016).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=8638158; DOI=10.1126/science.272.5265.1136;
RA   Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H.,
RA   Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT   "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8
RT   A.";
RL   Science 272:1136-1144(1996).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC   TISSUE=Heart;
RX   PubMed=10089392; DOI=10.1107/s0907444998006362;
RA   Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T.,
RA   Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT   "Structure analysis of bovine heart cytochrome c oxidase at 2.8 A
RT   resolution.";
RL   Acta Crystallogr. D 55:31-45(1999).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC   TISSUE=Heart;
RX   PubMed=10771420; DOI=10.1107/s0907444900002213;
RA   Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T.,
RA   Shinzawa-Itoh K., Nakashima R., Yoshikawa S.;
RT   "X-ray structure of azide-bound fully oxidized cytochrome c oxidase from
RT   bovine heart at 2.9 A resolution.";
RL   Acta Crystallogr. D 56:529-535(2000).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RX   PubMed=20385840; DOI=10.1073/pnas.0910410107;
RA   Muramoto K., Ohta K., Shinzawa-Itoh K., Kanda K., Taniguchi M.,
RA   Nabekura H., Yamashita E., Tsukihara T., Yoshikawa S.;
RT   "Bovine cytochrome c oxidase structures enable O2 reduction with
RT   minimization of reactive oxygens and provide a proton-pumping gate.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:7740-7745(2010).
RN   [9]
RP   STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS).
RX   PubMed=27830641; DOI=10.7554/elife.21290;
RA   Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT   "Functional asymmetry and electron flow in the bovine respirasome.";
RL   Elife 5:0-0(2016).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RX   PubMed=27605664; DOI=10.1074/jbc.m115.711770;
RA   Yano N., Muramoto K., Shimada A., Takemura S., Baba J., Fujisawa H.,
RA   Mochizuki M., Shinzawa-Itoh K., Yamashita E., Tsukihara T., Yoshikawa S.;
RT   "The Mg2+-containing water cluster of mammalian cytochrome c oxidase
RT   collects four pumping proton equivalents in each catalytic cycle.";
RL   J. Biol. Chem. 291:23882-23894(2016).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX   PubMed=31533957; DOI=10.1073/pnas.1907183116;
RA   Shinzawa-Itoh K., Sugimura T., Misaki T., Tadehara Y., Yamamoto S.,
RA   Hanada M., Yano N., Nakagawa T., Uene S., Yamada T., Aoyama H.,
RA   Yamashita E., Tsukihara T., Yoshikawa S., Muramoto K.;
RT   "Monomeric structure of an active form of bovine cytochrome c oxidase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:19945-19951(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 subunit 2 and heme A of subunit 1
CC       to the active site in subunit 1, a binuclear center (BNC) formed by
CC       heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC       water molecules using 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00420}.
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:0000250|UniProtKB:P00420};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000250|UniProtKB:P00420};
CC   -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC       multisubunit enzyme composed of 14 subunits. The complex is composed of
CC       a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC       the mitochondrial DNA, and 11 supernumerary subunits COX4I1 (or
CC       COX4I2), COX5A, COX5B, COX6A2 (or COX6A1), COX6B1 (or COX6B2), COX6C,
CC       COX7A1 (or COX7A2), COX7B, COX7C, COX8B and NDUFA4, which are encoded
CC       in the nuclear genome (PubMed:8638158). The complex exists as a monomer
CC       or a dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC       ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC       III, CIII), resulting in different assemblies (supercomplex
CC       SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:26698328,
CC       PubMed:27830641). {ECO:0000269|PubMed:26698328,
CC       ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:8638158}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:27605664,
CC       ECO:0000269|PubMed:31533957}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 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; V00654; CAA24003.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF490528; AAM08332.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF490529; AAM08345.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF493541; AAM12795.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF493542; AAM12808.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF492351; AAQ06599.1; -; Genomic_DNA.
DR   PIR; A00483; OTBO3.
DR   PDB; 1OCC; X-ray; 2.80 A; C/P=1-261.
DR   PDB; 1OCO; X-ray; 2.80 A; C/P=1-261.
DR   PDB; 1OCR; X-ray; 2.35 A; C/P=1-261.
DR   PDB; 1OCZ; X-ray; 2.90 A; C/P=1-261.
DR   PDB; 1V54; X-ray; 1.80 A; C/P=1-261.
DR   PDB; 1V55; X-ray; 1.90 A; C/P=1-261.
DR   PDB; 2DYR; X-ray; 1.80 A; C/P=1-261.
DR   PDB; 2DYS; X-ray; 2.20 A; C/P=1-261.
