COX2_CAEBR
ID COX2_CAEBR Reviewed; 231 AA.
AC Q8HEC3; A9YMI3; A9YMI8; A9YMI9; B1PE42; B1PE54; B1PED8; B1PEH4; B1PEL0;
AC Q8SEN0; Q8SFX6;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
GN Name=cox-2; Synonyms=coII;
OS Caenorhabditis briggsae.
OG Mitochondrion {ECO:0000312|EMBL:AAO13510.1}.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000312|EMBL:AAO13510.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PB800;
RX PubMed=12644560; DOI=10.1093/molbev/msg044;
RA Denver D.R., Morris K., Thomas W.K.;
RT "Phylogenetics in Caenorhabditis elegans: an analysis of divergence and
RT outcrossing.";
RL Mol. Biol. Evol. 20:393-400(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-16; THR-21; LEU-61;
RP ALA-141 AND HIS-142.
RC STRAIN=BW287, ED3032, ED3033, ED3034, ED3035, ED3036, ED3037, ED3083,
RC ED3092, ED3101, EG4181, EG4207A, HK104, HK105, JU403, JU439, JU516, JU725,
RC JU726, JU793, PB800, PB826, and VT847;
RX PubMed=18302772; DOI=10.1186/1471-2148-8-62;
RA Howe D.K., Denver D.R.;
RT "Muller's Ratchet and compensatory mutation in Caenorhabditis briggsae
RT mitochondrial genome evolution.";
RL BMC Evol. Biol. 8:62-62(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-231, AND VARIANT MET-16.
RC STRAIN=AF16, HK104, HK105, PB800, PB826, and VT847;
RX PubMed=12019226; DOI=10.1093/genetics/161.1.99;
RA Graustein A., Gaspar J.M., Walters J.R., Palopoli M.F.;
RT "Levels of DNA polymorphism vary with mating system in the nematode genus
RT Caenorhabditis.";
RL Genetics 161:99-107(2002).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-230, AND VARIANT MET-16.
RC STRAIN=AF16, DR1690, HK104, HK105, JU725, JU726, KT0001, PB800, PB826, and
RC VT847;
RA Thomas W.K., Abebe E.B., Jumba M., Gray V., Bonner K., Morris K.;
RT "An entomopathogenic Caenorhabditis.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P00410};
CC Note=Binds a dinuclear copper A center per subunit.
CC {ECO:0000250|UniProtKB:P00410};
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of a catalytic core of 3 subunits and
CC several supernumerary subunits. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00410}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00410}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00410}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; AY171103; AAO13510.1; -; Genomic_DNA.
DR EMBL; EU407781; ACB06109.1; -; Genomic_DNA.
DR EMBL; EU407782; ACB06121.1; -; Genomic_DNA.
DR EMBL; EU407783; ACB06133.1; -; Genomic_DNA.
DR EMBL; EU407784; ACB06145.1; -; Genomic_DNA.
DR EMBL; EU407785; ACB06157.1; -; Genomic_DNA.
DR EMBL; EU407786; ACB06169.1; -; Genomic_DNA.
DR EMBL; EU407787; ACB06181.1; -; Genomic_DNA.
DR EMBL; EU407788; ACB06193.1; -; Genomic_DNA.
DR EMBL; EU407789; ACB06205.1; -; Genomic_DNA.
DR EMBL; EU407790; ACB06217.1; -; Genomic_DNA.
DR EMBL; EU407791; ACB06229.1; -; Genomic_DNA.
DR EMBL; EU407792; ACB06241.1; -; Genomic_DNA.
DR EMBL; EU407793; ACB06253.1; -; Genomic_DNA.
DR EMBL; EU407794; ACB06265.1; -; Genomic_DNA.
DR EMBL; EU407795; ACB06277.1; -; Genomic_DNA.
DR EMBL; EU407796; ACB06289.1; -; Genomic_DNA.
DR EMBL; EU407797; ACB06301.1; -; Genomic_DNA.
DR EMBL; EU407798; ACB06313.1; -; Genomic_DNA.
DR EMBL; EU407799; ACB06325.1; -; Genomic_DNA.
DR EMBL; EU407800; ACB06337.1; -; Genomic_DNA.
DR EMBL; EU407801; ACB06349.1; -; Genomic_DNA.
DR EMBL; EU407802; ACB06361.1; -; Genomic_DNA.
DR EMBL; EU407803; ACB06373.1; -; Genomic_DNA.
DR EMBL; AC186293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF491452; AAM09746.1; -; Genomic_DNA.
DR EMBL; AF491453; AAM09747.1; -; Genomic_DNA.
DR EMBL; AF491454; AAM09748.1; -; Genomic_DNA.
DR EMBL; AF491455; AAM09749.1; -; Genomic_DNA.
DR EMBL; AF491456; AAM09750.1; -; Genomic_DNA.
DR EMBL; AF491457; AAM09751.1; -; Genomic_DNA.
DR EMBL; EU254734; ABX84167.1; -; Genomic_DNA.
DR EMBL; EU254735; ABX84168.1; -; Genomic_DNA.
DR EMBL; EU254736; ABX84169.1; -; Genomic_DNA.
DR EMBL; EU254737; ABX84170.1; -; Genomic_DNA.
DR EMBL; EU254738; ABX84171.1; -; Genomic_DNA.
DR EMBL; EU254739; ABX84172.1; -; Genomic_DNA.
DR EMBL; EU254740; ABX84173.1; -; Genomic_DNA.
DR EMBL; EU254741; ABX84174.1; -; Genomic_DNA.
DR EMBL; EU254742; ABX84175.1; -; Genomic_DNA.
DR EMBL; EU254743; ABX84176.1; -; Genomic_DNA.
DR RefSeq; YP_001504332.1; NC_009885.1.
DR AlphaFoldDB; Q8HEC3; -.
DR SMR; Q8HEC3; -.
DR GeneID; 5666631; -.
DR KEGG; cbr:COX2; -.
DR CTD; 4513; -.
DR InParanoid; Q8HEC3; -.
DR Proteomes; UP000008549; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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; -; 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; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 3: Inferred from homology;
KW Copper; Electron transport; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..231
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183525"
FT TOPO_DOM 1..30
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..64
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..231
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 164
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 199
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 199
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 201
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with subunit 1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 203
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 203
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 207
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 210
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT VARIANT 16
FT /note="L -> M (in strain: PB826)"
FT /evidence="ECO:0000269|PubMed:12019226,
FT ECO:0000269|PubMed:18302772, ECO:0000269|Ref.5"
FT VARIANT 21
FT /note="M -> T (in strain: ED3092 and ED3101)"
FT /evidence="ECO:0000269|PubMed:18302772"
FT VARIANT 61
FT /note="Q -> L (in strain: BW287)"
FT /evidence="ECO:0000269|PubMed:18302772"
FT VARIANT 141
FT /note="V -> A (in strain: JU403)"
FT /evidence="ECO:0000269|PubMed:18302772"
FT VARIANT 142
FT /note="D -> H (in strain: EG4207A)"
FT /evidence="ECO:0000269|PubMed:18302772"
SQ SEQUENCE 231 AA; 26590 MW; 646AA84FD14D11E0 CRC64;
MNNFFQGYNL LFQHSLFASY MDWFHAFNCS LLLGVLVFVT LLFGYLIFST FYFKSKKIEY
QFGELLCSIF PTIILLMQMV PSLSLLYYYG LMNLDSNLTV KVTGHQWYWS YEYSDIPGLE
FDSYMKSLDQ LNLGEPRLLE VDNRCVIPCD TNIRFCITSA DVIHAWALNS LSVKLDAMSG
ILSTFSYSFP MVGVFYGQCS EICGANHSFM PIALEVTLLD NFKSWCFGTM E
