ID G1MT76_MELGA Unreviewed; 1145 AA.
AC G1MT76;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Hyperpolarization activated cyclic nucleotide gated potassium channel 4 {ECO:0000313|Ensembl:ENSMGAP00000001587.3};
GN Name=HCN4 {ECO:0000313|Ensembl:ENSMGAP00000001587.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000001587.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000001587.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000001587.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the potassium channel HCN family.
CC {ECO:0000256|ARBA:ARBA00006305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; G1MT76; -.
DR Ensembl; ENSMGAT00000002250.3; ENSMGAP00000001587.3; ENSMGAG00000002045.3.
DR GeneTree; ENSGT00940000154743; -.
DR HOGENOM; CLU_005746_15_0_1; -.
DR TreeFam; TF318250; -.
DR Proteomes; UP000001645; Chromosome 12.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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:SF4; POTASSIUM_SODIUM HYPERPOLARIZATION-ACTIVATED CYCLIC NUCLEOTIDE-GATED CHANNEL 4; 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 3: Inferred from homology;
KW cAMP {ECO:0000256|ARBA:ARBA00023149};
KW cAMP-binding {ECO:0000256|ARBA:ARBA00022566};
KW Ion channel {ECO:0000256|ARBA:ARBA00022461};
KW Ion transport {ECO:0000256|ARBA:ARBA00022461};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022566};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022461}.
FT TRANSMEM 235..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 567..682
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 124726 MW; EF6F5081C0C89E05 CRC64;
MDKLPPSMRK RLYSLPQQIG PKASIMDEEE DSDKDTRRKS IRLKPLPSPS AGSTRALGGD
PGRGEDPGLV ETEAGSKGAK TSTNGDCRRF KGSLSSLTSR HLHDAAEEKR LIGGEGEPAS
PGEDKSPSGS GETQGLPAPP PPASPPEPQQ QPLRACSSTS IKVEGGGGCD QITPDEEQRL
GQAGFMQRQF GAMLQPGVNK FSLRMFGSQK AVEREQERVK SAGFWIIHPY SDFRFYWDLT
MLLLMVGNLI IIPVGITFFK DENTTPWIVF NVVSDTFFLI DLVLNFRTGI VVEDNTEIIL
DPQRIKMKYL KSWFVVDFIS SIPVDYIFLI VETRIDSEVY KTARALRIVR FTKILSLLRL
LRLSRLIRYI HQWEEIFHMT YDLASAVVRI VNLIGMMLLL CHWDGCLQFL VPMLQDFPDD
CWVSLNRMVN DSWGKQYSYA LFKAMSHMLC IGYGQQAPVG MSDVWLTMLS MIVGATCYAM
FIGHATALIQ SLDSSRRQYQ EKYKQVEQYM SFHKLPADMR QRIHDYYEHR YQGKMFDEES
ILGELSEPLR EEIINFNCRK LVASMPLFAN ADPNFVTSML TKLRFEVFQP GDYIIREGTI
GKKMYFIQHG VVSVLTKGNK ETKLADGSYF GEICLLTRGR RTASVRADTY CRLYSLSVDN
FNEVLEEYPM MRRAFETVAL DRLDRIGKKN SILLHKVQHD LNSGVFNYQE NEIIQQIVQH
DREMAHCAHN VQAAAAAAAA ASTPTPVIWT PLIQAPLQAA AATTSVAIAL THHPRLPTAI
FRPPVSVLGS LGQQSSQTPR QLKRLQSLIP STGPSAVGSP SSTPSQLHTP GFQVGSPPAG
SGQQGLSGAG FGHFQQAVAS SPSTSLTQLS SNSPPGLLNQ FQPATRPLQG GQLQQLSGSG
TLGGINHFQP PPSSNSPSSS LSQLAQASGG PSSGLCQTQP SALGSLTGTI AQLHQERSPF
VSASPLQQPG VASPCYTPSG LSPPTQSPVA TRTFQCGPLG ASGSHGSLLL PQTASPPPQI
LQSKSTPPVP PGRLNQDIKL ISASQPSLPQ ELAQTLSQSS HSSRESVSSF SPFPGGGTGL
LGKPCSSIPG RVTLPRQMSS GSLPHPLVFG ASAAGTASLT AGGRKESIVL TGDLEPVRSK
LPSNL
//
