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Potassium voltage-gated channel subfamily A member 2 (KC22) (Voltage-gated potassium channel subunit Kv1.2)

 KCNA2_RABIT             Reviewed;         499 AA.
Q09081; G1SW45; Q9MYX3; Q9TUK7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
07-JAN-2015, sequence version 2.
30-AUG-2017, entry version 113.
RecName: Full=Potassium voltage-gated channel subfamily A member 2;
AltName: Full=KC22;
AltName: Full=Voltage-gated potassium channel subunit Kv1.2;
Name=KCNA2;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INTERACTION WITH KCNA5 AND
KCNAB1, AND TISSUE SPECIFICITY.
PubMed=11717160; DOI=10.1161/hh2301.100817;
Thorneloe K.S., Chen T.T., Kerr P.M., Grier E.F., Horowitz B.,
Cole W.C., Walsh M.P.;
"Molecular composition of 4-aminopyridine-sensitive voltage-gated K(+)
channels of vascular smooth muscle.";
Circ. Res. 89:1030-1037(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Thorbecke;
The Genome Sequencing Platform;
Di Palma F., Heiman D., Young S., Gnerre S., Johnson J., Lander E.S.,
Lindblad-Toh K.;
"Genome Sequence of Oryctolagus cuniculus (European rabbit).";
Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 81-360.
STRAIN=New Zealand white; TISSUE=Kidney;
PubMed=1733291;
Desir G.V., Hamlin H.A., Puente E., Reilly R.F., Hildebrandt F.,
Igarashi P.;
"Isolation of putative voltage-gated epithelial K-channel isoforms
from rabbit kidney and LLC-PK1 cells.";
Am. J. Physiol. 262:F151-F157(1992).
[4]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=11717161; DOI=10.1161/hh2301.100803;
Kerr P.M., Clement-Chomienne O., Thorneloe K.S., Chen T.T., Ishii K.,
Sontag D.P., Walsh M.P., Cole W.C.;
"Heteromultimeric Kv1.2-Kv1.5 channels underlie 4-aminopyridine-
sensitive delayed rectifier K(+) current of rabbit vascular
myocytes.";
Circ. Res. 89:1038-1044(2001).
[5]
IDENTIFICATION IN A COMPLEX WITH KCNA4 AND FYN, INTERACTION WITH KCNA4
AND KCNA5, AND SUBCELLULAR LOCATION.
PubMed=11149959; DOI=10.1073/pnas.98.2.705;
Nitabach M.N., Llamas D.A., Araneda R.C., Intile J.L., Thompson I.J.,
Zhou Y.I., Holmes T.C.;
"A mechanism for combinatorial regulation of electrical activity:
Potassium channel subunits capable of functioning as Src homology 3-
dependent adaptors.";
Proc. Natl. Acad. Sci. U.S.A. 98:705-710(2001).
[6]
REVIEW.
PubMed=17917103; DOI=10.1007/s12035-007-8001-0;
Baranauskas G.;
"Ionic channel function in action potential generation: current
perspective.";
Mol. Neurobiol. 35:129-150(2007).
[7]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-440; SER-441
AND SER-449, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19389710; DOI=10.1074/jbc.M109.010918;
Johnson R.P., El-Yazbi A.F., Hughes M.F., Schriemer D.C., Walsh E.J.,
Walsh M.P., Cole W.C.;
"Identification and functional characterization of protein kinase A-
catalyzed phosphorylation of potassium channel Kv1.2 at serine 449.";
J. Biol. Chem. 284:16562-16574(2009).
-!- FUNCTION: Voltage-gated potassium channel that mediates
transmembrane potassium transport in excitable membranes,
primarily in the brain and the central nervous system, but also in
the cardiovascular system. Prevents aberrant action potential
firing and regulates neuronal output. Forms tetrameric potassium-
selective channels through which potassium ions pass in accordance
with their electrochemical gradient. The channel alternates
between opened and closed conformations in response to the voltage
difference across the membrane (PubMed:11717161). Can form
functional homotetrameric channels and heterotetrameric channels
that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5,
KCNA6, KCNA7, and possibly other family members as well; channel
properties depend on the type of alpha subunits that are part of
the channel (PubMed:11717161). Channel properties are modulated by
cytoplasmic beta subunits that regulate the subcellular location
of the alpha subunits and promote rapid inactivation of delayed
rectifier potassium channels (By similarity). In vivo, membranes
probably contain a mixture of heteromeric potassium channel
complexes, making it difficult to assign currents observed in
intact tissues to any particular potassium channel family member.
Homotetrameric KCNA2 forms a delayed-rectifier potassium channel
that opens in response to membrane depolarization, followed by
slow spontaneous channel closure (PubMed:11717161,
PubMed:19389710). In contrast, a heteromultimer formed by KCNA2
and KCNA4 shows rapid inactivation (By similarity). Regulates
neuronal excitability and plays a role as pacemaker in the
regulation of neuronal action potentials (By similarity). KCNA2-
containing channels play a presynaptic role and prevent
hyperexcitability and aberrant action potential firing (By
similarity). Response to toxins that are selective for KCNA2-
containing potassium channels suggests that in Purkinje cells,
dendritic subthreshold KCNA2-containing potassium channels prevent
random spontaneous calcium spikes, suppressing dendritic
hyperexcitability without hindering the generation of somatic
action potentials, and thereby play an important role in motor
coordination (By similarity). Plays a role in the induction of
long-term potentiation of neuron excitability in the CA3 layer of
the hippocampus (By similarity). May function as down-stream
effector for G protein-coupled receptors and inhibit GABAergic
inputs to basolateral amygdala neurons (By similarity). May
contribute to the regulation of neurotransmitter release, such as
gamma-aminobutyric acid (GABA) (By similarity). Contributes to the
regulation of the axonal release of the neurotransmitter dopamine
(By similarity). Reduced KCNA2 expression plays a role in the
perception of neuropathic pain after peripheral nerve injury, but
not acute pain (By similarity). Plays a role in the regulation of
the time spent in non-rapid eye movement (NREM) sleep (By
similarity). {ECO:0000250|UniProtKB:P63141,
ECO:0000250|UniProtKB:P63142, ECO:0000269|PubMed:11717161,
ECO:0000269|PubMed:19389710, ECO:0000305}.
-!- ENZYME REGULATION: Inhibited by 4-aminopyridine (4-AP)
(PubMed:11717161). Inhibited by dendrotoxin (DTX) and
charybdotoxin (CTX), but not by tetraethylammonium (TEA) (By
similarity). Inhibited by tityustoxin-K alpha (TsTX-Kalpha), a
toxin that is highly specific for KCNA2 (By similarity). Inhibited
by maurotoxin (By similarity). Inhibited by kappaM conotoxins
kappaM-RIIIJ and kappaM-RIIIK (By similarity).
{ECO:0000250|UniProtKB:P16389, ECO:0000250|UniProtKB:P63142,
ECO:0000269|PubMed:11717161}.
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-
forming alpha subunits, such as KCNA1, KCNA4, KCNA5, KCNA6 and
KCNA7. Channel activity is regulated by interaction with the beta
subunits, including KCNAB1 and KCNAB2. Identified in a complex
with KCNA1 and KCNAB2 (By similarity). Identified in a complex
with KCNA4 and FYN (PubMed:11149959). Identified in a complex with
KCNA5 and KCNAB1 (PubMed:11717160). Interacts with the beta
subunit KCNAB1 (PubMed:11717160,). Interacts with PTK2B (By
similarity). Interacts (via C-terminus) with CTTN (By similarity).
Interacts (via N-terminal cytoplasmic domain) with RHOA (GTP-bound
form); this regulates channel activity by reducing location at the
cell surface in response to CHRM1 activation (By similarity).
Interacts with DRD2 (By similarity). Interacts with SIGMAR1;
cocaine consumption leads to increased interaction (By
similarity). Interacts with ADAM22 (By similarity). Interacts with
CNTNAP2 (By similarity). Interacts (via C-terminus) with the PDZ
domains of DLG1, DLG2 and DLG4 (By similarity).
