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Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 (Brain cyclic nucleotide-gated channel 1) (BCNG-1)

 HCN1_HUMAN              Reviewed;         890 AA.
O60741;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 3.
31-JAN-2018, entry version 148.
RecName: Full=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1;
AltName: Full=Brain cyclic nucleotide-gated channel 1;
Short=BCNG-1;
Name=HCN1; Synonyms=BCNG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 122-862, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9630217; DOI=10.1016/S0092-8674(00)81434-8;
Santoro B., Liu D.T., Yao H., Bartsch D., Kandel E.R.,
Siegelbaum S.A., Tibbs G.R.;
"Identification of a gene encoding a hyperpolarization-activated
'pacemaker' channel of brain.";
Cell 93:717-729(1998).
[3]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=15351778; DOI=10.1038/sj.bjp.0705945;
Gill C.H., Randall A., Bates S.A., Hill K., Owen D., Larkman P.M.,
Cairns W., Yusaf S.P., Murdock P.R., Strijbos P.J., Powell A.J.,
Benham C.D., Davies C.H.;
"Characterization of the human HCN1 channel and its inhibition by
capsazepine.";
Br. J. Pharmacol. 143:411-421(2004).
[4] {ECO:0000244|PDB:5U6O, ECO:0000244|PDB:5U6P}
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF APOPROTEIN AND IN
COMPLEX WITH CAMP, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT,
AND ENZYME REGULATION.
PubMed=28086084; DOI=10.1016/j.cell.2016.12.023;
Lee C.H., MacKinnon R.;
"Structures of the human HCN1 hyperpolarization-activated channel.";
Cell 168:111-120(2017).
[5]
INVOLVEMENT IN EIEE24, VARIANTS EIEE24 VAL-47; PHE-100; PRO-272;
TYR-279; THR-297 AND HIS-401, AND CHARACTERIZATION OF VARIANTS EIEE24
PHE-100; PRO-272; TYR-279; THR-297 AND HIS-401.
PubMed=24747641; DOI=10.1038/ng.2952;
EuroEPINOMICS RES Consortium;
Nava C., Dalle C., Rastetter A., Striano P., de Kovel C.G.,
Nabbout R., Cances C., Ville D., Brilstra E.H., Gobbi G., Raffo E.,
Bouteiller D., Marie Y., Trouillard O., Robbiano A., Keren B.,
Agher D., Roze E., Lesage S., Nicolas A., Brice A., Baulac M.,
Vogt C., El Hajj N., Schneider E., Suls A., Weckhuysen S., Gormley P.,
Lehesjoki A.E., De Jonghe P., Helbig I., Baulac S., Zara F.,
Koeleman B.P., Haaf T., LeGuern E., Depienne C.;
"De novo mutations in HCN1 cause early infantile epileptic
encephalopathy.";
Nat. Genet. 46:640-645(2014).
[6]
VARIANTS EIEE24 ILE-153 AND ASP-391.
PubMed=27864847; DOI=10.1002/humu.23149;
Clinical Study Group;
Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D.,
Bigoni S., Barba C., Mari F., Montomoli M., Pisano T., Rosati A.,
Guerrini R.;
"Diagnostic targeted resequencing in 349 patients with drug-resistant
pediatric epilepsies identifies causative mutations in 30 different
genes.";
Hum. Mutat. 38:216-225(2017).
-!- FUNCTION: Hyperpolarization-activated ion channel exhibiting weak
selectivity for potassium over sodium ions (PubMed:28086084).
Contributes to the native pacemaker currents in heart (If) and in
neurons (Ih). May mediate responses to sour stimuli.
{ECO:0000269|PubMed:15351778, ECO:0000269|PubMed:28086084}.
-!- ENZYME REGULATION: Activated by cAMP, and at 10-100 times higher
concentrations, also by cGMP. cAMP binding promotes
tetramerization and formation of an active channel. Compared to
other family members, cAMP has less stimulatory effect on HCN1
because part of the molecules already contain bound cAMP and form
homotetramers when cAMP levels are low. Inhibited by Cs(1+),
zatebradine, capsazepine and ZD7288. {ECO:0000269|PubMed:15351778,
ECO:0000269|PubMed:28086084}.
-!- SUBUNIT: Homotetramer (PubMed:28086084). Heterotetramer with HCN2.
The potassium channel is composed of a homo- or heterotetrameric
complex of pore-forming subunits. Interacts with KCNE2. Interacts
with the SH3 domain of CSK (By similarity).
{ECO:0000250|UniProtKB:O88704, ECO:0000269|PubMed:28086084}.
-!- INTERACTION:
Q4ACU6-1:Shank3 (xeno); NbExp=4; IntAct=EBI-11173743, EBI-16201983;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15351778,
ECO:0000269|PubMed:28086084}; Multi-pass membrane protein
{ECO:0000269|PubMed:15351778, ECO:0000269|PubMed:28086084}.
-!- TISSUE SPECIFICITY: Detected in brain, in particular in amygdala
and hippocampus, while expression in caudate nucleus, corpus
callosum, substantia nigra, subthalamic nucleus and thalamus is
very low or not detectable. Detected at very low levels in muscle
and pancreas. {ECO:0000269|PubMed:9630217}.
-!- DOMAIN: The segment S4 is probably the voltage-sensor and is
characterized by a series of positively charged amino acids at
every third position. {ECO:0000305|PubMed:28086084}.
-!- DISEASE: Epileptic encephalopathy, early infantile, 24 (EIEE24)
[MIM:615871]: A disease characterized by early-onset seizures,
intellectual disability of varying degrees, and behavioral
disturbances or autistic features in most individuals.
{ECO:0000269|PubMed:24747641, ECO:0000269|PubMed:27864847}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the potassium channel HCN family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC39759.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AC099514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC114975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC117529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF064876; AAC39759.1; ALT_SEQ; mRNA.
CCDS; CCDS3952.1; -.
RefSeq; NP_066550.2; NM_021072.3.
UniGene; Hs.353176; -.
PDB; 5U6O; EM; 3.50 A; A/B/C/D=1-890.
PDB; 5U6P; EM; 3.51 A; A/B/C/D=1-890.
PDBsum; 5U6O; -.
PDBsum; 5U6P; -.
ProteinModelPortal; O60741; -.
SMR; O60741; -.
BioGrid; 131543; 5.
DIP; DIP-62038N; -.
IntAct; O60741; 1.
STRING; 9606.ENSP00000307342; -.
BindingDB; O60741; -.
ChEMBL; CHEMBL1795171; -.
GuidetoPHARMACOLOGY; 400; -.
iPTMnet; O60741; -.
PhosphoSitePlus; O60741; -.
BioMuta; HCN1; -.
MaxQB; O60741; -.
PaxDb; O60741; -.
PeptideAtlas; O60741; -.
PRIDE; O60741; -.
Ensembl; ENST00000303230; ENSP00000307342; ENSG00000164588.
GeneID; 348980; -.
KEGG; hsa:348980; -.
UCSC; uc003jok.4; human.
CTD; 348980; -.
DisGeNET; 348980; -.
EuPathDB; HostDB:ENSG00000164588.5; -.
GeneCards; HCN1; -.
H-InvDB; HIX0004850; -.
HGNC; HGNC:4845; HCN1.
HPA; HPA019195; -.
MalaCards; HCN1; -.
MIM; 602780; gene.
MIM; 615871; phenotype.
neXtProt; NX_O60741; -.
OpenTargets; ENSG00000164588; -.
Orphanet; 1934; Early infantile epileptic encephalopathy.
PharmGKB; PA77; -.
eggNOG; KOG0498; Eukaryota.
eggNOG; ENOG410XPSE; LUCA.
GeneTree; ENSGT00900000140801; -.
HOGENOM; HOG000230717; -.
HOVERGEN; HBG039489; -.
InParanoid; O60741; -.
KO; K04954; -.
OMA; TRTFHYA; -.
OrthoDB; EOG091G0JQU; -.
PhylomeDB; O60741; -.
TreeFam; TF318250; -.
Reactome; R-HSA-1296061; HCN channels.
ChiTaRS; HCN1; human.
GeneWiki; HCN1; -.
GenomeRNAi; 348980; -.
PRO; PR:O60741; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000164588; -.
CleanEx; HS_HCN1; -.
ExpressionAtlas; O60741; baseline and differential.
Genevisible; O60741; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0098855; C:HCN channel complex; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030552; F:cAMP binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0005222; F:intracellular cAMP activated cation channel activity; ISS:UniProtKB.
GO; GO:0005267; F:potassium channel activity; NAS:UniProtKB.
GO; GO:0022843; F:voltage-gated cation channel activity; IDA:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; IMP:UniProtKB.
GO; GO:0005248; F:voltage-gated sodium channel activity; IMP:UniProtKB.
GO; GO:0045176; P:apical protein localization; IEA:Ensembl.
GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0042391; P:regulation of membrane potential; IMP:UniProtKB.
GO; GO:0046549; P:retinal cone cell development; IEA:Ensembl.
GO; GO:0035725; P:sodium ion transmembrane transport; IMP:UniProtKB.
CDD; cd00038; CAP_ED; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR013621; Ion_trans_N.
InterPro; IPR030169; K/Na_HCN1.
InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
InterPro; IPR014710; RmlC-like_jellyroll.
PANTHER; PTHR10217:SF373; PTHR10217:SF373; 1.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF08412; Ion_trans_N; 1.
PRINTS; PR01463; EAGCHANLFMLY.
SMART; SM00100; cNMP; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS00888; CNMP_BINDING_1; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
1: Evidence at protein level;
3D-structure; cAMP; cAMP-binding; Cell membrane; Complete proteome;
Disease mutation; Epilepsy; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Membrane; Nucleotide-binding; Polymorphism;
Potassium; Potassium channel; Potassium transport; Reference proteome;
Sodium; Sodium channel; Sodium transport; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 890 Potassium/sodium hyperpolarization-
activated cyclic nucleotide-gated channel
1.
/FTId=PRO_0000054107.
TOPO_DOM 1 142 Cytoplasmic.
{ECO:0000269|PubMed:28086084}.
TRANSMEM 143 164 Helical; Name=Segment S1.
{ECO:0000269|PubMed:28086084}.
TOPO_DOM 165 173 Extracellular.
{ECO:0000269|PubMed:28086084}.
TRANSMEM 174 194 Helical; Name=Segment S2.
{ECO:0000269|PubMed:28086084}.
TOPO_DOM 195 215 Cytoplasmic.
{ECO:0000269|PubMed:28086084}.
TRANSMEM 216 236 Helical; Name=Segment S3.
{ECO:0000269|PubMed:28086084}.
TOPO_DOM 237 260 Extracellular.
{ECO:0000269|PubMed:28086084}.
TRANSMEM 261 281 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000269|PubMed:28086084}.
TOPO_DOM 282 295 Cytoplasmic.
{ECO:0000269|PubMed:28086084}.
TRANSMEM 296 318 Helical; Name=Segment S5.
{ECO:0000269|PubMed:28086084}.
TOPO_DOM 319 344 Extracellular.
{ECO:0000269|PubMed:28086084}.
INTRAMEM 345 366 Pore-forming; Name=Segment H5.
{ECO:0000269|PubMed:28086084}.
TOPO_DOM 367 371 Extracellular.
{ECO:0000269|PubMed:28086084}.
TRANSMEM 372 392 Helical; Name=Segment S6.
{ECO:0000269|PubMed:28086084}.
TOPO_DOM 393 890 Cytoplasmic.
{ECO:0000269|PubMed:28086084}.
NP_BIND 539 542 cAMP. {ECO:0000244|PDB:5U6P,
ECO:0000305|PubMed:28086084}.
NP_BIND 549 550 cAMP. {ECO:0000244|PDB:5U6P,
ECO:0000305|PubMed:28086084}.
NP_BIND 590 593 cAMP. {ECO:0000250|UniProtKB:O88704}.
REGION 1 93 Intrinsically disordered.
{ECO:0000305|PubMed:28086084}.
MOTIF 358 362 Selectivity filter.
{ECO:0000305|PubMed:28086084}.
COMPBIAS 1 80 Gly-rich.
COMPBIAS 726 756 Gln-rich.
COMPBIAS 857 863 Poly-Pro.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 42 42 P -> S (in dbSNP:rs56164833).
/FTId=VAR_061105.
VARIANT 47 47 G -> V (in EIEE24; unknown pathological
significance; dbSNP:rs544994462).
{ECO:0000269|PubMed:24747641}.
/FTId=VAR_071825.
VARIANT 100 100 S -> F (in EIEE24; dominant-negative
mutation resulting in gain of channel
function; dbSNP:rs587777492).
{ECO:0000269|PubMed:24747641}.
/FTId=VAR_071826.
VARIANT 153 153 M -> I (in EIEE24; dbSNP:rs1057519548).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078216.
VARIANT 272 272 S -> P (in EIEE24; dominant-negative
mutation resulting in loss of channel
currents; dbSNP:rs587777493).
{ECO:0000269|PubMed:24747641}.
/FTId=VAR_071827.
VARIANT 279 279 H -> Y (in EIEE24; results in a gain of
channel function; dbSNP:rs587777495).
{ECO:0000269|PubMed:24747641}.
/FTId=VAR_071828.
VARIANT 297 297 R -> T (in EIEE24; dominant-negative
mutation resulting in loss of channel
currents; dbSNP:rs587777494).
{ECO:0000269|PubMed:24747641}.
/FTId=VAR_071829.
VARIANT 391 391 G -> D (in EIEE24; dbSNP:rs1057519547).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078217.
VARIANT 401 401 D -> H (in EIEE24; results in a gain of
channel function; dbSNP:rs587777491).
{ECO:0000269|PubMed:24747641}.
/FTId=VAR_071830.
CONFLICT 786 786 L -> F (in Ref. 2; AAC39759).
{ECO:0000305}.
CONFLICT 789 789 S -> W (in Ref. 2; AAC39759).
{ECO:0000305}.
CONFLICT 841 841 L -> F (in Ref. 2; AAC39759).
{ECO:0000305}.
CONFLICT 857 857 P -> L (in Ref. 2; AAC39759).
{ECO:0000305}.
CONFLICT 861 861 P -> L (in Ref. 2; AAC39759).
{ECO:0000305}.
HELIX 95 102 {ECO:0000244|PDB:5U6O}.
HELIX 108 114 {ECO:0000244|PDB:5U6O}.
HELIX 117 127 {ECO:0000244|PDB:5U6O}.
STRAND 130 133 {ECO:0000244|PDB:5U6O}.
HELIX 140 166 {ECO:0000244|PDB:5U6O}.
HELIX 173 195 {ECO:0000244|PDB:5U6O}.
TURN 209 211 {ECO:0000244|PDB:5U6O}.
HELIX 212 218 {ECO:0000244|PDB:5U6O}.
TURN 219 221 {ECO:0000244|PDB:5U6O}.
HELIX 222 229 {ECO:0000244|PDB:5U6O}.
HELIX 232 241 {ECO:0000244|PDB:5U6O}.
HELIX 253 264 {ECO:0000244|PDB:5U6O}.
HELIX 265 269 {ECO:0000244|PDB:5U6O}.
HELIX 270 289 {ECO:0000244|PDB:5U6O}.
HELIX 293 322 {ECO:0000244|PDB:5U6O}.
HELIX 330 333 {ECO:0000244|PDB:5U6O}.
STRAND 337 339 {ECO:0000244|PDB:5U6O}.
HELIX 341 357 {ECO:0000244|PDB:5U6O}.
STRAND 362 364 {ECO:0000244|PDB:5U6O}.
HELIX 369 400 {ECO:0000244|PDB:5U6O}.
HELIX 402 421 {ECO:0000244|PDB:5U6O}.
HELIX 425 439 {ECO:0000244|PDB:5U6O}.
HELIX 446 452 {ECO:0000244|PDB:5U6O}.
HELIX 455 472 {ECO:0000244|PDB:5U6O}.
TURN 474 477 {ECO:0000244|PDB:5U6O}.
HELIX 481 490 {ECO:0000244|PDB:5U6O}.
STRAND 492 496 {ECO:0000244|PDB:5U6O}.
STRAND 501 503 {ECO:0000244|PDB:5U6O}.
STRAND 505 507 {ECO:0000244|PDB:5U6O}.
STRAND 511 523 {ECO:0000244|PDB:5U6O}.
STRAND 525 527 {ECO:0000244|PDB:5U6O}.
STRAND 541 545 {ECO:0000244|PDB:5U6O}.
STRAND 551 565 {ECO:0000244|PDB:5U6O}.
HELIX 566 575 {ECO:0000244|PDB:5U6O}.
HELIX 577 584 {ECO:0000244|PDB:5U6O}.
