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Potassium channel AKT1

 AKT1_ARATH              Reviewed;         857 AA.
Q38998; B9DI19; Q0WTF6; Q38797; Q84MA7;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
28-FEB-2018, entry version 150.
RecName: Full=Potassium channel AKT1;
Name=AKT1; OrderedLocusNames=At2g26650; ORFNames=F18A8.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Landsberg erecta;
PubMed=1585180; DOI=10.1126/science.1585180;
Sentenac H., Bonneaud N., Minet M., Lacroute F., Salmon J.-M.,
Gaymard F., Grignon C.;
"Cloning and expression in yeast of a plant potassium ion transport
system.";
Science 256:663-665(1992).
[2]
SEQUENCE REVISION.
Sentenac H.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Landsberg erecta;
PubMed=8555458; DOI=10.1007/BF00014968;
Basset M., Conejero G., Lepetit M., Fourcroy P., Sentenac H.;
"Organization and expression of the gene coding for the potassium
transport system AKT1 of Arabidopsis thaliana.";
Plant Mol. Biol. 29:947-958(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH20386.1};
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-857.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-857.
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[9]
TISSUE SPECIFICITY.
PubMed=8820606; DOI=10.1046/j.1365-313X.1996.09020195.x;
Lagarde D., Basset M., Lepetit M., Conejero G., Gaymard F., Astruc S.,
Grignon C.;
"Tissue-specific expression of Arabidopsis AKT1 gene is consistent
with a role in K+ nutrition.";
Plant J. 9:195-203(1996).
[10]
SUBUNIT.
PubMed=9218788; DOI=10.1093/emboj/16.12.3455;
Daram P., Urbach S., Gaymard F., Sentenac H., Cherel I.;
"Tetramerization of the AKT1 plant potassium channel involves its C-
terminal cytoplasmic domain.";
EMBO J. 16:3455-3463(1997).
[11]
FUNCTION.
PubMed=9572739; DOI=10.1126/science.280.5365.918;
Hirsch R.E., Lewis B.D., Spalding E.P., Sussman M.R.;
"A role for the AKT1 potassium channel in plant nutrition.";
Science 280:918-921(1998).
[12]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11500563; DOI=10.1104/pp.126.4.1646;
Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A.,
Guerinot M.L.;
"Phylogenetic relationships within cation transporter families of
Arabidopsis.";
Plant Physiol. 126:1646-1667(2001).
[13]
FUNCTION, INTERACTION WITH AKT2 AND KAT3, AND INDUCTION.
PubMed=12678562; DOI=10.1023/A:1022597102282;
Pilot G., Gaymard F., Mouline K., Cherel I., Sentenac H.;
"Regulated expression of Arabidopsis shaker K(+) channel genes
involved in K(+) uptake and distribution in the plant.";
Plant Mol. Biol. 51:773-787(2003).
[14]
FUNCTION, INTERACTION WITH CIPK23, PHOSPHORYLATION, AND SUBCELLULAR
LOCATION.
PubMed=16814720; DOI=10.1016/j.cell.2006.06.011;
Xu J., Li H.-D., Chen L.-Q., Wang Y., Liu L.-L., He L., Wu W.-H.;
"A protein kinase, interacting with two calcineurin B-like proteins,
regulates K+ transporter AKT1 in Arabidopsis.";
Cell 125:1347-1360(2006).
[15]
FUNCTION, INTERACTION WITH CIPK23, AND PHOSPHORYLATION.
PubMed=16895985; DOI=10.1073/pnas.0605129103;
Li L., Kim B.-G., Cheong Y.H., Pandey G.K., Luan S.;
"A Ca(2)+ signaling pathway regulates a K(+) channel for low-K
response in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 103:12625-12630(2006).
[16]
FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH AIP1; CIPK6; CIPK16
AND CIPK23.
PubMed=17898163; DOI=10.1073/pnas.0707912104;
Lee S.-C., Lan W.-Z., Kim B.-G., Li L., Cheong Y.H., Pandey G.K.,
Lu G., Buchanan B.B., Luan S.;
"A protein phosphorylation/dephosphorylation network regulates a plant
potassium channel.";
Proc. Natl. Acad. Sci. U.S.A. 104:15959-15964(2007).
[17]
FUNCTION.
PubMed=20413648; DOI=10.1104/pp.110.154369;
Pyo Y.J., Gierth M., Schroeder J.I., Cho M.H.;
"High-affinity K(+) transport in Arabidopsis: AtHAK5 and AKT1 are
vital for seedling establishment and postgermination growth under low-
potassium conditions.";
Plant Physiol. 153:863-875(2010).
[18]
INTERACTION WITH CBL10.
PubMed=23331977; DOI=10.1111/tpj.12123;
Ren X.L., Qi G.N., Feng H.Q., Zhao S., Zhao S.S., Wang Y., Wu W.H.;
"Calcineurin B-like protein CBL10 directly interacts with AKT1 and
modulates K+ homeostasis in Arabidopsis.";
Plant J. 74:258-266(2013).
[19]
CRYSTALLIZATION OF THE ANKYRIN-REPEAT DOMAIN.
PubMed=24699751; DOI=10.1107/S2053230X14005093;
Chaves-Sanjuan A., Sanchez-Barrena M.J., Gonzalez-Rubio J.M.,
Albert A.;
"Preliminary crystallographic analysis of the ankyrin-repeat domain of
Arabidopsis thaliana AKT1: identification of the domain boundaries for
protein crystallization.";
Acta Crystallogr. F Struct. Biol. Commun. 70:509-512(2014).
[20]
X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 518-702.
Chaves-Sanjuan A., Gonzalez-Rubio J.M., Sanchez-Barrena M.J.,
Albert A.;
"Structure of the Ankyrin Domain of Akt1.";
Submitted (JUL-2015) to the PDB data bank.
-!- FUNCTION: Highly selective inward-rectifying potassium channel
that mediate potassium uptake by plant roots in response to low
K(+) conditions, by a calcium-, CBL-, and CIPK-dependent pathway.
Positively regulated by phosphorylation by CIPK23. Negatively
regulated by a kinase-independent regulatory mechanism involving a
competing direct binding of CBL10. Involved in the stomatal
regulation by monitoring the turgor pressure in guard cells.
Assuming opened or closed conformations in response to the voltage
difference across the membrane, the channel is activated by
hyperpolarization. May interact with the cytoskeleton or with
regulatory proteins (PubMed:12678562, PubMed:16814720,
PubMed:16895985, PubMed:17898163, PubMed:9572739). Is essential
with POT5/HAK5 for high-affinity potassium uptake in roots during
seedling establishment and postgermination growth under low
potassium conditions (PubMed:20413648).
{ECO:0000269|PubMed:12678562, ECO:0000269|PubMed:16814720,
ECO:0000269|PubMed:16895985, ECO:0000269|PubMed:17898163,
ECO:0000269|PubMed:20413648, ECO:0000269|PubMed:9572739}.
-!- SUBUNIT: The potassium channel is probably composed of a homo- or
heterotetrameric complex of pore-forming subunits. Possible
heteromultimer with AKT2 or KAT3. Part of a K(+)-channel calcium-
sensing kinase/phosphatase complex composed by a calcium sensor
CBL (CBL1, CBL2, CBL3 or CBL9), a kinase CIPK (CIPK6, CIPK16 or
CIPK23), a phosphatase PP2C (AIP1) and a K(+)-channel (AKT1).
Interacts directly with AIP1, CBL10, CIPK6, CIPK16 and CIPK23.
{ECO:0000269|PubMed:12678562, ECO:0000269|PubMed:16814720,
ECO:0000269|PubMed:16895985, ECO:0000269|PubMed:17898163,
ECO:0000269|PubMed:23331977, ECO:0000269|PubMed:9218788}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-974289, EBI-974289;
Q38898:AKT2; NbExp=3; IntAct=EBI-974289, EBI-1552774;
Q93VD3:CIPK23; NbExp=6; IntAct=EBI-974289, EBI-974277;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16814720};
Multi-pass membrane protein {ECO:0000269|PubMed:16814720}.
-!- TISSUE SPECIFICITY: Preferentially expressed in the peripheral
cell layers of root mature including root cortex and root hairs.
Detected also, at a lower level, in the mesophyll of the leaves
and at restricted sites corresponding to hydathodes and guard
cells. {ECO:0000269|PubMed:8555458, ECO:0000269|PubMed:8820606}.
-!- INDUCTION: In roots, strongly reduced after 2,4-
dichlorophenoxyacetic acid (2,4-D) treatment and weakly reduced
after benzyladenine (BA) treatment. In shoots, strongly reduced
after abscisic acid (ABA) treatment and induced after
benzyladenine (BA) treatment. {ECO:0000269|PubMed:12678562}.
-!- DOMAIN: The segment S4 is probably the voltage-sensor and is
characterized by a series of positively charged amino acids. The
pore-forming region H5 is enclosed by the transmembrane segments
S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD
signature motif which seems to be involved in potassium
selectivity.
-!- DOMAIN: The KHA domain (rich in hydrophobic and acidic residues)
present in the C-terminal part is likely to be important for
tetramerization.
-!- PTM: Phosphorylated by CIPK proteins CIPK6, CIPK16 and CIPK23. The
activation by phosphorylation is induced by low K(+) conditions
and stimulates K(+) uptake and relocation. Dephosphorylation by
AIP1 repressed the transport activity.
{ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:16895985,
ECO:0000269|PubMed:17898163}.
-!- SIMILARITY: Belongs to the potassium channel family. Plant (TC
1.A.1.4) subfamily. {ECO:0000305}.
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EMBL; X62907; CAA44693.1; -; mRNA.
EMBL; U06745; AAA96810.1; -; Genomic_DNA.
EMBL; AC003105; AAB95299.1; -; Genomic_DNA.
EMBL; CP002685; AEC07870.1; -; Genomic_DNA.
EMBL; AK317729; BAH20386.1; -; mRNA.
EMBL; AK227601; BAE99592.1; -; mRNA.
EMBL; BT006442; AAP21250.1; -; mRNA.
PIR; S23606; S23606.
PIR; S62694; S62694.
RefSeq; NP_001324538.1; NM_001336078.1.
RefSeq; NP_180233.1; NM_128222.6.
UniGene; At.48521; -.
UniGene; At.68413; -.
PDB; 5AAR; X-ray; 1.87 A; A=518-702.
PDBsum; 5AAR; -.
ProteinModelPortal; Q38998; -.
SMR; Q38998; -.
BioGrid; 2558; 16.
DIP; DIP-36762N; -.
IntAct; Q38998; 7.
STRING; 3702.AT2G26650.1; -.
TCDB; 1.A.1.4.1; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q38998; -.
PaxDb; Q38998; -.
EnsemblPlants; AT2G26650.1; AT2G26650.1; AT2G26650.
GeneID; 817206; -.
Gramene; AT2G26650.1; AT2G26650.1; AT2G26650.
KEGG; ath:AT2G26650; -.
Araport; AT2G26650; -.
TAIR; locus:2043839; AT2G26650.
eggNOG; KOG0498; Eukaryota.
eggNOG; ENOG410XPSE; LUCA.
HOGENOM; HOG000238230; -.
InParanoid; Q38998; -.
KO; K21867; -.
OMA; TGLYACI; -.
OrthoDB; EOG093601WX; -.
PhylomeDB; Q38998; -.
BioCyc; ARA:AT2G26550-MONOMER; -.
BioCyc; MetaCyc:MONOMER-14552; -.
PRO; PR:Q38998; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q38998; baseline and differential.
Genevisible; Q38998; AT.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:TAIR.
GO; GO:0010107; P:potassium ion import; IDA:TAIR.
GO; GO:0006813; P:potassium ion transport; IMP:TAIR.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
GO; GO:0090333; P:regulation of stomatal closure; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
GO; GO:0048767; P:root hair elongation; IMP:TAIR.
CDD; cd00204; ANK; 1.
CDD; cd00038; CAP_ED; 1.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
InterPro; IPR021789; KHA_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
Pfam; PF12796; Ank_2; 2.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF11834; KHA; 1.
PRINTS; PR01415; ANKYRIN.
PRINTS; PR01463; EAGCHANLFMLY.
SMART; SM00248; ANK; 5.
SMART; SM00100; cNMP; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
PROSITE; PS50042; CNMP_BINDING_3; 1.
PROSITE; PS51490; KHA; 1.
1: Evidence at protein level;
3D-structure; ANK repeat; Cell membrane; Complete proteome;
Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
Potassium channel; Potassium transport; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 857 Potassium channel AKT1.
/FTId=PRO_0000054121.
TOPO_DOM 1 61 Cytoplasmic. {ECO:0000255}.
TRANSMEM 62 82 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 83 90 Extracellular. {ECO:0000255}.
TRANSMEM 91 111 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 112 134 Cytoplasmic. {ECO:0000255}.
TRANSMEM 135 155 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 156 158 Extracellular. {ECO:0000255}.
TRANSMEM 159 179 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 180 193 Cytoplasmic. {ECO:0000255}.
TRANSMEM 194 214 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 215 241 Extracellular. {ECO:0000255}.
INTRAMEM 242 261 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 262 265 Extracellular. {ECO:0000255}.
TRANSMEM 266 286 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 287 857 Cytoplasmic. {ECO:0000255}.
REPEAT 515 546 ANK 1. {ECO:0000255}.
REPEAT 550 579 ANK 2. {ECO:0000255}.
REPEAT 583 612 ANK 3. {ECO:0000255}.
REPEAT 614 643 ANK 4. {ECO:0000255}.
REPEAT 647 676 ANK 5. {ECO:0000255}.
REPEAT 680 709 ANK 6. {ECO:0000255}.
DOMAIN 790 857 KHA. {ECO:0000255|PROSITE-
ProRule:PRU00823}.
