KCNA5_MUSPF
ID KCNA5_MUSPF Reviewed; 601 AA.
AC P79197;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 5;
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.5;
GN Name=KCNA5;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Mustela.
OX NCBI_TaxID=9669;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart atrium;
RA Schwegel T., Folander K., Swanson R.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC potassium transport in excitable membranes. Forms tetrameric potassium-
CC selective channels through which potassium ions pass in accordance with
CC their electrochemical gradient. The channel alternates between opened
CC and closed conformations in response to the voltage difference across
CC the membrane (By similarity). Can form functional homotetrameric
CC channels and heterotetrameric channels that contain variable
CC proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family
CC members as well; channel properties depend on the type of alpha
CC subunits that are part of the channel (By similarity). Channel
CC properties are modulated by cytoplasmic beta subunits that regulate the
CC subcellular location of the alpha subunits and promote rapid
CC inactivation (By similarity). Homotetrameric channels display rapid
CC activation and slow inactivation (By similarity). May play a role in
CC regulating the secretion of insulin in normal pancreatic islets (By
CC similarity). {ECO:0000250|UniProtKB:P19024,
CC ECO:0000250|UniProtKB:P22460}.
CC -!- SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins.
CC Interacts with DLG1, which enhances channel currents. Forms a ternary
CC complex with DLG1 and CAV3 (By similarity). Interacts with KCNAB1 (By
CC similarity). Interacts with UBE2I (By similarity).
CC {ECO:0000250|UniProtKB:P19024, ECO:0000250|UniProtKB:P22460}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22460};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: The amino terminus may be important in determining the rate of
CC inactivation of the channel while the C-terminal PDZ-binding motif may
CC play a role in modulation of channel activity and/or targeting of the
CC channel to specific subcellular compartments. {ECO:0000250}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Kv1.5/KCNA5 sub-subfamily. {ECO:0000305}.
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DR EMBL; U45979; AAB41145.1; -; mRNA.
DR RefSeq; NP_001297131.1; NM_001310202.1.
DR AlphaFoldDB; P79197; -.
DR SMR; P79197; -.
DR STRING; 9668.ENSMPUP00000019031; -.
DR Ensembl; ENSMPUT00000019306; ENSMPUP00000019031; ENSMPUG00000019154.
DR GeneID; 101688777; -.
DR CTD; 3741; -.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000161860; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; P79197; -.
DR OMA; MNNTLSC; -.
DR Proteomes; UP000000715; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0034705; C:potassium channel complex; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
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:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
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:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0043266; P:regulation of potassium ion transport; IEA:Ensembl.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 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; IPR004052; K_chnl_volt-dep_Kv1.5.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01512; KV15CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Isopeptide bond;
KW Lipoprotein; Membrane; Palmitate; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..601
FT /note="Potassium voltage-gated channel subfamily A member
FT 5"
FT /id="PRO_0000053987"
FT TOPO_DOM 1..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 237..258
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 259..312
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 313..334
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 335..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 346..366
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 367..383
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 384..404
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 405..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 420..441
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 442..455
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 456..467
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 468..475
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 476..482
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 483..511
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 512..601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 19..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..419
FT /note="S4-S5 linker"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 521..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 468..473
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 599..601
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT LIPID 335
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 524
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 601 AA; 65889 MW; 142DB9F8CBB43FE0 CRC64;
MEIALVPLEN GGAMTVRGGG EAGTGCSQAI GGELQCPPTA GLSDGPKEPA PRARGTQRGV
DPGGRPLPPL PQDPQQPRRL PPEDEEGEGD PALGMAEDQV LGAGSLHHQR VLINISGLRF
ETQLGTLAQF PNTLLGDPAK RLRYFDPLRN EYFFDRNRPS FDGILYYYQS GGRLRRPVNV
SLDVFADEIR FYQLGDEAME RFREDEGFIK EEEKPLPRNE FQRQVWLIFE YPESSGSARG
IAIVSVLVIL ISIITFCLET LPEFRDEREL LRHPPVPHQP LGPSRGANGS GPLAPPSGPT
VAPLLPRTLA DPFFIVETTC VIWFTFELLV RFFACPSKAE FSRNIMNIID VVAIFPYFIT
LGTELAEQPG GGGGGQNGQQ AMSLAILRVI RLVRVFRIFK LSRHSKGLQI LGKTLQASMR
ELGLLIFFLF IGVILFSSAV YFAEADNQET HFSSIPDAFW WAVVTMTTVG YGDMRPVTVG
GKIVGSLCAI AGVLTIALPV PVIVSNFNYF YHRETDHEEQ AALKEEQGSQ SHGTGLDSGG
PRKASWSKGS LCKAGVSLEN ADGARRGSCP LEKCNLKAKS NVDLRRSLYA LCLDTSRETD
L
