KCNA5_RABIT
ID KCNA5_RABIT Reviewed; 598 AA.
AC P50638;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Japanese white; TISSUE=Heart;
RX PubMed=7556635; DOI=10.1016/0014-5793(95)00954-8;
RA Sasaki Y., Ishii K., Nunoki K., Yamagishi T., Taira N.;
RT "The voltage-dependent K+ channel (Kv1.5) cloned from rabbit heart and
RT facilitation of inactivation of the delayed rectifier current by the rat
RT beta subunit.";
RL FEBS Lett. 372:20-24(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Portal vein;
RA Clement-Chomienne O., Ishii K., Walsh M.P., Cole W.C.;
RT "Rabbit portal vein Kv1.5.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Smooth muscle;
RA Tate R.J., Osipenko O.N., Kempsil F.E.J., Gurney A.M.;
RT "Identification of a voltage-gated potassium channel (KV1.5) in rabbit
RT pulmonary artery smooth muscle.";
RL Submitted (MAY-1999) 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 (PubMed:7556635). 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 (PubMed:7556635). Homotetrameric channels display rapid
CC activation and slow inactivation (PubMed:7556635). 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, ECO:0000269|PubMed:7556635}.
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:0000269|PubMed:7556635};
CC Multi-pass membrane protein {ECO:0000305}.
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 -!- 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. Interacts with UBE2I.
CC {ECO:0000250}.
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; D45025; BAA08082.1; -; mRNA.
DR EMBL; AF056943; AAC13312.1; -; mRNA.
DR EMBL; AF149787; AAD56772.1; -; mRNA.
DR PIR; S66669; S66669.
DR RefSeq; NP_001075505.1; NM_001082036.1.
DR AlphaFoldDB; P50638; -.
DR SMR; P50638; -.
DR STRING; 9986.ENSOCUP00000017544; -.
DR Ensembl; ENSOCUT00000000674; ENSOCUP00000017544; ENSOCUG00000000674.
DR GeneID; 100008684; -.
DR KEGG; ocu:100008684; -.
DR CTD; 3741; -.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000161860; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; P50638; -.
DR OMA; MNNTLSC; -.
DR OrthoDB; 695337at2759; -.
DR TreeFam; TF313103; -.
DR Proteomes; UP000001811; Chromosome 8.
DR Bgee; ENSOCUG00000000674; Expressed in aorta and 16 other tissues.
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:0007219; P:Notch signaling pathway; 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 GO; GO:0019229; P:regulation of vasoconstriction; 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; Ion channel; Ion transport; Isopeptide bond; Lipoprotein;
KW Membrane; Palmitate; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..598
FT /note="Potassium voltage-gated channel subfamily A member
FT 5"
FT /id="PRO_0000053988"
FT TOPO_DOM 1..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 232..253
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 254..308
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 309..330
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 331..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 342..362
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 363..380
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 381..401
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 402..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 417..438
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 439..452
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 453..464
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 465..472
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 480..508
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 509..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..416
FT /note="S4-S5 linker"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 517..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 465..470
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 596..598
FT /note="PDZ-binding"
FT COMPBIAS 524..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 331
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 521
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 598 AA; 65476 MW; B06D235AC7A8E1F0 CRC64;
MEIALGPLEN GGAMTIRGGG EETAGCSQAA PTAGLGDGSQ EPAPRGRGCS ARRGAEPGER
PLPPQPPELP QSRRSPLEEE EGEGDPGLSV AEEQTLGAGA LHHQRVLINI SGLRFETQLG
TLAQFPNTLL GDPAKRLRYF DPLRNEYFFD RNRPSFDGIL YYYQSGGRLR RPVNVSLDVF
ADEIRFYQLG DEAMERFRED EGFIKDEEKP LPRNEFQRQV WLIFEYPESS GSARAIAIVS
VLVILISIIT FCLETLPEFK DERELLRHPP VPHQPPAAPA LGANGSGAVA PASGSTVAPL
LPRTLADPFF IVETTCVIWF TFELLVRFFA CPSKAEFSRN IMNIIDIVAI FPYFITLGTE
LAEQQPGGGG GGQNGQQAMS LAILRVIRLV RVFRIFKLSR HSKGLQILGK TLQASMRELG
LLIFFLFIGV ILFSSAVYFA EADNQGTHFS SIPDAFWWAV VTMTTVGYGD MRPITVGGKI
VGSLCAIAGV LTIALPVPVI VSNFNYFYHR ETDHEEQAAL KEEPGSQSRG TSLDAGGQRK
ASWSKASLCK AGGSLETADS VRRGSCLLEK YNLKAKSNVD LRRSLYALCL DTSRETDL
