GGLO_MOUSE
ID GGLO_MOUSE Reviewed; 440 AA.
AC P58710; Q8K152;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=L-gulonolactone oxidase;
DE Short=LGO;
DE EC=1.1.3.8;
DE AltName: Full=L-gulono-gamma-lactone oxidase;
DE Short=GLO;
GN Name=Gulo;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=14962674; DOI=10.1016/j.ygeno.2003.08.018;
RA Ha M.N., Graham F.L., D'Souza C.K., Muller W.J., Igdoura S.A.,
RA Schellhorn H.E.;
RT "Functional rescue of vitamin C synthesis deficiency in human cells using
RT adenoviral-based expression of murine l-gulono-gamma-lactone oxidase.";
RL Genomics 83:482-492(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 318-324, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-
CC xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
CC {ECO:0000269|PubMed:14962674}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-gulono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate;
CC Xref=Rhea:RHEA:32363, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17587, ChEBI:CHEBI:38290; EC=1.1.3.8;
CC Evidence={ECO:0000269|PubMed:14962674};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:14962674};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via UDP-alpha-
CC D-glucuronate pathway; L-ascorbate from UDP-alpha-D-glucuronate: step
CC 4/4.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver.
CC {ECO:0000269|PubMed:14962674}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AY453064; AAR15891.1; -; mRNA.
DR EMBL; AK077740; BAC36988.1; -; mRNA.
DR EMBL; AK167460; BAE39545.1; -; mRNA.
DR EMBL; BC019856; AAH19856.1; -; mRNA.
DR EMBL; BC028828; AAH28828.1; -; mRNA.
DR CCDS; CCDS36958.1; -.
DR RefSeq; NP_848862.1; NM_178747.3.
DR RefSeq; XP_006519129.1; XM_006519066.1.
DR AlphaFoldDB; P58710; -.
DR SMR; P58710; -.
DR STRING; 10090.ENSMUSP00000060912; -.
DR iPTMnet; P58710; -.
DR PhosphoSitePlus; P58710; -.
DR SwissPalm; P58710; -.
DR jPOST; P58710; -.
DR MaxQB; P58710; -.
DR PaxDb; P58710; -.
DR PeptideAtlas; P58710; -.
DR PRIDE; P58710; -.
DR ProteomicsDB; 265742; -.
DR DNASU; 268756; -.
DR Ensembl; ENSMUST00000059970; ENSMUSP00000060912; ENSMUSG00000034450.
DR GeneID; 268756; -.
DR KEGG; mmu:268756; -.
DR UCSC; uc007ujt.1; mouse.
DR CTD; 268756; -.
DR MGI; MGI:1353434; Gulo.
DR VEuPathDB; HostDB:ENSMUSG00000034450; -.
DR eggNOG; KOG4730; Eukaryota.
DR GeneTree; ENSGT00510000049722; -.
DR HOGENOM; CLU_003896_4_1_1; -.
DR InParanoid; P58710; -.
DR OMA; YPRFGEF; -.
DR OrthoDB; 1134169at2759; -.
DR PhylomeDB; P58710; -.
DR TreeFam; TF328994; -.
DR BRENDA; 1.1.3.8; 3474.
DR UniPathway; UPA00991; UER00939.
DR BioGRID-ORCS; 268756; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Gulo; mouse.
DR PRO; PR:P58710; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P58710; protein.
DR Bgee; ENSMUSG00000034450; Expressed in left lobe of liver and 43 other tissues.
DR Genevisible; P58710; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0050105; F:L-gulonolactone oxidase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR007173; ALO_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR010031; FAD_lactone_oxidase.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR InterPro; IPR030654; Sugar_lactone_oxidase.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43762; PTHR43762; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR01678; FAD_lactone_ox; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 1: Evidence at protein level;
KW Ascorbate biosynthesis; Direct protein sequencing; Endoplasmic reticulum;
KW FAD; Flavoprotein; Membrane; Microsome; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..440
FT /note="L-gulonolactone oxidase"
FT /id="PRO_0000128159"
FT TRANSMEM 251..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 17..187
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT MOD_RES 54
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CONFLICT 160
FT /note="N -> K (in Ref. 3; AAH19856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 50478 MW; D109B480E08E773B CRC64;
MVHGYKGVQF QNWAKTYGCS PEMYYQPTSV GEVREVLALA RQQNKKVKVV GGGHSPSDIA
CTDGFMIHMG KMNRVLQVDK EKKQVTVEAG ILLTDLHPQL DKHGLALSNL GAVSDVTVGG
VIGSGTHNTG IKHGILATQV VALTLMKADG TVLECSESSN ADVFQAARVH LGCLGVILTV
TLQCVPQFHL LETSFPSTLK EVLDNLDSHL KKSEYFRFLW FPHSENVSII YQDHTNKEPS
SASNWFWDYA IGFYLLEFLL WTSTYLPRLV GWINRFFFWL LFNCKKESSN LSHKIFSYEC
RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL LSPCFQRDSC
YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH NCTRKDFEKM YPAFHKFCDI
REKLDPTGMF LNSYLEKVFY
