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UniProtKB/Swiss-Prot entry P34838

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

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Entry information
Entry name COX1_ANOGA
Primary accession number P34838
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 58)
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: COI
From
Anopheles gambiae (African malaria mosquito) [TaxID: 7165] 
Encoded on Mitochondrion.
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Anophelinae; Anopheles.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=G3;
DOI=10.1111/j.1365-2583.1993.tb00131.x; PubMed=9087549 [NCBI, ExPASy, EBI, Israel, Japan]
Beard C.B., Hamm D.M., Collins F.H.;
"The mitochondrial genome of the mosquito Anopheles gambiae: DNA sequence, genome organization, and comparisons with mitochondrial sequences of other insects.";
Insect Mol. Biol. 2:103-104(1993).
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
L20934; AAD12191.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T09801; T09801.
3D structure databases
HSSP P00396; 2OCC. [HSSP ENTRY / PDB]
SMR P34838; 4-506.
ModBase P34838.
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 P34838.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; 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_0000183282
TRANSMEM   16    36  21     Potential. 
TRANSMEM   55    75  21     Potential. 
TRANSMEM   101   121  21     Potential. 
TRANSMEM   144   164  21     Potential. 
TRANSMEM   182   202  21     Potential. 
TRANSMEM   233   253  21     Potential. 
TRANSMEM   267   287  21     Potential. 
TRANSMEM   304   324  21     Potential. 
TRANSMEM   337   357  21     Potential. 
TRANSMEM   379   399  21     Potential. 
TRANSMEM   415   435  21     Potential. 
TRANSMEM   451   471  21     Potential. 
METAL   60    60        Iron (heme A axial ligand) (Probable). 
METAL   239   239        Copper B (Probable). 
METAL   243   243        Copper B (Probable). 
METAL   289   289        Copper B (Probable). 
METAL   290   290        Copper B (Probable). 
METAL   375   375        Iron (heme A3 axial ligand) (Probable). 
METAL   377   377        Iron (heme A axial ligand) (Probable). 
CROSSLNK   239   243        1'-histidyl-3'-tyrosine (His-Tyr) (By similarity). 
Sequence information
Length: 514 AA [This is the length of the unprocessed precursor] Molecular weight: 56841 Da [This is the MW of the unprocessed precursor] CRC64: 6459AC46AD258336 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSRQWLFSTN HKDIGTLYFI FGAWAGMVGT SLSILIRAEL GHPGAFIGDD QIYNVIVTAH 

        70         80         90        100        110        120 
AFIMIFFMVM PIMIGGFGNW LVPLMLGAPD MAFPRMNNMS FWMLPPSLTL LISSSMVENG 

       130        140        150        160        170        180 
AGTGWTVYPP LSSGIAHAGA SVDLAIFSLH LAGISSILGA VNFITTVINM RSPGITLDRM 

       190        200        210        220        230        240 
PLFVWSVVIT AVLLLLSLPV LAGAITMLLT DRNLNTSFFD PAGGGDPILY QHLFWFFGHP 

       250        260        270        280        290        300 
EVYILILPGF GMISHIITQE SGKKETFGNL GMIYAMLAIG LLGFIVWAHH MFTVGMDVDT 

       310        320        330        340        350        360 
RAYFTSATMI IAVPTGIKIF SWLATLHGTQ LTYSPAMLWA FGFVFLFTVG GLTGVVLANS 

       370        380        390        400        410        420 
SIDIVLHDTY YVVAHFHYVL SMGAVFAIMA GFVHWYPLLT GLTMNPTWLK IQFSIMFVGV 

       430        440        450        460        470        480 
NLTFFPQHFL GLAGMPRRYS DFPDSYLTWN VVSSLGSTIS LFAILYFLFI IWESMITQRT 

       490        500        510 
PAFPMQLSSS IEWYHTLPPA EHTYAELPLL TNNF
P34838 in FASTA format

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