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P29973

- CNGA1_HUMAN

UniProt

P29973 - CNGA1_HUMAN

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Protein

cGMP-gated cation channel alpha-1

Gene

CNGA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei546 – 5461cGMPSequence Analysis
Binding sitei561 – 5611cGMPSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi487 – 609123cGMPSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. cGMP binding Source: RefGenome
  2. intracellular cAMP activated cation channel activity Source: RefGenome
  3. intracellular cGMP activated cation channel activity Source: RefGenome
  4. voltage-gated potassium channel activity Source: RefGenome

GO - Biological processi

  1. phototransduction, visible light Source: Reactome
  2. potassium ion transmembrane transport Source: RefGenome
  3. regulation of membrane potential Source: RefGenome
  4. regulation of rhodopsin mediated signaling pathway Source: Reactome
  5. rhodopsin mediated signaling pathway Source: Reactome
  6. transport Source: ProtInc
  7. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel

Keywords - Biological processi

Ion transport, Sensory transduction, Transport, Vision

Keywords - Ligandi

cGMP, cGMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_163932. Activation of the phototransduction cascade.

Protein family/group databases

TCDBi1.A.1.5.3. the voltage-gated ion channel (vic) superfamily.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:2148. CNGA1.

Subcellular locationi

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
  2. photoreceptor outer segment membrane Source: Ensembl
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 49 (RP49) [MIM:613756]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti320 – 3201S → F in RP49. 1 Publication
Corresponds to variant rs62625014 [ dbSNP | Ensembl ].
VAR_009297

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

MIMi613756. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA26658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 690690cGMP-gated cation channel alpha-1PRO_0000219308Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi425 – 4251N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP29973.
PRIDEiP29973.

PTM databases

PhosphoSiteiP29973.

Expressioni

Tissue specificityi

Rod cells in the retina.

Gene expression databases

BgeeiP29973.
CleanExiHS_CNGA1.
ExpressionAtlasiP29973. baseline and differential.
GenevestigatoriP29973.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB14Q5ICW44EBI-8417095,EBI-7639273From a different organism.
Grb14Q9JLM92EBI-8417095,EBI-8347358From a different organism.

Protein-protein interaction databases

BioGridi107659. 1 interaction.
IntActiP29973. 2 interactions.
MINTiMINT-7004260.
STRINGi9606.ENSP00000384264.

Structurei

3D structure databases

ProteinModelPortaliP29973.
SMRiP29973. Positions 348-596, 623-672.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 164164CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini186 – 19813ExtracellularSequence AnalysisAdd
BLAST
Topological domaini218 – 24124CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini262 – 29938ExtracellularSequence AnalysisAdd
BLAST
Topological domaini323 – 37452CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini395 – 47884ExtracellularSequence AnalysisAdd
BLAST
Topological domaini500 – 690191CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei165 – 18521Helical; Name=H1Sequence AnalysisAdd
BLAST
Transmembranei199 – 21719Helical; Name=H2Sequence AnalysisAdd
BLAST
Transmembranei242 – 26120Helical; Name=H3Sequence AnalysisAdd
BLAST
Transmembranei300 – 32223Helical; Name=H4Sequence AnalysisAdd
BLAST
Transmembranei375 – 39420Helical; Name=H5Sequence AnalysisAdd
BLAST
Transmembranei479 – 49921Helical; Name=H6Sequence AnalysisAdd
BLAST

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili623 – 66644By similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300025.
GeneTreeiENSGT00760000118772.
HOGENOMiHOG000007898.
HOVERGENiHBG000281.
InParanoidiP29973.
KOiK04948.
OMAiWTMVIAR.
OrthoDBiEOG771268.
PhylomeDBiP29973.
TreeFamiTF319048.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P29973-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MKLSMKNNII NTQQSFVTMP NVIVPDIEKE IRRMENGACS SFSEDDDSAS
60 70 80 90 100
TSEESENENP HARGSFSYKS LRKGGPSQRE QYLPGAIALF NVNNSSNKDQ
110 120 130 140 150
EPEEKKKKKK EKKSKSDDKN ENKNDPEKKK KKKDKEKKKK EEKSKDKKEE
160 170 180 190 200
EKKEVVVIDP SGNTYYNWLF CITLPVMYNW TMVIARACFD ELQSDYLEYW
210 220 230 240 250
LILDYVSDIV YLIDMFVRTR TGYLEQGLLV KEELKLINKY KSNLQFKLDV
260 270 280 290 300
LSLIPTDLLY FKLGWNYPEI RLNRLLRFSR MFEFFQRTET RTNYPNIFRI
310 320 330 340 350
SNLVMYIVII IHWNACVFYS ISKAIGFGND TWVYPDINDP EFGRLARKYV
360 370 380 390 400
YSLYWSTLTL TTIGETPPPV RDSEYVFVVV DFLIGVLIFA TIVGNIGSMI
410 420 430 440 450
SNMNAARAEF QARIDAIKQY MHFRNVSKDM EKRVIKWFDY LWTNKKTVDE
460 470 480 490 500
KEVLKYLPDK LRAEIAINVH LDTLKKVRIF ADCEAGLLVE LVLKLQPQVY
510 520 530 540 550
SPGDYICKKG DIGREMYIIK EGKLAVVADD GVTQFVVLSD GSYFGEISIL
560 570 580 590 600
NIKGSKAGNR RTANIKSIGY SDLFCLSKDD LMEALTEYPD AKTMLEEKGK
610 620 630 640 650
QILMKDGLLD LNIANAGSDP KDLEEKVTRM EGSVDLLQTR FARILAEYES
660 670 680 690
MQQKLKQRLT KVEKFLKPLI DTEFSSIEGP GAESGPIDST
Length:690
Mass (Da):79,586
Last modified:June 16, 2009 - v3
Checksum:iF1045A210FE33DC0
GO
Isoform 2 (identifier: P29973-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MESRSSPRLECSGAISAHCSLHLPDSSDFQLIFVFLVEMGFHHVGQAGLELLISSDLPTSASQSAGITDM

Note: No experimental confirmation available.

Show »
Length:759
Mass (Da):86,900
Checksum:i5612065090CCE338
GO

Sequence cautioni

The sequence AAB22778.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351E → V in BAF84710. (PubMed:14702039)Curated
Sequence conflicti50 – 501S → Y in AAA52010. (PubMed:1372902)Curated
Sequence conflicti89 – 891L → I in AAA52010. (PubMed:1372902)Curated
Sequence conflicti150 – 1512EE → HH in AAA52010. (PubMed:1372902)Curated
Sequence conflicti209 – 2091I → V in BAF84710. (PubMed:14702039)Curated
Sequence conflicti543 – 5431Y → T in AAA52010. (PubMed:1372902)Curated
Sequence conflicti681 – 6822GA → WS in AAA52010. (PubMed:1372902)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321R → Q.1 Publication
Corresponds to variant rs76537883 [ dbSNP | Ensembl ].
VAR_009295
Natural varianti118 – 1181D → N.1 Publication
Corresponds to variant rs28642966 [ dbSNP | Ensembl ].
VAR_009296
Natural varianti122 – 1221N → D.
Corresponds to variant rs28642966 [ dbSNP | Ensembl ].
VAR_047385
Natural varianti320 – 3201S → F in RP49. 1 Publication
Corresponds to variant rs62625014 [ dbSNP | Ensembl ].
VAR_009297

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MESRSSPRLECSGAISAHCS LHLPDSSDFQLIFVFLVEMG FHHVGQAGLELLISSDLPTS ASQSAGITDM in isoform 2. 1 PublicationVSP_047170

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84741 mRNA. Translation: AAA52010.1.
S42457 mRNA. Translation: AAB22778.1. Different initiation.
AK292021 mRNA. Translation: BAF84710.1.
AC096749 Genomic DNA. No translation available.
AC107068 Genomic DNA. Translation: AAY40919.1.
CH471069 Genomic DNA. Translation: EAW93048.1.
S76062 Genomic DNA. Translation: AAD14206.1.
CCDSiCCDS43226.1. [P29973-1]
CCDS47050.1. [P29973-2]
PIRiA42161.
RefSeqiNP_000078.2. NM_000087.3. [P29973-1]
NP_001136036.1. NM_001142564.1. [P29973-2]
XP_005248106.1. XM_005248049.2. [P29973-1]
UniGeneiHs.1323.

Genome annotation databases

EnsembliENST00000358519; ENSP00000351320; ENSG00000198515. [P29973-1]
ENST00000402813; ENSP00000384264; ENSG00000198515. [P29973-2]
ENST00000420489; ENSP00000389881; ENSG00000198515. [P29973-1]
ENST00000514170; ENSP00000426862; ENSG00000198515. [P29973-1]
ENST00000544810; ENSP00000443401; ENSG00000198515. [P29973-2]
GeneIDi1259.
KEGGihsa:1259.
UCSCiuc003gxt.4. human. [P29973-1]

Polymorphism databases

DMDMi239938910.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the CNGA1 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84741 mRNA. Translation: AAA52010.1 .
S42457 mRNA. Translation: AAB22778.1 . Different initiation.
AK292021 mRNA. Translation: BAF84710.1 .
AC096749 Genomic DNA. No translation available.
AC107068 Genomic DNA. Translation: AAY40919.1 .
CH471069 Genomic DNA. Translation: EAW93048.1 .
S76062 Genomic DNA. Translation: AAD14206.1 .
CCDSi CCDS43226.1. [P29973-1 ]
CCDS47050.1. [P29973-2 ]
PIRi A42161.
RefSeqi NP_000078.2. NM_000087.3. [P29973-1 ]
NP_001136036.1. NM_001142564.1. [P29973-2 ]
XP_005248106.1. XM_005248049.2. [P29973-1 ]
UniGenei Hs.1323.