NP_BIND 372 493 cNMP. {ECO:0000255|PROSITE-
ProRule:PRU00060}.
HELIX 522 527 {ECO:0000244|PDB:5AAR}.
HELIX 531 539 {ECO:0000244|PDB:5AAR}.
HELIX 554 561 {ECO:0000244|PDB:5AAR}.
HELIX 564 572 {ECO:0000244|PDB:5AAR}.
HELIX 587 593 {ECO:0000244|PDB:5AAR}.
HELIX 597 605 {ECO:0000244|PDB:5AAR}.
HELIX 610 612 {ECO:0000244|PDB:5AAR}.
HELIX 615 624 {ECO:0000244|PDB:5AAR}.
HELIX 628 636 {ECO:0000244|PDB:5AAR}.
HELIX 651 657 {ECO:0000244|PDB:5AAR}.
HELIX 661 669 {ECO:0000244|PDB:5AAR}.
HELIX 684 690 {ECO:0000244|PDB:5AAR}.
HELIX 694 701 {ECO:0000244|PDB:5AAR}.
SEQUENCE 857 AA; 96990 MW; 28E1622BA3505F4C CRC64;
MRGGALLCGQ VQDEIEQLSR ESSHFSLSTG ILPSLGARSN RRVKLRRFVV SPYDHKYRIW
EAFLVVLVVY TAWVSPFEFG FLRKPRPPLS ITDNIVNAFF AIDIIMTFFV GYLDKSTYLI
VDDRKQIAFK YLRSWFLLDL VSTIPSEAAM RISSQSYGLF NMLRLWRLRR VGALFARLEK
DRNFNYFWVR CAKLVCVTLF AVHCAACFYY LIAARNSNPA KTWIGANVAN FLEESLWMRY
VTSMYWSITT LTTVGYGDLH PVNTKEMIFD IFYMLFNLGL TAYLIGNMTN LVVHGTSRTR
NFRDTIQAAS NFAHRNHLPP RLQDQMLAHL CLKYRTDSEG LQQQETLDAL PKAIRSSISH
FLFYSLMDKV YLFRGVSNDL LFQLVSEMKA EYFPPKEDVI LQNEAPTDFY ILVNGTADLV
DVDTGTESIV REVKAGDIIG EIGVLCYRPQ LFTVRTKRLC QLLRMNRTTF LNIIQANVGD
GTIIMNNLLQ HLKEMNDPVM TNVLLEIENM LARGKMDLPL NLCFAAIRED DLLLHQLLKR
GLDPNESDNN GRTPLHIAAS KGTLNCVLLL LEYHADPNCR DAEGSVPLWE AMVEGHEKVV
KVLLEHGSTI DAGDVGHFAC TAAEQGNLKL LKEIVLHGGD VTRPRATGTS ALHTAVCEEN
IEMVKYLLEQ GADVNKQDMH GWTPRDLAEQ QGHEDIKALF REKLHERRVH IETSSSVPIL
KTGIRFLGRF TSEPNIRPAS REVSFRIRET RARRKTNNFD NSLFGILANQ SVPKNGLATV
DEGRTGNPVR VTISCAEKDD IAGKLVLLPG SFKELLELGS NKFGIVATKV MNKDNNAEID
DVDVIRDGDH LIFATDS


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Y062354 Anti-Potassium Channel Kv<_SUB>1.6 (Voltage-gated, Delayed-Rectifier Potassium Channel; RCK2; KV2) produced in rabbit Antibody 100ul
18-003-43175 Potassium channel subfamily K member 5 - Acid-sensitive potassium channel protein TASK-2; TWIK-related acid-sensitive K(+) channel 2 Polyclonal 0.05 mg Aff Pur
Y062380 Anti-Potassium Channel KCa<_SUB>1.1, (BKCa<_SUB>) (1184-1200)(Large-conductance Ca2+<_SUP>-activated Potassium Channel) produced in rabbit Antibody 100ul
18-003-42631 Cyclic GMP gated potassium channel - Potassium voltage-gated channel. shaker-related subfamily. member 10 Polyclonal 0.1 mg Protein A
18-003-42634 Kv channel-interacting protein 1 - KChIP1; A-type potassium channel modulatory protein 1; Potassium channel-interacting protein 1; Vesicle APC-binding protein Polyclonal 0.1 mg Protein A
28-294 The M channel is a slowly activating and deactivating potassium channel that plays a critical role in the regulation of neuronal excitability. The M channel is formed by the association of the protein 0.05 mg
28-295 The M channel is a slowly activating and deactivating potassium channel that plays a critical role in the regulation of neuronal excitability. The M channel is formed by the association of the protein 0.1 mg


 

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