ID COX2_PONPY Reviewed; 227 AA.
AC Q37605; P92721; P92722; Q37606; Q37607;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 01-MAY-2013, entry version 92.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
GN Name=MT-CO2; Synonyms=COII, COXII, MTCO2;
OS Pongo pygmaeus (Bornean orangutan).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-4; SER-54; ILE-67;
RP LEU-184 AND THR-226.
RC STRAIN=Isolate San Diego zoo Ppy2, and Isolate San Diego zoo Ppy3;
RX PubMed=8090741; DOI=10.1073/pnas.91.19.8900;
RA Ruvolo M., Pan D., Zehr S., Goldberg T., Disotell T.R., von Dornum M.;
RT "Gene trees and hominoid phylogeny.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8900-8904(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7530363; DOI=10.1073/pnas.92.2.532;
RA Horai S., Hayasaka K., Kondo R., Tsugane K., Takahata N.;
RT "Recent African origin of modern humans revealed by complete sequences
RT of hominoid mitochondrial DNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:532-536(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-4; ILE-38 AND
RP ILE-67.
RC STRAIN=Isolate Anna, and Isolate Dennis;
RX PubMed=8875856;
RA Xu X., Arnason U.;
RT "The mitochondrial DNA molecule of Sumatran orangutan and a molecular
RT proposal for two (Bornean and Sumatran) species of orangutan.";
RL J. Mol. Evol. 43:431-437(1996).
CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC chain that catalyzes the reduction of oxygen to water. Subunits 1-
CC 3 form the functional core of the enzyme complex. Subunit 2
CC transfers the electrons from cytochrome c via its binuclear copper
CC A center to the bimetallic center of the catalytic subunit 1.
CC -!- COFACTOR: Copper A.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
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DR EMBL; U12703; AAA61412.1; -; Genomic_DNA.
DR EMBL; U12704; AAA61413.1; -; Genomic_DNA.
DR EMBL; D38115; BAA07308.1; -; Genomic_DNA.
DR EMBL; X97716; CAA66302.1; -; Genomic_DNA.
DR EMBL; X97712; CAA66298.1; -; Genomic_DNA.
DR PIR; I61892; I61892.
DR PIR; T14142; T14142.
DR RefSeq; NP_008228.1; NC_001646.1.
DR ProteinModelPortal; Q37605; -.
DR SMR; Q37605; 1-220.
DR GeneID; 807910; -.
DR CTD; 4513; -.
DR eggNOG; COG1622; -.
DR HOGENOM; HOG000264988; -.
DR HOVERGEN; HBG012727; -.
DR InParanoid; Q37605; -.
DR ProtClustDB; MTH00098; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR002429; Cyt_c_oxidase_su2_C.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; Cupredoxin; 1.
DR SUPFAM; SSF81464; Cyt_c_oxidase_II-like_TM; 1.
DR TIGRFAMs; TIGR02866; CoxB; 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; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Polymorphism; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 227 Cytochrome c oxidase subunit 2.
FT /FTId=PRO_0000183670.
FT TOPO_DOM 1 26 Mitochondrial intermembrane (Potential).
FT TRANSMEM 27 48 Helical; (Potential).
FT TOPO_DOM 49 62 Mitochondrial matrix (Potential).
FT TRANSMEM 63 82 Helical; (Potential).
FT TOPO_DOM 83 227 Mitochondrial intermembrane (Potential).
FT METAL 161 161 Copper A (By similarity).
FT METAL 196 196 Copper A (By similarity).
FT METAL 200 200 Copper A (By similarity).
FT METAL 204 204 Copper A (By similarity).
FT VARIANT 4 4 R -> A (in strain: Isolate San Diego zoo
FT Ppy3, Isolate Anna and Isolate Dennis).
FT /FTId=VAR_019058.
FT VARIANT 38 38 V -> I (in strain: Isolate Anna).
FT /FTId=VAR_019554.
FT VARIANT 54 54 N -> S (in strain: Isolate San Diego zoo
FT Ppy3, Isolate Anna and Isolate Dennis).
FT /FTId=VAR_019059.
FT VARIANT 67 67 T -> I (in strain: Isolate San Diego zoo
FT Ppy3).
FT /FTId=VAR_019060.
FT VARIANT 184 184 F -> L (in strain: Isolate San Diego zoo
FT Ppy3).
FT /FTId=VAR_019061.
FT VARIANT 226 226 A -> T (in strain: Isolate San Diego zoo
FT PPY3).
FT /FTId=VAR_019062.
SQ SEQUENCE 227 AA; 25652 MW; D027088B63F57A42 CRC64;
MAHRAQVGLQ DATSPIMEEL VIFHDHALMI IFLICFLVLY ALFLTLTTKL TNTNISDAQE
METIWTTLPA IILILIALPS LRILYLTDEI NDPSFTIKSI GHQWYWTYEY TDYGGLIFNS
YMLPPLFLEP GDLRLLDVDN RVVLPVEAPV RMMITSQDVL HSWTVPSLGL KTDAIPGRLN
QTTFTATRPG VYYGQCSEIC GANHSFMPIV LELIPLKIFE MGPVFAL
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