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Q64521 (GPDM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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:
Glycerol-3-phosphate dehydrogenase, mitochondrial

Short name=GPD-M
Short name=GPDH-M
EC=1.1.5.3
Alternative name(s):
Protein TISP38
Gene names
Name:Gpd2
Synonyms:Gdm1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length727 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.

Cofactor

FAD.

Enzyme regulation

Calcium-binding enhance the activity of the enzyme.

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1.

Subcellular location

Mitochondrion inner membrane.

Sequence similarities

Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.

Contains 2 EF-hand domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Mitochondrion By similarity
Chain43 – 727685Glycerol-3-phosphate dehydrogenase, mitochondrial
PRO_0000010430

Regions

Domain623 – 65836EF-hand 1
Domain659 – 69436EF-hand 2
Nucleotide binding71 – 9929FAD Potential
Calcium binding672 – 68312 Potential

Amino acid modifications

Modified residue6011Phosphotyrosine Ref.8

Experimental info

Sequence conflict261P → Q in AAB50545. Ref.1
Sequence conflict261P → Q in AAH21359. Ref.4
Sequence conflict421Missing in BAC28685. Ref.3
Sequence conflict1581L → V in AAB50545. Ref.1
Sequence conflict2951D → E in BAA08926. Ref.2
Sequence conflict4491D → N in AAH21359. Ref.4
Sequence conflict4981A → P in BAA08926. Ref.2
Sequence conflict5821N → D in AAB50545. Ref.1
Sequence conflict5931E → G in AAB50545. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q64521 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 319F52E31CFDFC44

FASTA72780,954
        10         20         30         40         50         60 
MAFQKAVKGT ILVGGGALAT VLGLSPFAHY RRKQVSLAYV EAAGYLTEPV NREPPSREAQ 

        70         80         90        100        110        120 
LMTLKNTPEF DILVIGGGAT GCGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR 

       130        140        150        160        170        180 
YLQKAIMNLD VEQYRMVKEA LHERANLLEI APHLSAPLPI MLPLYKWWQL PYYWVGIKMY 

       190        200        210        220        230        240 
DLVAGSQCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG 

       250        260        270        280        290        300 
AATANYMEVV SLLKKTDPET GKERVSGARC KDVLTGQEFD VRAKCVINAS GPFTDSVRKM 

       310        320        330        340        350        360 
DDKNVVPICQ PSAGVHIVMP GYYSPENMGL LDPATSDGRV IFFLPWEKMT IAGTTDTPTD 

       370        380        390        400        410        420 
VTHHPIPSEE DINFILNEVR NYLSSDVEVR RGDVLAAWSG IRPLVTDPKS ADTQSISRNH 

       430        440        450        460        470        480 
VVDISDSGLI TIAGGKWTTY RSMAEDTVDA AVKFHNLNAG PSRTVGLFLQ GGKDWSPTLY 

       490        500        510        520        530        540 
IRLVQDYGLE SEVAQHLAKT YGDKAFEVAK MASVTGKRWP VVGVRLVSEF PYIEAEVKYG 

       550        560        570        580        590        600 
IKEYACTAVD MISRRTRLAF LNVQAAEEAL PRIVELMGRE LNWSELRKQE ELETATRFLY 

       610        620        630        640        650        660 
YEMGYKSRTE QLTDSTEISL LPSDIDRYKK RFHKFDEDEK GFITIVDVQR VLESINVQMD 

       670        680        690        700        710        720 
ENTLHEILCE VDLNKNGQVE LHEFLQLMSA VQKGRVSGSR LAILMKTAEE NLDRRVPIPV 


DRSCGGL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and tissue-dependent RNA expression of mouse FAD-linked glycerol-3-phosphate dehydrogenase."
Koza R.A., Kozak U.C., Brown L.J., Leiter E.H., Macdonald M.J., Kozak L.P.
Arch. Biochem. Biophys. 336:97-104(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Adipocyte.
[2]"Effect of mitochondrial and/or cytosolic glycerol 3-phosphate dehydrogenase overexpression on glucose-stimulated insulin secretion from MIN6 and HIT cells."
Ishihara H., Nakazaki M., Kanegae Y., Inukai K., Asano T., Katagiri H., Yazaki Y., Kikuchi M., Miyazaki J., Saito I., Oka Y.
Diabetes 45:1238-1244(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[3]"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: Bone marrow, Diencephalon and Lung.
[4]"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: Czech II.
Tissue: Mammary tumor.
[5]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 58-91; 95-110; 125-135; 167-178; 200-209; 212-254; 285-298; 340-348; 381-390; 392-409; 442-453; 464-473; 483-499; 519-538; 558-579; 598-606; 609-627 AND 635-693.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"Genomic sequence of mouse mitochondrial glycerol-3-phosphate dehydrogenase (mGPDH)."
Weitzel J.M.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 390-686.
Strain: 129/Sv.
Tissue: Liver.
[7]"Mus musculus TISP38 mRNA."
Tamura K., Nishimune Y., Nojima H.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 611-727.
Tissue: Testis.
[8]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U60987 mRNA. Translation: AAB50545.1.
D50430 mRNA. Translation: BAA08926.1.
AK034353 mRNA. Translation: BAC28685.1.
AK144716 mRNA. Translation: BAE26028.1.
AK149851 mRNA. Translation: BAE29123.1.
AK167152 mRNA. Translation: BAE39294.1.
BC021359 mRNA. Translation: AAH21359.1.
AH009802 Genomic DNA. Translation: AAG12342.1.
AB045714 mRNA. Translation: BAB97201.1.
RefSeqNP_001139292.1. NM_001145820.1.
NP_034404.3. NM_010274.3.
UniGeneMm.3711.

3D structure databases

ProteinModelPortalQ64521.
SMRQ64521. Positions 53-716.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ64521. 4 interactions.
MINTMINT-4119960.

PTM databases

PhosphoSiteQ64521.

2D gel databases

REPRODUCTION-2DPAGEQ64521.

Proteomic databases

PaxDbQ64521.
PRIDEQ64521.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028167; ENSMUSP00000028167; ENSMUSG00000026827.
ENSMUST00000169687; ENSMUSP00000130992; ENSMUSG00000026827.
GeneID14571.
KEGGmmu:14571.
UCSCuc008jsc.2. mouse.

Organism-specific databases

CTD2820.
MGIMGI:99778. Gpd2.

Phylogenomic databases

eggNOGCOG0578.
GeneTreeENSGT00390000001718.
HOVERGENHBG005897.
KOK00111.

Enzyme and pathway databases

UniPathwayUPA00618; UER00673.

Gene expression databases

ArrayExpressQ64521.
BgeeQ64521.
CleanExMM_GPD2.
GenevestigatorQ64521.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
[Graphical view]
PfamPF01266. DAO. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
PRINTSPR01001. FADG3PDH.
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGPD2. mouse.
NextBio286290.
PROQ64521.
SOURCESearch...

Entry information

Entry nameGPDM_MOUSE
AccessionPrimary (citable) accession number: Q64521
Secondary accession number(s): Q3TK51 expand/collapse secondary AC list , Q3UDY8, Q61507, Q8CBX6, Q8K4U5, Q8VDT0, Q9ERP0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 128 of the entry and version 2 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