DR   PDB; 2EIJ; X-ray; 1.90 A; C/P=1-261.
DR   PDB; 2EIK; X-ray; 2.10 A; C/P=1-261.
DR   PDB; 2EIL; X-ray; 2.10 A; C/P=1-261.
DR   PDB; 2EIM; X-ray; 2.60 A; C/P=1-261.
DR   PDB; 2EIN; X-ray; 2.70 A; C/P=1-261.
DR   PDB; 2OCC; X-ray; 2.30 A; C/P=1-261.
DR   PDB; 2Y69; X-ray; 1.95 A; C/P=1-261.
DR   PDB; 2YBB; EM; 19.00 A; N=1-261.
DR   PDB; 2ZXW; X-ray; 2.50 A; C/P=1-261.
DR   PDB; 3ABK; X-ray; 2.00 A; C/P=1-261.
DR   PDB; 3ABL; X-ray; 2.10 A; C/P=1-261.
DR   PDB; 3ABM; X-ray; 1.95 A; C/P=1-261.
DR   PDB; 3AG1; X-ray; 2.20 A; C/P=1-261.
DR   PDB; 3AG2; X-ray; 1.80 A; C/P=1-261.
DR   PDB; 3AG3; X-ray; 1.80 A; C/P=1-261.
DR   PDB; 3AG4; X-ray; 2.05 A; C/P=1-261.
DR   PDB; 3ASN; X-ray; 3.00 A; C/P=1-261.
DR   PDB; 3ASO; X-ray; 2.30 A; C/P=1-261.
DR   PDB; 3WG7; X-ray; 1.90 A; C/P=1-261.
DR   PDB; 3X2Q; X-ray; 2.00 A; C/P=1-261.
DR   PDB; 5B1A; X-ray; 1.50 A; C/P=1-261.
DR   PDB; 5B1B; X-ray; 1.60 A; C/P=1-261.
DR   PDB; 5B3S; X-ray; 1.68 A; C/P=1-261.
DR   PDB; 5IY5; X-ray; 2.00 A; C/P=3-261.
DR   PDB; 5LUF; EM; 9.10 A; z=1-261.
DR   PDB; 5W97; X-ray; 2.30 A; C/c=1-261.
DR   PDB; 5WAU; X-ray; 1.95 A; C/c=1-261.
DR   PDB; 5X19; X-ray; 2.20 A; C/P=1-261.
DR   PDB; 5X1B; X-ray; 2.40 A; C/P=1-261.
DR   PDB; 5X1F; X-ray; 2.20 A; C/P=1-261.
DR   PDB; 5XDQ; X-ray; 1.77 A; C/P=1-261.
DR   PDB; 5XDX; X-ray; 1.99 A; C/P=2-261.
DR   PDB; 5XTH; EM; 3.90 A; z=1-261.
DR   PDB; 5XTI; EM; 17.40 A; Bz/z=1-261.
DR   PDB; 5Z84; X-ray; 1.85 A; C/P=1-261.
DR   PDB; 5Z85; X-ray; 1.85 A; C/P=1-261.
DR   PDB; 5Z86; X-ray; 1.85 A; C/P=1-261.
DR   PDB; 5ZCO; X-ray; 1.90 A; C/P=1-261.
DR   PDB; 5ZCP; X-ray; 1.65 A; C/P=1-261.
DR   PDB; 5ZCQ; X-ray; 1.65 A; C/P=1-261.
DR   PDB; 6J8M; X-ray; 1.90 A; C/P=1-261.
DR   PDB; 6JUW; X-ray; 1.80 A; C/P=3-261.
DR   PDB; 6JY3; X-ray; 1.85 A; C=1-261.
DR   PDB; 6JY4; X-ray; 1.95 A; C=1-261.
DR   PDB; 6NKN; X-ray; 2.50 A; C/P=1-261.
DR   PDB; 6NMF; X-ray; 2.80 A; C/P=1-261.
DR   PDB; 6NMP; X-ray; 2.90 A; C/P=1-261.
DR   PDB; 7COH; X-ray; 1.30 A; C/P=1-261.
DR   PDB; 7CP5; X-ray; 1.76 A; C/P=3-261.
DR   PDB; 7D5W; X-ray; 1.84 A; C/P=3-261.
DR   PDB; 7D5X; X-ray; 1.74 A; C/P=3-261.
DR   PDB; 7DGQ; EM; 5.00 A; A9=1-261.
DR   PDB; 7DGR; EM; 4.60 A; C2=1-261.
DR   PDB; 7DGS; EM; 7.80 A; B7=1-261.
