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Protein

Cytochrome c oxidase subunit 1

Gene

Mtco1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611Iron (heme A axial ligand)Curated
Metal bindingi240 – 2401Copper BCurated
Metal bindingi244 – 2441Copper BCurated
Metal bindingi290 – 2901Copper BCurated
Metal bindingi291 – 2911Copper BCurated
Metal bindingi376 – 3761Iron (heme A3 axial ligand)Curated
Metal bindingi378 – 3781Iron (heme A axial ligand)Curated

GO - Molecular functioni

  1. cytochrome-c oxidase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. aerobic respiration Source: InterPro
  2. aging Source: RGD
  3. cerebellum development Source: RGD
  4. hydrogen ion transmembrane transport Source: GOC
  5. oxidative phosphorylation Source: UniProtKB-UniPathway
  6. response to copper ion Source: RGD
  7. response to electrical stimulus Source: RGD
  8. response to oxidative stress Source: RGD
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

UniPathwayiUPA00705.

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:Mtco1
Synonyms:Coi, mt-Co1
Encoded oniMitochondrion
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Mitochondrion

Organism-specific databases

RGDi621871. mt-Co1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei17 – 3721HelicalSequence AnalysisAdd
BLAST
Transmembranei56 – 7621HelicalSequence AnalysisAdd
BLAST
Transmembranei102 – 12221HelicalSequence AnalysisAdd
BLAST
Transmembranei145 – 16521HelicalSequence AnalysisAdd
BLAST
Transmembranei183 – 20321HelicalSequence AnalysisAdd
BLAST
Transmembranei234 – 25421HelicalSequence AnalysisAdd
BLAST
Transmembranei268 – 28821HelicalSequence AnalysisAdd
BLAST
Transmembranei310 – 33021HelicalSequence AnalysisAdd
BLAST
Transmembranei338 – 35821HelicalSequence AnalysisAdd
BLAST
Transmembranei380 – 40021HelicalSequence AnalysisAdd
BLAST
Transmembranei414 – 43421HelicalSequence AnalysisAdd
BLAST
Transmembranei456 – 47621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: UniProtKB-SubCell
  3. mitochondrion Source: RGD
  4. respiratory chain complex IV Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 514514Cytochrome c oxidase subunit 1PRO_0000183406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki240 ↔ 2441'-histidyl-3'-tyrosine (His-Tyr)By similarity

Proteomic databases

PaxDbiP05503.
PRIDEiP05503.

Expressioni

Gene expression databases

GenevestigatoriP05503.

Structurei

3D structure databases

ProteinModelPortaliP05503.
SMRiP05503. Positions 1-514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0843.
HOGENOMiHOG000085274.
HOVERGENiHBG003841.
InParanoidiP05503.
PhylomeDBiP05503.

Family and domain databases

Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. 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.

