Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 161 (22 Apr 2020)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Cytochrome c oxidase subunit 1

Gene

MT-CO1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: oxidative phosphorylation

This protein is involved in the pathway oxidative phosphorylation, which is part of Energy metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway oxidative phosphorylation and in Energy metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi40Sodium or calcium1 Publication1 Publication1
Metal bindingi45Sodium or calcium; via carbonyl oxygen1 Publication1 Publication1
Metal bindingi61Iron 1 (low-spin heme A axial ligand); via tele nitrogen2 Publications1
Metal bindingi240Copper B; via pros nitrogen2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei244OxygenCurated1
Metal bindingi290Copper B; via tele nitrogen2 Publications1
Metal bindingi291Copper B; via tele nitrogen2 Publications1
Metal bindingi368Magnesium; shared with MT-CO22 Publications1
Metal bindingi369Magnesium; shared with MT-CO22 Publications1
Metal bindingi376Iron 2 (high-spin heme A3 axial ligand); via tele nitrogen2 Publications1
Metal bindingi378Iron 1 (low-spin heme A axial ligand); via tele nitrogen2 Publications1
Metal bindingi441Sodium or calcium; via carbonyl oxygen1 Publication1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTranslocase
Biological processElectron transport, Respiratory chain, Transport
LigandCalcium, Copper, Heme, Iron, Magnesium, Metal-binding, Sodium

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.9.3.1 908

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00396

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00705

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.D.4.7.1 the proton-translocating cytochrome oxidase (cox) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cytochrome c oxidase subunit 1 (EC:7.1.1.9)
Alternative name(s):
Cytochrome c oxidase polypeptide I
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MT-CO1
Synonyms:COI, COXI, MTCO1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniMitochondrion
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Mitochondrion

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 11Mitochondrial matrix2 PublicationsAdd BLAST11
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei12 – 40Helical; Name=I1 PublicationAdd BLAST29
Topological domaini41 – 50Mitochondrial intermembrane2 Publications10
Transmembranei51 – 86Helical; Name=II1 PublicationAdd BLAST36
Topological domaini87 – 94Mitochondrial matrix2 Publications8
Transmembranei95 – 117Helical; Name=III1 PublicationAdd BLAST23
Topological domaini118 – 140Mitochondrial intermembrane2 PublicationsAdd BLAST23
Transmembranei141 – 170Helical; Name=IV1 PublicationAdd BLAST30
Topological domaini171 – 182Mitochondrial matrix2 PublicationsAdd BLAST12
Transmembranei183 – 212Helical; Name=V1 PublicationAdd BLAST30
Topological domaini213 – 227Mitochondrial intermembrane2 PublicationsAdd BLAST15
Transmembranei228 – 261Helical; Name=VI1 PublicationAdd BLAST34
Topological domaini262 – 269Mitochondrial matrix2 Publications8
Transmembranei270 – 286Helical; Name=VII1 PublicationAdd BLAST17
Topological domaini287 – 298Mitochondrial intermembrane2 PublicationsAdd BLAST12
Transmembranei299 – 327Helical; Name=VIII1 PublicationAdd BLAST29
Topological domaini328 – 335Mitochondrial matrix1 Publication8
Transmembranei336 – 357Helical; Name=IX1 PublicationAdd BLAST22
Topological domaini358 – 370Mitochondrial intermembrane1 PublicationAdd BLAST13
Transmembranei371 – 400Helical; Name=X1 PublicationAdd BLAST30
Topological domaini401 – 406Mitochondrial matrix2 Publications6
Transmembranei407 – 433Helical; Name=XI1 PublicationAdd BLAST27
Topological domaini434 – 446Mitochondrial intermembrane1 PublicationAdd BLAST13
Transmembranei447 – 478Helical; Name=XII1 PublicationAdd BLAST32
Topological domaini479 – 514Mitochondrial matrix2 PublicationsAdd BLAST36

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001832941 – 514Cytochrome c oxidase subunit 1Add BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-formylmethionine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki240 ↔ 2441'-histidyl-3'-tyrosine (His-Tyr)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

His-240 and Tyr-244 are involved in the formation of a copper-coordinated covalent cross-link at the active site of the catalytic subunit I.

Keywords - PTMi

Formylation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P00396

PRoteomics IDEntifications database

More...
PRIDEi
P00396

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00396

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 14 subunits. The complex is composed of a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in the mitochondrial DNA, and 11 supernumerary subunits COX4I1 (or COX4I2), COX5A, COX5B, COX6A2 (or COX6A1), COX6B1 (or COX6B2), COX6C, COX7A1 (or COX7A2), COX7B, COX7C, COX8B and NDUFA4, which are encoded in the nuclear genome (PubMed:8638158). The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in different assemblies (supercomplex SCI1III2IV1 and megacomplex MCI2III2IV2) (PubMed:26698328, PubMed:27830641). As a newly synthesized protein, rapidly incorporates into a multi-subunit assembly intermediate in the inner membrane, called MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase) complex, whose core components are COA3/MITRAC12 and COX14. Within the MITRAC complex, interacts with COA3 and with SMIM20/MITRAC7; the interaction with SMIM20 stabilizes the newly synthesized MT-CO1 and prevents its premature turnover.

Interacts with TMEM177 in a COX20-dependent manner (By similarity).

By similarity3 Publications

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P00396

Database of interacting proteins

More...
DIPi
DIP-60937N

Protein interaction database and analysis system

More...
IntActi
P00396, 13 interactors

Molecular INTeraction database

More...
MINTi
P00396

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000053147

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1514
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P00396

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00396

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4769 Eukaryota
COG0843 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00396

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01663 Cyt_c_Oxidase_I, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.210.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023616 Cyt_c_oxase-like_su1_dom
IPR036927 Cyt_c_oxase-like_su1_sf
IPR000883 Cyt_C_Oxase_1
IPR023615 Cyt_c_Oxase_su1_BS
IPR033944 Cyt_c_oxase_su1_dom

The PANTHER Classification System

More...
PANTHERi
PTHR10422 PTHR10422, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00115 COX1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01165 CYCOXIDASEI

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81442 SSF81442, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50855 COX1, 1 hit
PS00077 COX1_CUB, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P00396-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFINRWLFST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLLGD
60 70 80 90 100
DQIYNVVVTA HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM
110 120 130 140 150
SFWLLPPSFL LLLASSMVEA GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL
160 170 180 190 200
HLAGVSSILG AINFITTIIN MKPPAMSQYQ TPLFVWSVMI TAVLLLLSLP
210 220 230 240 250
VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH PEVYILILPG
260 270 280 290 300
FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD
310 320 330 340 350
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMMW ALGFIFLFTV
360 370 380 390 400
GGLTGIVLAN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFVHWFPLF
410 420 430 440 450
SGYTLNDTWA KIHFAIMFVG VNMTFFPQHF LGLSGMPRRY SDYPDAYTMW
460 470 480 490 500
NTISSMGSFI SLTAVMLMVF IIWEAFASKR EVLTVDLTTT NLEWLNGCPP
510
PYHTFEEPTY VNLK
Length:514
Mass (Da):57,032
Last modified:July 21, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0D7C807D7FA3996C
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
V00654 Genomic DNA Translation: CAA23999.1
AF490528 Genomic DNA Translation: AAM08330.1
AF490529 Genomic DNA Translation: AAM08343.1
AF493541 Genomic DNA Translation: AAM12791.1
AF493542 Genomic DNA Translation: AAM12804.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A00464 ODBO1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00654 Genomic DNA Translation: CAA23999.1
AF490528 Genomic DNA Translation: AAM08330.1
AF490529 Genomic DNA Translation: AAM08343.1
AF493541 Genomic DNA Translation: AAM12791.1
AF493542 Genomic DNA Translation: AAM12804.1
PIRiA00464 ODBO1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OCCX-ray2.80A/N1-514[»]
1OCOX-ray2.80A/N1-514[»]
1OCRX-ray2.35A/N1-514[»]
1OCZX-ray2.90A/N1-514[»]
1V54X-ray1.80A/N1-514[»]
1V55X-ray1.90A/N1-514[»]
2DYRX-ray1.80A/N1-514[»]
2DYSX-ray2.20A/N1-514[»]
2EIJX-ray1.90A/N1-514[»]
2EIKX-ray2.10A/N1-514[»]
2EILX-ray2.10A/N1-514[»]
2EIMX-ray2.60A/N1-514[»]
2EINX-ray2.70A/N1-514[»]
2OCCX-ray2.30A/N1-514[»]
2Y69X-ray1.95A/N1-514[»]
2YBBelectron microscopy19.00L1-514[»]
2ZXWX-ray2.50A/N1-514[»]
3ABKX-ray2.00A/N1-514[»]
3ABLX-ray2.10A/N1-514[»]
3ABMX-ray1.95A/N1-514[»]
3AG1X-ray2.20A/N1-514[»]
3AG2X-ray1.80A/N1-514[»]
3AG3X-ray1.80A/N1-514[»]
3AG4X-ray2.05A/N1-514[»]
3ASNX-ray3.00A/N1-514[»]
3ASOX-ray2.30A/N1-514[»]
3WG7X-ray1.90A/N1-514[»]
3X2QX-ray2.00A/N1-514[»]
5B1AX-ray1.50A/N1-514[»]
5B1BX-ray1.60A/N1-514[»]
5B3SX-ray1.68A/N2-514[»]
5GPNelectron microscopy5.40y1-514[»]
5IY5X-ray2.00A/N1-514[»]
5LUFelectron microscopy9.10x1-514[»]
5W97X-ray2.30A/a1-514[»]
5WAUX-ray1.95A/a1-514[»]
5X19X-ray2.20A/N1-514[»]
5X1BX-ray2.40A/N1-514[»]
5X1FX-ray2.20A/N1-514[»]
5XDQX-ray1.77A/N1-514[»]
5XDXX-ray1.99A/N1-514[»]
5XTHelectron microscopy3.90x1-514[»]
5XTIelectron microscopy17.40Bx/x1-514[»]
5Z84X-ray1.85A/N1-514[»]
5Z85X-ray1.85A/N1-514[»]
5Z86X-ray1.85A/N1-514[»]
5ZCOX-ray1.90A/N1-514[»]
5ZCPX-ray1.65A/N1-514[»]
5ZCQX-ray1.65A/N1-514[»]
6J8MX-ray1.90A/N1-514[»]
6JY3X-ray1.85A1-514[»]
6JY4X-ray1.95A1-514[»]
6NKNX-ray2.50A/N1-514[»]
6NMFX-ray2.80A/N1-514[»]
6NMPX-ray2.90A/N1-514[»]
SMRiP00396
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

CORUMiP00396
DIPiDIP-60937N
IntActiP00396, 13 interactors
MINTiP00396
STRINGi9913.ENSBTAP00000053147

Protein family/group databases

TCDBi3.D.4.7.1 the proton-translocating cytochrome oxidase (cox) superfamily

PTM databases

iPTMnetiP00396

Proteomic databases

PaxDbiP00396
PRIDEiP00396

Phylogenomic databases

eggNOGiKOG4769 Eukaryota
COG0843 LUCA
InParanoidiP00396

Enzyme and pathway databases

UniPathwayiUPA00705
BRENDAi1.9.3.1 908
SABIO-RKiP00396

Miscellaneous databases

EvolutionaryTraceiP00396

Family and domain databases

CDDicd01663 Cyt_c_Oxidase_I, 1 hit
Gene3Di1.20.210.10, 1 hit
InterProiView protein in InterPro
IPR023616 Cyt_c_oxase-like_su1_dom
IPR036927 Cyt_c_oxase-like_su1_sf
IPR000883 Cyt_C_Oxase_1
IPR023615 Cyt_c_Oxase_su1_BS
IPR033944 Cyt_c_oxase_su1_dom
PANTHERiPTHR10422 PTHR10422, 1 hit
PfamiView protein in Pfam
PF00115 COX1, 1 hit
PRINTSiPR01165 CYCOXIDASEI
SUPFAMiSSF81442 SSF81442, 1 hit
PROSITEiView protein in PROSITE
PS50855 COX1, 1 hit
PS00077 COX1_CUB, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCOX1_BOVIN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00396
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 22, 2020
This is version 161 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again