ID A0A2Y9K415_ENHLU Unreviewed; 1202 AA.
AC A0A2Y9K415;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 {ECO:0000313|RefSeq:XP_022367938.1};
GN Name=LOC111153294 {ECO:0000313|RefSeq:XP_022367938.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022367938.1};
RN [1] {ECO:0000313|RefSeq:XP_022367938.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022367938.1};
RG RefSeq;
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}.
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DR RefSeq; XP_022367938.1; XM_022512230.1.
DR AlphaFoldDB; A0A2Y9K415; -.
DR STRING; 391180.A0A2Y9K415; -.
DR KEGG; elk:111153294; -.
DR OrthoDB; 74296at2759; -.
DR Proteomes; UP000248482; Unplaced.
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:UP000248482};
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 265..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 597..712
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 19..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1072
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 128837 MW; EEBF1A35E5C0411B CRC64;
MDKLPPSMRK RLYSLPQQVG AKAWIMDEEE DAEEEGTGGR QDPSRRSIRL RPLPSPSPSA
AAGGTEPRGA ALGAADGEGP ARGAGKSSTN GDCRRFRGSL ASLGSRGGGG GGAGAGGGSS
HGHLHDSAEE RRLIAEGDAS PGEDRTPPGL AAEPERPGTS AQPAASPPPP QQPPQPASAS
CEQPSVDTAI KVEGGAAAGD QILPEAEVRL GQAGFMQRQF GAMLQPGVNK FSLRMFGSQK
AVEREQERVK SAGFWIIHPY SDFRFYWDLT MLLLMVGNLI IIPVGITFFK DENTTPWIVF
NVVSDTFFLI DLVLNFRTGI VVEDNTEIIL DPQRIKMKYL KSWFVVDFIS SIPVDYIFLI
VETRIDSEVY KTARALRIVR FTKILSLLRL LRLSRLIRYI HQWEEIFHMT YDLASAVVRI
VNLIGMMLLL CHWDGCLQFL VPMLQDFPDD CWVSINNMVN NSWGKQYSYA LFKAMSHMLC
IGYGRQAPVG MSDVWLTMLS MIVGATCYAM FIGHATALIQ SLDSSRRQYQ EKYKQVEQYM
SFHKLPPDTR QRIHDYYEHR YQGKMFDEES ILGELSEPLR EEIINFNCRK LVASMPLFAN
ADPNFVTSML TKLRFEVFQP GDYIIREGTI GKKMYFIQHG VVSVLTKGNK ETKLADGSYF
GEICLLTRGR RTASVRADTY CRLYSLSVDN FNEVLEEYPM MRRAFETVAL DRLDRIGKKN
SILLHKVQHD LNSGVFNYQE NEIIQQIVQH DREMAHCAHR VQAAASATPT PTPVIWTPLI
QAPLQAAAAT TSVAIALTHH PRLPAAIFRP PPGPGIGGLG AGQTPRHLKR LQSLIPSALG
SASPASSPSQ VDTPSSSSFH IQQLAGFSAP AGLSPLLPSS GSSPPPGLGG SSPAPTPSAS
EVATAAAGFG HFHKALGGSL SSSDSPLLTP LQSGARSPQA NQPPPPLPGA RGGLGLLEHF
LPPPPSSRSP SASPGQLGQP PGELSPGLAA GPPSTPETPP RQPERPSFVA GASGGASPVA
FPPRGGLSPQ GHSPGPPRTF PSAPPRASGS HGSLLLPPAS SPPAPQVPQR RGTPPLTPGR
LTQDLKLISA SQPALPQDGA QTLRRASPHS SGESVAAFPL VPRAGGASGG SGGFVSPGRP
YGAVPGQHVT LPRKTSSGSL PPPLSLFGAR AASSGGPPLT AAPQREPGAR SEPVRSKLPS
NL
//
