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Protein

cGMP-gated cation channel alpha-1

Gene

Cnga1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei538cGMPSequence analysis1
Binding sitei553cGMPSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi479 – 601cGMPSequence analysisAdd BLAST123

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel
Biological processIon transport, Sensory transduction, Transport, Vision
LigandcGMP, cGMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2485179 Activation of the phototransduction cascade
R-MMU-2514859 Inactivation, recovery and regulation of the phototransduction cascade

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-gated cation channel alpha-1
Alternative name(s):
Cyclic nucleotide-gated cation channel 1
Cyclic nucleotide-gated channel alpha-1
Short name:
CNG channel alpha-1
Short name:
CNG-1
Short name:
CNG1
Cyclic nucleotide-gated channel, photoreceptor
Rod photoreceptor cGMP-gated channel subunit alpha
Gene namesi
Name:Cnga1
Synonyms:Cncg, Cncg1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:88436 Cnga1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 156CytoplasmicSequence analysisAdd BLAST156
Transmembranei157 – 177Helical; Name=H1Sequence analysisAdd BLAST21
Topological domaini178 – 190ExtracellularSequence analysisAdd BLAST13
Transmembranei191 – 209Helical; Name=H2Sequence analysisAdd BLAST19
Topological domaini210 – 233CytoplasmicSequence analysisAdd BLAST24
Transmembranei234 – 253Helical; Name=H3Sequence analysisAdd BLAST20
Topological domaini254 – 291ExtracellularSequence analysisAdd BLAST38
Transmembranei292 – 314Helical; Name=H4Sequence analysisAdd BLAST23
Topological domaini315 – 366CytoplasmicSequence analysisAdd BLAST52
Transmembranei367 – 386Helical; Name=H5Sequence analysisAdd BLAST20
Topological domaini387 – 470ExtracellularSequence analysisAdd BLAST84
Transmembranei471 – 491Helical; Name=H6Sequence analysisAdd BLAST21
Topological domaini492 – 684CytoplasmicSequence analysisAdd BLAST193

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002193091 – 684cGMP-gated cation channel alpha-1Add BLAST684

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi417N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP29974
PaxDbiP29974
PRIDEiP29974

PTM databases

iPTMnetiP29974
PhosphoSitePlusiP29974

Expressioni

Tissue specificityi

Rod cells in the retina and inner medulla of kidney.

Gene expression databases

BgeeiENSMUSG00000067220
CleanExiMM_CNGA1
ExpressionAtlasiP29974 baseline and differential
GenevisibleiP29974 MM

Interactioni

Subunit structurei

Tetramer formed of three CNGA1 and one CNGB1 modulatory subunits.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000084464

Structurei

3D structure databases

ProteinModelPortaliP29974
SMRiP29974
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili615 – 658By similarityAdd BLAST44

Domaini

The C-terminal coiled-coil domain mediates homotrimerization of CNGA subunits.By similarity

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0500 Eukaryota
ENOG410YWWI LUCA
GeneTreeiENSGT00900000140801
HOGENOMiHOG000007898
HOVERGENiHBG000281
InParanoidiP29974
KOiK04948
OMAiMRHFKVK
OrthoDBiEOG091G03EW
PhylomeDBiP29974
TreeFamiTF319048

Family and domain databases

CDDicd00038 CAP_ED, 1 hit
Gene3Di2.60.120.10, 1 hit
InterProiView protein in InterPro
IPR032406 CLZ_dom
IPR032945 CNGA1
IPR018490 cNMP-bd-like
IPR018488 cNMP-bd_CS
IPR000595 cNMP-bd_dom
IPR005821 Ion_trans_dom
IPR014710 RmlC-like_jellyroll
PANTHERiPTHR10217:SF387 PTHR10217:SF387, 1 hit
PfamiView protein in Pfam
PF16526 CLZ, 1 hit
PF00027 cNMP_binding, 1 hit
PF00520 Ion_trans, 1 hit
SMARTiView protein in SMART
SM00100 cNMP, 1 hit
SUPFAMiSSF51206 SSF51206, 1 hit
PROSITEiView protein in PROSITE
PS00888 CNMP_BINDING_1, 1 hit
PS00889 CNMP_BINDING_2, 1 hit
PS50042 CNMP_BINDING_3, 1 hit

Sequencei

Sequence statusi: Complete.

P29974-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTNIINTWH SFVNIPNVIV PAIEKEIRRM ENGACSSFSD DDNGSLSEES
60 70 80 90 100
ENEDSFFRSN SYKRRGPSQR EQHLPGTMAL FNVNNSSNKD QEPKEKKKKK
110 120 130 140 150
KEKKSKADDK NENKKDPEKK KKKEKEKEKK KKEEKTKEKK EEEKKEVVVI
160 170 180 190 200
DPSGNTYYNW LFCITLPVMY NWTMIIARAC FDELQSDYLE YWLIFDYVSD
210 220 230 240 250
VVYLADMFVR TRTGYLEQGL LVKDRMKLIE KYKANLQFKL DVLSVIPTDL
260 270 280 290 300
LYIKFGWNYP EIRLNRLLRI SRMFEFFQRT ETRTNYPNIF RISNLVMYIV
310 320 330 340 350
IIIHWNACVY YSISKAIGFG NDTWVYPDVN DPEFGRLARK YVYSLYWSTL
360 370 380 390 400
TLTTIGETPP PVLDSEYIFV VVDFLIGVLI FATIVGNIGS MISNMNAARA
410 420 430 440 450
EFQSRVDAIK QYMNFRNVSK DMEKRVIKWF DYLWTNKKTV DEREVLRYLP
460 470 480 490 500
DKLRAEIAIN VHLDTLKKVR IFADCEAGLL VELVLKLQPQ VYSPGDYICK
510 520 530 540 550
KGDIGREMYI IKEGKLAVVA DDGITQFVVL SDGSYFGEIS ILNIKGSKAG
560 570 580 590 600
NRRTANIKSI GYSDLFCLSK DDLMEALTEY PDAKTMLEEK GRQILMKDGL
610 620 630 640 650
LDINIANMGS DPKDLEEKVT RMEGSVDLLQ TRFARILAEY ESMQQKLKQR
660 670 680
LTKVEKFLKP LIETEFSALE EPGGESELTE SLQD
Length:684
Mass (Da):79,460
Last modified:November 1, 1997 - v2
Checksum:i13EC2A405B6B8CBF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti113 – 114NK → I in AAA37425 (PubMed:1372902).Curated2
Sequence conflicti200D → N in AAA37425 (PubMed:1372902).Curated1
Sequence conflicti576A → V in AAA37425 (PubMed:1372902).Curated1
Sequence conflicti635R → C in AAA37425 (PubMed:1372902).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84742 mRNA Translation: AAA37425.1
U19717 mRNA Translation: AAA85702.1
U19715 mRNA Translation: AAA85700.1
U19716 mRNA Translation: AAA85701.1
BC141261 mRNA Translation: AAI41262.1
CCDSiCCDS19333.1
RefSeqiNP_031749.2, NM_007723.2
UniGeneiMm.436652

Genome annotation databases

EnsembliENSMUST00000087213; ENSMUSP00000084464; ENSMUSG00000067220
ENSMUST00000169997; ENSMUSP00000132329; ENSMUSG00000067220
ENSMUST00000201463; ENSMUSP00000143881; ENSMUSG00000067220
GeneIDi12788
KEGGimmu:12788
UCSCiuc008xrr.1 mouse

Similar proteinsi

Entry informationi

Entry nameiCNGA1_MOUSE
AccessioniPrimary (citable) accession number: P29974
Secondary accession number(s): B9EJ09, Q60776
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 155 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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