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P58710

- GGLO_MOUSE

UniProt

P58710 - GGLO_MOUSE

Protein

L-gulonolactone oxidase

Gene

Gulo

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.1 Publication

    Catalytic activityi

    L-gulono-1,4-lactone + O2 = L-ascorbate + H2O2.1 Publication

    Cofactori

    FAD.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. D-arabinono-1,4-lactone oxidase activity Source: InterPro
    2. flavin adenine dinucleotide binding Source: UniProtKB
    3. L-gulonolactone oxidase activity Source: UniProtKB
    4. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro

    GO - Biological processi

    1. L-ascorbic acid biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Ascorbate biosynthesis

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    UniPathwayiUPA00991; UER00939.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-gulonolactone oxidase (EC:1.1.3.8)
    Short name:
    LGO
    Alternative name(s):
    L-gulono-gamma-lactone oxidase
    Short name:
    GLO
    Gene namesi
    Name:Gulo
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1353434. Gulo.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 440439L-gulonolactone oxidasePRO_0000128159Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541Pros-8alpha-FAD histidineBy similarity

    Proteomic databases

    MaxQBiP58710.
    PaxDbiP58710.
    PRIDEiP58710.

    PTM databases

    PhosphoSiteiP58710.

    Expressioni

    Tissue specificityi

    Highly expressed in liver.1 Publication

    Gene expression databases

    BgeeiP58710.
    CleanExiMM_GULO.
    GenevestigatoriP58710.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000060912.

    Structurei

    3D structure databases

    ProteinModelPortaliP58710.
    SMRiP58710. Positions 33-207, 308-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei251 – 27323HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 187171FAD-binding PCMH-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0277.
    GeneTreeiENSGT00510000049722.
    HOGENOMiHOG000252847.
    HOVERGENiHBG005834.
    InParanoidiQ8K152.
    KOiK00103.
    OMAiYWFPHTD.
    OrthoDBiEOG7N8ZV8.
    TreeFamiTF328994.

    Family and domain databases

    Gene3Di3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    InterProiIPR007173. ALO.
    IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR010031. FAD_lactone_oxidase.
    IPR010032. FAD_linked_OxRdtase_bac.
    IPR023595. LGO_GLO.
    IPR006094. Oxid_FAD_bind_N.
    IPR006093. Oxy_OxRdtase_FAD_BS.
    [Graphical view]
    PfamiPF04030. ALO. 1 hit.
    PF01565. FAD_binding_4. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000136. LGO_GLO. 1 hit.
    SUPFAMiSSF56176. SSF56176. 1 hit.
    TIGRFAMsiTIGR01679. bact_FAD_ox. 1 hit.
    TIGR01678. FAD_lactone_ox. 1 hit.
    PROSITEiPS51387. FAD_PCMH. 1 hit.
    PS00862. OX2_COVAL_FAD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P58710-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVHGYKGVQF QNWAKTYGCS PEMYYQPTSV GEVREVLALA RQQNKKVKVV    50
    GGGHSPSDIA CTDGFMIHMG KMNRVLQVDK EKKQVTVEAG ILLTDLHPQL 100
    DKHGLALSNL GAVSDVTVGG VIGSGTHNTG IKHGILATQV VALTLMKADG 150
    TVLECSESSN ADVFQAARVH LGCLGVILTV TLQCVPQFHL LETSFPSTLK 200
    EVLDNLDSHL KKSEYFRFLW FPHSENVSII YQDHTNKEPS SASNWFWDYA 250
    IGFYLLEFLL WTSTYLPRLV GWINRFFFWL LFNCKKESSN LSHKIFSYEC 300
    RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL 350
    LSPCFQRDSC YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH 400
    NCTRKDFEKM YPAFHKFCDI REKLDPTGMF LNSYLEKVFY 440
    Length:440
    Mass (Da):50,478
    Last modified:July 27, 2011 - v3
    Checksum:iD109B480E08E773B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti160 – 1601N → K in AAH19856. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY453064 mRNA. Translation: AAR15891.1.
    AK077740 mRNA. Translation: BAC36988.1.
    AK167460 mRNA. Translation: BAE39545.1.
    BC019856 mRNA. Translation: AAH19856.1.
    BC028828 mRNA. Translation: AAH28828.1.
    CCDSiCCDS36958.1.
    RefSeqiNP_848862.1. NM_178747.3.
    XP_006519129.1. XM_006519066.1.
    UniGeneiMm.26207.

