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P43304 (GPDM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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):
mtGPD
Gene names
Name:GPD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

Sequence similarities

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

Contains 2 EF-hand domains.

Sequence caution

The sequence BAD92636.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P43304-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P43304-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-126: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Mitochondrion By similarity
Chain43 – 727685Glycerol-3-phosphate dehydrogenase, mitochondrial
PRO_0000010429

Regions

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

Amino acid modifications

Modified residue6011Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 126126Missing in isoform 2.
VSP_017134
Natural variant2641R → H. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9
Corresponds to variant rs2116665 [ dbSNP | Ensembl ].
VAR_049113
Natural variant4531K → Q.
Corresponds to variant rs35096779 [ dbSNP | Ensembl ].
VAR_049114
Natural variant5251R → H. Ref.1 Ref.4
Corresponds to variant rs1051916 [ dbSNP | Ensembl ].
VAR_025215

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 5, 2009. Version 3.
Checksum: 70D8B4E5CB4F2EFD

FASTA72780,853
        10         20         30         40         50         60 
MAFQKAVKGT ILVGGGALAT VLGLSQFAHY RRKQMNLAYV KAADCISEPV NREPPSREAQ 

        70         80         90        100        110        120 
LLTLQNTSEF DILVIGGGAT GSGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR 

       130        140        150        160        170        180 
YLQKAIMKLD IEQYRMVKEA LHERANLLEI APHLSAPLPI MLPVYKWWQL PYYWVGIKLY 

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

       250        260        270        280        290        300 
AATANYMEVV SLLKKTDPQT GKVRVSGARC KDVLTGQEFD VRAKCVINAT GPFTDSVRKM 

       310        320        330        340        350        360 
DDKDAAAICQ PSAGVHIVMP GYYSPESMGL LDPATSDGRV IFFLPWQKMT IAGTTDTPTD 

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

       430        440        450        460        470        480 
VVDISESGLI TIAGGKWTTY RSMAEDTINA AVKTHNLKAG PSRTVGLFLQ GGKDWSPTLY 

       490        500        510        520        530        540 
IRLVQDYGLE SEVAQHLAAT YGDKAFEVAK MASVTGKRWP IVGVRLVSEF PYIEAEVKYG 

       550        560        570        580        590        600 
IKEYACTAVD MISRRTRLAF LNVQAAEEAL PRIVELMGRE LNWDDYKKQE QLETARKFLY 

       610        620        630        640        650        660 
YEMGYKSRSE QLTDRSEISL LPSDIDRYKK RFHKFDADQK GFITIVDVQR VLESINVQMD 

       670        680        690        700        710        720 
ENTLHEILNE VDLNKNGQVE LNEFLQLMSA IQKGRVSGSR LAILMKTAEE NLDRRVPIPV 


DRSCGGL 

« Hide

Isoform 2 [UniParc].

Checksum: 1953A7AC32B5DF02
Show »

FASTA60167,531

References

« Hide 'large scale' references
[1]"The sequence of a human mitochondrial glycerol-3-phosphate dehydrogenase-encoding cDNA."
Lehn D.A., Brown L.J., Simonson G.D., Moran S.M., McDonald M.J.
Gene 150:417-418(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS HIS-264 AND HIS-525.
[2]"Mitochondrial glycerol-3-phosphate dehydrogenase. Cloning of an alternatively spliced human islet-cell cDNA, tissue distribution, physical mapping, and identification of a polymorphic genetic marker."
Ferrer J., Aoki M., Behn P., Nestorowicz A., Riggs A., Permutt M.A.
Diabetes 45:262-266(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HIS-264.
[3]"Structural organization and mapping of the human mitochondrial glycerol phosphate dehydrogenase-encoding gene and pseudogene."
Brown L.J., Stoffel M., Moran S.M., Fernald A.A., Lehn D.A., LeBeau M.M., MacDonald M.J.
Gene 172:309-312(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-264.
[4]"A novel glycerol-3-phosphate dehydrogenase 3 from adult testis."
Yin L.L., Li J.M., Sha J.H.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS HIS-264 AND HIS-525.
Tissue: Testis.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT HIS-264.
Tissue: Testis and Trachea.
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-264.
Tissue: Brain.
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-264.
[9]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-408, VARIANT HIS-264.
Tissue: Brain.
[10]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 212-227 AND 558-572, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[11]Bienvenut W.V., Claeys D.
Submitted (JAN-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 340-348; 410-418; 526-538; 558-572 AND 715-722, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12424 mRNA. Translation: AAA65701.1.
U36310 mRNA. Translation: AAB60403.1.
U40367 expand/collapse EMBL AC list , U40353, U40354, U40355, U40357, U40358, U40359, U40360, U40361, U40362, U40363, U40364, U40365 Genomic DNA. Translation: AAC50556.1.
AF311325 mRNA. Translation: AAG33851.1.
AK093198 mRNA. Translation: BAG52671.1.
AK291065 mRNA. Translation: BAF83754.1.
AK292817 mRNA. Translation: BAF85506.1.
AB209399 mRNA. Translation: BAD92636.1. Different initiation.
AC011308 Genomic DNA. No translation available.
AC092686 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11453.1.
U79250 mRNA. Translation: AAB50200.1.
PIRG02093.
RefSeqNP_000399.3. NM_000408.4.
NP_001076581.2. NM_001083112.2.
XP_005246526.1. XM_005246469.1.
UniGeneHs.512382.

3D structure databases

ProteinModelPortalP43304.
SMRP43304. Positions 63-693.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109081. 3 interactions.
IntActP43304. 1 interaction.
MINTMINT-4530883.
STRING9606.ENSP00000308610.

PTM databases

PhosphoSiteP43304.

Polymorphism databases

DMDM229462943.

2D gel databases

REPRODUCTION-2DPAGEIPI00017895.
UCD-2DPAGEP43304.

Proteomic databases

PaxDbP43304.
PRIDEP43304.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310454; ENSP00000308610; ENSG00000115159. [P43304-1]
ENST00000409674; ENSP00000386425; ENSG00000115159. [P43304-1]
ENST00000409861; ENSP00000386626; ENSG00000115159. [P43304-1]
ENST00000438166; ENSP00000409708; ENSG00000115159. [P43304-1]
GeneID2820.
KEGGhsa:2820.
UCSCuc002tzd.4. human. [P43304-1]

Organism-specific databases

CTD2820.
GeneCardsGC02P157291.
H-InvDBHIX0002519.
HGNCHGNC:4456. GPD2.
HPAHPA008012.
MIM138430. gene.
neXtProtNX_P43304.
PharmGKBPA28837.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0578.
HOGENOMHOG000004813.
HOVERGENHBG005897.
InParanoidP43304.
KOK00111.
OMASYFLTKS.
OrthoDBEOG74TWZ2.
PhylomeDBP43304.
TreeFamTF300359.

Enzyme and pathway databases

BioCycMetaCyc:HS03841-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00618; UER00673.

Gene expression databases

ArrayExpressP43304.
BgeeP43304.
CleanExHS_GPD2.
GenevestigatorP43304.

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

GenomeRNAi2820.
NextBio11111.
PROP43304.
SOURCESearch...

Entry information

Entry nameGPDM_HUMAN
AccessionPrimary (citable) accession number: P43304
Secondary accession number(s): A8K4V0 expand/collapse secondary AC list , B3KSA9, Q59FR1, Q9HAP9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM