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Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4

 HCN4_HUMAN              Reviewed;        1203 AA.
Q9Y3Q4; Q9UMQ7;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
20-JUN-2018, entry version 160.
RecName: Full=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4;
Name=HCN4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Heart;
PubMed=10228147; DOI=10.1093/emboj/18.9.2323;
Ludwig A., Zong X., Stieber J., Hullin R., Hofmann F., Biel M.;
"Two pacemaker channels from human heart with profoundly different
activation kinetics.";
EMBO J. 18:2323-2329(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Thalamus;
PubMed=10430953; DOI=10.1073/pnas.96.16.9391;
Seifert R., Scholten A., Gauss R., Mincheva A., Lichter P.,
Kaupp U.B.;
"Molecular characterization of a slowly gating human
hyperpolarization-activated channel predominantly expressed in
thalamus, heart, and testis.";
Proc. Natl. Acad. Sci. U.S.A. 96:9391-9396(1999).
[3]
FUNCTION, AND INVOLVEMENT IN BRGDA8.
PubMed=19165230; DOI=10.1038/jhg.2008.16;
Ueda K., Hirano Y., Higashiuesato Y., Aizawa Y., Hayashi T.,
Inagaki N., Tana T., Ohya Y., Takishita S., Muratani H., Hiraoka M.,
Kimura A.;
"Role of HCN4 channel in preventing ventricular arrhythmia.";
J. Hum. Genet. 54:115-121(2009).
[4]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 521-739 IN COMPLEX WITH CAMP,
NUCLEOTIDE-BINDING, FUNCTION, ENZYME REGULATION, AND SUBUNIT.
PubMed=20829353; DOI=10.1074/jbc.M110.152033;
Xu X., Vysotskaya Z.V., Liu Q., Zhou L.;
"Structural basis for the cAMP-dependent gating in the human HCN4
channel.";
J. Biol. Chem. 285:37082-37091(2010).
[5]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 521-723 IN COMPLEX WITH CAMP,
NUCLEOTIDE-BINDING, ENZYME REGULATION, AND SUBUNIT.
PubMed=22006928; DOI=10.1074/jbc.M111.297606;
Lolicato M., Nardini M., Gazzarrini S., Moller S., Bertinetti D.,
Herberg F.W., Bolognesi M., Martin H., Fasolini M., Bertrand J.A.,
Arrigoni C., Thiel G., Moroni A.;
"Tetramerization dynamics of C-terminal domain underlies isoform-
specific cAMP gating in hyperpolarization-activated cyclic nucleotide-
gated channels.";
J. Biol. Chem. 286:44811-44820(2011).
[6]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 521-724, AND CHARACTERIZATION
OF VARIANT SSS2 ARG-672.
PubMed=23103389; DOI=10.1016/j.str.2012.09.017;
Xu X., Marni F., Wu S., Su Z., Musayev F., Shrestha S., Xie C.,
Gao W., Liu Q., Zhou L.;
"Local and global interpretations of a disease-causing mutation near
the ligand entry path in hyperpolarization-activated cAMP-gated
channel.";
Structure 20:2116-2123(2012).
[7]
VARIANT SSS2 ASN-553.
PubMed=15123648; DOI=10.1074/jbc.M311953200;
Ueda K., Nakamura K., Hayashi T., Inagaki N., Takahashi M.,
Arimura T., Morita H., Higashiuesato Y., Hirano Y., Yasunami M.,
Takishita S., Yamashina A., Ohe T., Sunamori M., Hiraoka M.,
Kimura A.;
"Functional characterization of a trafficking-defective HCN4 mutation,
D553N, associated with cardiac arrhythmia.";
J. Biol. Chem. 279:27194-27198(2004).
[8]
VARIANT SSS2 ARG-672, FUNCTION, ENZYME REGULATION, SUBCELLULAR
LOCATION, AND CHARACTERIZATION OF VARIANT SSS2 ARG-672.
PubMed=16407510; DOI=10.1056/NEJMoa052475;
Milanesi R., Baruscotti M., Gnecchi-Ruscone T., DiFrancesco D.;
"Familial sinus bradycardia associated with a mutation in the cardiac
pacemaker channel.";
N. Engl. J. Med. 354:151-157(2006).
[9]
VARIANT SSS2 VAL-485, AND CHARACTERIZATION OF VARIANT SSS2 VAL-485.
PubMed=20662977; DOI=10.1111/j.1540-8167.2010.01844.x;
Laish-Farkash A., Glikson M., Brass D., Marek-Yagel D., Pras E.,
Dascal N., Antzelevitch C., Nof E., Reznik H., Eldar M., Luria D.;
"A novel mutation in the HCN4 gene causes symptomatic sinus
bradycardia in Moroccan Jews.";
J. Cardiovasc. Electrophysiol. 21:1365-1372(2010).
-!- FUNCTION: Hyperpolarization-activated ion channel with very slow
activation and inactivation exhibiting weak selectivity for
potassium over sodium ions. Contributes to the native pacemaker
currents in heart (If) that regulate the rhythm of heart beat. May
contribute to the native pacemaker currents in neurons (Ih). May
mediate responses to sour stimuli. {ECO:0000269|PubMed:10228147,
ECO:0000269|PubMed:10430953, ECO:0000269|PubMed:16407510,
ECO:0000269|PubMed:19165230, ECO:0000269|PubMed:20829353}.
-!- ENZYME REGULATION: Activated by cAMP. cAMP binding causes a
conformation change that leads to the assembly of an active
tetramer and channel opening. {ECO:0000269|PubMed:16407510,
ECO:0000269|PubMed:20829353, ECO:0000269|PubMed:22006928}.
-!- SUBUNIT: Homotetramer. The potassium channel is composed of a
homo- or heterotetrameric complex of pore-forming subunits.
{ECO:0000269|PubMed:20829353, ECO:0000269|PubMed:22006928}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1753521, EBI-1753521;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10228147,
ECO:0000269|PubMed:10430953, ECO:0000269|PubMed:16407510}; Multi-
pass membrane protein {ECO:0000269|PubMed:10228147,
ECO:0000269|PubMed:10430953, ECO:0000269|PubMed:16407510}.
-!- TISSUE SPECIFICITY: Highly expressed in thalamus, testis and in
heart, both in ventricle and atrium. Detected at much lower levels
in amygdala, substantia nigra, cerebellum and hippocampus.
{ECO:0000269|PubMed:10228147, ECO:0000269|PubMed:10430953}.
-!- DOMAIN: The segment S4 is probably the voltage-sensor and is
characterized by a series of positively charged amino acids at
every third position.
-!- DISEASE: Sick sinus syndrome 2 (SSS2) [MIM:163800]: The term 'sick
sinus syndrome' encompasses a variety of conditions caused by
sinus node dysfunction. The most common clinical manifestations
are syncope, presyncope, dizziness, and fatigue. Electrocardiogram
typically shows sinus bradycardia, sinus arrest, and/or sinoatrial
block. Episodes of atrial tachycardias coexisting with sinus
bradycardia ('tachycardia-bradycardia syndrome') are also common
in this disorder. SSS occurs most often in the elderly associated
with underlying heart disease or previous cardiac surgery, but can
also occur in the fetus, infant, or child without heart disease or
other contributing factors. SSS2 onset is in utero or at birth.
{ECO:0000269|PubMed:15123648, ECO:0000269|PubMed:16407510,
ECO:0000269|PubMed:20662977, ECO:0000269|PubMed:23103389}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Brugada syndrome 8 (BRGDA8) [MIM:613123]: A
tachyarrhythmia characterized by right bundle branch block and ST
segment elevation on an electrocardiogram (ECG). It can cause the
ventricles to beat so fast that the blood is prevented from
circulating efficiently in the body. When this situation occurs,
the individual will faint and may die in a few minutes if the
heart is not reset. {ECO:0000269|PubMed:19165230}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: Inhibited by extracellular cesium ions.
-!- SIMILARITY: Belongs to the potassium channel HCN family.
{ECO:0000305}.
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EMBL; AJ132429; CAB42604.1; -; mRNA.
EMBL; AJ238850; CAB52754.1; -; mRNA.
CCDS; CCDS10248.1; -.
RefSeq; NP_005468.1; NM_005477.2.
