HCN3_RAT
ID HCN3_RAT Reviewed; 780 AA.
AC Q9JKA8;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3;
GN Name=Hcn3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11000485; DOI=10.1016/s0169-328x(00)00155-8;
RA Monteggia L.M., Eisch A.J., Tang M.D., Kaczmarek L.K., Nestler E.J.;
RT "Cloning and localization of the hyperpolarization-activated cyclic
RT nucleotide-gated channel family in rat brain.";
RL Brain Res. Mol. Brain Res. 81:129-139(2000).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Hyperpolarization-activated potassium channel. May also
CC facilitate the permeation of sodium ions (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. The potassium channel is probably composed of a
CC homo- or heterotetrameric complex of pore-forming subunits. Interacts
CC with KCTD3 and PEX5L. {ECO:0000250|UniProtKB:O88705,
CC ECO:0000250|UniProtKB:Q9UL51}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88705};
CC Multi-pass membrane protein {ECO:0000255}.
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.
CC -!- SIMILARITY: Belongs to the potassium channel HCN family. {ECO:0000305}.
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DR EMBL; AF247452; AAF62175.1; -; mRNA.
DR RefSeq; NP_446137.1; NM_053685.1.
DR AlphaFoldDB; Q9JKA8; -.
DR SMR; Q9JKA8; -.
DR STRING; 10116.ENSRNOP00000027785; -.
DR GlyGen; Q9JKA8; 1 site.
DR iPTMnet; Q9JKA8; -.
DR PhosphoSitePlus; Q9JKA8; -.
DR PaxDb; Q9JKA8; -.
DR PRIDE; Q9JKA8; -.
DR ABCD; Q9JKA8; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000027785; ENSRNOP00000027785; ENSRNOG00000020444.
DR GeneID; 114245; -.
DR KEGG; rno:114245; -.
DR UCSC; RGD:620691; rat.
DR CTD; 57657; -.
DR RGD; 620691; Hcn3.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000162023; -.
DR HOGENOM; CLU_005746_15_1_1; -.
DR InParanoid; Q9JKA8; -.
DR OMA; VSINHMA; -.
DR OrthoDB; 281394at2759; -.
DR PhylomeDB; Q9JKA8; -.
DR TreeFam; TF318250; -.
DR Reactome; R-RNO-1296061; HCN channels.
DR PRO; PR:Q9JKA8; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000020444; Expressed in liver and 11 other tissues.
DR Genevisible; Q9JKA8; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0044316; C:cone cell pedicle; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098855; C:HCN channel complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:RGD.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; ISO:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:1903351; P:cellular response to dopamine; IEP:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0003254; P:regulation of membrane depolarization; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0072718; P:response to cisplatin; IEP:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:RGD.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
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 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; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW cAMP; cAMP-binding; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Sodium; Sodium channel; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..780
FT /note="Potassium/sodium hyperpolarization-activated cyclic
FT nucleotide-gated channel 3"
FT /id="PRO_0000054116"
FT TOPO_DOM 1..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 297..318
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..328
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..780
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..90
FT /note="Involved in subunit assembly"
FT /evidence="ECO:0000250"
FT REGION 353..780
FT /note="Interaction with KCTD3"
FT /evidence="ECO:0000250|UniProtKB:O88705"
FT REGION 549..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 491..494
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 501..502
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 542..545
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 780 AA; 86809 MW; EF77A05D00E2F016 CRC64;
MEEEARPAVG DGEAATPARE TPPAAPAQAR AASGGVPESA PEPKRRQLGT LLQPTVNKFS
LRVFGSHKAV EIEQERVKSA GAWIIHPYSD FRFYWDLIML LLMVGNLIVL PVGITFFKEE
NSPPWIVFNV LSDTFFLLDL VLNFRTGIVV EEGAEILLAP RAIRTRYLRT WFLVDLISSI
PVDYIFLVVE LEPRLDAEVY KTARALRIVR FTKILSLLRL LRLSRLIRYM HQWEEIFHMT
YDLASAVVRI FNLIGMMLLL CHWDGCLQFL VPMLQDFPSD CWVSMNRMVN HSWGRQYSHA
LFKAMSHMLC IGYGQQAPVG MPDVWLTMLS MIVGATCYAM FIGHATALIQ SLDSSRRQYQ
EKYKQVEQYM SFHKLPADTR QRIHEYYEHR YQGKMFDEES ILGELSEPLR EEIINFTCRG
LVAHMPLFAH ADPSFVTAVL TKLRFEVFQP GDLVVREGSV GRKMYFIQHG LLSVLARGAR
DTRLTDGSYF GEICLLTRGR RTASVRADTY CRLYSLSVDH FNAVLEEFPM MRRAFETVAM
DRLRRIGKKN SILQRKRSEP SPGSSSGGVM EQHLVQHDRD MARGIRGLAP GTGARLSGKP
VLWEPLVHAP LQAAAVTSNV AIALTHQRGP LPLSPDSPAT LLARSARRSA GSPASPLVPV
RAGPLLARGP WASTSRLPAP PARTLHASLS RTGRSQVSLL GPPPGGGGRR LGPRGRPLSA
SQPSLPQRAT GDGSPRRKGS GSERLPPSGL LAKPPGTVQP SRSSVPEPVT PRGPQISANM
