GenomeNet

Database: UniProt
Entry: F1LSH6_RAT
LinkDB: F1LSH6_RAT
Original site: F1LSH6_RAT 
ID   F1LSH6_RAT              Unreviewed;       902 AA.
AC   F1LSH6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   30-AUG-2017, entry version 55.
DE   SubName: Full=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 {ECO:0000313|Ensembl:ENSRNOP00000073952};
GN   Name=Hcn1 {ECO:0000313|Ensembl:ENSRNOP00000073952,
GN   ECO:0000313|RGD:620688};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000073952, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000073952, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000073952,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000073952}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000073952};
RG   Ensembl;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSRNOP00000073952}.
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DR   EMBL; AABR07008268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07008269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07008270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07008271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07008272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PaxDb; F1LSH6; -.
DR   PRIDE; F1LSH6; -.
DR   Ensembl; ENSRNOT00000089218; ENSRNOP00000073952; ENSRNOG00000055382.
DR   RGD; 620688; Hcn1.
DR   eggNOG; KOG0498; Eukaryota.
DR   eggNOG; ENOG410XPSE; LUCA.
DR   GeneTree; ENSGT00760000118772; -.
DR   OMA; TRTFHYA; -.
DR   OrthoDB; EOG091G0JQU; -.
DR   Reactome; R-RNO-1296061; HCN channels.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000055382; -.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0098855; C:HCN channel complex; IEA:Ensembl.
DR   GO; GO:0030552; F:cAMP binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005222; F:intracellular cAMP activated cation channel activity; IEA:Ensembl.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:Ensembl.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:Ensembl.
DR   GO; GO:0045176; P:apical protein localization; IEA:Ensembl.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR   GO; GO:0046549; P:retinal cone cell development; IEA:Ensembl.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR013621; Ion_trans_N.
DR   InterPro; IPR030169; K/Na_HCN1.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   PANTHER; PTHR10217:SF567; PTHR10217:SF567; 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; SSF51206; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Ion channel {ECO:0000256|SAAS:SAAS00091826};
KW   Ion transport {ECO:0000256|SAAS:SAAS00502700};
KW   Membrane {ECO:0000256|SAAS:SAAS00502630, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|SAAS:SAAS00807593};
KW   Potassium channel {ECO:0000256|SAAS:SAAS00807732};
KW   Potassium transport {ECO:0000256|SAAS:SAAS00807568};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00137614,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00137754,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00502637};
KW   Voltage-gated channel {ECO:0000256|SAAS:SAAS00807693}.
FT   TRANSMEM    132    156       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    361    386       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      464    570       Cyclic nucleotide-binding.
FT                                {ECO:0000259|PROSITE:PS50042}.
FT   COILED      746    767       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   902 AA;  101429 MW;  6C99D3A66AA7EA38 CRC64;
     MEGGGKPNSA SNSRDDGNSV YPSKAPATGP AAADKRLGTP 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
     QPQPQLQQSQ VQQTQPQPQP QPQQPQQQQQ QQQQQQQQQQ QQQQQQQPQT PGSSTPKNEV
     HKSTQALHNT NLTREVRPLS ASQPSLPHEV STMISRPHPT VGESLASIPQ PMATVHSTGL
     QAGSRSTVPQ RVTLFRQMSS GAIPPNRGVP PAPPPPAAVQ RESPSVLNKD PDAEKPRFAS
     NL
//
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