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Database: UniProt
Entry: U3JVR6_FICAL
LinkDB: U3JVR6_FICAL
Original site: U3JVR6_FICAL 
ID   U3JVR6_FICAL            Unreviewed;       634 AA.
AC   U3JVR6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Potassium voltage-gated channel subfamily A member 5 {ECO:0000313|Ensembl:ENSFALP00000006870.2};
GN   Name=KCNA5 {ECO:0000313|Ensembl:ENSFALP00000006870.2};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000006870.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000006870.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000006870.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   AlphaFoldDB; U3JVR6; -.
DR   STRING; 59894.ENSFALP00000006870; -.
DR   Ensembl; ENSFALT00000006899.2; ENSFALP00000006870.2; ENSFALG00000006589.2.
DR   eggNOG; KOG1545; Eukaryota.
DR   GeneTree; ENSGT00940000161860; -.
DR   HOGENOM; CLU_011722_4_0_1; -.
DR   Proteomes; UP000016665; Chromosome 1A.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR   GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
DR   GO; GO:0005251; F:delayed rectifier potassium channel activity; IEA:Ensembl.
DR   GO; GO:0015271; F:outward rectifier potassium channel activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR   GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; IEA:Ensembl.
DR   GO; GO:0086087; F:voltage-gated potassium channel activity involved in bundle of His cell action potential repolarization; IEA:Ensembl.
DR   GO; GO:0086090; F:voltage-gated potassium channel activity involved in SA node cell action potential repolarization; IEA:Ensembl.
DR   GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
DR   GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; IEA:Ensembl.
DR   GO; GO:0097623; P:potassium ion export across plasma membrane; IEA:Ensembl.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR   GO; GO:0043266; P:regulation of potassium ion transport; IEA:Ensembl.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR11537:SF250; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY A MEMBER 5; 1.
DR   PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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:UP000016665};
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   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT   TRANSMEM        320..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        477..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        532..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          189..289
FT                   /note="BTB"
FT                   /evidence="ECO:0000259|SMART:SM00225"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   634 AA;  70885 MW;  AB4BAEE542020F75 CRC64;
     MSFAGFWSRT NSAGNSREQE QGEQKQSGEK NPYQIPSFAL IPLGNGEGGT RQEAPEESPG
     LSALIFARSA RGLAARSARC AQCLQRANQR GGRSVIPGER SAPGPEGSPR LQPQPLPESH
     TSAHLWASPG PAGRGGTRHP GSRGLLPLPK VFANVNMKVA WQKCRLLAFG AALIQRETRG
     SRSRENKSKR VLINISGLRF ETQLGTLNQF PDTLLGDPDK RIRYFDPLRN EYFFDRNRPS
     FDGILYFYQS GGKLRRPVNV SIDVFADEIR FYQLGEEAME RFREDEGFIK EEEKPLPRNE
     FQRQVWLIFE YPESSSSARA IAIVSVLVIL ISIITFCLET LPEFRDEREM PVPLPPQGGG
     LNGTPGDSPP MQPASSLADP FFIIETTCVI WFTFELLVRF FACPSKPEFS RNIMNIIDIV
     AIIPYFITLG TELAHEQQQP GAGIIRLVRV FRIFKLSRHS KGLQILGQTL KASMRELGLL
     IFFLFIGVIL FSSTDDPDSL FTSIPDAFWW AVVSMTTVGY GDMYPMTIGG KIVGSLCAIA
     GVLTIALPVP VIVSNFNYFY HRETDHEEQY PPVLCLKKKK RKKVHRSKSS LLLVTIHHVS
     KTGFKQSTGL VKILCVLSLS QPYLCQCPDV NWLL
//
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