Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glycerol-3-phosphate dehydrogenase, mitochondrial

Gene

Gpd2

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

Functioni

Catalytic activityi

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

Cofactori

Enzyme regulationi

Calcium-binding enhance the activity of the enzyme.

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi71 – 9929FADSequence AnalysisAdd
BLAST
Calcium bindingi672 – 68312PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. camera-type eye development Source: MGI
  2. gluconeogenesis Source: MGI
  3. glycerol-3-phosphate metabolic process Source: MGI
  4. glycerol catabolic process Source: UniProtKB-UniPathway
  5. multicellular organism growth Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, FAD, Flavoprotein, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_256522. Fatty acid, triacylglycerol, and ketone body metabolism.
UniPathwayiUPA00618; UER00673.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase, mitochondrial (EC:1.1.5.3)
Short name:
GPD-M
Short name:
GPDH-M
Alternative name(s):
Protein TISP38
Gene namesi
Name:Gpd2
Synonyms:Gdm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:99778. Gpd2.

Subcellular locationi

GO - Cellular componenti

  1. glycerol-3-phosphate dehydrogenase complex Source: MGI
  2. mitochondrial inner membrane Source: MGI
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242MitochondrionBy similarityAdd
BLAST
Chaini43 – 727685Glycerol-3-phosphate dehydrogenase, mitochondrialPRO_0000010430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei601 – 6011Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ64521.
PaxDbiQ64521.
PRIDEiQ64521.

2D gel databases

REPRODUCTION-2DPAGEQ64521.

PTM databases

PhosphoSiteiQ64521.

Expressioni

Gene expression databases

BgeeiQ64521.
CleanExiMM_GPD2.
ExpressionAtlasiQ64521. baseline and differential.
GenevestigatoriQ64521.

Interactioni

Protein-protein interaction databases

IntActiQ64521. 4 interactions.
MINTiMINT-4119960.

Structurei

3D structure databases

ProteinModelPortaliQ64521.
SMRiQ64521. Positions 69-597, 628-689.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini623 – 65836EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini659 – 69436EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0578.
GeneTreeiENSGT00390000001718.
HOVERGENiHBG005897.
InParanoidiQ64521.
KOiK00111.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. 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]
PfamiPF01266. DAO. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
PRINTSiPR01001. FADG3PDH.
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64521-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFQKAVKGT ILVGGGALAT VLGLSPFAHY RRKQVSLAYV EAAGYLTEPV
60 70 80 90 100
NREPPSREAQ LMTLKNTPEF DILVIGGGAT GCGCALDAVT RGLKTALVER
110 120 130 140 150
DDFSSGTSSR STKLIHGGVR YLQKAIMNLD VEQYRMVKEA LHERANLLEI
160 170 180 190 200
APHLSAPLPI MLPLYKWWQL PYYWVGIKMY DLVAGSQCLK SSYVLSKSRA
210 220 230 240 250
LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG AATANYMEVV
260 270 280 290 300
SLLKKTDPET GKERVSGARC KDVLTGQEFD VRAKCVINAS GPFTDSVRKM
310 320 330 340 350
DDKNVVPICQ PSAGVHIVMP GYYSPENMGL LDPATSDGRV IFFLPWEKMT
360 370 380 390 400
IAGTTDTPTD VTHHPIPSEE DINFILNEVR NYLSSDVEVR RGDVLAAWSG
410 420 430 440 450
IRPLVTDPKS ADTQSISRNH VVDISDSGLI TIAGGKWTTY RSMAEDTVDA
460 470 480 490 500
AVKFHNLNAG PSRTVGLFLQ GGKDWSPTLY IRLVQDYGLE SEVAQHLAKT
510 520 530 540 550
YGDKAFEVAK MASVTGKRWP VVGVRLVSEF PYIEAEVKYG IKEYACTAVD
560 570 580 590 600
MISRRTRLAF LNVQAAEEAL PRIVELMGRE LNWSELRKQE ELETATRFLY
610 620 630 640 650
YEMGYKSRTE QLTDSTEISL LPSDIDRYKK RFHKFDEDEK GFITIVDVQR
660 670 680 690 700
VLESINVQMD ENTLHEILCE VDLNKNGQVE LHEFLQLMSA VQKGRVSGSR
710 720
LAILMKTAEE NLDRRVPIPV DRSCGGL
Length:727
Mass (Da):80,954
Last modified:May 1, 2007 - v2
Checksum:i319F52E31CFDFC44
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261P → Q in AAB50545 (PubMed:8951039).Curated
Sequence conflicti26 – 261P → Q in AAH21359 (PubMed:15489334).Curated
Sequence conflicti42 – 421Missing in BAC28685 (PubMed:16141072).Curated
Sequence conflicti158 – 1581L → V in AAB50545 (PubMed:8951039).Curated
Sequence conflicti295 – 2951D → E in BAA08926 (PubMed:8772729).Curated
Sequence conflicti449 – 4491D → N in AAH21359 (PubMed:15489334).Curated
Sequence conflicti498 – 4981A → P in BAA08926 (PubMed:8772729).Curated
Sequence conflicti582 – 5821N → D in AAB50545 (PubMed:8951039).Curated
Sequence conflicti593 – 5931E → G in AAB50545 (PubMed:8951039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16045.1.
RefSeqiNP_001139292.1. NM_001145820.1.
NP_034404.3. NM_010274.3.
UniGeneiMm.3711.

Genome annotation databases

EnsembliENSMUST00000028167; ENSMUSP00000028167; ENSMUSG00000026827.
ENSMUST00000169687; ENSMUSP00000130992; ENSMUSG00000026827.
GeneIDi14571.
KEGGimmu:14571.
UCSCiuc008jsc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16045.1.
RefSeqiNP_001139292.1. NM_001145820.1.
NP_034404.3. NM_010274.3.
UniGeneiMm.3711.

3D structure databases

ProteinModelPortaliQ64521.
SMRiQ64521. Positions 69-597, 628-689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ64521. 4 interactions.
MINTiMINT-4119960.

PTM databases

PhosphoSiteiQ64521.

2D gel databases

REPRODUCTION-2DPAGEQ64521.

Proteomic databases

MaxQBiQ64521.
PaxDbiQ64521.
PRIDEiQ64521.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028167; ENSMUSP00000028167; ENSMUSG00000026827.
ENSMUST00000169687; ENSMUSP00000130992; ENSMUSG00000026827.
GeneIDi14571.
KEGGimmu:14571.
UCSCiuc008jsc.2. mouse.

Organism-specific databases

CTDi2820.
MGIiMGI:99778. Gpd2.

Phylogenomic databases

eggNOGiCOG0578.
GeneTreeiENSGT00390000001718.
HOVERGENiHBG005897.
InParanoidiQ64521.
KOiK00111.

Enzyme and pathway databases

UniPathwayiUPA00618; UER00673.
ReactomeiREACT_256522. Fatty acid, triacylglycerol, and ketone body metabolism.

Miscellaneous databases

ChiTaRSiGpd2. mouse.
NextBioi286290.
PROiQ64521.
SOURCEiSearch...

Gene expression databases

BgeeiQ64521.
CleanExiMM_GPD2.
ExpressionAtlasiQ64521. baseline and differential.
GenevestigatoriQ64521.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. 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]
PfamiPF01266. DAO. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
PRINTSiPR01001. FADG3PDH.
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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
    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.

Entry informationi

Entry nameiGPDM_MOUSE
AccessioniPrimary (citable) accession number: Q64521
Secondary accession number(s): Q3TK51
, Q3UDY8, Q61507, Q8CBX6, Q8K4U5, Q8VDT0, Q9ERP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 2007
Last modified: January 7, 2015
This is version 135 of the entry and version 2 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.