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P05503

- COX1_RAT

UniProt

P05503 - COX1_RAT

Protein

Cytochrome c oxidase subunit 1

Gene

Mtco1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (01 Oct 1989)
      Previous versions | rss
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    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

    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

    Organism-specific databases

    RGDi621871. mt-Co1.

    Subcellular locationi

    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

    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...

    Transmembrane

    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

    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

    MFVNRWLFST NHKDIGTLYL LFGAWAGMVG TALSILIRAE LGQPGALLGD    50
    DQIYNVIVTA HAFVMIFFMV MPMMIGGFGN WLVPLMIGAP DMAFPRMNNM 100
    SFWLLPPSFL LLLASSMVEA GAGTGWTVYP PLAGNLAHAG VSVDLTIFSL 150
    HLAGVSSILG AINFITTIIN MKPPAMTQYQ TPLFVWSVLI TAVLLLLSLP 200
    VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH PEVYILILPG 250
    FGIISHVVTY YSGKKEPFGY MGMVWTMMSI GFLGFIVWAH HMFTVGLDVD 300
    TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMLW ALGFIFLFTV 350
    GGLTGIVLSN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AGFVHWFPLF 400
    SGYTLNDTWA KAHFAIMFVG VNMTFFPQHF LGLAGMPRRY SDYPDAYTTW 450
    NTVSSMGSFI SLTAVLVMIF MIWEAFASKR EVLSISYSST NLEWLHGCPP 500
    PYHTFEEPSY VKVK 514
    Length:514
    Mass (Da):56,937
    Last modified:October 1, 1989 - v2
    Checksum:i20BCE1C7857ED6FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51R → G in AAD15016. 1 PublicationCurated
    Sequence conflicti12 – 121H → P in AAD15016. 1 PublicationCurated
    Sequence conflicti44 – 441P → L in AAD15016. 1 PublicationCurated
    Sequence conflicti57 – 571I → L in AAD15016. 1 PublicationCurated
    Sequence conflicti216 – 2183NTT → EFP in AAB21298. (PubMed:1664046)Curated
    Sequence conflicti227 – 2271D → G in AAD15016. 1 PublicationCurated
    Sequence conflicti249 – 2491P → L in AAD15016. 1 PublicationCurated
    Sequence conflicti252 – 2521G → E in AAD15016. 1 PublicationCurated
    Sequence conflicti276 – 2761T → A in AAB21298. (PubMed:1664046)Curated
    Sequence conflicti392 – 3921G → C in AAD15016. 1 PublicationCurated
    Sequence conflicti392 – 3921G → C in AAB21298. (PubMed:1664046)Curated
    Sequence conflicti413 – 4131H → L in AAD15016. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14848 Genomic DNA. Translation: CAA32956.1.
    J01435 Genomic DNA. Translation: AAD15016.1.
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14848 Genomic DNA. Translation: CAA32956.1 .
    J01435 Genomic DNA. Translation: AAD15016.1 .
    V00676 Genomic DNA. Translation: CAA24046.1 .
    V00678 Genomic DNA. Translation: CAA24050.1 .
    S79304 mRNA. Translation: AAB21298.2 .
    PIRi S04749.
    RefSeqi AP_004894.1. AC_000022.2.

    3D structure databases

    ProteinModelPortali P05503.
    SMRi P05503. Positions 1-514.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P05503.
    PRIDEi P05503.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    RGDi 621871. mt-Co1.

    Phylogenomic databases

    eggNOGi COG0843.
    HOGENOMi HOG000085274.
    HOVERGENi HBG003841.
    InParanoidi P05503.
    PhylomeDBi P05503.

    Enzyme and pathway databases

    UniPathwayi UPA00705 .

    Miscellaneous databases

    NextBioi 35584672.
    PROi P05503.

    Gene expression databases

    Genevestigatori P05503.

    Family and domain databases

    Gene3Di 1.20.210.10. 1 hit.
    InterProi IPR000883. COX1.
    IPR023615. Cyt_c_Oxase_su1_BS.
    IPR023616. Cyt_c_Oxase_su1_dom.
    [Graphical view ]
    PANTHERi PTHR10422. PTHR10422. 1 hit.
    Pfami PF00115. COX1. 1 hit.
    [Graphical view ]
    PRINTSi PR01165. CYCOXIDASEI.
    SUPFAMi SSF81442. SSF81442. 1 hit.
    PROSITEi PS50855. COX1. 1 hit.
    PS00077. COX1_CUB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(1989) [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(1981)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Sprague-Dawley.
      Tissue: Liver.
    3. "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(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
    4. "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(1991) [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: November 1, 1988
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 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