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P36552

- HEM6_MOUSE

UniProt

P36552 - HEM6_MOUSE

Protein

Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Gene

Cpox

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (21 Jun 2004)
      Previous versions | rss
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    Functioni

    Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX By similarity.By similarity

    Catalytic activityi

    Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei233 – 2331SubstrateBy similarity
    Active sitei247 – 2471Proton donorBy similarity
    Sitei316 – 3161Important for dimerizationBy similarity

    GO - Molecular functioni

    1. coproporphyrinogen oxidase activity Source: MGI
    2. protein homodimerization activity Source: UniProtKB
    3. sodium:potassium-exchanging ATPase activity Source: MGI
    4. structural constituent of eye lens Source: MGI

    GO - Biological processi

    1. heme biosynthetic process Source: MGI
    2. potassium ion transport Source: MGI
    3. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
    4. response to arsenic-containing substance Source: Ensembl
    5. response to insecticide Source: Ensembl
    6. response to iron ion Source: Ensembl
    7. response to lead ion Source: Ensembl
    8. response to methylmercury Source: Ensembl
    9. sodium ion transmembrane transport Source: GOC
    10. sodium ion transport Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Heme biosynthesis, Porphyrin biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_203298. Heme biosynthesis.
    UniPathwayiUPA00251; UER00322.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial (EC:1.3.3.3)
    Short name:
    COX
    Short name:
    Coprogen oxidase
    Short name:
    Coproporphyrinogenase
    Gene namesi
    Name:Cpox
    Synonyms:Cpo
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:104841. Cpox.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. mitochondrial intermembrane space Source: UniProtKB-SubCell
    3. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 9898Mitochondrion1 PublicationAdd
    BLAST
    Chaini99 – 443345Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrialPRO_0000006030Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei393 – 3931N6-acetyllysine; alternate1 Publication
    Modified residuei393 – 3931N6-succinyllysine; alternate1 Publication

    Post-translational modificationi

    Acetylation of Lys-360 is observed in liver mitochondria from fasted mice but not from fed mice.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP36552.
    PaxDbiP36552.
    PRIDEiP36552.

    PTM databases

    PhosphoSiteiP36552.

    Expressioni

    Tissue specificityi

    Erythroid cells and non erythroid cells such as liver.

    Gene expression databases

    ArrayExpressiP36552.
    BgeeiP36552.
    CleanExiMM_CPOX.
    GenevestigatoriP36552.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiP36552. 1 interaction.
    MINTiMINT-1844590.

    Structurei

    3D structure databases

    ProteinModelPortaliP36552.
    SMRiP36552. Positions 110-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni182 – 19110Important for dimerizationBy similarity
    Regioni249 – 2513Substrate bindingBy similarity
    Regioni381 – 41737Important for dimerizationBy similarityAdd
    BLAST
    Regioni400 – 4056Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0408.
    GeneTreeiENSGT00390000017311.
    HOGENOMiHOG000262768.
    HOVERGENiHBG051897.
    InParanoidiP36552.
    KOiK00228.
    OMAiRYFETAN.
    OrthoDBiEOG7BZVSG.
    PhylomeDBiP36552.
    TreeFamiTF300703.

    Family and domain databases

    Gene3Di3.40.1500.10. 1 hit.
    InterProiIPR001260. Coprogen_oxidase_aer.
    IPR018375. Coprogen_oxidase_CS.
    [Graphical view]
    PANTHERiPTHR10755. PTHR10755. 1 hit.
    PfamiPF01218. Coprogen_oxidas. 1 hit.
    [Graphical view]
    PRINTSiPR00073. COPRGNOXDASE.
    SUPFAMiSSF102886. SSF102886. 1 hit.
    PROSITEiPS01021. COPROGEN_OXIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P36552-1 [UniParc]FASTAAdd to Basket

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    MALRLGRLGS DPWWRAVLGD YAQLRAASPR CASARVCQLP GTAGPQPRRG    50
    LGYGPWARGG SGLGTRLAAT LAGLAGLAAA AFGHVQRAEM VPKSSGARSP 100
    SPGRREEDGD ELARRCSTFM SSPVTELREL RRRPEDMKTK MELMIMETQA 150
    QVCRALAQVD GVADFTVDRW ERKEGGGGIT CVLQDGRVFE KAGVSISVVH 200
    GNLSEEAANQ MRGRGKTLKT KDSKLPFTAM GVSSVIHPKN PYAPTMHFNY 250
    RYFEVEEADG NTHWWFGGGC DLTPTYLNQE DAVHFHRTLK EACDQHGPDI 300
    YPKFKKWCDD YFFIVHRGER RGIGGIFFDD LDSPSKEEAF RFVKTCAEAV 350
    VPSYVPIVKK HCDDSYTPRD KLWQQLRRGR YVEFNLLYDR GTKFGLFTPG 400
    SRIESILMSL PLTARWEYMH SPPENSKEAE ILEVLRHPKD WVH 443
    Length:443
    Mass (Da):49,715
    Last modified:June 21, 2004 - v2
    Checksum:i9F3D5E8E420645F0
    GO