P05503-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVNRWLFST NHKDIGTLYL LFGAWAGMVG TALSILIRAE LGQPGALLGD
60 70 80 90 100
DQIYNVIVTA HAFVMIFFMV MPMMIGGFGN WLVPLMIGAP DMAFPRMNNM
110 120 130 140 150
SFWLLPPSFL LLLASSMVEA GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL
160 170 180 190 200
HLAGVSSILG AINFITTIIN MKPPAMTQYQ TPLFVWSVLI TAVLLLLSLP
210 220 230 240 250
VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH PEVYILILPG
260 270 280 290 300
FGIISHVVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGLDVD
310 320 330 340 350
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMLW ALGFIFLFTV
360 370 380 390 400
GGLTGIVLSN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AGFVHWFPLF
410 420 430 440 450
SGYTLNDTWA KAHFAIMFVG VNMTFFPQHF LGLAGMPRRY SDYPDAYTTW
460 470 480 490 500
NTVSSMGSFI SLTAVLVMIF MIWEAFASKR EVLSISYSST NLEWLHGCPP
510
PYHTFEEPSY VKVK
Length:514
Mass (Da):56,845
Last modified:March 31, 2015 - v3
Checksum:i68FF852A1E7D6D70
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21L → F in CAA32956 (PubMed:2504926).Curated
Sequence conflicti2 – 21L → F in AAD15016 (Ref. 2) Curated
Sequence conflicti2 – 21L → F in CAA24046 (PubMed:6300770).Curated
Sequence conflicti5 – 51R → G in AAD15016 (Ref. 2) Curated
Sequence conflicti12 – 121H → P in AAD15016 (Ref. 2) Curated
Sequence conflicti44 – 441P → L in AAD15016 (Ref. 2) Curated
Sequence conflicti57 – 571I → L in AAD15016 (Ref. 2) Curated
Sequence conflicti141 – 1411A → V in CAA32956 (PubMed:2504926).Curated
Sequence conflicti141 – 1411A → V in AAD15016 (Ref. 2) Curated
Sequence conflicti216 – 2183NTT → EFP in AAB21298 (PubMed:1664046).Curated
Sequence conflicti227 – 2271D → G in AAD15016 (Ref. 2) Curated
Sequence conflicti249 – 2491P → L in AAD15016 (Ref. 2) Curated
Sequence conflicti252 – 2521G → E in AAD15016 (Ref. 2) Curated
Sequence conflicti276 – 2761A → T in CAA32956 (PubMed:2504926).Curated
Sequence conflicti276 – 2761A → T in AAD15016 (Ref. 2) Curated
Sequence conflicti392 – 3921G → C in AAD15016 (Ref. 2) Curated
Sequence conflicti392 – 3921G → C in AAB21298 (PubMed:1664046).Curated
Sequence conflicti413 – 4131H → L in AAD15016 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14848 Genomic DNA. Translation: CAA32956.1.
J01435 Genomic DNA. Translation: AAD15016.1.
AY172581 Genomic DNA. Translation: AAN77596.1.
V00676 Genomic DNA. Translation: CAA24046.1.
V00678 Genomic DNA. Translation: CAA24050.1.
S79304 mRNA. Translation: AAB21298.2.
PIRiS04749.
RefSeqiAP_004894.1. AC_000022.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14848 Genomic DNA. Translation: CAA32956.1.
J01435 Genomic DNA. Translation: AAD15016.1.
AY172581 Genomic DNA. Translation: AAN77596.1.
V00676 Genomic DNA. Translation: CAA24046.1.
V00678 Genomic DNA. Translation: CAA24050.1.
S79304 mRNA. Translation: AAB21298.2.
PIRiS04749.
RefSeqiAP_004894.1. AC_000022.2.

3D structure databases

ProteinModelPortaliP05503.
SMRiP05503. Positions 1-514.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiP05503.
PRIDEiP05503.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi621871. mt-Co1.

Phylogenomic databases

eggNOGiCOG0843.
HOGENOMiHOG000085274.
HOVERGENiHBG003841.
InParanoidiP05503.
PhylomeDBiP05503.

Enzyme and pathway databases

UniPathwayiUPA00705.

Miscellaneous databases

NextBioi35584672.
PROiP05503.

Gene expression databases

GenevestigatoriP05503.

Family and domain databases

Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. 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...

Publicationsi

« Hide 'large scale' publications
  1. "The complete nucleotide sequence of the Rattus norvegicus mitochondrial genome: cryptic signals revealed by comparative analysis between vertebrates."
    Gadaleta G., Pepe G., de Candia G., Quagliariello C., Sbisa E., Saccone C.
    J. Mol. Evol. 28:497-516(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
  2. "Analysis of a DNA segment from rat liver mitochondria containing the genes for the cytochrome oxidase subunits I, II, II, ATPase subunit 6, and several tRNA genes."
    Grosskopf R., Feldmann H.
    Curr. Genet. 4:151-158(1980)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. "Tumor-associated mutations of rat mitochondrial transfer RNA genes."
    Taira M., Yoshida E., Kobayashi M., Yaginuma K., Koike K.
    Nucleic Acids Res. 11:1635-1643(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
  5. "Hormonal regulation of cytochrome oxidase subunit messenger RNAs in rat Sertoli cells."
    Ku C.Y., Lu Q., Ussuf K.K., Weinstock G.M., Sanborn B.M.
    Mol. Endocrinol. 5:1669-1676(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 216-514.
    Tissue: Sertoli cell.

Entry informationi

Entry nameiCOX1_RAT
AccessioniPrimary (citable) accession number: P05503
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1988
Last sequence update: March 31, 2015
Last modified: March 31, 2015
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.