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Database: UniProt
Entry: A0A7L0B1R2_9AVES
LinkDB: A0A7L0B1R2_9AVES
Original site: A0A7L0B1R2_9AVES 
ID   A0A7L0B1R2_9AVES        Unreviewed;      1187 AA.
AC   A0A7L0B1R2;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   18-JUN-2025, entry version 17.
DE   SubName: Full=HCN4 protein {ECO:0000313|EMBL:NXJ40988.1};
DE   Flags: Fragment;
GN   Name=Hcn4_0 {ECO:0000313|EMBL:NXJ40988.1};
GN   ORFNames=CICMAG_R07776 {ECO:0000313|EMBL:NXJ40988.1};
OS   Ciconia maguari.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Aequornithes; Ciconiiformes;
OC   Ciconiidae; Ciconia.
OX   NCBI_TaxID=52777 {ECO:0000313|EMBL:NXJ40988.1, ECO:0000313|Proteomes:UP000537039};
RN   [1] {ECO:0000313|EMBL:NXJ40988.1, ECO:0000313|Proteomes:UP000537039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B10K-DU-001-47 {ECO:0000313|EMBL:NXJ40988.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXJ40988.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) 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:NXJ40988.1}.
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DR   EMBL; VXAE01014128; NXJ40988.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7L0B1R2; -.
DR   Proteomes; UP000537039; Unassembled WGS sequence.
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: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   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:UP000537039};
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        236..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        467..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          568..683
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          1..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          858..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1016..1073
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1088..1126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..152
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..890
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..921
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..940
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        956..967
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1038..1051
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1097
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1098..1115
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXJ40988.1"
FT   NON_TER         1187
FT                   /evidence="ECO:0000313|EMBL:NXJ40988.1"
SQ   SEQUENCE   1187 AA;  129413 MW;  4570F5212C58F20D CRC64;
     MDKLPPSMRK RLYSLPQQIG PKASIMDEEE DSDKDTRRKS IRLKPLPSPS AGSTRALGGD
     PGRGGDPGFL ETEAGSKGAK TSTNGDCRRF KGSLSSLTSR HLHDAAEEKR LIGGEGEPAS
     PSEDKSLPGS GELEQGLPAP PPPASPPEPQ QQPPRACSST SIKVEGGGGC DQITPDEEQR
     LGQAGFMQRQ FGAMLQPGVN KFSLRMFGSQ KAVEREQERV KSAGFWIIHP YSDFRFYWDL
     TMLLLMVGNL IIIPVGITFF KDENTTPWIV FNVVSDTFFL IDLVLNFRTG IVVEDNTEII
     LDPQRIKMKY LKSWFVVDFI SSIPVDYIFL IVETRIDSEV YKTARALRIV RFTKILSLLR
     LLRLSRLIRY IHQWEEIFHM TYDLASAVVR IVNLIGMMLL LCHWDGCLQF LVPMLQDFPD
     DCWVSLNRMV NDSWGKQYSY ALFKAMSHML CIGYGQQAPM GMSDVWLTML SMIVGATCYA
     MFIGHATALI QSLDSSRRQY QEKYKQVEQY MSFHKLPADM RQRIHDYYEH RYQGKMFDEE
     SILGELSEPL REEIINFNCR KLVASMPLFA NADPNFVTSM LTKLRFEVFQ PGDYIIREGT
     IGKKMYFIQH GVVSVLTKGN KETKLADGSY FGEICLLTRG RRTASVRADT YCRLYSLSVD
     NFNEVLEEYP MMRRAFETVA LDRLDRIGKK NSILLHKVQH DLNSGVFNYQ ENEIIQQIVQ
     HDREMAHCAH NVQAAAAAAA AAASTPTPVI WTPLIQAPLQ AAAATTSVAI ALTHHPRLPT
     AIFRPPVSVL GSLGQQSNQT PRQLKRLQSL IPSTGPSAVG SPSSTPSQLH TPGAETPSSS
     SFHIQQLAGF SAAASLGQFQ VGSPPGGSSQ LAQPMQQQQQ QQQQPALPSS GFGHFQQATT
     SSPSTSLTQL SSNSPPSLLN QFQPTTRPLQ GGQLQQLSGS GTLGGMNHFQ PPPSSNSPSS
     SLSQLAQGSG GPSSGLCQTH PSALGSLTGT IAQLHQERPP FASMSPLQQA GIASPCYTPS
     GLSPPSQSPV ATRTFHCGPS GASGSHGSLL LPQTASPPPQ ILQSKSTPPV PLGRLSQDIK
     LISASQPSLP QDLAQTLSQS SPHSSRESVS SFSPFPGGGT GLLGKPCSSI PGRVTLPRQM
     SSGSLPHPLV FGASAAGATS LTAGGRKESI VLTGDLEPVR SKLPSNL
//
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