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Database: UniProt
Entry: O21042
LinkDB: O21042
Original site: O21042 
ID   COX1_DICDI              Reviewed;         764 AA.
AC   O21042; P92625; Q23893; Q7GET3;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-SEP-2014, entry version 100.
DE   RecName: Full=Cytochrome c oxidase subunit 1+2;
DE            EC=1.9.3.1;
DE   AltName: Full=Cytochrome c oxidase polypeptide I+II;
GN   Name=cox1/2; Synonyms=cox1, coxI, Ddmco; ORFNames=DDB_G0294088;
OS   Dictyostelium discoideum (Slime mold).
OG   Mitochondrion.
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AX3;
RX   PubMed=9000384; DOI=10.1007/s002940050179;
RA   Ogawa S., Matsuo K., Angata K., Yanagisawa K., Tanaka Y.;
RT   "Group-I introns in the cytochrome c oxidase genes of Dictyostelium
RT   discoideum: two related ORFs in one loop of a group-I intron, a cox1/2
RT   hybrid gene and an unusually large cox3 gene.";
RL   Curr. Genet. 31:80-88(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX3;
RX   PubMed=10821186; DOI=10.1007/s004380051196;
RA   Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K.,
RA   Matsuo K., Morio T., Urushihara H., Yanagisawa K., Tanaka Y.;
RT   "The mitochondrial DNA of Dictyostelium discoideum: complete sequence,
RT   gene content and genome organization.";
RL   Mol. Gen. Genet. 263:514-519(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 83-205.
RC   STRAIN=AX3;
RA   Mueller-Taubenberger A.;
RT   "Dictyostelium discoideum Ddmco gene sequence.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-764.
RC   STRAIN=AX3;
RX   PubMed=9186775; DOI=10.1016/S0005-2728(97)00010-8;
RA   Pellizzari R., Anjard C., Bisson R.;
RT   "Subunits I and II of Dictyostelium cytochrome c oxidase are specified
RT   by a single open reading frame transcribed into a large polycistronic
RT   RNA.";
RL   Biochim. Biophys. Acta 1320:1-7(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-341.
RC   STRAIN=AX2;
RA   Anjard C., Reymond C.D.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
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. CO I is the
CC       catalytic subunit of the enzyme. Electrons originating in
CC       cytochrome c are transferred via the copper A center of subunit 2
CC       and heme A of subunit 1 to the bimetallic center formed by heme A3
CC       and copper B (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC       ferricytochrome c + 2 H(2)O.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the heme-copper
CC       respiratory oxidase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC       oxidase subunit 2 family.
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DR   EMBL; D50297; BAA21123.1; -; Genomic_DNA.
DR   EMBL; AB000109; BAA78055.1; -; Genomic_DNA.
DR   EMBL; U87391; AAB42021.1; -; mRNA.
DR   EMBL; X81884; CAA57467.1; -; Genomic_DNA.
DR   EMBL; X95896; CAA65139.1; -; Genomic_DNA.
DR   PIR; T43751; T43751.
DR   RefSeq; NP_050073.1; NC_000895.1.
DR   ProteinModelPortal; O21042; -.
DR   SMR; O21042; 20-494.
DR   STRING; 44689.DidioMp06; -.
DR   GeneID; 2193894; -.
DR   KEGG; ddi:DidioMp06; -.
DR   dictyBase; DDB_G0294088; cox1/2.
DR   eggNOG; COG1622; -.
DR   KO; K02256; -.
DR   OMA; MISAMSA; -.
DR   PhylomeDB; O21042; -.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:O21042; -.
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: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:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:dictyBase.
DR   GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.287.90; -; 1.
DR   Gene3D; 1.20.210.10; -; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR000883; COX1.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR023616; Cyt_c_Oxase_su1_dom.
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   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   SUPFAM; SSF81464; SSF81464; 1.
DR   TIGRFAMs; TIGR02866; CoxB; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Copper; Electron transport; Heme; Iron; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    764       Cytochrome c oxidase subunit 1+2.
FT                                /FTId=PRO_0000312383.
FT   TRANSMEM     36     56       Helical; (Potential).
