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Database: UniProt
Entry: HCN3_HUMAN
LinkDB: HCN3_HUMAN
Original site: HCN3_HUMAN 
ID   HCN3_HUMAN              Reviewed;         774 AA.
AC   Q9P1Z3; D3DV90; Q4VX12; Q8N6W6; Q9BWQ2;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 2.
DT   25-OCT-2017, entry version 148.
DE   RecName: Full=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3;
GN   Name=HCN3; Synonyms=KIAA1535;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-774.
RC   TISSUE=Brain;
RX   PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVII.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 7:143-150(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-774.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ENZYME
RP   REGULATION.
RX   PubMed=16043489; DOI=10.1074/jbc.M502508200;
RA   Stieber J., Stockl G., Herrmann S., Hassfurth B., Hofmann F.;
RT   "Functional expression of the human HCN3 channel.";
RL   J. Biol. Chem. 280:34635-34643(2005).
CC   -!- FUNCTION: Hyperpolarization-activated potassium channel. May also
CC       facilitate the permeation of sodium ions.
CC       {ECO:0000269|PubMed:16043489}.
CC   -!- ENZYME REGULATION: Inhibited by Cs(1+) and ZD7288. Is apparently
CC       not activated by cAMP. {ECO:0000269|PubMed:16043489}.
CC   -!- SUBUNIT: Homotetramer. The potassium channel is probably composed
CC       of a homo- or heterotetrameric complex of pore-forming subunits.
CC       Interacts with KCTD3 and PEX5L. {ECO:0000250|UniProtKB:O88705,
CC       ECO:0000250|UniProtKB:Q9UL51}.
CC   -!- INTERACTION:
CC       Q4ACU6-1:Shank3 (xeno); NbExp=3; IntAct=EBI-11178054, EBI-16201983;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16043489};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16043489}.
CC   -!- TISSUE SPECIFICITY: Detected in brain.
CC       {ECO:0000269|PubMed:16043489}.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel HCN family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH28024.2; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AL713999; CAI95100.1; -; Genomic_DNA.
DR   EMBL; AB040968; BAA96059.2; -; mRNA.
DR   EMBL; CH471121; EAW53084.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53086.1; -; Genomic_DNA.
DR   EMBL; BC000066; AAH00066.1; -; mRNA.
DR   EMBL; BC028024; AAH28024.2; ALT_INIT; mRNA.
DR   CCDS; CCDS1108.1; -.
DR   RefSeq; NP_065948.1; NM_020897.2.
DR   UniGene; Hs.706960; -.
DR   ProteinModelPortal; Q9P1Z3; -.
DR   SMR; Q9P1Z3; -.
DR   BioGrid; 121691; 3.
DR   DIP; DIP-62039N; -.
DR   IntAct; Q9P1Z3; 2.
DR   STRING; 9606.ENSP00000357342; -.
DR   BindingDB; Q9P1Z3; -.
DR   ChEMBL; CHEMBL1795173; -.
DR   GuidetoPHARMACOLOGY; 402; -.
DR   iPTMnet; Q9P1Z3; -.
DR   PhosphoSitePlus; Q9P1Z3; -.
DR   DMDM; 29840780; -.
DR   PaxDb; Q9P1Z3; -.
DR   PeptideAtlas; Q9P1Z3; -.
DR   PRIDE; Q9P1Z3; -.
DR   DNASU; 57657; -.
DR   Ensembl; ENST00000368358; ENSP00000357342; ENSG00000143630.
DR   Ensembl; ENST00000575670; ENSP00000458364; ENSG00000263324.
DR   GeneID; 57657; -.
DR   KEGG; hsa:57657; -.
DR   UCSC; uc001fjz.3; human.
DR   CTD; 57657; -.
DR   DisGeNET; 57657; -.
DR   EuPathDB; HostDB:ENSG00000143630.9; -.
DR   GeneCards; HCN3; -.
DR   H-InvDB; HIX0001125; -.
DR   HGNC; HGNC:19183; HCN3.
DR   HPA; HPA026584; -.
DR   MIM; 609973; gene.
DR   neXtProt; NX_Q9P1Z3; -.
DR   OpenTargets; ENSG00000143630; -.
DR   PharmGKB; PA38821; -.
DR   eggNOG; KOG0498; Eukaryota.
DR   eggNOG; ENOG410XPSE; LUCA.
DR   GeneTree; ENSGT00900000140801; -.
DR   HOGENOM; HOG000230717; -.
DR   HOVERGEN; HBG039489; -.
DR   InParanoid; Q9P1Z3; -.
DR   KO; K04956; -.
DR   OMA; VMEQHLV; -.
DR   OrthoDB; EOG091G0JQU; -.
DR   PhylomeDB; Q9P1Z3; -.
DR   TreeFam; TF318250; -.
DR   Reactome; R-HSA-1296061; HCN channels.
DR   ChiTaRS; HCN3; human.
DR   GeneWiki; HCN3; -.