{ECO:0000250|UniProtKB:P16389, ECO:0000250|UniProtKB:P63141,
ECO:0000250|UniProtKB:P63142, ECO:0000269|PubMed:11149959,
ECO:0000269|PubMed:11717160, ECO:0000269|PubMed:11717161,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11717161,
ECO:0000269|PubMed:19389710}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P63142, ECO:0000305}. Membrane
{ECO:0000269|PubMed:11149959}. Cell projection, axon
{ECO:0000250|UniProtKB:P63142}. Cell junction, synapse
{ECO:0000269|PubMed:11149959}. Cell junction, synapse, presynaptic
cell membrane {ECO:0000250|UniProtKB:P63141}. Cell junction,
synapse, synaptosome {ECO:0000250|UniProtKB:P63141}. Endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P63142}. Cell
projection, dendrite {ECO:0000250|UniProtKB:P63141}. Cell
projection, lamellipodium membrane {ECO:0000250|UniProtKB:P63142}.
Cell junction, paranodal septate junction
{ECO:0000250|UniProtKB:P63141}. Note=KCNA2 by itself is detected
both at the endoplasmic reticulum and at the cell membrane.
Coexpression with KCNA4 or with beta subunits promotes expression
at the cell membrane. Coexpression with KCNA1 inhibits cell
surface expression. In myelinated peripheral axons, clustered in
the juxtaparadonal region and at an internodal line located along
the mesaxon and below the Schmidt-Lanterman incisures (By
similarity). {ECO:0000250|UniProtKB:P63141,
ECO:0000250|UniProtKB:P63142}.
-!- TISSUE SPECIFICITY: Detected in portal vein myocytes (at protein
level) (PubMed:11717160). Detected in portal vein
(PubMed:11717160). Brain, liver and kidney.
{ECO:0000269|PubMed:11717160}.
-!- DOMAIN: The cytoplasmic N-terminus is important for
tetramerization. Interactions between the different subunits
modulate the gating characteristics (By similarity). Besides, the
cytoplasmic N-terminal domain mediates interaction with RHOA and
thus is required for RHOA-mediated endocytosis (By similarity).
{ECO:0000250|UniProtKB:P63142}.
-!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
and is characterized by a series of positively charged amino acids
at every third position. Channel opening and closing is effected
by a conformation change that affects the position and orientation
of the voltage-sensor paddle formed by S3 and S4 within the
membrane. A transmembrane electric field that is positive inside
would push the positively charged S4 segment outwards, thereby
opening the pore, while a field that is negative inside would pull
the S4 segment inwards and close the pore. Changes in the position
and orientation of S4 are then transmitted to the activation gate
formed by the inner helix bundle via the S4-S5 linker region.
{ECO:0000250|UniProtKB:P63142}.
-!- PTM: Phosphorylated on tyrosine residues; phosphorylation
increases in response to ischemia (By similarity). Phosphorylated
on tyrosine residues by activated PTK2B/PYK2 (By similarity).
Phosphorylation on tyrosine residues suppresses ion channel
activity (By similarity). Phosphorylated on tyrosine residues in
response to CHRM1 activation; this abolishes interaction with
CTTN. This is probably due to endocytosis of the phosphorylated
channel subunits (By similarity). Phosphorylated on serine
residues in response to increased cAMP levels; phosphorylation is
apparently not catalyzed by PKA (By similarity).
{ECO:0000250|UniProtKB:P63142}.
-!- PTM: N-glycosylated, with complex, sialylated N-glycans.
{ECO:0000250|UniProtKB:P63142}.
-!- MISCELLANEOUS: The delay or D-type current observed in hippocampus
pyramidal neurons is probably mediated by potassium channels
containing KCNA2 plus KCNA1 or other family members. It is
activated at about -50 mV, i.e. below the action potential
threshold, and is characterized by slow inactivation, extremely
slow recovery from inactivation, sensitivity to dendrotoxin (DTX)
and to 4-aminopyridine (4-AP). {ECO:0000305|PubMed:17917103}.
-!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
(TC 1.A.1.2) subfamily. Kv1.2/KCNA2 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF284420; AAF91476.1; -; mRNA.
EMBL; AAGW02000935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M81351; AAD43820.1; -; mRNA.
RefSeq; NP_001076191.1; NM_001082722.1.
RefSeq; XP_008262207.1; XM_008263985.2.
RefSeq; XP_008262208.1; XM_008263986.2.
RefSeq; XP_008262210.1; XM_008263988.2.
UniGene; Ocu.2363; -.
SMR; Q09081; -.
STRING; 9986.ENSOCUP00000007687; -.
iPTMnet; Q09081; -.
Ensembl; ENSOCUT00000008904; ENSOCUP00000007687; ENSOCUG00000008908.
GeneID; 100009479; -.
KEGG; ocu:100009479; -.
CTD; 3737; -.
eggNOG; KOG1545; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOGENOM; HOG000231015; -.
HOVERGEN; HBG052230; -.
KO; K04875; -.
OMA; PEPDHEC; -.
OrthoDB; EOG091G10NU; -.
TreeFam; TF313103; -.
Proteomes; UP000001811; Chromosome 13.
Bgee; ENSOCUG00000008908; -.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0044224; C:juxtaparanode region of axon; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
GO; GO:0019228; P:neuronal action potential; ISS:UniProtKB.
GO; GO:0021633; P:optic nerve structural organization; IEA:Ensembl.
GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0045188; P:regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl.
GO; GO:0014059; P:regulation of dopamine secretion; ISS:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003972; K_chnl_volt-dep_Kv1.
InterPro; IPR004049; K_chnl_volt-dep_Kv1.2.
InterPro; IPR011333; SKP1/BTB/POZ.
InterPro; IPR003131; T1-type_BTB.
InterPro; IPR028325; VG_K_chnl.
PANTHER; PTHR11537; PTHR11537; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01509; KV12CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01496; SHAKERCHANEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Potassium;
Potassium channel; Potassium transport; Reference proteome; Synapse;
Synaptosome; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
CHAIN 1 499 Potassium voltage-gated channel subfamily
A member 2.
/FTId=PRO_0000053974.
TOPO_DOM 1 160 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 161 182 Helical; Name=Segment S1.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 183 221 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 222 243 Helical; Name=Segment S2.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 244 254 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 255 275 Helical; Name=Segment S3.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 276 289 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 290 310 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 311 325 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 326 347 Helical; Name=Segment S5.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 348 361 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 362 373 Helical; Name=Pore helix.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 374 381 {ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 382 388 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 389 417 Helical; Name=Segment S6.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 418 499 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
REGION 1 125 Tetramerization domain.
{ECO:0000250|UniProtKB:P63142}.
REGION 312 325 S4-S5 linker.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 374 379 Selectivity filter.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 497 499 PDZ-binding.
{ECO:0000250|UniProtKB:P63142}.
SITE 252 252 Important for normal, slow channel
gating. {ECO:0000250|UniProtKB:P63142}.
SITE 381 381 Important for binding with the scorpion
mesomartoxin; when the scorpion
mesomartoxin-rKv1.2/KCNA2 interaction is
modeled, this residue is close to the 'Y-
57' residue of the toxin.
{ECO:0000250|UniProtKB:P63142}.
MOD_RES 429 429 Phosphotyrosine.
{ECO:0000250|UniProtKB:P63141}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P63141}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000269|PubMed:19389710}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000269|PubMed:19389710}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000269|PubMed:19389710}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000250|UniProtKB:P63141}.
LIPID 244 244 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CONFLICT 6 6 E -> G (in Ref. 1; AAF91476).
{ECO:0000305}.
CONFLICT 93 93 Q -> L (in Ref. 3; AAD43820).
{ECO:0000305}.
CONFLICT 99 100 RR -> P (in Ref. 3; AAD43820).
{ECO:0000305}.
CONFLICT 153 153 F -> S (in Ref. 3; AAD43820).
{ECO:0000305}.
CONFLICT 175 175 I -> M (in Ref. 3; AAD43820).
{ECO:0000305}.
CONFLICT 260 260 I -> T (in Ref. 3; AAD43820).
{ECO:0000305}.
SEQUENCE 499 AA; 56765 MW; D9C5CC8E018B4494 CRC64;
MTVATEDPAD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT LAQFPETLLG
DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR PVNVPLDIFS EEIRFYELGE
EAMEMFREDE GYIKEEERPL PENEFQRQVW LLFEYPESSG PARIIAIVSV MVILISIVSF
CLETLPIFRD ENEDMHGSGM TFHTYSNSTA GYQQSTSFTD PFFIVETLCI IWFSFEFLVR
FFACPSKAGF FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR
VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE ADERDSQFPS
IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL TIALPVPVIV SNFNYFYHRE
TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA STISKSDYME IQEGVNNSNE DFREENLKTA
NCTLANTNYV NITKMLTDV


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