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UniProtKB/Swiss-Prot entry Q1HKA1

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COX1_CANLU
Primary accession number Q1HKA1
Secondary accession number Q3L6Z2
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on June 13, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 20)
Name and origin of the protein
Protein name Cytochrome c oxidase subunit 1
Synonyms EC 1.9.3.1
Cytochrome c oxidase polypeptide I
Gene name
Name: MT-CO1
Synonyms: COI, COXI, MTCO1
From
Canis lupus (Gray wolf) [TaxID: 9612] 
Encoded on Mitochondrion.
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-512.
DOI=10.1016/j.ympev.2005.04.025; PubMed=15964215 [NCBI, ExPASy, EBI, Israel, Japan]
Delisle I., Strobeck C.;
"A phylogeny of the Caniformia (order Carnivora) based on 12 complete protein-coding mitochondrial genes.";
Mol. Phylogenet. Evol. 37:192-201(2005).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-512.
DOI=10.1101/gr.5117706; PubMed=16809672 [NCBI, ExPASy, EBI, Israel, Japan]
Bjornerfeldt S., Webster M.T., Vila C.;
"Relaxation of selective constraint on dog mitochondrial DNA following domestication.";
Genome Res. 16:990-994(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY598496; AAU00442.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ480503; ABE48157.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ480504; ABE48170.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ480505; ABE48183.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ480506; ABE48196.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ480507; ABE48209.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ480508; ABE48222.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_626730.1; -.
3D structure databases
SMR Q1HKA1; 1-511.
ModBase Q1HKA1.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005746; Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004129; Molecular function: cytochrome-c oxidase activity (inferred from electronic annotation from EC).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0009060; Biological process: aerobic respiration (inferred from electronic annotation from InterPro).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000883; COX1.
Graphical view of domain structure.
Gene3D G3DSA:1.20.210.10; COX1; 1.
PANTHER PTHR10422; COX1; 1.
Pfam PF00115; COX1; 1.
Pfam graphical view of domain structure.
PRINTS PR01165; CYCOXIDASEI.
PROSITE PS50855; COX1; 1.
PS00077; COX1_CUB; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q1HKA1.
Genome annotation databases
GeneID 4097766; -.
Phylogenomic databases
HOVERGEN Q1HKA1; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Copper; Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Respiratory chain; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   514  514     Cytochrome c oxidase subunit 1. PRO_0000269704
TOPO_DOM   1    11  11     Mitochondrial matrix (By similarity). 
TRANSMEM   12    40  29     I (By similarity). 
TOPO_DOM   41    50  10     Mitochondrial intermembrane (By similarity). 
TRANSMEM   51    86  36     II (By similarity). 
TOPO_DOM   87    94  8     Mitochondrial matrix (By similarity). 
TRANSMEM   95   117  23     III (By similarity). 
TOPO_DOM   118   140  23     Mitochondrial intermembrane (By similarity). 
TRANSMEM   141   170  30     IV (By similarity). 
TOPO_DOM   171   182  12     Mitochondrial matrix (By similarity). 
TRANSMEM   183   212  30     V (By similarity). 
TOPO_DOM   213   227  15     Mitochondrial intermembrane (By similarity). 
TRANSMEM   228   261  34     VI (By similarity). 
TOPO_DOM   262   269  8     Mitochondrial matrix (By similarity). 
TRANSMEM   270   286  17     VII (By similarity). 
TOPO_DOM   287   298  12     Mitochondrial intermembrane (By similarity). 
TRANSMEM   299   327  29     VIII (By similarity). 
TOPO_DOM   328   335  8     Mitochondrial matrix (By similarity). 
TRANSMEM   336   357  22     IX (By similarity). 
TOPO_DOM   358   370  13     Mitochondrial intermembrane (By similarity). 
TRANSMEM   371   400  30     X (By similarity). 
TOPO_DOM   401   406  6     Mitochondrial matrix (By similarity). 
TRANSMEM   407   433  27     XI (By similarity). 
TOPO_DOM   434   446  13     Mitochondrial intermembrane (By similarity). 
TRANSMEM   447   478  32     XII (By similarity). 
TOPO_DOM   479   514  36     Mitochondrial matrix (By similarity). 
METAL   61    61        Iron (heme A axial ligand) (Probable). 
METAL   244   244        Copper B (Probable). 
METAL   290   290        Copper B (Probable). 
METAL   291   291        Copper B (Probable). 
METAL   376   376        Iron (heme A3 axial ligand) (Probable). 
METAL   378   378        Iron (heme A axial ligand) (Probable). 
CROSSLNK   240   244        1'-histidyl-3'-tyrosine (His-Tyr) (By similarity). 
VARIANT   512   512  1     I -> V. 
Sequence information
Length: 514 AA [This is the length of the unprocessed precursor] Molecular weight: 57039 Da [This is the MW of the unprocessed precursor] CRC64: 44D2B3E8E04CBF6F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MFINRWLFST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLLGD DQIYNVIVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSMVEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAMSQYQ 

       190        200        210        220        230        240 
TPLFVWSVLI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH 

       250        260        270        280        290        300 
PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMLW ALGFIFLFTV GGLTGIVLAN 

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFAHWFPLF SGYTLNDTWA KIHFTIMFVG 

       430        440        450        460        470        480 
VNMTFFPQHF LGLSGMPRRY SDYPDAYTTW NTVSSMGSFI SLTAVMLMIF MIWEAFASKR 

       490        500        510 
EVAMVELTTT NIEWLHGCPP PYHTFEEPTY VIQK
Q1HKA1 in FASTA format

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