KCNA5_RAT
ID KCNA5_RAT Reviewed; 602 AA.
AC P19024; Q6LEB7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 5;
DE AltName: Full=RCK7;
DE AltName: Full=RK4;
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.5;
GN Name=Kcna5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=2361015; DOI=10.1016/0896-6273(90)90146-7;
RA Swanson R., Marshall J., Smith J., Williams J., Boyle M.B., Folander K.,
RA Luneau C.J., Antanavage J., Oliva C., Buhrow S.A., Bennett C., Stein R.B.,
RA Kaczmarek L.M.;
RT "Cloning and expression of cDNA and genomic clones encoding three delayed
RT rectifier potassium channels in rat brain.";
RL Neuron 4:929-939(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=1705709; DOI=10.1073/pnas.88.5.1798;
RA Roberds S.L., Tamkun M.M.;
RT "Cloning and tissue-specific expression of five voltage-gated potassium
RT channel cDNAs expressed in rat heart.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1798-1802(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RX PubMed=8253777; DOI=10.1016/s0021-9258(19)74340-3;
RA Mori Y., Matsubara H., Folco E., Siegel A., Koren G.;
RT "The transcription of a mammalian voltage-gated potassium channel is
RT regulated by cAMP in a cell-specific manner.";
RL J. Biol. Chem. 268:26482-26493(1993).
RN [4]
RP INTERACTION WITH DLG1, AND MUTAGENESIS OF 600-THR--LEU-602.
RX PubMed=11709425; DOI=10.1152/ajpheart.2001.281.6.h2575;
RA Murata M., Buckett P.D., Zhou J., Brunner M., Folco E., Koren G.;
RT "SAP97 interacts with Kv1.5 in heterologous expression systems.";
RL Am. J. Physiol. 281:H2575-H2584(2001).
RN [5]
RP INTERACTION WITH DLG1 AND CAV3, AND FUNCTION IN CELL EXCITATION.
RX PubMed=15277200; DOI=10.1152/ajpheart.00152.2004;
RA Folco E.J., Liu G.-X., Koren G.;
RT "Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the
RT voltage-gated potassium channel Kv1.5.";
RL Am. J. Physiol. 287:H681-H690(2004).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15618540; DOI=10.1161/01.res.0000154070.06421.25;
RA Plane F., Johnson R., Kerr P., Wiehler W., Thorneloe K., Ishii K., Chen T.,
RA Cole W.;
RT "Heteromultimeric Kv1 channels contribute to myogenic control of arterial
RT diameter.";
RL Circ. Res. 96:216-224(2005).
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 (PubMed:2361015, PubMed:15618540). Can form functional
CC homotetrameric channels and heterotetrameric channels that contain
CC variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other
CC family members as well; channel properties depend on the type of alpha
CC subunits that are part of the channel (PubMed:15618540). Channel
CC properties are modulated by cytoplasmic beta subunits that regulate the
CC subcellular location of the alpha subunits and promote rapid
CC inactivation (PubMed:15618540). Homotetrameric channels display rapid
CC activation and slow inactivation. May play a role in regulating the
CC secretion of insulin in normal pancreatic islets (By similarity).
CC {ECO:0000250|UniProtKB:P22460, ECO:0000269|PubMed:15277200,
CC ECO:0000269|PubMed:15618540, ECO:0000269|PubMed:2361015}.
CC -!- SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins.
CC Interacts with DLG1, which enhances channel currents (PubMed:11709425).
CC Forms a ternary complex with DLG1 and CAV3 (PubMed:15277200). Interacts
CC with KCNAB1 (By similarity). Interacts with UBE2I (By similarity).
CC {ECO:0000250|UniProtKB:P22460, ECO:0000269|PubMed:11709425,
CC ECO:0000269|PubMed:15277200}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15618540,
CC ECO:0000269|PubMed:2361015}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed equally in atrium, ventricle, aorta and
CC skeletal muscle. Weaker expression in brain.
CC {ECO:0000269|PubMed:1705709}.
CC -!- INDUCTION: Expression regulated by cAMP in a tissue-specific manner. In
CC primary cardiac cells, levels increase by 6-fold, and in GH3 cells,
CC levels decrease 5-6-fold.
CC -!- DOMAIN: The N-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.
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; M27158; AAA41498.1; -; Genomic_DNA.
DR EMBL; L23434; AAA42337.1; -; Genomic_DNA.
DR PIR; JH0166; JH0166.
DR RefSeq; NP_037104.1; NM_012972.1.
DR AlphaFoldDB; P19024; -.
DR SMR; P19024; -.
DR BioGRID; 247503; 6.
DR CORUM; P19024; -.
DR IntAct; P19024; 4.
DR MINT; P19024; -.
DR STRING; 10116.ENSRNOP00000026691; -.
DR ChEMBL; CHEMBL4295724; -.
DR PaxDb; P19024; -.
DR PRIDE; P19024; -.
DR ABCD; P19024; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000026691; ENSRNOP00000026691; ENSRNOG00000019719.
DR GeneID; 25470; -.
DR KEGG; rno:25470; -.
DR UCSC; RGD:2953; rat.
DR CTD; 3741; -.
DR RGD; 2953; Kcna5.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000161860; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; P19024; -.
DR OMA; MNNTLSC; -.
DR OrthoDB; 695337at2759; -.
DR PhylomeDB; P19024; -.
DR TreeFam; TF313103; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:P19024; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000019719; Expressed in skeletal muscle tissue and 10 other tissues.
DR Genevisible; P19024; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:RGD.
DR GO; GO:0046691; C:intracellular canaliculus; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:RGD.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:RGD.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IMP:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:RGD.
DR GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; ISO:RGD.
DR GO; GO:0086087; F:voltage-gated potassium channel activity involved in bundle of His cell action potential repolarization; ISO:RGD.
DR GO; GO:0086090; F:voltage-gated potassium channel activity involved in SA node cell action potential repolarization; ISO:RGD.
DR GO; GO:0086014; P:atrial cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0060081; P:membrane hyperpolarization; ISO:RGD.
DR GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0086050; P:membrane repolarization during bundle of His cell action potential; ISO:RGD.
DR GO; GO:0086052; P:membrane repolarization during SA node cell action potential; ISO:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:RGD.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IDA:RGD.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IMP:RGD.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; ISO:RGD.
DR GO; GO:0051259; P:protein complex oligomerization; IMP:RGD.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:RGD.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:RGD.
DR GO; GO:0043266; P:regulation of potassium ion transport; ISO:RGD.
DR GO; GO:0019229; P:regulation of vasoconstriction; ISO:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
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 1: Evidence at protein level;
KW Cell membrane; Ion channel; Ion transport; Isopeptide bond; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..602
FT /note="Potassium voltage-gated channel subfamily A member
FT 5"
FT /id="PRO_0000053989"
FT TOPO_DOM 1..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 239..260
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 261..314
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 315..336
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 337..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 348..368
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 369..384
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 385..405
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 406..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 421..442
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 443..456
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 457..468
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 469..476
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 477..483
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 484..512
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 513..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 58..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..420
FT /note="S4-S5 linker"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 523..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 469..474
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 600..602
FT /note="PDZ-binding"
FT COMPBIAS 523..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine; by CK2 and PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 535
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 546
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 569
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT LIPID 337
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 525
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT MUTAGEN 600..602
FT /note="TDL->AAA: Loss of interaction with DLG1."
FT /evidence="ECO:0000269|PubMed:11709425"
FT CONFLICT 553
FT /note="C -> S (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 66553 MW; 6A784535FF226ED7 CRC64;
MEISLVPLEN GSAMTLRGGG EAGASCVQTP RGECGCPPTS GLNNQSKETL LRGRTTLEDA
NQGGRPLPPM AQELPQPRRL SAEDEEGEGD PGLGTVEEDQ APQDAGSLHH QRVLINISGL
RFETQLGTLA QFPNTLLGDP AKRLHYFDPL RNEYFFDRNR PSFDGILYYY QSGGRLRRPV
NVSLDVFADE IRFYQLGDEA MERFREDEGF IKEEEKPLPR NEFQRQVWLI FEYPESSGSA
RAIAIVSVLV ILISIITFCL ETLPEFRDER ELLRHPPVPP QPPAPAPGIN GSVSGALSSG
PTVAPLLPRT LADPFFIVET TCVIWFTFEL LVRFFACPSK AEFSRNIMNI IDVVAIFPYF
ITLGTELAEQ QPGGGGQNGQ QAMSLAILRV IRLVRVFRIF KLSRHSKGLQ ILGKTLQASM
RELGLLIFFL FIGVILFSSA VYFAEADNHG SHFSSIPDAF WWAVVTMTTV GYGDMRPITV
GGKIVGSLCA IAGVLTIALP VPVIVSNFNY FYHRETDHEE QAALKEEQGN QRRESGLDTG
GQRKVSCSKA SFCKTGGSLE SSDSIRRGSC PLEKCHLKAK SNVDLRRSLY ALCLDTSRET
DL
