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UniProtKB/Swiss-Prot entry Q5EA88


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPDA_BOVIN
Primary accession number Q5EA88
Secondary accession number Q2HJE6
Integrated into Swiss-Prot on November 28, 2006
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 26)
Name and origin of the protein
Protein name Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic
Synonyms GPDH-C
GPD-C
EC 1.1.1.8
Gene name
Name: GPD1
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan]
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-349.
STRAIN=Hereford;
TISSUE=Ascending colon;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BT020681; AAX08698.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105513; AAI05514.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001030431.1; -.
UniGene Bt.5002
3D structure databases
ModBase Q5EA88.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from sequence or structural similarity from AgBase).
GO:0004368; Molecular function: glycerol-3-phosphate dehydrogenase activity (inferred from sequence or structural similarity from AgBase).
GO:0006094; Biological process: gluconeogenesis (inferred from sequence or structural similarity from AgBase).
GO:0006072; Biological process: glycerol-3-phosphate metabolic process (inferred from sequence or structural similarity from AgBase).
QuickGo view.
Family and domain databases
InterPro IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR017751; NAD-dep_Gly3P_DH_euk.
IPR006168; NAD-dep_Gly3P_DHase.
IPR011128; NAD-dep_Gly3P_DHase_N.
IPR006109; NAD_Gly3P_DHase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR11728; NAD_Gly3P_DH; 1.
Pfam PF07479; NAD_Gly3P_dh_C; 1.
PF01210; NAD_Gly3P_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000114; Glycerol-3-P_dh; 1.
PRINTS PR00077; GPDHDRGNASE.
ProDom PD001278; NAD_Gly3P_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00957; NAD_G3PDH; 1.
BLOCKS Q5EA88.
Genome annotation databases
Ensembl ENSBTAG00000016296; Bos taurus. [Contig view]
GeneID 525042; -.
KEGG bta:525042; -.
Phylogenomic databases
HOVERGEN Q5EA88; -.
Other
ProtoNet Q5EA88.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   349  348     Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic. PRO_0000262289
NP_BIND   10    15  6     NAD (By similarity). 
REGION   269   270  2     Substrate binding (By similarity). 
ACT_SITE   204   204        Proton acceptor (Potential). 
BINDING   41    41        NAD (By similarity). 
BINDING   97    97        NAD (By similarity). 
BINDING   120   120        Substrate (By similarity). 
BINDING   153   153        NAD; via amide nitrogen (By similarity). 
BINDING   269   269        NAD (By similarity). 
BINDING   296   296        NAD; via amide nitrogen (By similarity). 
BINDING   298   298        NAD (By similarity). 
CONFLICT   122   122        V -> L (in Ref. 1; AAX08698). 
CONFLICT   313   313        K -> R (in Ref. 1; AAX08698). 
Sequence information
Length: 349 AA [This is the length of the unprocessed precursor] Molecular weight: 37648 Da [This is the MW of the unprocessed precursor] CRC64: 59E7DFADE8FC1A80 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTGKKVCIVG SGNWGSAIAK IVGGNAAQLA HFDPRVTMWV FEEDIGGRKL TEIINTQHEN 

        70         80         90        100        110        120 
VKYLPGHKLP PNVVAVPDVV QAAADADILI FVVPHQFIGK ICDQLKGHLK ADTIGVSLIK 

       130        140        150        160        170        180 
GVDEGPKGLK LISEVIGERL GIPMSVLMGA NIANEVADEK FCETTIGSKN QAHGQLLKEL 

       190        200        210        220        230        240 
MQTPNFRITV VQEVDTVEIC GALKNIVAVG AGFCDGLGFG DNTKAAVIRL GLMEMIAFAK 

       250        260        270        280        290        300 
LFCSGSVSSA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE MLNGQKLQGP 

       310        320        330        340 
QTARELHSIL QHKGMVDKFP LFTAVYKVCY ENQPVGEFIH CLQNHPEHV 

Q5EA88 in FASTA format

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