ID COX2_BOVIN Reviewed; 227 AA. AC P68530; P00404; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 24-JAN-2024, entry version 145. DE RecName: Full=Cytochrome c oxidase subunit 2; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide II; GN Name=MT-CO2; Synonyms=COII, COX2, COXII, MTCO2; 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 PROTEIN SEQUENCE, AND FORMYLATION AT MET-1. RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136}; TISSUE=Heart; RX PubMed=220175; RA Steffens G.J., Buse G.; RT "Studies on cytochrome c oxidase, IV[1-3]. Primary structure and function RT of subunit II."; RL Hoppe-Seyler's Z. Physiol. Chem. 360:613-619(1979). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6265319; DOI=10.1016/0378-1119(80)90108-0; RA Young I.G., Anderson S.; RT "The genetic code in bovine mitochondria: sequence of genes for the RT cytochrome oxidase subunit II and two tRNAs."; RL Gene 12:257-265(1980). RN [4] 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 [5] 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 [6] 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 [7] 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 [8] 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 [9] 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 [10] 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 [11] 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 [12] 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:P00410}. 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:P00410}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000250|UniProtKB:P00410}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158}; CC Note=Binds a dinuclear copper A center per subunit. CC {ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158}; 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). Found in a complex with TMEM177, COA6, COX18, COX20, CC SCO1 and SCO2. Interacts with TMEM177 in a COX20-dependent manner. CC Interacts with COX20. Interacts with COX16 (By similarity). CC {ECO:0000250|UniProtKB:P00403, 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 2 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; CAA24000.1; -; Genomic_DNA. DR EMBL; M10544; AAA31644.1; -; Genomic_DNA. DR EMBL; AF490528; AAM08331.1; -; Genomic_DNA. DR EMBL; AF490529; AAM08344.1; -; Genomic_DNA. DR EMBL; AF493541; AAM12792.1; -; Genomic_DNA. DR EMBL; AF493542; AAM12805.1; -; Genomic_DNA. DR PIR; B00152; OBBO2. DR RefSeq; YP_209208.1; NC_006853.1. DR PDB; 1OCC; X-ray; 2.80 A; B/O=1-227. DR PDB; 1OCO; X-ray; 2.80 A; B/O=1-227. DR PDB; 1OCR; X-ray; 2.35 A; B/O=1-227. DR PDB; 1OCZ; X-ray; 2.90 A; B/O=1-227. DR PDB; 1V54; X-ray; 1.80 A; B/O=1-227. DR PDB; 1V55; X-ray; 1.90 A; B/O=1-227. DR PDB; 2DYR; X-ray; 1.80 A; B/O=1-227. DR PDB; 2DYS; X-ray; 2.20 A; B/O=1-227. DR PDB; 2EIJ; X-ray; 1.90 A; B/O=1-227. DR PDB; 2EIK; X-ray; 2.10 A; B/O=1-227. DR PDB; 2EIL; X-ray; 2.10 A; B/O=1-227. DR PDB; 2EIM; X-ray; 2.60 A; B/O=1-227. DR PDB; 2EIN; X-ray; 2.70 A; B/O=1-227. DR PDB; 2OCC; X-ray; 2.30 A; B/O=1-227. DR PDB; 2Y69; X-ray; 1.95 A; B/O=1-227. DR PDB; 2YBB; EM; 19.00 A; M=1-227. DR PDB; 2ZXW; X-ray; 2.50 A; B/O=1-227. DR PDB; 3ABK; X-ray; 2.00 A; B/O=1-227. DR PDB; 3ABL; X-ray; 2.10 A; B/O=1-227. DR PDB; 3ABM; X-ray; 1.95 A; B/O=1-227. DR PDB; 3AG1; X-ray; 2.20 A; B/O=1-227. DR PDB; 3AG2; X-ray; 1.80 A; B/O=1-227. DR PDB; 3AG3; X-ray; 1.80 A; B/O=1-227. DR PDB; 3AG4; X-ray; 2.05 A; B/O=1-227. DR PDB; 3ASN; X-ray; 3.00 A; B/O=1-227. DR PDB; 3ASO; X-ray; 2.30 A; B/O=1-227. DR PDB; 3WG7; X-ray; 1.90 A; B/O=1-227. DR PDB; 3X2Q; X-ray; 2.00 A; B/O=1-227. DR PDB; 5B1A; X-ray; 1.50 A; B/O=1-227. DR PDB; 5B1B; X-ray; 1.60 A; B/O=1-227. DR PDB; 5B3S; X-ray; 1.68 A; B/O=2-227. DR PDB; 5GPN; EM; 5.40 A; z=1-227. DR PDB; 5IY5; X-ray; 2.00 A; B/O=1-227. DR PDB; 5LUF; EM; 9.10 A; y=1-227. DR PDB; 5W97; X-ray; 2.30 A; B/b=1-227. DR PDB; 5WAU; X-ray; 1.95 A; B/b=1-227. DR PDB; 5X19; X-ray; 2.20 A; B/O=1-227. DR PDB; 5X1B; X-ray; 2.40 A; B/O=1-227. DR PDB; 5X1F; X-ray; 2.20 A; B/O=1-227. DR PDB; 5XDQ; X-ray; 1.77 A; B/O=1-227. DR PDB; 5XDX; X-ray; 1.99 A; B/O=1-227. DR PDB; 5XTH; EM; 3.90 A; y=1-227. DR PDB; 5XTI; EM; 17.40 A; By/y=1-227. DR PDB; 5Z84; X-ray; 1.85 A; B/O=1-227. DR PDB; 5Z85; X-ray; 1.85 A; B/O=1-227. DR PDB; 5Z86; X-ray; 1.85 A; B/O=1-227. DR PDB; 5ZCO; X-ray; 1.90 A; B/O=1-227. DR PDB; 5ZCP; X-ray; 1.65 A; B/O=1-227. DR PDB; 5ZCQ; X-ray; 1.65 A; B/O=1-227. DR PDB; 6J8M; X-ray; 1.90 A; B/O=1-227. DR PDB; 6JUW; X-ray; 1.80 A; B/O=1-227. DR PDB; 6JY3; X-ray; 1.85 A; B=1-227. DR PDB; 6JY4; X-ray; 1.95 A; B=1-227. DR PDB; 6NKN; X-ray; 2.50 A; B/O=1-227. DR PDB; 6NMF; X-ray; 2.80 A; B/O=1-227. DR PDB; 6NMP; X-ray; 2.90 A; B/O=1-227. DR PDB; 7COH; X-ray; 1.30 A; B/O=1-227. DR PDB; 7CP5; X-ray; 1.76 A; B/O=1-227. DR PDB; 7D5W; X-ray; 1.84 A; B/O=1-227. DR PDB; 7D5X; X-ray; 1.74 A; B/O=1-227. DR PDB; 7DGQ; EM; 5.00 A; C1=1-227. DR PDB; 7DGR; EM; 4.60 A; C4=1-227. DR PDB; 7DGS; EM; 7.80 A; B9=1-227. DR PDB; 7DKF; EM; 8.30 A; B3=1-227. DR PDB; 7EV7; X-ray; 1.70 A; B/O=1-227. DR PDB; 7THU; X-ray; 1.93 A; BBB/OOO=1-227. DR PDB; 7TIE; X-ray; 1.90 A; BBB/OOO=1-227. DR PDB; 7TIH; X-ray; 2.35 A; BBB/OOO=1-227. DR PDB; 7TII; X-ray; 2.45 A; BBB/OOO=1-227. DR PDB; 7VUW; X-ray; 1.60 A; B/O=1-227. DR PDB; 7VVR; X-ray; 1.65 A; B/O=1-227. DR PDB; 7W3E; X-ray; 1.45 A; B/O=1-227. DR PDB; 7XMA; X-ray; 2.20 A; B/O=1-227. DR PDB; 7XMB; X-ray; 2.20 A; B/O=1-227. DR PDB; 7Y44; X-ray; 1.90 A; B/O=1-227. DR PDB; 7YPY; X-ray; 1.50 A; B/O=1-227. DR PDB; 8D4T; EM; 3.10 A; O=1-227. DR PDB; 8GBT; X-ray; 2.80 A; B/O=1-227. DR PDB; 8GCQ; X-ray; 2.38 A; B/O=1-227. DR PDB; 8GVM; X-ray; 1.85 A; B/O=1-227. DR PDB; 8H8R; X-ray; 1.70 A; B/O=1-227. DR PDB; 8H8S; X-ray; 1.70 A; B/O=1-227. DR PDB; 8IJN; X-ray; 1.80 A; B/O=1-227. 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; 5GPN; -. 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; P68530; -. 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 EMDB; EMD-9534; -. DR SMR; P68530; -. DR CORUM; P68530; -. DR DIP; DIP-39024N; -. DR IntAct; P68530; 2. DR STRING; 9913.ENSBTAP00000053151; -. DR TCDB; 3.D.4.7.1; the proton-translocating cytochrome oxidase (cox) superfamily. DR iPTMnet; P68530; -. DR PaxDb; 9913-ENSBTAP00000053151; -. DR PeptideAtlas; P68530; -. DR Ensembl; ENSBTAT00000060549.1; ENSBTAP00000053151.1; ENSBTAG00000043556.1. DR GeneID; 3283880; -. DR KEGG; bta:3283880; -. DR CTD; 4513; -. DR VEuPathDB; HostDB:ENSBTAG00000043556; -. DR eggNOG; KOG4767; Eukaryota. DR GeneTree; ENSGT00390000017410; -. DR HOGENOM; CLU_036876_2_3_1; -. DR InParanoid; P68530; -. DR OMA; WSYEYTD; -. DR OrthoDB; 5390623at2759; -. DR TreeFam; TF344269; -. DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-BTA-611105; Respiratory electron transport. DR Reactome; R-BTA-9707564; Cytoprotection by HMOX1. DR EvolutionaryTrace; P68530; -. DR Proteomes; UP000009136; Mitochondrion. DR Bgee; ENSBTAG00000043556; Expressed in tongue muscle and 104 other cell types or tissues. DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:Ensembl. DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central. DR CDD; cd13912; CcO_II_C; 1. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1. DR InterPro; IPR045187; CcO_II. DR InterPro; IPR002429; CcO_II-like_C. DR InterPro; IPR034210; CcO_II_C. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR014222; Cyt_c_oxidase_su2. DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom. DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf. DR NCBIfam; TIGR02866; CoxB; 1. DR PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1. DR PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR PRINTS; PR01166; CYCOXIDASEII. DR SUPFAM; SSF49503; Cupredoxins; 1. DR SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 1. DR PROSITE; PS00078; COX2; 1. DR PROSITE; PS50857; COX2_CUA; 1. DR PROSITE; PS50999; COX2_TM; 1. PE 1: Evidence at protein level; KW 3D-structure; Copper; Direct protein sequencing; Electron transport; KW Formylation; Magnesium; Membrane; Metal-binding; Mitochondrion; KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome; KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..227 FT /note="Cytochrome c oxidase subunit 2" FT /id="PRO_0000183517" FT TOPO_DOM 1..14 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:27605664" FT TRANSMEM 15..45 FT /note="Helical; Name=I" FT /evidence="ECO:0000269|PubMed:27605664" FT TOPO_DOM 46..59 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000269|PubMed:27605664" FT TRANSMEM 60..87 FT /note="Helical; Name=II" FT /evidence="ECO:0000269|PubMed:27605664" FT TOPO_DOM 88..227 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:27605664" FT BINDING 161 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000269|PubMed:20385840, FT ECO:0000269|PubMed:8638158" FT BINDING 196 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000269|PubMed:20385840, FT ECO:0000269|PubMed:8638158" FT BINDING 196 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000269|PubMed:20385840, FT ECO:0000269|PubMed:8638158" FT BINDING 198 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000269|PubMed:20385840, FT ECO:0000269|PubMed:8638158" FT BINDING 198 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with MT-CO1" FT /evidence="ECO:0000269|PubMed:20385840, FT ECO:0000269|PubMed:8638158" FT BINDING 200 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000269|PubMed:20385840, FT ECO:0000269|PubMed:8638158" FT BINDING 200 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000269|PubMed:20385840, FT ECO:0000269|PubMed:8638158" FT BINDING 204 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000269|PubMed:20385840, FT ECO:0000269|PubMed:8638158" FT BINDING 207 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000269|PubMed:20385840, FT ECO:0000269|PubMed:8638158" FT MOD_RES 1 FT /note="N-formylmethionine" FT /evidence="ECO:0000269|PubMed:220175" FT MOD_RES 218 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P00406" FT CONFLICT 58 FT /note="A -> P (in Ref. 3; AAA31644)" FT /evidence="ECO:0000305" FT CONFLICT 118 FT /note="F -> L (in Ref. 3; AAA31644)" FT /evidence="ECO:0000305" FT HELIX 15..45 FT /evidence="ECO:0007829|PDB:7COH" FT HELIX 59..88 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 94..102 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 116..120 FT /evidence="ECO:0007829|PDB:7COH" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:7COH" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 150..159 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:7COH" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 180..184 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:7COH" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:7COH" FT STRAND 209..214 FT /evidence="ECO:0007829|PDB:7COH" FT HELIX 216..225 FT /evidence="ECO:0007829|PDB:7COH" SQ SEQUENCE 227 AA; 26021 MW; C562D5B39FA9771A CRC64; MAYPMQLGFQ DATSPIMEEL LHFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE VETIWTILPA IILILIALPS LRILYMMDEI NNPSLTVKTM GHQWYWSYEY TDYEDLSFDS YMIPTSELKP GELRLLEVDN RVVLPMEMTI RMLVSSEDVL HSWAVPSLGL KTDAIPGRLN QTTLMSSRPG LYYGQCSEIC GSNHSFMPIV LELVPLKYFE KWSASML //