    Genome annotation databases

    EnsembliENSMUST00000059970; ENSMUSP00000060912; ENSMUSG00000034450.
    GeneIDi268756.
    KEGGimmu:268756.
    UCSCiuc007ujt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY453064 mRNA. Translation: AAR15891.1 .
    AK077740 mRNA. Translation: BAC36988.1 .
    AK167460 mRNA. Translation: BAE39545.1 .
    BC019856 mRNA. Translation: AAH19856.1 .
    BC028828 mRNA. Translation: AAH28828.1 .
    CCDSi CCDS36958.1.
    RefSeqi NP_848862.1. NM_178747.3.
    XP_006519129.1. XM_006519066.1.
    UniGenei Mm.26207.

    3D structure databases

    ProteinModelPortali P58710.
    SMRi P58710. Positions 33-207, 308-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000060912.

    PTM databases

    PhosphoSitei P58710.

    Proteomic databases

    MaxQBi P58710.
    PaxDbi P58710.
    PRIDEi P58710.

    Protocols and materials databases

    DNASUi 268756.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000059970 ; ENSMUSP00000060912 ; ENSMUSG00000034450 .
    GeneIDi 268756.
    KEGGi mmu:268756.
    UCSCi uc007ujt.1. mouse.

    Organism-specific databases

    CTDi 268756.
    MGIi MGI:1353434. Gulo.

    Phylogenomic databases

    eggNOGi COG0277.
    GeneTreei ENSGT00510000049722.
    HOGENOMi HOG000252847.
    HOVERGENi HBG005834.
    InParanoidi Q8K152.
    KOi K00103.
    OMAi YWFPHTD.
    OrthoDBi EOG7N8ZV8.
    TreeFami TF328994.

    Enzyme and pathway databases

    UniPathwayi UPA00991 ; UER00939 .

    Miscellaneous databases

    ChiTaRSi GULOP. mouse.
    NextBioi 392483.
    PROi P58710.
    SOURCEi Search...

    Gene expression databases

    Bgeei P58710.
    CleanExi MM_GULO.
    Genevestigatori P58710.

    Family and domain databases

    Gene3Di 3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    InterProi IPR007173. ALO.
    IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR010031. FAD_lactone_oxidase.
    IPR010032. FAD_linked_OxRdtase_bac.
    IPR023595. LGO_GLO.
    IPR006094. Oxid_FAD_bind_N.
    IPR006093. Oxy_OxRdtase_FAD_BS.
    [Graphical view ]
    Pfami PF04030. ALO. 1 hit.
    PF01565. FAD_binding_4. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000136. LGO_GLO. 1 hit.
    SUPFAMi SSF56176. SSF56176. 1 hit.
    TIGRFAMsi TIGR01679. bact_FAD_ox. 1 hit.
    TIGR01678. FAD_lactone_ox. 1 hit.
    PROSITEi PS51387. FAD_PCMH. 1 hit.
    PS00862. OX2_COVAL_FAD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional rescue of vitamin C synthesis deficiency in human cells using adenoviral-based expression of murine l-gulono-gamma-lactone oxidase."
      Ha M.N., Graham F.L., D'Souza C.K., Muller W.J., Igdoura S.A., Schellhorn H.E.
      Genomics 83:482-492(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY.
      Strain: C57BL/6.
      Tissue: Liver.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo and Placenta.
    3. "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].
      Strain: FVB/N.
      Tissue: Liver.
    4. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 318-324, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiGGLO_MOUSE
    AccessioniPrimary (citable) accession number: P58710
    Secondary accession number(s): Q8K152
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 116 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, 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