SEQUENCE 890 AA; 98796 MW; A62F5E79C01257A2 CRC64;
MEGGGKPNSS SNSRDDGNSV FPAKASATGA GPAAAEKRLG TPPGGGGAGA KEHGNSVCFK
VDGGGGGGGG GGGGEEPAGG FEDAEGPRRQ YGFMQRQFTS MLQPGVNKFS LRMFGSQKAV
EKEQERVKTA GFWIIHPYSD FRFYWDLIML IMMVGNLVII PVGITFFTEQ TTTPWIIFNV
ASDTVFLLDL IMNFRTGTVN EDSSEIILDP KVIKMNYLKS WFVVDFISSI PVDYIFLIVE
KGMDSEVYKT ARALRIVRFT KILSLLRLLR LSRLIRYIHQ WEEIFHMTYD LASAVVRIFN
LIGMMLLLCH WDGCLQFLVP LLQDFPPDCW VSLNEMVNDS WGKQYSYALF KAMSHMLCIG
YGAQAPVSMS DLWITMLSMI VGATCYAMFV GHATALIQSL DSSRRQYQEK YKQVEQYMSF
HKLPADMRQK IHDYYEHRYQ GKIFDEENIL NELNDPLREE IVNFNCRKLV ATMPLFANAD
PNFVTAMLSK LRFEVFQPGD YIIREGAVGK KMYFIQHGVA GVITKSSKEM KLTDGSYFGE
ICLLTKGRRT ASVRADTYCR LYSLSVDNFN EVLEEYPMMR RAFETVAIDR LDRIGKKNSI
LLQKFQKDLN TGVFNNQENE ILKQIVKHDR EMVQAIAPIN YPQMTTLNST SSTTTPTSRM
RTQSPPVYTA TSLSHSNLHS PSPSTQTPQP SAILSPCSYT TAVCSPPVQS PLAARTFHYA
SPTASQLSLM QQQPQQQVQQ SQPPQTQPQQ PSPQPQTPGS STPKNEVHKS TQALHNTNLT
REVRPLSASQ PSLPHEVSTL ISRPHPTVGE SLASIPQPVT AVPGTGLQAG GRSTVPQRVT
LFRQMSSGAI PPNRGVPPAP PPPAAALPRE SSSVLNTDPD AEKPRFASNL


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EIAAB08171 cGMP-gated cation channel alpha-1,Cncg,Cncg1,CNG channel alpha-1,CNG1,CNG-1,Cnga1,Cyclic nucleotide-gated cation channel 1,Cyclic nucleotide-gated channel alpha-1,Cyclic nucleotide-gated channel, phot
EIAAB08172 cGMP-gated cation channel alpha-1,Cncg,Cncg1,CNG channel alpha-1,CNG1,CNG-1,Cnga1,Cyclic nucleotide-gated cation channel 1,Cyclic nucleotide-gated channel alpha-1,Cyclic nucleotide-gated channel, phot
EIAAB08169 cGMP-gated cation channel alpha-1,CNCG,CNCG1,CNG channel alpha-1,CNG1,CNG-1,CNGA1,Cyclic nucleotide-gated cation channel 1,Cyclic nucleotide-gated channel alpha-1,Cyclic nucleotide-gated channel, phot
HCN3_MOUSE ELISA Kit FOR Potassium per sodium hyperpolarization-activated cyclic nucleotide-gated channel 3; organism: Mouse; gene name: Hcn3 96T
HCN1_MOUSE ELISA Kit FOR Potassium per sodium hyperpolarization-activated cyclic nucleotide-gated channel 1; organism: Mouse; gene name: Hcn1 96T
HCN2_MOUSE ELISA Kit FOR Potassium per sodium hyperpolarization-activated cyclic nucleotide-gated channel 2; organism: Mouse; gene name: Hcn2 96T
HCN4_MOUSE ELISA Kit FOR Potassium per sodium hyperpolarization-activated cyclic nucleotide-gated channel 4; organism: Mouse; gene name: Hcn4 96T
EIAAB08173 Bos taurus,Bovine,cGMP-gated cation channel alpha-1,CNCG,CNCG1,CNG channel alpha-1,CNG1,CNG-1,CNGA1,Cyclic nucleotide-gated cation channel 1,Cyclic nucleotide-gated channel alpha-1,Cyclic nucleotide-g
EIAAB08186 CNCG2,CNCG3L,CNCG4,CNG channel 4,CNG channel beta-1,CNG4,CNG-4,CNGB1,Cyclic nucleotide-gated cation channel 4,Cyclic nucleotide-gated cation channel beta-1,Cyclic nucleotide-gated cation channel gamma
HCP5 HCN3 Gene hyperpolarization activated cyclic nucleotide-gated potassium channel 3
HCN4 HCN2 Gene hyperpolarization activated cyclic nucleotide-gated potassium channel 2


 

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