Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-367110-01122
Entry Name
UniProt Accession
Theoretical PI
7.82
Molecular Weight
61522.15
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Cytochrome c oxidase subunit 1
Protein Synonyms/Alias
1.9.3.1; Cytochrome c oxidase polypeptide I;
Gene Name
cox-1
Gene Synonyms/Alias
coi; cox1; NCM025; NCU16016;
Created Date
23-OCT-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
324
Canonical
IAVPTGIKIFSWLAT
[1]
N-Myristoylation
Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS 1257 / FGSC 987)
NCBI Taxa ID
367110
Reference
[1] Vassilev AO, Plesofsky-Vig N, Brambl R. Cytochrome c oxidase in Neurosporacrassa contains myristic acid covalently linked to subunit 1. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8680-4.[PMID:7567996]
Functional Description
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Sequence Annotation
Transmembrane: 22 42 Helical.
Transmembrane: 69 89 Helical.
Transmembrane: 106 126 Helical.
Transmembrane: 151 171 Helical.
Transmembrane: 187 207 Helical.
Transmembrane: 240 260 Helical.
Transmembrane: 272 292 Helical.
Transmembrane: 310 330 Helical.
Transmembrane: 343 363 Helical.
Transmembrane: 378 398 Helical.
Transmembrane: 418 438 Helical.
Transmembrane: 457 477 Helical.
Metal binding site: 67 67 Iron (heme A axial ligand).
Metal binding site: 246 246 Copper B.
Metal binding site: 250 250 Copper B.
Metal binding site: 295 295 Copper B.
Metal binding site: 296 296 Copper B.
Metal binding site: 381 381 Iron (heme A3 axial ligand).
Metal binding site: 383 383 Iron (heme A axial ligand).
Protein Length
557 AA.
Protein Sequence
(Canonical)
MSSISIWTER WFLSTNAKDI GVLYLIFALF SGLLGTAFSV LIRMELSGPG VQYIADNQLY  60
NAIITAHAIL MIFFMVMPAL IGGFGNFLLP LLVGGPDMAF PRLNNISFWL LPPSLLLLVF  120
SACIEGGAGT GWTIYPPLSG VQSHSGPSVD LAIFALHLSG VSSLLGSINF ITTIVNMRTP  180
GIRLHKLALF GWAVVITAVL LLLSLPVLAG AITMLLTDRN FNTSFFETAG GGDPILFQHL  240
FWFFGHPEVY ILIIPGFGII STTISAYSNK SVFGYIGMVY AMMSIGILGF IVWSHHMYTV  300
GLDVDTRAYF TAATLIIAVP TGIKIFSWLA TCYGGSIRLT PSMLFALGFV FMFTIGGLSG  360
VVLANASLDI AFHDTYYVVA HFHYVLSMGA VFAMFSGWYH WVPKILGLNY NMVLSKAQFW  420
LLFIGVNLTF FPQHFLGLQG MPRRISDYPD AFSGWNLISS FGSIVSVVAS WLFLYIVYIQ  480
LVQGEYAGRY PWSIPQFYTD SLRALLNRSY PSLEWSISSP PKPHSFVSLP LQSSSFFLSF  540
FRLSSYGEQK EISGRQN                                                 557
FASTA
(Canonical)
>LipidDB-367110-01122|P03945
MSSISIWTERWFLSTNAKDIGVLYLIFALFSGLLGTAFSVLIRMELSGPGVQYIADNQLY
NAIITAHAILMIFFMVMPALIGGFGNFLLPLLVGGPDMAFPRLNNISFWLLPPSLLLLVF
SACIEGGAGTGWTIYPPLSGVQSHSGPSVDLAIFALHLSGVSSLLGSINFITTIVNMRTP
GIRLHKLALFGWAVVITAVLLLLSLPVLAGAITMLLTDRNFNTSFFETAGGGDPILFQHL
FWFFGHPEVYILIIPGFGIISTTISAYSNKSVFGYIGMVYAMMSIGILGFIVWSHHMYTV
GLDVDTRAYFTAATLIIAVPTGIKIFSWLATCYGGSIRLTPSMLFALGFVFMFTIGGLSG
VVLANASLDIAFHDTYYVVAHFHYVLSMGAVFAMFSGWYHWVPKILGLNYNMVLSKAQFW
LLFIGVNLTFFPQHFLGLQGMPRRISDYPDAFSGWNLISSFGSIVSVVASWLFLYIVYIQ
LVQGEYAGRYPWSIPQFYTDSLRALLNRSYPSLEWSISSPPKPHSFVSLPLQSSSFFLSF
FRLSSYGEQKEISGRQN
Gene Ontology
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW
GO:0070469; C:respiratory chain; IEA:UniProtKB-KW
GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC
GO:0020037; F:heme binding; IEA:InterPro
GO:0005506; F:iron ion binding; IEA:InterPro
GO:0009060; P:aerobic respiration; IEA:InterPro
GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway
Interpro
InterPro; IPR000883; COX1
InterPro; IPR023615; Cyt_c_Oxase_su1_BS
InterPro; IPR023616; Cyt_c_Oxase_su1_dom
Pfam
Pfam; PF00115; COX1;
SMART
PROSITE
PROSITE; PS50855; COX1;
PROSITE; PS00077; COX1_CUB;
PRINTS
PRINTS; PR01165; CYCOXIDASEI;