CNGA1 Membrane Protein Introduction

Introduction of CNGA1

Cyclic nucleotide-gated channel alpha 1, also known as CNGA1, CNG1 or CNCG1, is encoded by the gene CNGA1. CNGA1 contains six transmembrane segments (6 TMs) with a pore domain between TM5 and TM6, a cytoplasmic N terminal tail and a C terminal comprising a cNMP binding site and a leucine zipper homology domain (CLZ). Along with another protein, CNGA1 forms a cGMP-gated cation channel in the plasma membrane, allowing depolarization of rod photoreceptors. CNGA1 forms a heterotetramer with CNGB1 formed by three A and one B subunits.

Basic Information of CNGA1
Protein Name	cGMP-gated cation channel alpha-1
Gene Name	CNGA1
Aliases	Cyclic nucleotide-gated cation channel 1, Cyclic nucleotide-gated channel alpha-1, CNG channel alpha-1, CNG-1, CNG1, Cyclic nucleotide-gated channel, photoreceptor, Rod photoreceptor cGMP-gated channel subunit alpha, CNCG, CNCG1
Organism	Homo sapiens (Human)
UniProt ID	P29973
Transmembrane Times	6
Length (aa)	690
Sequence	MKLSMKNNIINTQQSFVTMPNVIVPDIEKEIRRMENGACSSFSEDDDSASTSEESENENPHARGSFSYKSLRKGGPSQREQYLPGAIALFNVNNSSNKDQEPEEKKKKKKEKKSKSDDKNENKNDPEKKKKKKDKEKKKKEEKSKDKKEEEKKEVVVIDPSGNTYYNWLFCITLPVMYNWTMVIARACFDELQSDYLEYWLILDYVSDIVYLIDMFVRTRTGYLEQGLLVKEELKLINKYKSNLQFKLDVLSLIPTDLLYFKLGWNYPEIRLNRLLRFSRMFEFFQRTETRTNYPNIFRISNLVMYIVIIIHWNACVFYSISKAIGFGNDTWVYPDINDPEFGRLARKYVYSLYWSTLTLTTIGETPPPVRDSEYVFVVVDFLIGVLIFATIVGNIGSMISNMNAARAEFQARIDAIKQYMHFRNVSKDMEKRVIKWFDYLWTNKKTVDEKEVLKYLPDKLRAEIAINVHLDTLKKVRIFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVVLSDGSYFGEISILNIKGSKAGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPDAKTMLEEKGKQILMKDGLLDLNIANAGSDPKDLEEKVTRMEGSVDLLQTRFARILAEYESMQQKLKQRLTKVEKFLKPLIDTEFSSIEGPGAESGPIDST

Function of CNGA1 Membrane Protein

CNGA1 is an important member of CNG channels, which are important mediators in the visual and olfactory transduction pathways. They are expressed in rod photoreceptors and open in response to direct binding of cyclic nucleotides, and also present in a variety of other tissues where they likely function to facilitate Ca²⁺ entry. In rod photoreceptors, CNG channels open in dark conditions and a steady inward current - referred to as the dark current - flows through them keeping photoreceptor membrane depolarized. CNG channels are also expressed throughout the brain, where they can modulate neuronal excitability and long-term potentiation. CNG channels have been known to be blocked by divalent cations such as Ca²⁺ and Mg²⁺. GRB14 interacts with the CNGA1 and decreases its affinity for cyclic guanosine monophosphate.

Fig.1 An example of the role of cyclic nucleotide-gated ion channels in sea urchin sperm chemotaxis.

Application of CNGA1 Membrane Protein in Literature

Aman T.K., et al. Regulation of CNGA1 Channel Gating by Interactions with the Membrane. J Biol Chem. 2016, 291(19): 9939-9947. PubMed ID: 26969165

This article shows that restraining the A' helix following the S6 transmembrane segment to the plasma membrane potentiates CNGA1 channel opening.
Maity S., et al. Conformational rearrangements in the transmembrane domain of CNGA1 channels revealed by single-molecule force spectroscopy. Nat Commun. 2015, 6: 7093. PubMed ID: 25963832

This article reveals that CNG transmembrane domains have dynamic structure and establishes SMFS as a tool for probing conformational change in ion channels.
Wiik A.C., et al. Progressive retinal atrophy in Shetland sheepdog is associated with a mutation in the CNGA1 gene. Anim Genet. 2015, 46(5): 515-521. PubMed ID: 26202106

This article shows that genetic heterogeneity as the mutation is present in all PRA-affected individuals in one large family of Shelties, whereas some other cases in the studied Sheltie population are not associated with this CNGA1 mutation.
Arcangeletti M., et al. Multiple mechanisms underlying rectification in retinal cyclic nucleotide-gated (CNGA1) channels. Physiol Rep. 2013, 1(6): e00148. PubMed ID: 24400150

The authors demonstrate that there exist distinct mechanisms underlying rectification in CNG channels. Restricted motion of the S4 helix together with an inefficient coupling to the channel gate renders CNGA1 channels poorly sensitive to voltage in the presence of physiological Na(+) and K(+).
Marchesi A., et al. A ring of threonines in the inner vestibule of the pore of CNGA1 channels constitutes a binding site for permeating ions. J Physiol. 2012, 590(20): 5075-5090. PubMed ID: 22869010

This article reveals that the ring of Thr360 at the intracellular entrance of the selectivity filter forms another ion binding site in the CNGA1 channel.

CNGA1 Preparation Options

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-CNGA1 antibody development services.

Creative Biolabs' skillful scientists are glad to leverage our expertise and advanced technologies to help you with the member protein research. If you are interested, please feel free to contact us for more details.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

	USA: Europe: Germany:
	Call us at: USA: UK: Germany:
	Fax:
	Email: