Q3UW12 (CNGA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclic nucleotide-gated cation channel alpha-4

Alternative name(s):
Cyclic nucleotide-gated channel alpha-4
Short name=CNG channel alpha-4
Short name=CNG-4
Short name=CNG4

Gene names

Name:

Cnga4

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Second messenger, cAMP, causes the opening of cation-selective cyclic nucleotide-gated (CNG) channels and depolarization of the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory subunit of this channel which is known to play a central role in the transduction of odorant signals and subsequent adaptation. By accelerating the calcium-mediated negative feedback in olfactory signaling it allows rapid adaptation to odor stimulation and extends its range of odor detection. Ref.3 Ref.4
Enzyme regulation	Calcium-calmodulin exerts its inhibitory effect in cAMP sensitivity by binding to IQ-like motif of CNGA4 and preferably binds to the channel in the closed state. Inhibition by PIP3 of the CNG channel probably occurs via CGNA2 binding By similarity.
Subunit structure	Heterotetramer composed of two subunits of CNGA2, one of CNGA4 and one of CNGB1b. The complex forms the cyclic nucleotide-gated (CNG) channel of olfactory neurons By similarity.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Domain	The C-terminal coiled-coil domain mediates trimerization of CNGA subunits By similarity.
Sequence similarities	Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family. CNGA4 subfamily. [View classification] Contains 1 cyclic nucleotide-binding domain.

Ontologies

Keywords
Biological process	Ion transport Olfaction Sensory transduction Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	Nucleotide-binding cAMP cAMP-binding
Molecular function	Ion channel Ligand-gated ion channel
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to stimulus Inferred from electronic annotation. Source: UniProtKB-KW sensory perception of smell Inferred from mutant phenotype Ref.3Ref.4. Source: MGI
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW ion channel activity Traceable author statement Ref.4. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q3UW12-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q3UW12-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-103: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 575	575	Cyclic nucleotide-gated cation channel alpha-4		PRO_0000317108
Regions
	Topological domain	1 – 33	33	Cytoplasmic Potential
	Transmembrane	34 – 54	21	Helical; Name=H1; Potential
	Topological domain	55 – 65	11	Extracellular Potential
	Transmembrane	66 – 86	21	Helical; Name=H2; Potential
	Topological domain	87 – 112	26	Cytoplasmic Potential
	Transmembrane	113 – 133	21	Helical; Name=H3; Potential
	Topological domain	134 – 168	35	Extracellular Potential
	Transmembrane	169 – 189	21	Helical; Name=H4; Potential
	Topological domain	190 – 218	29	Cytoplasmic Potential
	Transmembrane	219 – 239	21	Helical; Name=H5; Potential
	Topological domain	240 – 244	5	Extracellular Potential
	Transmembrane	245 – 265	21	Helical; Name=H6; Potential
	Topological domain	266 – 575	310	Cytoplasmic Potential
	Nucleotide binding	348 – 471	124	cNMP
	Coiled coil	493 – 536	44	By similarity
	Motif	292 – 302	11	IQ-type By similarity
Natural variations
	Alternative sequence	1 – 103	103	Missing in isoform 2.		VSP_030873

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 2E79D58D658D4930	FASTA	575	65,835
	10 20 30 40 50 60 MSQDSKVKTT ESTPPAPTKA RKWLPVLDPS GDYYYWWLNT MVFPIMYNLI IVVCRACFPD 70 80 90 100 110 120 LQHSYLVAWF VLDYTSDLLY LLDIGVRFHT GFLEQGILVV DKSMIASRYV RTWSFLLDLA 130 140 150 160 170 180 SLVPTDAAYV QLGPHIPTLR LNRFLRVPRL FEAFDRTETR TAYPNAFRIA KLMIYIFVVI 190 200 210 220 230 240 HWNSCLYFAL SRYLGFGRDA WVYPDPAQPG FERLRRQYLY SFYFSTLILT TVGDTPLPAR 250 260 270 280 290 300 EEEYLFMVGD FLLAVMGFAT IMGSMSSVIY NMNTADAAFY PDHALVKKYM KLQHVNRRLE 310 320 330 340 350 360 RRVIDWYQHL QINKKMTNEV AILQHLPERL RAEVAVSVHL STLSRVQIFQ NCEASLLEEL 370 380 390 400 410 420 VLKLQPQTYS PGEYVCRKGD IGREMYIIRE GQLAVVADDG VTQYAVLGAG LYFGEISIIN 430 440 450 460 470 480 IKGNMSGNRR TANIKSLGYS DLFCLSKEDL REVLSEYPQA QAVMEEKGRE ILLKMNKLDV 490 500 510 520 530 540 NAEAAEIALQ EATESRLKGL DQQLDDLQTK FARLLAELES SALKIAYRIE RLEWQTREWP 550 560 570 MPDDMGEADD EAEPGEGTSK DGEEKAGQEG PSGLE
	Isoform 2 [UniParc]. Checksum: 1918AAA0241CD635	FASTA	472	53,899
	10 20 30 40 50 60 MIASRYVRTW SFLLDLASLV PTDAAYVQLG PHIPTLRLNR FLRVPRLFEA FDRTETRTAY 70 80 90 100 110 120 PNAFRIAKLM IYIFVVIHWN SCLYFALSRY LGFGRDAWVY PDPAQPGFER LRRQYLYSFY 130 140 150 160 170 180 FSTLILTTVG DTPLPAREEE YLFMVGDFLL AVMGFATIMG SMSSVIYNMN TADAAFYPDH 190 200 210 220 230 240 ALVKKYMKLQ HVNRRLERRV IDWYQHLQIN KKMTNEVAIL QHLPERLRAE VAVSVHLSTL 250 260 270 280 290 300 SRVQIFQNCE ASLLEELVLK LQPQTYSPGE YVCRKGDIGR EMYIIREGQL AVVADDGVTQ 310 320 330 340 350 360 YAVLGAGLYF GEISIINIKG NMSGNRRTAN IKSLGYSDLF CLSKEDLREV LSEYPQAQAV 370 380 390 400 410 420 MEEKGREILL KMNKLDVNAE AAEIALQEAT ESRLKGLDQQ LDDLQTKFAR LLAELESSAL 430 440 450 460 470 KIAYRIERLE WQTREWPMPD DMGEADDEAE PGEGTSKDGE EKAGQEGPSG LE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Epididymis.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[3]	"Central role of the CNGA4 channel subunit in Ca2+-calmodulin-dependent odor adaptation." Munger S.D., Lane A.P., Zhong H., Leinders-Zufall T., Yau K.-W., Zufall F., Reed R.R. Science 294:2172-2175(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Importance of the CNGA4 channel gene for odor discrimination and adaptation in behaving mice." Kelliher K.R., Ziesmann J., Munger S.D., Reed R.R., Zufall F. Proc. Natl. Acad. Sci. U.S.A. 100:4299-4304(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK136723 mRNA. Translation: BAE23107.1. BC107347 mRNA. Translation: AAI07348.1. BC107348 mRNA. Translation: AAI07349.1.
IPI	IPI00135600. IPI00885977.
RefSeq	NP_001028489.1. NM_001033317.3.
UniGene	Mm.99556.
3D structure databases
ProteinModelPortal	Q3UW12.
SMR	Q3UW12. Positions 286-465.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000033187.
Protein family/group databases
TCDB	1.A.1.5.4. voltage-gated ion channel (VIC) superfamily.
Proteomic databases
PRIDE	Q3UW12.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000033187; ENSMUSP00000033187; ENSMUSG00000030897.
GeneID	233649.
KEGG	mmu:233649.
UCSC	uc009iyc.1. mouse.
Organism-specific databases
CTD	1262.
MGI	MGI:2664099. Cnga4.
Phylogenomic databases
eggNOG	NOG300831.
GeneTree	ENSGT00550000074376.
HOGENOM	HOG000007898.
HOVERGEN	HBG000281.
InParanoid	Q3UW12.
KO	K04951.
OMA	VGHEMYI.
OrthoDB	EOG4229JG.
Gene expression databases
Bgee	Q3UW12.
CleanEx	MM_CNGA4.
Genevestigator	Q3UW12.
Family and domain databases
Gene3D	2.60.120.10. 1 hit.
InterPro	IPR018490. cNMP-bd-like. IPR018488. cNMP-bd_CS. IPR000595. cNMP-bd_dom. IPR005821. Ion_trans_dom. IPR014710. RmlC-like_jellyroll. [Graphical view]
Pfam	PF00027. cNMP_binding. 1 hit. PF00520. Ion_trans. 1 hit. [Graphical view]
SMART	SM00100. cNMP. 1 hit. [Graphical view]
SUPFAM	SSF51206. cNMP_binding. 1 hit.
PROSITE	PS00888. CNMP_BINDING_1. 1 hit. PS00889. CNMP_BINDING_2. 1 hit. PS50042. CNMP_BINDING_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	381781.
SOURCE	Search...

Entry information

Entry name

CNGA4_MOUSE

Accession

Primary (citable) accession number: Q3UW12
Secondary accession number(s): Q08EL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 11, 2005
Last modified:	May 29, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program