    Sequence cautioni

    The sequence BAA03840.1 differs from that shown. Reason: Frameshift at positions 22, 43 and 76.
    The sequence AAH17680.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71R → P in BAA03840. (PubMed:8407975)Curated
    Sequence conflicti101 – 1011S → T AA sequence (PubMed:8159699)Curated
    Sequence conflicti116 – 1172CS → SD AA sequence (PubMed:8159699)Curated
    Sequence conflicti122 – 1221S → T AA sequence (PubMed:8159699)Curated
    Sequence conflicti124 – 1241V → P AA sequence (PubMed:8159699)Curated
    Sequence conflicti138 – 1381K → N in BAC79229. (PubMed:15482256)Curated
    Sequence conflicti275 – 2751T → R in BAA03840. (PubMed:8407975)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16333 mRNA. Translation: BAA03840.1. Frameshift.
    BC017680 mRNA. Translation: AAH17680.2. Different initiation.
    AY382578 Genomic DNA. Translation: AAQ88103.1.
    AB099924 Genomic DNA. Translation: BAC79229.1.
    CCDSiCCDS49878.1.
    PIRiA48049.
    RefSeqiNP_031783.2. NM_007757.2.
    UniGeneiMm.291519.

    Genome annotation databases

    EnsembliENSMUST00000060077; ENSMUSP00000055455; ENSMUSG00000022742.
    GeneIDi12892.
    KEGGimmu:12892.
    UCSCiuc007znz.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16333 mRNA. Translation: BAA03840.1 . Frameshift.
    BC017680 mRNA. Translation: AAH17680.2 . Different initiation.
    AY382578 Genomic DNA. Translation: AAQ88103.1 .
    AB099924 Genomic DNA. Translation: BAC79229.1 .
    CCDSi CCDS49878.1.
    PIRi A48049.
    RefSeqi NP_031783.2. NM_007757.2.
    UniGenei Mm.291519.

    3D structure databases

    ProteinModelPortali P36552.
    SMRi P36552. Positions 110-442.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P36552. 1 interaction.
    MINTi MINT-1844590.

    PTM databases

    PhosphoSitei P36552.

    Proteomic databases

    MaxQBi P36552.
    PaxDbi P36552.
    PRIDEi P36552.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000060077 ; ENSMUSP00000055455 ; ENSMUSG00000022742 .
    GeneIDi 12892.
    KEGGi mmu:12892.
    UCSCi uc007znz.2. mouse.

    Organism-specific databases

    CTDi 1371.
    MGIi MGI:104841. Cpox.

    Phylogenomic databases

    eggNOGi COG0408.
    GeneTreei ENSGT00390000017311.
    HOGENOMi HOG000262768.
    HOVERGENi HBG051897.
    InParanoidi P36552.
    KOi K00228.
    OMAi RYFETAN.
    OrthoDBi EOG7BZVSG.
    PhylomeDBi P36552.
    TreeFami TF300703.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00322 .
    Reactomei REACT_203298. Heme biosynthesis.

    Miscellaneous databases

    ChiTaRSi CPOX. mouse.
    NextBioi 282498.
    PROi P36552.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36552.
    Bgeei P36552.
    CleanExi MM_CPOX.
    Genevestigatori P36552.

    Family and domain databases

    Gene3Di 3.40.1500.10. 1 hit.
    InterProi IPR001260. Coprogen_oxidase_aer.
    IPR018375. Coprogen_oxidase_CS.
    [Graphical view ]
    PANTHERi PTHR10755. PTHR10755. 1 hit.
    Pfami PF01218. Coprogen_oxidas. 1 hit.
    [Graphical view ]
    PRINTSi PR00073. COPRGNOXDASE.
    SUPFAMi SSF102886. SSF102886. 1 hit.
    PROSITEi PS01021. COPROGEN_OXIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation."
      Kohno H., Furukawa T., Yoshinaga T., Tokunaga R., Taketani S.
      J. Biol. Chem. 268:21359-21363(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    3. "Examination of mitochondrial protein targeting of haem synthetic enzymes: in vivo identification of three functional haem-responsive motifs in 5-aminolaevulinate synthase."
      Dailey T.A., Woodruff J.H., Dailey H.A.
      Biochem. J. 386:381-386(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139.
    4. "The long, but not the short, presequence of human coproporphyrinogen oxidase is essential for its import and sorting to mitochondria."
      Susa S., Daimon M., Ono H., Li S., Yoshida T., Kato T.
      Tohoku J. Exp. Med. 200:39-45(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144.
    5. "Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase."
      Martasek P., Camadro J.-M., Delfau-Larue M.H., Dumas J.B., Montagne J.J., de Verneuil H., Labbe P., Grandchamp B.
      Proc. Natl. Acad. Sci. U.S.A. 91:3024-3028(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 99-125 AND 248-258.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiHEM6_MOUSE
    AccessioniPrimary (citable) accession number: P36552
    Secondary accession number(s): Q7TQ36, Q8VD08
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 21, 2004
    Last modified: October 1, 2014
    This is version 130 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, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3