DR   GenomeRNAi; 57657; -.
DR   PRO; PR:Q9P1Z3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000143630; -.
DR   CleanEx; HS_HCN3; -.
DR   Genevisible; Q9P1Z3; HS.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0044316; C:cone cell pedicle; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IMP:UniProtKB.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IMP:UniProtKB.
DR   GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IMP:UniProtKB.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:UniProtKB.
DR   GO; GO:0072718; P:response to cisplatin; IEA:Ensembl.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IMP:UniProtKB.
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; Complete proteome; Glycoprotein;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome; Sodium;
KW   Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN         1    774       Potassium/sodium hyperpolarization-
FT                                activated cyclic nucleotide-gated channel
FT                                3.
FT                                /FTId=PRO_0000054114.
FT   TOPO_DOM      1     97       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     98    118       Helical; Name=Segment S1. {ECO:0000255}.
FT   TOPO_DOM    119    124       Extracellular. {ECO:0000255}.
FT   TRANSMEM    125    145       Helical; Name=Segment S2. {ECO:0000255}.
FT   TOPO_DOM    146    171       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    172    192       Helical; Name=Segment S3. {ECO:0000255}.
FT   TOPO_DOM    193    201       Extracellular. {ECO:0000255}.
FT   TRANSMEM    202    222       Helical; Voltage-sensor; Name=Segment S4.
FT                                {ECO:0000255}.
FT   TOPO_DOM    223    253       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    254    274       Helical; Name=Segment S5. {ECO:0000255}.
FT   TOPO_DOM    275    297       Extracellular. {ECO:0000255}.
FT   INTRAMEM    298    319       Pore-forming; Name=Segment H5.
FT                                {ECO:0000255}.
FT   TOPO_DOM    320    329       Extracellular. {ECO:0000255}.
FT   TRANSMEM    330    350       Helical; Name=Segment S6. {ECO:0000255}.
FT   TOPO_DOM    351    774       Cytoplasmic. {ECO:0000255}.
FT   NP_BIND     492    495       cAMP. {ECO:0000250}.
FT   NP_BIND     502    503       cAMP. {ECO:0000250}.
FT   NP_BIND     543    546       cAMP. {ECO:0000250}.
FT   REGION       46     91       Involved in subunit assembly.
FT                                {ECO:0000250}.
FT   REGION      354    774       Interaction with KCTD3.
FT                                {ECO:0000250|UniProtKB:O88705}.
FT   COMPBIAS    696    765       Pro-rich.
FT   MOD_RES     634    634       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O88705}.
FT   CARBOHYD    291    291       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VARIANT     630    630       P -> L (in dbSNP:rs35001694).
FT                                /FTId=VAR_048746.
FT   CONFLICT    206    206       A -> G (in Ref. 4; AAH00066).
FT                                {ECO:0000305}.
FT   CONFLICT    734    734       S -> T (in Ref. 3; BAA96059).
FT                                {ECO:0000305}.
SQ   SEQUENCE   774 AA;  86032 MW;  37B9BC13E5E2C097 CRC64;
     MEAEQRPAAG ASEGATPGLE AVPPVAPPPA TAASGPIPKS GPEPKRRHLG TLLQPTVNKF
     SLRVFGSHKA VEIEQERVKS AGAWIIHPYS DFRFYWDLIM LLLMVGNLIV LPVGITFFKE
     ENSPPWIVFN VLSDTFFLLD LVLNFRTGIV VEEGAEILLA PRAIRTRYLR TWFLVDLISS
     IPVDYIFLVV ELEPRLDAEV YKTARALRIV RFTKILSLLR LLRLSRLIRY IHQWEEIFHM
     TYDLASAVVR IFNLIGMMLL LCHWDGCLQF LVPMLQDFPP DCWVSINHMV NHSWGRQYSH
     ALFKAMSHML CIGYGQQAPV GMPDVWLTML SMIVGATCYA MFIGHATALI QSLDSSRRQY
     QEKYKQVEQY MSFHKLPADT RQRIHEYYEH RYQGKMFDEE SILGELSEPL REEIINFTCR
     GLVAHMPLFA HADPSFVTAV LTKLRFEVFQ PGDLVVREGS VGRKMYFIQH GLLSVLARGA
     RDTRLTDGSY FGEICLLTRG RRTASVRADT YCRLYSLSVD HFNAVLEEFP MMRRAFETVA
     MDRLLRIGKK NSILQRKRSE PSPGSSGGIM EQHLVQHDRD MARGVRGRAP STGAQLSGKP
     VLWEPLVHAP LQAAAVTSNV AIALTHQRGP LPLSPDSPAT LLARSAWRSA GSPASPLVPV
     RAGPWASTSR LPAPPARTLH ASLSRAGRSQ VSLLGPPPGG GGRRLGPRGR PLSASQPSLP
     QRATGDGSPG RKGSGSERLP PSGLLAKPPR TAQPPRPPVP EPATPRGLQL SANM
//
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