3D structure databases

ProteinModelPortali P29973.
SMRi P29973. Positions 348-596, 623-672.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107659. 1 interaction.
IntActi P29973. 2 interactions.
MINTi MINT-7004260.
STRINGi 9606.ENSP00000384264.

Chemistry

ChEMBLi CHEMBL1628476.
GuidetoPHARMACOLOGYi 394.

Protein family/group databases

TCDBi 1.A.1.5.3. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSitei P29973.

Polymorphism databases

DMDMi 239938910.

Proteomic databases

PaxDbi P29973.
PRIDEi P29973.

Protocols and materials databases

DNASUi 1259.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358519 ; ENSP00000351320 ; ENSG00000198515 . [P29973-1 ]
ENST00000402813 ; ENSP00000384264 ; ENSG00000198515 . [P29973-2 ]
ENST00000420489 ; ENSP00000389881 ; ENSG00000198515 . [P29973-1 ]
ENST00000514170 ; ENSP00000426862 ; ENSG00000198515 . [P29973-1 ]
ENST00000544810 ; ENSP00000443401 ; ENSG00000198515 . [P29973-2 ]
GeneIDi 1259.
KEGGi hsa:1259.
UCSCi uc003gxt.4. human. [P29973-1 ]

Organism-specific databases

CTDi 1259.
GeneCardsi GC04M047853.
GeneReviewsi CNGA1.
H-InvDB HIX0031530.
HIX0031590.
HGNCi HGNC:2148. CNGA1.
MIMi 123825. gene.
613756. phenotype.
neXtProti NX_P29973.
Orphaneti 791. Retinitis pigmentosa.
PharmGKBi PA26658.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300025.
GeneTreei ENSGT00760000118772.
HOGENOMi HOG000007898.
HOVERGENi HBG000281.
InParanoidi P29973.
KOi K04948.
OMAi WTMVIAR.
OrthoDBi EOG771268.
PhylomeDBi P29973.
TreeFami TF319048.

Enzyme and pathway databases

Reactomei REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_163932. Activation of the phototransduction cascade.

Miscellaneous databases

GeneWikii Cyclic_nucleotide-gated_channel_alpha_1.
GenomeRNAii 1259.
NextBioi 35535235.
PROi P29973.
SOURCEi Search...

Gene expression databases

Bgeei P29973.
CleanExi HS_CNGA1.
ExpressionAtlasi P29973. baseline and differential.
Genevestigatori P29973.

Family and domain databases

Gene3Di 2.60.120.10. 1 hit.
InterProi IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view ]
Pfami PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view ]
SMARTi SM00100. cNMP. 1 hit.
[Graphical view ]
SUPFAMi SSF51206. SSF51206. 1 hit.
PROSITEi PS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure and chromosomal localization of human and mouse rod photoreceptor cGMP-gated cation channel."
    Pittler S.J., Lee A.K., Altherr M.R., Howard T.A., Seldin M.F., Hurwitz R.L., Wasmuth J.J., Baehr W.
    J. Biol. Chem. 267:6257-6262(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  2. "Human rod photoreceptor cGMP-gated channel: amino acid sequence, gene structure, and functional expression."
    Dhallan R.S., Macke J.P., Eddy R.L., Shows T.B., Reed R.R., Yau K.-W., Nathans J.
    J. Neurosci. 12:3248-3256(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Retina.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Spleen.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells."
    Distler M., Biel M., Flockerzi V., Hofmann F.
    Neuropharmacology 33:1275-1282(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 317-577.
  7. "Mutations in the gene encoding the alpha subunit of the rod cGMP-gated channel in autosomal recessive retinitis pigmentosa."
    Dryja T.P., Finn J.T., Peng Y.-W., McGee T.L., Berson E.L., Yau K.-W.
    Proc. Natl. Acad. Sci. U.S.A. 92:10177-10181(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RP49 PHE-320, VARIANTS GLN-32 AND ASN-118.
  8. "Autosomal recessive retinitis pigmentosa in a Pakistani family mapped to CNGA1 with identification of a novel mutation."
    Zhang Q., Zulfiqar F., Riazuddin S.A., Xiao X., Ahmad Z., Riazuddin S., Hejtmancik J.F.
    Mol. Vis. 10:884-889(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RP49.

Entry informationi

Entry nameiCNGA1_HUMAN
AccessioniPrimary (citable) accession number: P29973
Secondary accession number(s): A8K7K6
, J3KPZ2, Q16279, Q16485, Q4W5E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 16, 2009
Last modified: October 29, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3