ID HCN1_MOUSE Reviewed; 910 AA.
AC O88704; O54899; Q9D613;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 200.
DE RecName: Full=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1;
DE AltName: Full=Brain cyclic nucleotide-gated channel 1 {ECO:0000303|PubMed:9405696};
DE Short=BCNG-1 {ECO:0000303|PubMed:9405696};
DE AltName: Full=Hyperpolarization-activated cation channel 2 {ECO:0000303|PubMed:9634236};
DE Short=HAC-2 {ECO:0000303|PubMed:9634236};
GN Name=Hcn1; Synonyms=Bcng1 {ECO:0000303|PubMed:9405696}, Hac2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-327,
RP AND INTERACTION WITH CSK.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9405696; DOI=10.1073/pnas.94.26.14815;
RA Santoro B., Grant S.G.N., Bartsch D., Kandel E.R.;
RT "Interactive cloning with the SH3 domain of N-src identifies a new brain
RT specific ion channel protein, with homology to eag and cyclic nucleotide-
RT gated channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14815-14820(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9634236; DOI=10.1038/31255;
RA Ludwig A., Zong X., Jeglitsch M., Hofmann F., Biel M.;
RT "A family of hyperpolarization-activated cation channels.";
RL Nature 393:587-591(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 377-910.
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=9630217; DOI=10.1016/s0092-8674(00)81434-8;
RA Santoro B., Liu D.T., Yao H., Bartsch D., Kandel E.R., Siegelbaum S.A.,
RA Tibbs G.R.;
RT "Identification of a gene encoding a hyperpolarization-activated
RT 'pacemaker' channel of brain.";
RL Cell 93:717-729(1998).
RN [5]
RP INTERACTION WITH KCNE2.
RX PubMed=11420311; DOI=10.1161/hh1201.093511;
RA Yu H., Wu J., Potapova I., Wymore R.T., Holmes B., Zuckerman J., Pan Z.,
RA Wang H., Shi W., Robinson R.B., El-Maghrabi M.R., Benjamin W., Dixon J.E.,
RA McKinnon D., Cohen I.S., Wymore R.;
RT "MinK-related peptide 1: a beta subunit for the HCN ion channel subunit
RT family enhances expression and speeds activation.";
RL Circ. Res. 88:E84-E87(2001).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=11459060; DOI=10.1038/35081088;
RA Wainger B.J., DeGennaro M., Santoro B., Siegelbaum S.A., Tibbs G.R.;
RT "Molecular mechanism of cAMP modulation of HCN pacemaker channels.";
RL Nature 411:805-810(2001).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11675786; DOI=10.1038/35098087;
RA Stevens D.R., Seifert R., Bufe B., Mueller F., Kremmer E., Gauss R.,
RA Meyerhof W., Kaupp U.B., Lindemann B.;
RT "Hyperpolarization-activated channels HCN1 and HCN4 mediate responses to
RT sour stimuli.";
RL Nature 413:631-635(2001).
RN [8]
RP INTERACTION WITH HCN2, AND MUTAGENESIS OF GLY-349; TYR-350 AND GLY-351.
RX PubMed=12089064; DOI=10.1161/01.res.0000024390.97889.c6;
RA Xue T., Marban E., Li R.A.;
RT "Dominant-negative suppression of HCN1- and HCN2-encoded pacemaker currents
RT by an engineered HCN1 construct: insights into structure-function
RT relationships and multimerization.";
RL Circ. Res. 90:1267-1273(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH HCN2.
RX PubMed=12034718; DOI=10.1074/jbc.m200504200;
RA Proenza C., Tran N., Angoli D., Zahynacz K., Balcar P., Accili E.A.;
RT "Different roles for the cyclic nucleotide binding domain and amino
RT terminus in assembly and expression of hyperpolarization-activated, cyclic
RT nucleotide-gated channels.";
RL J. Biol. Chem. 277:29634-29642(2002).
RN [10]
RP MUTAGENESIS OF CYS-303 AND CYS-318.
