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P58710 (GGLO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-gulonolactone oxidase

Short name=LGO
EC=1.1.3.8
Alternative name(s):
L-gulono-gamma-lactone oxidase
Short name=GLO
Gene names
Name:Gulo
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

FAD. Ref.1

Pathway

Cofactor biosynthesis; L-ascorbate biosynthesis via UDP-alpha-D-glucuronate pathway; L-ascorbate from UDP-alpha-D-glucuronate: step 4/4.

Subcellular location

Microsome membrane; Single-pass membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.

Tissue specificity

Highly expressed in liver. Ref.1

Sequence similarities

Belongs to the oxygen-dependent FAD-linked oxidoreductase family.

Contains 1 FAD-binding PCMH-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 440439L-gulonolactone oxidase
PRO_0000128159

Regions

Transmembrane251 – 27323Helical; Potential
Domain17 – 187171FAD-binding PCMH-type

Amino acid modifications

Modified residue541Pros-8alpha-FAD histidine By similarity

Experimental info

Sequence conflict1601N → K in AAH19856. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P58710 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: D109B480E08E773B

FASTA44050,478
        10         20         30         40         50         60 
MVHGYKGVQF QNWAKTYGCS PEMYYQPTSV GEVREVLALA RQQNKKVKVV GGGHSPSDIA 

        70         80         90        100        110        120 
CTDGFMIHMG KMNRVLQVDK EKKQVTVEAG ILLTDLHPQL DKHGLALSNL GAVSDVTVGG 

       130        140        150        160        170        180 
VIGSGTHNTG IKHGILATQV VALTLMKADG TVLECSESSN ADVFQAARVH LGCLGVILTV 

       190        200        210        220        230        240 
TLQCVPQFHL LETSFPSTLK EVLDNLDSHL KKSEYFRFLW FPHSENVSII YQDHTNKEPS 

       250        260        270        280        290        300 
SASNWFWDYA IGFYLLEFLL WTSTYLPRLV GWINRFFFWL LFNCKKESSN LSHKIFSYEC 

       310        320        330        340        350        360 
RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL LSPCFQRDSC 

       370        380        390        400        410        420 
YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH NCTRKDFEKM YPAFHKFCDI 

       430        440 
REKLDPTGMF LNSYLEKVFY 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS36958.1.
RefSeqNP_848862.1. NM_178747.3.
XP_006519129.1. XM_006519066.1.
UniGeneMm.26207.

3D structure databases

ProteinModelPortalP58710.
SMRP58710. Positions 33-207, 308-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000060912.

PTM databases

PhosphoSiteP58710.

Proteomic databases

MaxQBP58710.
PaxDbP58710.
PRIDEP58710.

Protocols and materials databases

DNASU268756.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000059970; ENSMUSP00000060912; ENSMUSG00000034450.
GeneID268756.
KEGGmmu:268756.
UCSCuc007ujt.1. mouse.

Organism-specific databases

CTD268756.
MGIMGI:1353434. Gulo.

Phylogenomic databases

eggNOGCOG0277.
GeneTreeENSGT00510000049722.
HOGENOMHOG000252847.
HOVERGENHBG005834.
InParanoidQ8K152.
KOK00103.
OMAYWFPHTD.
OrthoDBEOG7N8ZV8.
TreeFamTF328994.

Enzyme and pathway databases

UniPathwayUPA00991; UER00939.

Gene expression databases

BgeeP58710.
CleanExMM_GULO.
GenevestigatorP58710.

Family and domain databases

Gene3D3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProIPR007173. 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]
PfamPF04030. ALO. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
PIRSFPIRSF000136. LGO_GLO. 1 hit.
SUPFAMSSF56176. SSF56176. 1 hit.
TIGRFAMsTIGR01679. bact_FAD_ox. 1 hit.
TIGR01678. FAD_lactone_ox. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGULOP. mouse.
NextBio392483.
PROP58710.
SOURCESearch...

Entry information

Entry nameGGLO_MOUSE
AccessionPrimary (citable) accession number: P58710
Secondary accession number(s): Q8K152
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot