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Protein

L-gulonolactone oxidase

Gene

Gulo

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

FAD1 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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Ascorbate biosynthesis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.1.3.8. 3474.
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 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1353434. Gulo.

Subcellular locationi

Topology

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

GO - Cellular componenti

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

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.
ExpressionAtlasiP58710. baseline and differential.
GenevestigatoriP58710.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000060912.

Structurei

3D structure databases

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

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.
InParanoidiP58710.
KOiK00103.
OMAiMDCLFSQ.
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.
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.
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

        10         20         30         40         50
MVHGYKGVQF QNWAKTYGCS PEMYYQPTSV GEVREVLALA RQQNKKVKVV
60 70 80 90 100
GGGHSPSDIA CTDGFMIHMG KMNRVLQVDK EKKQVTVEAG ILLTDLHPQL
110 120 130 140 150
DKHGLALSNL GAVSDVTVGG VIGSGTHNTG IKHGILATQV VALTLMKADG
160 170 180 190 200
TVLECSESSN ADVFQAARVH LGCLGVILTV TLQCVPQFHL LETSFPSTLK
210 220 230 240 250
EVLDNLDSHL KKSEYFRFLW FPHSENVSII YQDHTNKEPS SASNWFWDYA
260 270 280 290 300
IGFYLLEFLL WTSTYLPRLV GWINRFFFWL LFNCKKESSN LSHKIFSYEC
310 320 330 340 350
RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL
360 370 380 390 400
LSPCFQRDSC YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH
410 420 430 440
NCTRKDFEKM YPAFHKFCDI REKLDPTGMF LNSYLEKVFY
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000060912.

PTM databases

PhosphoSiteiP58710.

Proteomic databases

MaxQBiP58710.
PaxDbiP58710.
PRIDEiP58710.

Protocols and materials databases

DNASUi268756.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi268756.
MGIiMGI:1353434. Gulo.

Phylogenomic databases

eggNOGiCOG0277.
GeneTreeiENSGT00510000049722.
HOGENOMiHOG000252847.
HOVERGENiHBG005834.
InParanoidiP58710.
KOiK00103.
OMAiMDCLFSQ.
OrthoDBiEOG7N8ZV8.
TreeFamiTF328994.

Enzyme and pathway databases

UniPathwayiUPA00991; UER00939.
BRENDAi1.1.3.8. 3474.

Miscellaneous databases

NextBioi392483.
PROiP58710.
SOURCEiSearch...

Gene expression databases

BgeeiP58710.
CleanExiMM_GULO.
ExpressionAtlasiP58710. baseline and differential.
GenevestigatoriP58710.

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.
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.
PROSITEiPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2003) [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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  4. Lubec G., Kang S.U.
    Submitted (MAR-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: April 1, 2015
This is version 121 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

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.