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Protein

Glycerol-3-phosphate dehydrogenase, mitochondrial

Gene

GPD2

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

FADBy similarity

Enzyme regulationi

Calcium-binding enhance the activity of the enzyme.By similarity

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. glycerol-3-phosphate metabolic process Source: InterPro
  2. glycerol catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, FAD, Flavoprotein, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00618; UER00674.

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):
mGPD
Gene namesi
Name:GPD2
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. glycerol-3-phosphate dehydrogenase complex Source: InterPro
  2. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242MitochondrionBy similarityAdd
BLAST
Chaini43 – 727685Glycerol-3-phosphate dehydrogenase, mitochondrialPRO_0000355968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei601 – 6011PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiA7DZP8.

Structurei

3D structure databases

ProteinModelPortaliA7DZP8.
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

HOVERGENiHBG005897.

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.

A7DZP8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFQKAVKRT VLVCGGALAT VLGLSQCSHY RRKQVNLACL KAAGCHTEPV
60 70 80 90 100
NREPPSREAQ LLTLQNTSEF DILVIGGGAT GSGCALDAVT RGLKTALVER
110 120 130 140 150
DDFSSGTSSR STKLIHGGVR YLQKAIMKLD VEQYRMVKEA LHERANLLEI
160 170 180 190 200
APHLSAPLPI MLPIYKWWQL PYYWVGIKLY DLVAGSNCLK SSYVLSKSRA
210 220 230 240 250
LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG AATANYREVV
260 270 280 290 300
SLLKKTDPET GKERVSGARC KDVLTGLEFD VRAKCVINAT GPFTDSVRKM
310 320 330 340 350
DDNKAPAICQ PSAGVHIVMP GYYSPESMGL LDPATSDGRV IFFLPWENMT
360 370 380 390 400
IAGTTDSPTK NTHHPIPSEE DINFILNEVR NYLSCDVEVR RGDVLAAWSG
410 420 430 440 450
IRPLVIDPKS ADTQSISRNH VVDVSESGLI TIAGGKWTTY RSMAEDTVDT
460 470 480 490 500
AIKVHNLKAG PCRTVGLFLQ GGKDWSPTLY IRLVQDYGLE SEVAQHLATT
510 520 530 540 550
YGDKAFEVAK MAKVTGKRWP IVGVRLVSEF PYIEAEVKYG IKEYACTAVD
560 570 580 590 600
MISRRTRLAF LNIQAAEEAL PRIVELMGRE LDWSEIRKQA ELETATKFLY
610 620 630 640 650
YEMGSKSRSE QLTDRTEISL RPSDIERYTK RFHKFDADEK GFITIVDVQR
660 670 680 690 700
VLENINVKID ENTLHEILSE VDLNKNGQVE LNEFLQLMSA IQKGRVSGSR
710 720
LAILMKTAEE NLDRRVPIPV DRSCGGL
Length:727
Mass (Da):80,857
Last modified:September 11, 2007 - v1
Checksum:i89C18A4C8D0205DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM774032 mRNA. Translation: CAO79918.1.
RefSeqiNP_001268609.1. NM_001281680.1.

Genome annotation databases

GeneIDi101825992.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM774032 mRNA. Translation: CAO79918.1.
RefSeqiNP_001268609.1. NM_001281680.1.

3D structure databases

ProteinModelPortaliA7DZP8.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA7DZP8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101825992.

Organism-specific databases

CTDi2820.

Phylogenomic databases

HOVERGENiHBG005897.

Enzyme and pathway databases

UniPathwayiUPA00618; UER00674.

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

  1. "Hamster sperm capacitation: role of FAD linked glycerol-3-phosphate dehydrogenase."
    Venkatesh K., Shivaji S.
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
    Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
    Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiGPDM_MESAU
AccessioniPrimary (citable) accession number: A7DZP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: September 11, 2007
Last modified: January 7, 2015
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.