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Protein

Cytochrome c oxidase subunit 1

Gene

MT-CO1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Pathwayi: oxidative phosphorylation

This protein is involved in the pathway oxidative phosphorylation, which is part of Energy metabolism.
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
Metal bindingi61Iron (heme A axial ligand)1 Publication1
Metal bindingi240Copper B1 Publication1
Binding sitei244OxygenCurated1
Metal bindingi290Copper B1 Publication1
Metal bindingi291Copper B1 Publication1
Metal bindingi368Magnesium; shared with chain II1 Publication1
Metal bindingi376Iron (heme A3 axial ligand)1 Publication1
Metal bindingi378Iron (heme A axial ligand)1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.9.3.1. 908.
SABIO-RKP00396.
UniPathwayiUPA00705.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 1 (EC:1.9.3.1)
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene namesi
Name:MT-CO1
Synonyms:COI, COXI, MTCO1
Encoded oniMitochondrion
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Mitochondrion

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 11Mitochondrial matrix1 PublicationAdd BLAST11
Transmembranei12 – 40Helical; Name=IAdd BLAST29
Topological domaini41 – 50Mitochondrial intermembrane1 Publication10
Transmembranei51 – 86Helical; Name=IIAdd BLAST36
Topological domaini87 – 94Mitochondrial matrix1 Publication8
Transmembranei95 – 117Helical; Name=IIIAdd BLAST23
Topological domaini118 – 140Mitochondrial intermembrane1 PublicationAdd BLAST23
Transmembranei141 – 170Helical; Name=IVAdd BLAST30
Topological domaini171 – 182Mitochondrial matrix1 PublicationAdd BLAST12
Transmembranei183 – 212Helical; Name=VAdd BLAST30
Topological domaini213 – 227Mitochondrial intermembrane1 PublicationAdd BLAST15
Transmembranei228 – 261Helical; Name=VIAdd BLAST34
Topological domaini262 – 269Mitochondrial matrix1 Publication8
Transmembranei270 – 286Helical; Name=VIIAdd BLAST17
Topological domaini287 – 298Mitochondrial intermembrane1 PublicationAdd BLAST12
Transmembranei299 – 327Helical; Name=VIIIAdd BLAST29
Topological domaini328 – 335Mitochondrial matrix8
Transmembranei336 – 357Helical; Name=IXAdd BLAST22
Topological domaini358 – 370Mitochondrial intermembraneAdd BLAST13
Transmembranei371 – 400Helical; Name=XAdd BLAST30
Topological domaini401 – 406Mitochondrial matrix1 Publication6
Transmembranei407 – 433Helical; Name=XIAdd BLAST27
Topological domaini434 – 446Mitochondrial intermembraneAdd BLAST13
Transmembranei447 – 478Helical; Name=XIIAdd BLAST32
Topological domaini479 – 514Mitochondrial matrix1 PublicationAdd BLAST36

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001832941 – 514Cytochrome c oxidase subunit 1Add BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-formylmethionine1 Publication1
Cross-linki240 ↔ 2441'-histidyl-3'-tyrosine (His-Tyr)1 Publication

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

PaxDbiP00396.
PRIDEiP00396.

PTM databases

iPTMnetiP00396.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

DIPiDIP-60937N.
IntActiP00396. 1 interactor.
STRINGi9913.ENSBTAP00000053147.

Structurei

Secondary structure

1514
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 6Combined sources5
Helixi12 – 41Combined sources30
Beta strandi43 – 45Combined sources3
Beta strandi47 – 49Combined sources3
Helixi51 – 67Combined sources17
Helixi70 – 74Combined sources5
Turni75 – 77Combined sources3
Helixi78 – 86Combined sources9
Helixi95 – 103Combined sources9
Helixi105 – 117Combined sources13
Turni125 – 128Combined sources4
Turni130 – 133Combined sources4
Turni135 – 137Combined sources3
Helixi141 – 170Combined sources30
Helixi178 – 180Combined sources3
Helixi183 – 214Combined sources32
Helixi222 – 224Combined sources3
Helixi228 – 261Combined sources34
Helixi270 – 283Combined sources14
Helixi288 – 291Combined sources4
Helixi293 – 295Combined sources3
Helixi299 – 311Combined sources13
Helixi313 – 327Combined sources15
Helixi336 – 359Combined sources24
Helixi361 – 367Combined sources7
Helixi371 – 381Combined sources11
Turni382 – 384Combined sources3
Helixi385 – 401Combined sources17
Helixi407 – 433Combined sources27
Beta strandi437 – 439Combined sources3
Helixi445 – 447Combined sources3
Helixi448 – 478Combined sources31
Beta strandi481 – 484Combined sources4
Helixi488 – 490Combined sources3
Helixi492 – 494Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP00396.
SMRiP00396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00396.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4769. Eukaryota.
COG0843. LUCA.
HOGENOMiHOG000085274.
HOVERGENiHBG003841.
InParanoidiP00396.

Family and domain databases

CDDicd01663. Cyt_c_Oxidase_I. 1 hit.
Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023616. Cyt_c_oxase-like_su1_dom.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR033944. Cyt_c_oxase_su1_dom.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]

Sequencei

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
Checksum:i0D7C807D7FA3996C
GO

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.

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:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP00396.
SMRiP00396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60937N.
IntActiP00396. 1 interactor.
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.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG4769. Eukaryota.
COG0843. LUCA.
HOGENOMiHOG000085274.
HOVERGENiHBG003841.
InParanoidiP00396.

Enzyme and pathway databases

UniPathwayiUPA00705.
BRENDAi1.9.3.1. 908.
SABIO-RKP00396.

Miscellaneous databases

EvolutionaryTraceiP00396.

Family and domain databases

CDDicd01663. Cyt_c_Oxidase_I. 1 hit.
Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023616. Cyt_c_oxase-like_su1_dom.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR033944. Cyt_c_oxase_su1_dom.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOX1_BOVIN
AccessioniPrimary (citable) accession number: P00396
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.