GPD1/YDL022W Protein Information

Standard Name	Gpd1p 1, 2
Systematic Name	Ydl022wp
Alias	Dar1p 3 , Hor1p 4 , Osg1p 5 , Osr5p
ORF Classification	Verified
Description	NAD-dependent glycerol-3-phosphate dehydrogenase; key enzyme of glycerol synthesis, essential for growth under osmotic stress; expression regulated by high-osmolarity glycerol response pathway; protein abundance increases in response to DNA replication stress; constitutively inactivated via phosphorylation by the protein kinases YPK1 and YPK2, dephosphorylation increases catalytic activity; GPD1 has a paralog, GPD2, that arose from the whole genome duplication (10, 6, 7, 8, 9)
Name Description	Glycerol-3-Phosphate Dehydrogenase 7

Experimental Data
Molecules/cell	807 11

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	391
Molecular Weight (Da)	42,869
Isoelectric Point (pI)	5.26

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Gpd1p (InterPro)
Physical Interactions	There are 18 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000037A2B \| Q00055 MIPS: YDL022W NCBI: 1430995 \| 148337551 \| 394741 \| 411024297 \| 411024298 \| 436875 \| 439686 \| 462197 \| 47420051 \| 47420057 \| 495705 \| 6320181 \| 683675 \| NP_010262.1 \| NM_001180081.1 GenBank/EMBL/DDBJ: DAA11828.1 \| AY598965 \| AY598968 \| EF596737 \| M38740 \| U04621 \| X76859 \| Z24454 \| Z48432 \| Z74071
External Classifications	EC: 1.1.1.8 [Glycerol-3-phosphate dehydrogenase (NAD(+))]

Amino Acid Sequence (or in FASTA format)
1 MSAAADRLNL TSGHLNAGRK RSSSSVSLKA AEKPFKVTVI GSGNWGTTIA 51 KVVAENCKGY PEVFAPIVQM WVFEEEINGE KLTEIINTRH QNVKYLPGIT 101 LPDNLVANPD LIDSVKDVDI IVFNIPHQFL PRICSQLKGH VDSHVRAISC 151 LKGFEVGAKG VQLLSSYITE ELGIQCGALS GANIATEVAQ EHWSETTVAY 201 HIPKDFRGEG KDVDHKVLKA LFHRPYFHVS VIEDVAGISI CGALKNVVAL 251 GCGFVEGLGW GNNASAAIQR VGLGEIIRFG QMFFPESREE TYYQESAGVA 301 DLITTCAGGR NVKVARLMAT SGKDAWECEK ELLNGQSAQG LITCKEVHEW 351 LETCGSVEDF PLFEAVYQIV YNNYPMKNLP DMIEELDLHE D*

Amino Acid Sequence (or in FASTA format)

       1  MSAAADRLNL TSGHLNAGRK RSSSSVSLKA AEKPFKVTVI GSGNWGTTIA
      51  KVVAENCKGY PEVFAPIVQM WVFEEEINGE KLTEIINTRH QNVKYLPGIT
     101  LPDNLVANPD LIDSVKDVDI IVFNIPHQFL PRICSQLKGH VDSHVRAISC
     151  LKGFEVGAKG VQLLSSYITE ELGIQCGALS GANIATEVAQ EHWSETTVAY
     201  HIPKDFRGEG KDVDHKVLKA LFHRPYFHVS VIEDVAGISI CGALKNVVAL
     251  GCGFVEGLGW GNNASAAIQR VGLGEIIRFG QMFFPESREE TYYQESAGVA
     301  DLITTCAGGR NVKVARLMAT SGKDAWECEK ELLNGQSAQG LITCKEVHEW
     351  LETCGSVEDF PLFEAVYQIV YNNYPMKNLP DMIEELDLHE D*

external links for Gpd1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastGFP
Candida (CGD)	CYC2008 (complexes)	Pfam domains	YeastRC Public Image Repository
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Gpd1p

1)	Andre, B., et al., (1995) The sequence of a 42 kb segment located on the left arm of chromosome IV from Saccharomyces cerevisiae. Unpublished
2)	Ronnow, B. and Kielland-Brandt, M.C. (1992) Personal Communication, Mortimer Map Edition 11
3)	Wang HT, et al. (1994) Cloning, sequence, and disruption of the Saccharomyces diastaticus DAR1 gene encoding a glycerol-3-phosphate dehydrogenase. J Bacteriol 176(22):7091-5
4)	Hirayama T, et al. (1995) Cloning and characterization of seven cDNAs for hyperosmolarity-responsive (HOR) genes of Saccharomyces cerevisiae. Mol Gen Genet 249(2):127-38
5)	Nevoigt E and Stahl U (1997) Osmoregulation and glycerol metabolism in the yeast Saccharomyces cerevisiae. FEMS Microbiol Rev 21(3):231-41
6)	Nevoigt E and Stahl U (1996) Reduced pyruvate decarboxylase and increased glycerol-3-phosphate dehydrogenase [NAD+] levels enhance glycerol production in Saccharomyces cerevisiae. Yeast 12(13):1331-7
7)	Albertyn J, et al. (1994) GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway. Mol Cell Biol 14(6):4135-44
8)	Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
9)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
10)	Lee YJ, et al. (2012) Reciprocal phosphorylation of yeast glycerol-3-phosphate dehydrogenases in adaptation to distinct types of stress. Mol Cell Biol 32(22):4705-17
11)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41