ID A0A9D3SV21_MEGAT Unreviewed; 1154 AA.
AC A0A9D3SV21;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 13.
DE RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0000259|PROSITE:PS50042};
GN ORFNames=MATL_G00240140 {ECO:0000313|EMBL:KAG7456837.1};
OS Megalops atlanticus (Tarpon) (Clupea gigantea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Elopiformes; Megalopidae; Megalops.
OX NCBI_TaxID=7932 {ECO:0000313|EMBL:KAG7456837.1, ECO:0000313|Proteomes:UP001046870};
RN [1] {ECO:0000313|EMBL:KAG7456837.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YG-15Mar2019-1 {ECO:0000313|EMBL:KAG7456837.1};
RC TISSUE=Brain {ECO:0000313|EMBL:KAG7456837.1};
RA Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA Lampietro C., Louis A., Herpin A., Echchiki A., Berthelot C., Parey E.,
RA Roest-Crollius H., Braasch I., Postlethwait J., Bobe J., Montfort J.,
RA Bouchez O., Begum T., Mejri S., Adams A., Chen W.-J., Guiguen Y.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00034430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000256|ARBA:ARBA00036239};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the potassium channel HCN family.
CC {ECO:0000256|ARBA:ARBA00006305}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG7456837.1}.
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DR EMBL; JAFDVH010000022; KAG7456837.1; -; Genomic_DNA.
DR OrthoDB; 421226at2759; -.
DR Proteomes; UP001046870; Chromosome 22.
DR GO; GO:0030424; C:axon; IEA:TreeGrafter.
DR GO; GO:0030425; C:dendrite; IEA:TreeGrafter.
DR GO; GO:0098855; C:HCN channel complex; IEA:TreeGrafter.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0003254; P:regulation of membrane depolarization; IEA:TreeGrafter.
DR CDD; cd00038; CAP_ED; 1.
DR FunFam; 1.10.287.70:FF:000031; Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1, putative; 1.
DR FunFam; 1.10.287.630:FF:000002; Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4; 1.
DR FunFam; 2.60.120.10:FF:000007; Putative potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2; 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; IPR051413; K/Na_HCN_channel.
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:SF11; POTASSIUM_SODIUM HYPERPOLARIZATION-ACTIVATED CYCLIC NUCLEOTIDE-GATED CHANNEL 2; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP001046870};
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:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 388..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 617..642
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 720..826
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..40
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..74
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..100
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..276
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1071
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1119
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 124211 MW; B87AD5AC18A17F7C CRC64;
MHKKEDFPGS AATMRKRTSS SGSGHNITAG AVTTSAASGK STKSCFAFVS TAAPGLKPGA
GSDALMDEAE DGEEEPKFQQ PRLRRAGGSG SGGGGGGGGS IRMKNFSSGG GVTSTPSKNL
NNNELCLLQG EGSTRAASVA NPTTAKTCQG DGSGRGGTSR GGGGDAGAGL AATAEVTSAS
GDGSNGTAPI TDMKCNKNGE CRRDSGSAGR QSPVAPKQEK QSGDEVGVED GSKRAACNST
TAGMDGPATP AGCLAQAQGQ GSETATTGVS TAVTAVSEKK DSKVSFSNAP SRKASSSVHG
PGQTQSQQPR NSVTFLKSED GPQLVTEDGE PRGSQASFMQ RQFSSMLQPG VNKFSLRMFG
SQKAVEREQE RVKSAGNWII HPYSDFRFYW DFTMLLFMVG NLIIIPVGIT FFKEETTTPW
IIFNVVSDTF FLTDLVLNFR TGIVIEDNAD IVLDPEKIKK KYLKTWFVVD FVSSIPVDYI
FLIVEKGIDS EVYKTARALR IVRFTKILSL LRLLRLSRLI RYIHQWEEIF HMTYDLASAV
MRIFNLIGMM LLLCHWDGCL QFLVPMLQEF PPDCWVSLNR MVNDSWSEQY SFAVFKAMSH
MLCIGYGRQA PESLSDIWLT MLSMIVGATC YAVFIGHATA LIQSLDSSRR QYQEKYKQVE
QYMSFHKLPA DFRQKIHDYY EHRYQGKMFD EESILGELNE PLREEIVNFN CRKLVASMPL
FANAEPNFVT AMLTKLRFEV FQPRDYIIRE GTIGKKMYFI QHGVVSVLTK GTMGMKLSDG
SYFGEICLLT RGRRTASVRA ETYCRLYSLS VDNFNEVLEE YPMMRRAFET VAIDRLNRIG
KKNSILMHKV QHDLNSGVFN NHENELIQEI VKYDREMVQL VDLQRSRAMS MTPPTQGTIF
GPAGQPQSGS AIATLQQAVA MSFCPQMVSP LVGPMSLQSP RMVRRFQVVQ NLSSPVSASP
LQSQQPSAGA FASAVSSPPV QSPLAAGGRT FQYTAGPGSA AGPLGSQLSL VQHHAPAPAP
GPAQRTASHK SAHPLQGGGL GQDARALSAS QSSLPQEGAP PASPSQPPSP TVGPAQAQPS
MPGAPGLRGS GPQKAPLPPK MPEGSLSSGS PSEAPPGKGT VTGPSPLDPG APKKDSVVSL
SETDPARSRL SSNL
//
