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InterPro: IPR008145 Guanylate kinase/L-type calcium channel

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3129 proteins

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Accession

IPR008145 Guanylate_kin/L-typ_Ca_channel

Secondary

IPR000619

Type

Domain

Signatures Help

Database	ID	Name	Proteins
SMART	SM00072	GuKc	3129
Signatures in BioMart

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IPR008144 Guanylate kinase

Found in

IPR000584 Voltage-dependent calcium channel, L-type, beta subunit
IPR005419 Zona occludens protein ZO-2
IPR005420 Zona occludens protein ZO-3
IPR005443 Voltage-dependent calcium channel, L-type, beta-1 subunit
IPR005444 Voltage-dependent calcium channel, L-type, beta-2 subunit
IPR008079 Voltage-dependent calcium channel, L-type, beta-3 subunit
IPR012699 Phosphonate metabolism, 1,5-bisphosphokinase (PRPP-forming) PhnN

Contains

IPR020590 Guanylate kinase, conserved site

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a domain found in guanylate kinase (EC:2.7.4.8) and in L-type calcium channel.

Guanylate kinase (EC:2.7.4.8) (GK) [1] catalyzes the ATP-dependent phosphorylation of GMP into GDP. It is essential for recycling GMP and indirectly, cGMP. In prokaryotes (such as Escherichia coli), lower eukaryotes (such as yeast) and in vertebrates, GK is a highly conserved monomeric protein of about 200 amino acids. GK has been shown [2, 3, 4] to be structurally similar to protein A57R (or SalG2R) from various strains of Vaccinia virus.

L-type calcium channnels are formed from different alpha-1 subunit isoforms that determine the pharmacological properties of the channel, since they form the drug binding domain. Other properties, such as gating voltage-dependence, G protein modulation and kinase susceptibility, are influenced by alpha-2, delta and beta subunits.

Structural links Help

PDB - click here

SCOP: c.37.1.1

CATH: 3.30.63.10 , 3.40.50.300

Database links Help

Blocks: IPB008145

Interactions Help

This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008145

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00305 Voltage-dependent L-type calcium channel subunit beta-4

O70589 Peripheral plasma membrane protein CASK

P15454 Guanylate kinase

P31007 Disks large 1 tumor suppressor protein

P54936 Protein lin-2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008145	Guanylate kinase/L-type calcium channel
IPR000584	Voltage-dependent calcium channel, L-type, beta subunit
IPR008144	Guanylate kinase
IPR017442	Serine/threonine-protein kinase-like domain
IPR001452	Src homology-3 domain
IPR004172	L27
IPR008266	Tyrosine-protein kinase, active site
IPR015143	L27-1
IPR017665	Guanylate kinase, sub-group
IPR011009	Protein kinase-like domain
IPR020590	Guanylate kinase, conserved site
IPR001478	PDZ/DHR/GLGF
IPR014775	L27, C-terminal
IPR000719	Protein kinase, catalytic domain
IPR002290	Serine/threonine-protein kinase domain
IPR011511	Variant SH3
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Stehle T, Schulz GE. Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution. J. Mol. Biol. 224 1127-41 1992 [PubMed: 1314905] http://dx.doi.org/10.1016/0022-2836(92)90474-X
2.	Bryant PJ, Woods DF. A major palmitoylated membrane protein of human erythrocytes shows homology to yeast guanylate kinase and to the product of a Drosophila tumor suppressor gene. Cell 68 621-2 1992 [PubMed: 1310897] http://dx.doi.org/10.1016/0092-8674(92)90136-Z
3.	Zschocke PD, Schiltz E, Schulz GE. Purification and sequence determination of guanylate kinase from pig brain. Eur. J. Biochem. 213 263-9 1993 [PubMed: 8097461] http://dx.doi.org/10.1111/j.1432-1033.1993.tb17757.x
4.	Goebl MG. Is the erythrocyte protein p55 a membrane-bound guanylate kinase? Trends Biochem. Sci. 17 99 1992 [PubMed: 1329277] http://dx.doi.org/10.1016/0968-0004(92)90244-4

Additional Reading Open in usermanual
	Hible G, Renault L, Schaeffer F, Christova P, Zoe Radulescu A, Evrin C, Gilles AM, Cherfils J. Calorimetric and crystallographic analysis of the oligomeric structure of Escherichia coli GMP kinase. J. Mol. Biol. 352 2005 1044-59 [PubMed: 16140325] http://dx.doi.org/10.1016/j.jmb.2005.07.042
	Hible G, Christova P, Renault L, Seclaman E, Thompson A, Girard E, Munier-Lehmann H, Cherfils J. Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase. Proteins 62 2006 489-500 [PubMed: 16288457] http://dx.doi.org/10.1002/prot.20662
	Zhang Y, Luan Z, Liu A, Hu G. The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins. FEBS Lett. 497 2001 99-102 [PubMed: 11377421] http://dx.doi.org/10.1016/S0014-5793(01)02450-4
	Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R. Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Mol. Biochem. Parasitol. 151 2007 100-10 [PubMed: 17125854] http://dx.doi.org/10.1016/j.molbiopara.2006.10.011
	Hanada T, Lin L, Tibaldi EV, Reinherz EL, Chishti AH. GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes. J. Biol. Chem. 275 2000 28774-84 [PubMed: 10859302] http://dx.doi.org/10.1074/jbc.M000715200
	Hible G, Daalova P, Gilles AM, Cherfils J. Crystal structures of GMP kinase in complex with ganciclovir monophosphate and Ap5G. Biochimie 88 2006 1157-64 [PubMed: 16690197] http://dx.doi.org/10.1016/j.biochi.2006.04.002
	Van Petegem F, Clark KA, Chatelain FC, Minor DL Jr. Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain. Nature 429 2004 671-5 [PubMed: 15141227] http://dx.doi.org/10.1038/nature02588

InterPro 24.0