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P58710

- GGLO_MOUSE

UniProt

P58710 - GGLO_MOUSE

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Protein

L-gulonolactone oxidase

Gene
Gulo
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei251 – 27323Helical; Reviewed predictionAdd
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 – 11Removed By similarity
Chaini2 – 440439L-gulonolactone oxidasePRO_0000128159Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541Pros-8alpha-FAD histidine By 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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601N → K in AAH19856. 1 Publication

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

« 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(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: July 9, 2014
This is version 115 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

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