RX PubMed=12351622; DOI=10.1074/jbc.m204915200;
RA Xue T., Li R.A.;
RT "An external determinant in the S5-P linker of the pacemaker (HCN) channel
RT identified by sulfhydryl modification.";
RL J. Biol. Chem. 277:46233-46242(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=26269648; DOI=10.1523/jneurosci.1346-15.2015;
RA Kole M.J., Qian J., Waase M.P., Klassen T.L., Chen T.T., Augustine G.J.,
RA Noebels J.L.;
RT "Selective Loss of Presynaptic Potassium Channel Clusters at the Cerebellar
RT Basket Cell Terminal Pinceau in Adam11 Mutants Reveals Their Role in
RT Ephaptic Control of Purkinje Cell Firing.";
RL J. Neurosci. 35:11433-11444(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 390-592 IN COMPLEX WITH CAMP,
RP FUNCTION, SUBCELLULAR LOCATION, NUCLEOTIDE-BINDING, ACTIVITY REGULATION,
RP MUTAGENESIS OF ARG-538, AND SUBUNIT.
RX PubMed=22006928; DOI=10.1074/jbc.m111.297606;
RA Lolicato M., Nardini M., Gazzarrini S., Moller S., Bertinetti D.,
RA Herberg F.W., Bolognesi M., Martin H., Fasolini M., Bertrand J.A.,
RA Arrigoni C., Thiel G., Moroni A.;
RT "Tetramerization dynamics of C-terminal domain underlies isoform-specific
RT cAMP gating in hyperpolarization-activated cyclic nucleotide-gated
RT channels.";
RL J. Biol. Chem. 286:44811-44820(2011).
CC -!- FUNCTION: Hyperpolarization-activated ion channel exhibiting weak
CC selectivity for potassium over sodium ions. Contributes to the native
CC pacemaker currents in heart (If) and in neurons (Ih). May mediate
CC responses to sour stimuli. {ECO:0000269|PubMed:11459060,
CC ECO:0000269|PubMed:11675786, ECO:0000269|PubMed:12034718,
CC ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9630217}.
CC -!- ACTIVITY REGULATION: Activated by cAMP, and at 10-100 times higher
CC concentrations, also by cGMP. cAMP binding causes a conformation change
CC that leads to the assembly of an active tetramer and channel opening.
CC Compared to other family members, cAMP has less stimulatory effect on
CC HCN1 because part of the molecules already contain bound cAMP and form
CC homotetramers when cAMP levels are low. {ECO:0000269|PubMed:11459060,
CC ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9630217}.
CC -!- SUBUNIT: Homotetramer. Heterotetramer with HCN2. The potassium channel
CC is composed of a homo- or heterotetrameric complex of pore-forming
CC subunits. Interacts with KCNE2. Interacts with the SH3 domain of CSK
CC (PubMed:9405696). {ECO:0000269|PubMed:11420311,
CC ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:12089064,
CC ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9405696}.
CC -!- INTERACTION:
CC O88704; O88704: Hcn1; NbExp=2; IntAct=EBI-8766347, EBI-8766347;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11459060,
CC ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9630217}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11459060,
CC ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9630217}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain (PubMed:9405696).
CC Highly expressed in apical dendrites of pyramidal neurons in the
CC cortex, in the layer corresponding to the stratum lacunosum-moleculare
CC in the hippocampus and in axons of basket cells in the cerebellum (at
CC protein level) (PubMed:9405696, PubMed:26269648). Expressed in a subset
CC of elongated cells in taste buds (PubMed:11675786).
CC {ECO:0000269|PubMed:11675786, ECO:0000269|PubMed:26269648,
CC ECO:0000269|PubMed:9405696}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000250|UniProtKB:O60741}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9405696}.
CC -!- MISCELLANEOUS: Inhibited by extracellular cesium ions.
CC -!- SIMILARITY: Belongs to the potassium channel HCN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK014722; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF028737; AAC53518.1; -; mRNA.
DR EMBL; AJ225123; CAA12407.1; -; mRNA.
DR EMBL; AK014722; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS26793.1; -.
DR RefSeq; NP_034538.2; NM_010408.3.
DR PDB; 3U0Z; X-ray; 2.90 A; A/B=390-592.
DR PDBsum; 3U0Z; -.
DR AlphaFoldDB; O88704; -.
DR SMR; O88704; -.
DR BioGRID; 200252; 45.
DR ComplexPortal; CPX-260; HCN1 channel complex.
DR IntAct; O88704; 40.
DR STRING; 10090.ENSMUSP00000006991; -.
DR BindingDB; O88704; -.
DR ChEMBL; CHEMBL1250401; -.
DR DrugCentral; O88704; -.
DR GuidetoPHARMACOLOGY; 400; -.
DR TCDB; 1.A.1.5.2; the voltage-gated ion channel (vic) superfamily.