DR   PDB; 7DKF; EM; 8.30 A; C3=1-261.
DR   PDB; 7EV7; X-ray; 1.70 A; C/P=1-261.
DR   PDB; 7THU; X-ray; 1.93 A; CCC/PPP=1-261.
DR   PDB; 7TIE; X-ray; 1.90 A; CCC/PPP=1-261.
DR   PDB; 7TIH; X-ray; 2.35 A; CCC/PPP=1-261.
DR   PDB; 7TII; X-ray; 2.45 A; CCC/PPP=1-261.
DR   PDB; 7VUW; X-ray; 1.60 A; C/P=3-261.
DR   PDB; 7VVR; X-ray; 1.65 A; C/P=3-261.
DR   PDB; 7W3E; X-ray; 1.45 A; C/P=3-261.
DR   PDB; 7XMA; X-ray; 2.20 A; C/P=1-261.
DR   PDB; 7XMB; X-ray; 2.20 A; C/P=1-261.
DR   PDB; 7Y44; X-ray; 1.90 A; C/P=1-261.
DR   PDB; 7YPY; X-ray; 1.50 A; C/P=1-261.
DR   PDB; 8D4T; EM; 3.10 A; P=4-261.
DR   PDB; 8GBT; X-ray; 2.80 A; C/P=1-261.
DR   PDB; 8GCQ; X-ray; 2.38 A; C/P=1-261.
DR   PDB; 8GVM; X-ray; 1.85 A; C/P=1-261.
DR   PDB; 8H8R; X-ray; 1.70 A; C/P=1-261.
DR   PDB; 8H8S; X-ray; 1.70 A; C/P=1-261.
DR   PDB; 8IJN; X-ray; 1.80 A; C/P=1-261.
DR   PDBsum; 1OCC; -.
DR   PDBsum; 1OCO; -.
DR   PDBsum; 1OCR; -.
DR   PDBsum; 1OCZ; -.
DR   PDBsum; 1V54; -.
DR   PDBsum; 1V55; -.
DR   PDBsum; 2DYR; -.
DR   PDBsum; 2DYS; -.
DR   PDBsum; 2EIJ; -.
DR   PDBsum; 2EIK; -.
DR   PDBsum; 2EIL; -.
DR   PDBsum; 2EIM; -.
DR   PDBsum; 2EIN; -.
DR   PDBsum; 2OCC; -.
DR   PDBsum; 2Y69; -.
DR   PDBsum; 2YBB; -.
DR   PDBsum; 2ZXW; -.
DR   PDBsum; 3ABK; -.
DR   PDBsum; 3ABL; -.
DR   PDBsum; 3ABM; -.
DR   PDBsum; 3AG1; -.
DR   PDBsum; 3AG2; -.
DR   PDBsum; 3AG3; -.
DR   PDBsum; 3AG4; -.
DR   PDBsum; 3ASN; -.
DR   PDBsum; 3ASO; -.
DR   PDBsum; 3WG7; -.
DR   PDBsum; 3X2Q; -.
DR   PDBsum; 5B1A; -.
DR   PDBsum; 5B1B; -.
DR   PDBsum; 5B3S; -.
DR   PDBsum; 5IY5; -.
DR   PDBsum; 5LUF; -.
DR   PDBsum; 5W97; -.
DR   PDBsum; 5WAU; -.
DR   PDBsum; 5X19; -.
DR   PDBsum; 5X1B; -.
DR   PDBsum; 5X1F; -.
DR   PDBsum; 5XDQ; -.
DR   PDBsum; 5XDX; -.
DR   PDBsum; 5XTH; -.
DR   PDBsum; 5XTI; -.
DR   PDBsum; 5Z84; -.
DR   PDBsum; 5Z85; -.
DR   PDBsum; 5Z86; -.
DR   PDBsum; 5ZCO; -.
DR   PDBsum; 5ZCP; -.
DR   PDBsum; 5ZCQ; -.
DR   PDBsum; 6J8M; -.
DR   PDBsum; 6JUW; -.
DR   PDBsum; 6JY3; -.
DR   PDBsum; 6JY4; -.
DR   PDBsum; 6NKN; -.
DR   PDBsum; 6NMF; -.
DR   PDBsum; 6NMP; -.
DR   PDBsum; 7COH; -.
DR   PDBsum; 7CP5; -.
DR   PDBsum; 7D5W; -.
DR   PDBsum; 7D5X; -.
DR   PDBsum; 7DGQ; -.
DR   PDBsum; 7DGR; -.
DR   PDBsum; 7DGS; -.
DR   PDBsum; 7DKF; -.
