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Search results 101 to 122 out of 122 for Gpcpd1

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0.019s

Type

Details

Score

Publication

12933806 | J:86372

First Author:	Yanaka N
Year:	2003
Journal:	J Biol Chem
Title:	Novel membrane protein containing glycerophosphodiester phosphodiesterase motif is transiently expressed during osteoblast differentiation.
Volume:	278
Issue:	44
Pages:	43595-602

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Publication

15276213 | -

First Author:	Nogusa Y
Year:	2004
Journal:	Gene
Title:	Isolation and characterization of two serpentine membrane proteins containing glycerophosphodiester phosphodiesterase, GDE2 and GDE6.
Volume:	337

Pages:	173-9

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Publication

15162496 | -

First Author:	Santelli E
Year:	2004
Journal:	Proteins
Title:	Crystal structure of a glycerophosphodiester phosphodiesterase (GDPD) from Thermotoga maritima (TM1621) at 1.60 A resolution.
Volume:	56
Issue:	1
Pages:	167-70

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Publication

12576545 | -

First Author:	Zheng B
Year:	2003
Journal:	Proc Natl Acad Sci U S A
Title:	GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors.
Volume:	100
Issue:	4
Pages:	1745-50

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Publication

18991142 | -

First Author:	Chang PA
Year:	2008
Journal:	Mol Membr Biol
Title:	Isolation, characterization and molecular 3D model of human GDE4, a novel membrane protein containing glycerophosphodiester phosphodiesterase domain.
Volume:	25
Issue:	6-7
Pages:	557-66

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Protein Domain

IPR030395 | GP_PDE_dom

Type:

Domain

Description:

This entry represents the GP-PDE domain.The glycerophosphodiester phosphodiesterases (GD-PDEs) were initiallycharacterised in bacteria, where they have functional roles for production ofmetabolic carbon and phosphate sources from glycerophosphodiesters and inadherence to and degradation of mammalian host-cell membranes. Mammalian GP-GDEs have been identified more recently and shown to be implicated in severalphysiological functions. GD-PDEs are involved in glycerol metabolism andcatalyze the reaction of glycerophosphodiester and water to alcohol andsn-glycerol-3-phosphate. They display broad specificity forglycerophosphodiesters, such as glycerophosphocholine,glycerophosphoethanolamine, glycerophosphoglycerol andbis(glycerophosphoglycerol).The GP-PDE domain adopts the ubiquitous triosephosphate isomerase (TIM) barrelalpha/beta fold. The TIM barrel iscomprised of an eight-stranded parallel β-sheet barrel surrounded by eightα-helices. There is a small insertion to the conventional TIM barrelstructure referred to as the GDPD-insertion (GDPD-I). The GDPD-I is comprisedof beta strands, α-helices (H3 and H4), and 3/10 helices. Although the TIMbarrel and a small insertion are unique for GP-PDE family, there are subtledifferences in size and topology of each domain [, ].Some proteins known to contain a GP-PDE domain are listed below:Bacterial glycerophosphoryl diester phosphodiesterase GlpQ (EC 3.1.4.46).Bacterial gylcerophosphoryl diester phosphodiesterase UgpQ (EC 3.1.4.46).Mammalian glycerophosphodiester phosphodiesterase 1 (GDE1) (EC 3.1.4.44)(or MMIR16) [], an integral membrane glycoprotein that interacts withregulator of G protein signaling proteins. It hydrolyzesglycerophosphoinositols (GPIs) producing inositol and glycerol 3-phosphate.Mammalian glycerophosphodiester phosphodiesterase domain-containing protein5 (GDPD5) (EC 3.1.-.-) (or GDE2) [].Mammalian glycerophosphoinositol inositolphosphodiesterase GDPD2 (or GDE3)(EC 3.1.4.43) [], up-regulated during osteoblast differentiation and canaffect cell morpholgy. It hydrolyzes glycerophosphoinositol (GroPIns),producing inositol 1-phosphate and glycerol.Mammalian glycerophosphodiester phosphodiesterase domain-containing protein1 (GDPD1) (EC 3.1.-.-) (or GDE4) [].Mammalian glycerophosphocholine phosphodiesterase GPCPD1 (EC 3.1.4.2) (orGDE5), selectively hydrolyzes glycerophosphocholine (GroPCho) and controlsskeletal muscle development [].Mammalian glycerophosphodiester phosphodiesterase domain-containing protein4 (GDPD4) (EC 3.1.-.-) (or GDE6) [].

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Protein

Q9JL56

Organism:	Mus musculus/domesticus
Length:	331
Fragment?:	false

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Protein

Q9CRY7

Organism:	Mus musculus/domesticus
Length:	314
Fragment?:	false

•

Protein

Q9ESM6

Organism:	Mus musculus/domesticus
Length:	539
Fragment?:	false

•

Protein

Q99LY2

Organism:	Mus musculus/domesticus
Length:	330
Fragment?:	false

•

Protein

Q3TT99

Organism:	Mus musculus/domesticus
Length:	632
Fragment?:	false

•

Protein

Q640M6

Organism:	Mus musculus/domesticus
Length:	607
Fragment?:	false

•

Protein

D3Z3E2

Organism:	Mus musculus/domesticus
Length:	186
Fragment?:	true

•

Protein

A0A140LJJ4

Organism:	Mus musculus/domesticus
Length:	107
Fragment?:	true

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Protein

A0A1L1STK0

Organism:	Mus musculus/domesticus
Length:	612
Fragment?:	false

•

Protein

A0A140LJK8

Organism:	Mus musculus/domesticus
Length:	108
Fragment?:	false

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Protein

B2RU67

Organism:	Mus musculus/domesticus
Length:	565
Fragment?:	false

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Publication

16909422 | -

First Author:	Rao KN
Year:	2006
Journal:	Proteins
Title:	Crystal structure of glycerophosphodiester phosphodiesterase from Agrobacterium tumefaciens by SAD with a large asymmetric unit.
Volume:	65
Issue:	2
Pages:	514-8

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Publication

18034455 | -

First Author:	Ballif BA
Year:	2008
Journal:	J Proteome Res
Title:	Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.
Volume:	7
Issue:	1
Pages:	311-8

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Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

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Publication

21183079 | J:292518

First Author:	Huttlin EL
Year:	2010
Journal:	Cell
Title:	A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume:	143
Issue:	7
Pages:	1174-89

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Publication

19468303 | -

First Author:	Church DM
Year:	2009
Journal:	PLoS Biol
Title:	Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume:	7
Issue:	5
Pages:	e1000112

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