DR GlyCosmos; O88704; 1 site, No reported glycans.
DR GlyGen; O88704; 11 sites, 1 O-linked glycan (10 sites).
DR iPTMnet; O88704; -.
DR PhosphoSitePlus; O88704; -.
DR SwissPalm; O88704; -.
DR MaxQB; O88704; -.
DR PaxDb; 10090-ENSMUSP00000006991; -.
DR PeptideAtlas; O88704; -.
DR ProteomicsDB; 269769; -.
DR ABCD; O88704; 1 sequenced antibody.
DR Antibodypedia; 23274; 410 antibodies from 33 providers.
DR DNASU; 15165; -.
DR Ensembl; ENSMUST00000006991.9; ENSMUSP00000006991.8; ENSMUSG00000021730.9.
DR GeneID; 15165; -.
DR KEGG; mmu:15165; -.
DR UCSC; uc007ryo.2; mouse.
DR AGR; MGI:1096392; -.
DR CTD; 348980; -.
DR MGI; MGI:1096392; Hcn1.
DR VEuPathDB; HostDB:ENSMUSG00000021730; -.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000158207; -.
DR HOGENOM; CLU_005746_15_1_1; -.
DR InParanoid; O88704; -.
DR OMA; FQYATPT; -.
DR OrthoDB; 74296at2759; -.
DR PhylomeDB; O88704; -.
DR TreeFam; TF318250; -.
DR Reactome; R-MMU-1296061; HCN channels.
DR BioGRID-ORCS; 15165; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Hcn1; mouse.
DR PRO; PR:O88704; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O88704; Protein.
DR Bgee; ENSMUSG00000021730; Expressed in retrosplenial region and 91 other cell types or tissues.
DR Genevisible; O88704; MM.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098855; C:HCN channel complex; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0036477; C:somatodendritic compartment; ISO:MGI.
DR GO; GO:0030552; F:cAMP binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IDA:MGI.
DR GO; GO:0140232; F:intracellular cAMP-activated cation channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0022843; F:voltage-gated monoatomic cation channel activity; ISS:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IMP:UniProtKB.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; ISO:MGI.
DR GO; GO:0045176; P:apical protein localization; IMP:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; IMP:UniProtKB.
DR GO; GO:0051867; P:general adaptation syndrome, behavioral process; IDA:MGI.
DR GO; GO:0045759; P:negative regulation of action potential; ISO:MGI.
DR GO; GO:0019228; P:neuronal action potential; IDA:MGI.
DR GO; GO:1902632; P:positive regulation of membrane hyperpolarization; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0003254; P:regulation of membrane depolarization; ISO:MGI.
DR GO; GO:1902630; P:regulation of membrane hyperpolarization; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0046549; P:retinal cone cell development; IMP:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR013621; Ion_trans_N.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45689; I[[H]] CHANNEL, ISOFORM E; 1.
DR PANTHER; PTHR45689:SF3; POTASSIUM_SODIUM HYPERPOLARIZATION-ACTIVATED CYCLIC NUCLEOTIDE-GATED CHANNEL 1; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF08412; Ion_trans_N; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; cAMP; cAMP-binding; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..910
FT /note="Potassium/sodium hyperpolarization-activated cyclic
FT nucleotide-gated channel 1"
FT /id="PRO_0000054108"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TRANSMEM 132..153
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TOPO_DOM 154..162
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TRANSMEM 163..183
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TOPO_DOM 184..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TRANSMEM 205..225
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TOPO_DOM 226..249
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TRANSMEM 250..270
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TOPO_DOM 271..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TRANSMEM 285..307
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TOPO_DOM 308..333
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT INTRAMEM 334..355
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TOPO_DOM 356..360
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TRANSMEM 361..381
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT TOPO_DOM 382..910
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O60741"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 347..351
FT /note="Selectivity filter"
FT /evidence="ECO:0000305|PubMed:12089064"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..888
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 528..531
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:22006928,
FT ECO:0007744|PDB:3U0Z"
FT BINDING 538..539
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:22006928,
FT ECO:0007744|PDB:3U0Z"
FT BINDING 579..582
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:22006928,
FT ECO:0007744|PDB:3U0Z"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:9405696"
FT MUTAGEN 303
FT /note="C->S: Abolishes conductivity."
FT /evidence="ECO:0000269|PubMed:12351622"
FT MUTAGEN 318
FT /note="C->S: Abolishes sensitivity to sulfhydryl
FT modification."
FT /evidence="ECO:0000269|PubMed:12351622"
FT MUTAGEN 349
FT /note="G->A: Abolishes conductivity; when associated with
FT A-350 and A-351."
FT /evidence="ECO:0000269|PubMed:12089064"
FT MUTAGEN 350
FT /note="Y->A: Abolishes conductivity; when associated with
FT A-349 and A-351."
FT /evidence="ECO:0000269|PubMed:12089064"
FT MUTAGEN 351
FT /note="G->A: Abolishes conductivity; when associated with
FT A-349 and A-350."
FT /evidence="ECO:0000269|PubMed:12089064"
FT MUTAGEN 538
FT /note="R->E: Reduces affinity for cAMP and impairs
FT tetramerization."
FT /evidence="ECO:0000269|PubMed:22006928"
FT CONFLICT 42
FT /note="G -> R (in Ref. 1; AAC53518)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="R -> S (in Ref. 3; AK014722)"
FT /evidence="ECO:0000305"
FT HELIX 391..410
FT /evidence="ECO:0007829|PDB:3U0Z"
FT HELIX 414..428
FT /evidence="ECO:0007829|PDB:3U0Z"
FT HELIX 435..440
FT /evidence="ECO:0007829|PDB:3U0Z"
FT HELIX 444..454
FT /evidence="ECO:0007829|PDB:3U0Z"
FT HELIX 456..460
FT /evidence="ECO:0007829|PDB:3U0Z"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:3U0Z"
FT HELIX 470..478
FT /evidence="ECO:0007829|PDB:3U0Z"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:3U0Z"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:3U0Z"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:3U0Z"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:3U0Z"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:3U0Z"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:3U0Z"
FT HELIX 529..534
FT /evidence="ECO:0007829|PDB:3U0Z"
FT STRAND 540..546
FT /evidence="ECO:0007829|PDB:3U0Z"
FT STRAND 548..554
FT /evidence="ECO:0007829|PDB:3U0Z"
FT HELIX 555..564
FT /evidence="ECO:0007829|PDB:3U0Z"
FT HELIX 567..583
FT /evidence="ECO:0007829|PDB:3U0Z"
SQ SEQUENCE 910 AA; 102432 MW; 56FD5F328DD972E9 CRC64;
MEGGGKPNSA SNSRDDGNSV FPSKAPATGP VAADKRLGTP PGGGAAGKEH GNSVCFKVDG
GGGEEPAGSF EDAEGPRRQY GFMQRQFTSM LQPGVNKFSL RMFGSQKAVE KEQERVKTAG
FWIIHPYSDF RFYWDLIMLI MMVGNLVIIP VGITFFTEQT TTPWIIFNVA SDTVFLLDLI
MNFRTGTVNE DSSEIILDPK VIKMNYLKSW FVVDFISSIP VDYIFLIVEK GMDSEVYKTA
RALRIVRFTK ILSLLRLLRL SRLIRYIHQW EEIFHMTYDL ASAVVRIFNL IGMMLLLCHW
DGCLQFLVPL LQDFPPDCWV SLNEMVNDSW GKQYSYALFK AMSHMLCIGY GAQAPVSMSD
LWITMLSMIV GATCYAMFVG HATALIQSLD SSRRQYQEKY KQVEQYMSFH KLPADMRQKI
HDYYEHRYQG KIFDEENILS ELNDPLREEI VNFNCRKLVA TMPLFANADP NFVTAMLSKL
RFEVFQPGDY IIREGAVGKK MYFIQHGVAG VITKSSKEMK LTDGSYFGEI CLLTKGRRTA
SVRADTYCRL YSLSVDNFNE VLEEYPMMRR AFETVAIDRL DRIGKKNSIL LQKFQKDLNT
GVFNNQENEI LKQIVKHDRE MVQAIPPINY PQMTALNCTS STTTPTSRMR TQSPPVYTAT
SLSHSNLHSP SPSTQTPQPS AILSPCSYTT AVCSPPIQSP LATRTFHYAS PTASQLSLMQ
QPQQQLPQSQ VQQTQTQTQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQPQTPG
SSTPKNEVHK STQALHNTNL TKEVRPLSAS QPSLPHEVST LISRPHPTVG ESLASIPQPV
AAVHSTGLQA GSRSTVPQRV TLFRQMSSGA IPPNRGVPPA PPPPAAVQRE SPSVLNTDPD
AEKPRFASNL
//