FT   TRANSMEM     82    102       Helical; (Potential).
FT   TRANSMEM    121    141       Helical; (Potential).
FT   TRANSMEM    164    184       Helical; (Potential).
FT   TRANSMEM    202    222       Helical; (Potential).
FT   TRANSMEM    253    273       Helical; (Potential).
FT   TRANSMEM    285    305       Helical; (Potential).
FT   TRANSMEM    329    349       Helical; (Potential).
FT   TRANSMEM    356    376       Helical; (Potential).
FT   TRANSMEM    390    410       Helical; (Potential).
FT   TRANSMEM    438    458       Helical; (Potential).
FT   TRANSMEM    477    497       Helical; (Potential).
FT   TRANSMEM    545    565       Helical; (Potential).
FT   TRANSMEM    594    614       Helical; (Potential).
FT   REGION        1    485       COX1.
FT   REGION      486    764       COX2.
FT   METAL        80     80       Iron (heme A axial ligand) (By
FT                                similarity).
FT   METAL       259    259       Copper B (By similarity).
FT   METAL       263    263       Copper B (By similarity).
FT   METAL       308    308       Copper B (By similarity).
FT   METAL       309    309       Copper B (By similarity).
FT   METAL       394    394       Iron (heme A3 axial ligand) (By
FT                                similarity).
FT   METAL       396    396       Iron (heme A axial ligand) (By
FT                                similarity).
FT   METAL       699    699       Copper A (By similarity).
FT   METAL       734    734       Copper A (By similarity).
FT   METAL       738    738       Copper A (By similarity).
FT   METAL       742    742       Copper A (By similarity).
FT   CROSSLNK    259    263       1'-histidyl-3'-tyrosine (His-Tyr) (By
FT                                similarity).
FT   CONFLICT     83     89       IMIFFVV -> MKVFMNC (in Ref. 3; AAB42021).
FT   CONFLICT    104    104       I -> II (in Ref. 3; AAB42021).
FT   CONFLICT    198    198       S -> P (in Ref. 3; AAB42021).
FT   CONFLICT    259    259       H -> D (in Ref. 5; CAA65139).
SQ   SEQUENCE   764 AA;  85501 MW;  BF363A039A0BA912 CRC64;
     MKILEIYDKQ IAEKEGNIFI FISKWIISVD HKNIGTMYTN FSILAGIVGT LLSLVIRMEL
     STGNMLDGDG QQYNVIVTAH GLIMIFFVVM PAMLGGFANW FIPIMVGSPD VAFPRLNNIS
     LWLIIVSFFL LLTSSCVGIG VGTGWTVYPP LSTMEYHPGH AVDVGILSLH IAGASSLLGA
     INFLTTVFNM KIAGLSWSKV SLFVWSILIT AVLLVLSLPV LAGGLTMLIT DRNFETTFFD
     PIGGGDPILY QHLFWFFGHP EVYILILPGF GLVSIILSKY SNKGIFGVKG MISAMSAIGF
     LGFLVWAHHM YTVGLDVDTR AYFTAATMII AIPTGIKIFS WLATLWGGVI KITTPMLFVI
     GFLVLFTIGG LTGVVLANGG LDISLHDTYY VVAHFHYVLS MGAIFAIFAG YYYYYSIMNS
     TRLFGVVRYN EQLGRIHFWT MFIGVNVTFF PMHFLGLAGM PRRIGDYPDA YIGWNLIASY
     GSLITAFGLL FFVVNIFTPY IRRSVNIKNG AIILMGLDFA RDWQIGFQDP ATPIMEGIID
     LHNYIFFYLI VVAVFIGWVM GRILWRFSYK WSYPTIGDIE IFKNFTAYNQ IIHGTVIEIV
     WTLIPTVILY LIAIPSFTLL YAMDEIINPT VTIKIIGHQW YWSYEYGDNA SNLIEFDSYM
     VYERDLAEGQ LRLLEVDNAM VVPVKTHIRL IITSGDVLHS WAIPSFGIKV DAVPGRLNQI
     GLYVKREGTF YGQCSELCGV DHGFMPIKVQ AVKLGEYFSK LNEK
//
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