Swiss-Prot entry
ID HCN3_MOUSE STANDARD; PRT; 779 AA.
AC O88705;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated
DE channel 3 (Hyperpolarization-activated cation channel 3) (HAC-3).
GN Name=Hcn3; Synonyms=Hac3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muridae; Murinae; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/c;
RX MEDLINE=98295993; PubMed=9634236 [NCBI, ExPASy, EBI, Israel, Japan]; 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX MEDLINE=22354683; PubMed=12466851 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/nature01266;
RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S.,
RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H.,
RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T.,
RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J.,
RA Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W.,
RA Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S.,
RA Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S.,
RA Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J.,
RA Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D.,
RA Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L.,
RA Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A.,
RA Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H.,
RA Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G.,
RA Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S.,
RA Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M.,
RA Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K.,
RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M.,
RA Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C.,
RA Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L.,
RA Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N.,
RA Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K.,
RA Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S.,
RA Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I.,
RA Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A.,
RA Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J.,
RA Birney E., Hayashizaki Y.;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX MEDLINE=98292171; PubMed=9630217 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S0092-8674(00)81434-8;
RA Santoro B., Liu D.T., Yao H., Bartsch D., Kandel E.R.,
RA Siegelbaum S.A., Tibbs G.R.;
RT "Identification of a gene encoding a hyperpolarization-activated
RT 'pacemaker' channel of brain.";
RL Cell 93:717-729(1998).
CC -!- FUNCTION: Putative hyperpolarization-activated ion channel
CC exhibiting weak selectivity for potassium over sodium ions.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits.
CC -!- SUBCELLULAR LOCATION: Integral membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and heart, in
CC particular in ventricle, atrium and in sinoatrial node (SAN).
CC Detected at low levels in skeletal muscle and lung.
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 family. HCN
CC subfamily.
CC -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; AJ225124; CAA12408.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AK032225; BAC27769.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC039156; AAH39156.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR SMR; O88705; 353-553.
DR Ensembl; ENSMUSG00000032338; Mus_musculus
DR MGI; MGI:1298211; Hcn3.
DR GO; GO:0016021; C:integral to membrane; TAS.
DR InterPro; IPR000595; cNMP_binding.
DR InterPro; IPR003938; EAG_ELK_ERG.
DR InterPro; IPR005821; Ion_trans.
DR InterPro; IPR005820; M+channel_nlg.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR CMR; O88705.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; O88705.
DR ProtoNet; O88705.
DR ProtoMap; O88705.
DR PRESAGE; O88705.
DR DIP; O88705.
DR ModBase; O88705.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW cAMP; cAMP-binding; Glycoprotein; Ion transport; Ionic channel;
KW Nucleotide-binding; Potassium; Potassium channel; Potassium transport;
KW Sodium; Sodium channel; Sodium transport; Transmembrane; Transport;
KW Voltage-gated channel.
FT TOPO_DOM 1 96 Cytoplasmic (Potential).
FT TRANSMEM 97 117 Segment S1 (Potential).
FT TRANSMEM 124 144 Segment S2 (Potential).
FT TOPO_DOM 145 170 Cytoplasmic (Potential).
FT TRANSMEM 171 191 Segment S3 (Potential).
FT TRANSMEM 201 221 Segment S4 (Potential).
FT TOPO_DOM 222 252 Cytoplasmic (Potential).
FT TRANSMEM 253 273 Segment S5 (Potential).
FT TRANSMEM 297 318 Segment H5 (pore-forming) (Potential).
FT TRANSMEM 329 349 Segment S6 (Potential).
FT TOPO_DOM 350 779 Cytoplasmic (Potential).
FT NP_BIND 427 544 cAMP.
FT REGION 45 90 Involved in subunit assembly (By
FT similarity).
FT CARBOHYD 290 290 N-linked (GlcNAc...) (Potential).
SQ SEQUENCE 779 AA; 86641 MW; D4FF151F174DECAE CRC64;
MEEEARPAAG AGEAATPARE TPPAAPAQAR AASGGVPESA PEPKRRQLGT LLQPTVNKFS
LRVFGSHKAV EIEQERVKSA GAWIIHPYSD FRFYWDLIML LLMVGNLIVL PVGITFFKEE
NSPPWIVFNV LSDTFFLLDL VLNFRTGIVV EEGAEILLAP RAIRTRYLRT WFLVDLISSI
PVDYIFLVVE LEPRLDAEVY KTARALRIVR FTKILSLLRL LRLSRLIRYI 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 SPGSSGGVME QHLVQHDRDM ARGVRGLAPG TGARLSGKPV
LWEPLVHAPL QAAAVTSNVA IALTHQRGPL PLSPDSPATL LARSARRSAG SPASPLVPVR
AGPLLARGPW ASTSRLPAPP ARTLHASLSR TGRSQVSLLG PPPGGGARRL GPRGRPLSAS
QPSLPQRATG DGSPRRKGSG SERLPPSGLL AKPPGTVQPP RSSVPEPVTP RGPQISANM
//