DR   PDBsum; 7EV7; -.
DR   PDBsum; 7THU; -.
DR   PDBsum; 7TIE; -.
DR   PDBsum; 7TIH; -.
DR   PDBsum; 7TII; -.
DR   PDBsum; 7VUW; -.
DR   PDBsum; 7VVR; -.
DR   PDBsum; 7W3E; -.
DR   PDBsum; 7XMA; -.
DR   PDBsum; 7XMB; -.
DR   PDBsum; 7Y44; -.
DR   PDBsum; 7YPY; -.
DR   PDBsum; 8D4T; -.
DR   PDBsum; 8GBT; -.
DR   PDBsum; 8GCQ; -.
DR   PDBsum; 8GVM; -.
DR   PDBsum; 8H8R; -.
DR   PDBsum; 8H8S; -.
DR   PDBsum; 8IJN; -.
DR   AlphaFoldDB; P00415; -.
DR   EMDB; EMD-27196; -.
DR   EMDB; EMD-30673; -.
DR   EMDB; EMD-30674; -.
DR   EMDB; EMD-30675; -.
DR   EMDB; EMD-30706; -.
DR   EMDB; EMD-4107; -.
DR   SMR; P00415; -.
DR   CORUM; P00415; -.
DR   DIP; DIP-60938N; -.
DR   IntAct; P00415; 1.
DR   STRING; 9913.ENSBTAP00000053157; -.
DR   TCDB; 3.D.4.7.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR   PaxDb; 9913-ENSBTAP00000053157; -.
DR   eggNOG; KOG4664; Eukaryota.
DR   HOGENOM; CLU_044071_0_0_1; -.
DR   InParanoid; P00415; -.
DR   BRENDA; 7.1.1.9; 908.
DR   EvolutionaryTrace; P00415; -.
DR   Proteomes; UP000009136; Mitochondrion.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0008535; P:respiratory chain complex IV assembly; ISS:UniProtKB.
DR   CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.120.80; Cytochrome c oxidase, subunit III, four-helix bundle; 1.
DR   InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR   InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR   InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR   InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR   InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR   PANTHER; PTHR11403:SF7; CYTOCHROME C OXIDASE SUBUNIT 3; 1.
DR   PANTHER; PTHR11403; CYTOCHROME C OXIDASE SUBUNIT III; 1.
DR   Pfam; PF00510; COX3; 1.
DR   SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 1.
DR   PROSITE; PS50253; COX3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..261
FT                   /note="Cytochrome c oxidase subunit 3"
FT                   /id="PRO_0000183746"
FT   TOPO_DOM        1..15
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TRANSMEM        16..34
FT                   /note="Helical; Name=I"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TOPO_DOM        35..40
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TRANSMEM        41..66
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TOPO_DOM        67..72
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TRANSMEM        73..105
FT                   /note="Helical; Name=III"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TOPO_DOM        106..128
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TRANSMEM        129..152
FT                   /note="Helical; Name=IV"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TOPO_DOM        153..155
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TRANSMEM        156..183
FT                   /note="Helical; Name=V"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TOPO_DOM        184..190
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TRANSMEM        191..223
FT                   /note="Helical; Name=VI"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TOPO_DOM        224..232
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TRANSMEM        233..256
FT                   /note="Helical; Name=VII"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TOPO_DOM        257..261
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   CONFLICT        238
FT                   /note="A -> G (in Ref. 1; CAA24003)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:3AG1"
FT   HELIX           16..37
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   HELIX           41..65
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   HELIX           73..106
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   TURN            126..128
FT                   /evidence="ECO:0007829|PDB:5X19"
FT   HELIX           129..152
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   HELIX           156..183
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   HELIX           191..223
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   HELIX           233..255
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   TURN            256..260
FT                   /evidence="ECO:0007829|PDB:7COH"
SQ   SEQUENCE   261 AA;  29933 MW;  A521E76A9089B3FC CRC64;
     MTHQTHAYHM VNPSPWPLTG ALSALLMTSG LTMWFHFNSM TLLMIGLTTN MLTMYQWWRD
     VIRESTFQGH HTPAVQKGLR YGMILFIISE VLFFTGFFWA FYHSSLAPTP ELGGCWPPTG
     IHPLNPLEVP LLNTSVLLAS GVSITWAHHS LMEGDRKHML QALFITITLG VYFTLLQASE
     YYEAPFTISD GVYGSTFFVA TGFHGLHVII GSTFLIVCFF RQLKFHFTSN HHFGFEAAAW
     YWHFVDVVWL FLYVSIYWWG S
//