UniGene; Hs.86941; -.
PDB; 2MNG; NMR; -; A=579-707.
PDB; 3OTF; X-ray; 2.40 A; A=521-739.
PDB; 3U11; X-ray; 2.50 A; A/B=521-723.
PDB; 4HBN; X-ray; 2.60 A; A=521-724.
PDB; 4KL1; X-ray; 2.70 A; A/B/C/D=521-713.
PDB; 4NVP; X-ray; 2.50 A; A=521-723.
PDBsum; 2MNG; -.
PDBsum; 3OTF; -.
PDBsum; 3U11; -.
PDBsum; 4HBN; -.
PDBsum; 4KL1; -.
PDBsum; 4NVP; -.
ProteinModelPortal; Q9Y3Q4; -.
SMR; Q9Y3Q4; -.
BioGrid; 115338; 3.
ComplexPortal; CPX-131; HCN4 channel complex.
DIP; DIP-52325N; -.
IntAct; Q9Y3Q4; 3.
STRING; 9606.ENSP00000261917; -.
BindingDB; Q9Y3Q4; -.
ChEMBL; CHEMBL1250417; -.
GuidetoPHARMACOLOGY; 403; -.
TCDB; 1.A.1.5.10; the voltage-gated ion channel (vic) superfamily.
TCDB; 1.A.1.5.11; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q9Y3Q4; -.
PhosphoSitePlus; Q9Y3Q4; -.
BioMuta; HCN4; -.
DMDM; 38605641; -.
EPD; Q9Y3Q4; -.
MaxQB; Q9Y3Q4; -.
PaxDb; Q9Y3Q4; -.
PeptideAtlas; Q9Y3Q4; -.
PRIDE; Q9Y3Q4; -.
ProteomicsDB; 86060; -.
DNASU; 10021; -.
Ensembl; ENST00000261917; ENSP00000261917; ENSG00000138622.
GeneID; 10021; -.
KEGG; hsa:10021; -.
UCSC; uc002avp.3; human.
CTD; 10021; -.
DisGeNET; 10021; -.
EuPathDB; HostDB:ENSG00000138622.3; -.
GeneCards; HCN4; -.
GeneReviews; HCN4; -.
HGNC; HGNC:16882; HCN4.
MalaCards; HCN4; -.
MIM; 163800; phenotype.
MIM; 605206; gene.
MIM; 613123; phenotype.
neXtProt; NX_Q9Y3Q4; -.
OpenTargets; ENSG00000138622; -.
Orphanet; 130; Brugada syndrome.
Orphanet; 166282; Familial sick sinus syndrome.
PharmGKB; PA394; -.
eggNOG; KOG0498; Eukaryota.
eggNOG; ENOG410XPSE; LUCA.
GeneTree; ENSGT00900000140801; -.
HOGENOM; HOG000230717; -.
HOVERGEN; HBG039490; -.
InParanoid; Q9Y3Q4; -.
KO; K04957; -.
OMA; AIPGQHV; -.
OrthoDB; EOG091G0JQU; -.
PhylomeDB; Q9Y3Q4; -.
TreeFam; TF318250; -.
Reactome; R-HSA-1296061; HCN channels.
SIGNOR; Q9Y3Q4; -.
ChiTaRS; HCN4; human.
EvolutionaryTrace; Q9Y3Q4; -.
GeneWiki; HCN4; -.
GenomeRNAi; 10021; -.
PRO; PR:Q9Y3Q4; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000138622; -.
CleanEx; HS_HCN4; -.
Genevisible; Q9Y3Q4; HS.
GO; GO:0098855; C:HCN channel complex; IDA:BHF-UCL.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005222; F:intracellular cAMP activated cation channel activity; IDA:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0086041; F:voltage-gated potassium channel activity involved in SA node cell action potential depolarization; IMP:BHF-UCL.
GO; GO:0005248; F:voltage-gated sodium channel activity; IMP:UniProtKB.
GO; GO:0008015; P:blood circulation; NAS:ProtInc.
GO; GO:0006812; P:cation transport; IDA:BHF-UCL.
GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
GO; GO:0071321; P:cellular response to cGMP; IDA:UniProtKB.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; IC:BHF-UCL.
GO; GO:0086046; P:membrane depolarization during SA node cell action potential; IMP:BHF-UCL.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; IMP:BHF-UCL.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; IMP:UniProtKB.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0003254; P:regulation of membrane depolarization; IDA:BHF-UCL.
GO; GO:0042391; P:regulation of membrane potential; IMP:UniProtKB.
GO; GO:0086015; P:SA node cell action potential; IMP:BHF-UCL.
GO; GO:0098719; P:sodium ion import across plasma membrane; IDA:BHF-UCL.
GO; GO:0035725; P:sodium ion transmembrane transport; IMP:UniProtKB.
CDD; cd00038; CAP_ED; 1.
Gene3D; 1.20.120.350; -; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR030173; HCN4.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR013621; Ion_trans_N.
InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR10217:SF375; PTHR10217:SF375; 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; Brugada syndrome; cAMP; cAMP-binding; Cell membrane;
Complete proteome; Disease mutation; Glycoprotein; Ion channel;
Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
Phosphoprotein; Potassium; Potassium channel; Potassium transport;
Reference proteome; Sodium; Sodium channel; Sodium transport;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 1203 Potassium/sodium hyperpolarization-
activated cyclic nucleotide-gated channel
4.
/FTId=PRO_0000054117.
TOPO_DOM 1 266 Cytoplasmic. {ECO:0000255}.
TRANSMEM 267 287 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 288 293 Extracellular. {ECO:0000255}.
TRANSMEM 294 314 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 315 340 Cytoplasmic. {ECO:0000255}.
TRANSMEM 341 361 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 362 368 Extracellular. {ECO:0000255}.
TRANSMEM 369 389 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 390 420 Cytoplasmic. {ECO:0000255}.
TRANSMEM 421 441 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 442 464 Extracellular. {ECO:0000255}.
INTRAMEM 465 486 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 487 496 Extracellular. {ECO:0000255}.
TRANSMEM 497 517 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 518 1203 Cytoplasmic. {ECO:0000255}.
NP_BIND 659 662 cAMP. {ECO:0000269|PubMed:20829353,
ECO:0000269|PubMed:22006928}.
NP_BIND 669 670 cAMP. {ECO:0000269|PubMed:20829353,
ECO:0000269|PubMed:22006928}.
NP_BIND 710 713 cAMP. {ECO:0000269|PubMed:20829353,
ECO:0000269|PubMed:22006928}.
REGION 209 260 Involved in subunit assembly.
{ECO:0000250}.
COMPBIAS 924 1076 Pro-rich.
MOD_RES 138 138 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JKA7}.
MOD_RES 1105 1105 Phosphoserine.
{ECO:0000250|UniProtKB:O70507}.
MOD_RES 1108 1108 Phosphoserine.
{ECO:0000250|UniProtKB:O70507}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 485 485 A -> V (in SSS2; results in a significant
reduction of current density compared to
wild-type).
{ECO:0000269|PubMed:20662977}.
/FTId=VAR_066614.
VARIANT 553 553 D -> N (in SSS2; dbSNP:rs104894485).
{ECO:0000269|PubMed:15123648}.
/FTId=VAR_026534.
VARIANT 672 672 S -> R (in SSS2; results in decreased
affinity for cAMP but does not abolish
channel activation; shifts the current
activation range to hyperpolarized
voltages; slows channel opening and
speeds up channel closure;
dbSNP:rs104894488).
{ECO:0000269|PubMed:16407510,
ECO:0000269|PubMed:23103389}.
/FTId=VAR_026535.
CONFLICT 110 110 S -> T (in Ref. 2; CAB52754).
{ECO:0000305}.
HELIX 522 540 {ECO:0000244|PDB:3OTF}.
HELIX 545 559 {ECO:0000244|PDB:3OTF}.
HELIX 566 571 {ECO:0000244|PDB:3OTF}.
HELIX 575 585 {ECO:0000244|PDB:3OTF}.
HELIX 587 591 {ECO:0000244|PDB:3OTF}.
HELIX 594 597 {ECO:0000244|PDB:3OTF}.
HELIX 601 608 {ECO:0000244|PDB:3OTF}.
STRAND 612 616 {ECO:0000244|PDB:3OTF}.
STRAND 621 623 {ECO:0000244|PDB:3OTF}.
STRAND 631 637 {ECO:0000244|PDB:3OTF}.
STRAND 640 643 {ECO:0000244|PDB:3OTF}.
STRAND 645 647 {ECO:0000244|PDB:3OTF}.
STRAND 650 652 {ECO:0000244|PDB:3OTF}.
HELIX 661 665 {ECO:0000244|PDB:3OTF}.
STRAND 666 668 {ECO:0000244|PDB:4KL1}.
STRAND 670 677 {ECO:0000244|PDB:3OTF}.
STRAND 679 685 {ECO:0000244|PDB:3OTF}.
HELIX 686 695 {ECO:0000244|PDB:3OTF}.
HELIX 697 699 {ECO:0000244|PDB:3OTF}.
HELIX 700 712 {ECO:0000244|PDB:3OTF}.
SEQUENCE 1203 AA; 129042 MW; 7EFDD2D69CF1F9D9 CRC64;
MDKLPPSMRK RLYSLPQQVG AKAWIMDEEE DAEEEGAGGR QDPSRRSIRL RPLPSPSPSA
AAGGTESRSS ALGAADSEGP ARGAGKSSTN GDCRRFRGSL ASLGSRGGGS GGTGSGSSHG
HLHDSAEERR LIAEGDASPG EDRTPPGLAA EPERPGASAQ PAASPPPPQQ PPQPASASCE
QPSVDTAIKV EGGAAAGDQI LPEAEVRLGQ AGFMQRQFGA MLQPGVNKFS LRMFGSQKAV
EREQERVKSA GFWIIHPYSD FRFYWDLTML LLMVGNLIII PVGITFFKDE NTTPWIVFNV
VSDTFFLIDL VLNFRTGIVV EDNTEIILDP QRIKMKYLKS WFMVDFISSI PVDYIFLIVE
TRIDSEVYKT ARALRIVRFT KILSLLRLLR LSRLIRYIHQ WEEIFHMTYD LASAVVRIVN
LIGMMLLLCH WDGCLQFLVP MLQDFPDDCW VSINNMVNNS WGKQYSYALF KAMSHMLCIG
YGRQAPVGMS DVWLTMLSMI VGATCYAMFI GHATALIQSL DSSRRQYQEK YKQVEQYMSF
HKLPPDTRQR IHDYYEHRYQ GKMFDEESIL GELSEPLREE IINFNCRKLV ASMPLFANAD
PNFVTSMLTK LRFEVFQPGD YIIREGTIGK KMYFIQHGVV SVLTKGNKET KLADGSYFGE
ICLLTRGRRT ASVRADTYCR LYSLSVDNFN EVLEEYPMMR RAFETVALDR LDRIGKKNSI
LLHKVQHDLN SGVFNYQENE IIQQIVQHDR EMAHCAHRVQ AAASATPTPT PVIWTPLIQA
PLQAAAATTS VAIALTHHPR LPAAIFRPPP GSGLGNLGAG QTPRHLKRLQ SLIPSALGSA
SPASSPSQVD TPSSSSFHIQ QLAGFSAPAG LSPLLPSSSS SPPPGACGSP SAPTPSAGVA
ATTIAGFGHF HKALGGSLSS SDSPLLTPLQ PGARSPQAAQ PSPAPPGARG GLGLPEHFLP
PPPSSRSPSS SPGQLGQPPG ELSLGLATGP LSTPETPPRQ PEPPSLVAGA SGGASPVGFT
PRGGLSPPGH SPGPPRTFPS APPRASGSHG SLLLPPASSP PPPQVPQRRG TPPLTPGRLT
QDLKLISASQ PALPQDGAQT LRRASPHSSG ESMAAFPLFP RAGGGSGGSG SSGGLGPPGR
PYGAIPGQHV TLPRKTSSGS LPPPLSLFGA RATSSGGPPL TAGPQREPGA RPEPVRSKLP
SNL


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CSB-EL010219RB Rabbit hyperpolarization activated cyclic nucleotide-gated potassium channel 4 (HCN4) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T


 

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