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P63142

- KCNA2_RAT

UniProt

P63142 - KCNA2_RAT

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Protein

Potassium voltage-gated channel subfamily A member 2

Gene

Kcna2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.1 Publication

GO - Molecular functioni

  1. delayed rectifier potassium channel activity Source: RefGenome
  2. outward rectifier potassium channel activity Source: RGD

GO - Biological processi

  1. optic nerve structural organization Source: Ensembl
  2. protein homooligomerization Source: InterPro
  3. protein oligomerization Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiREACT_199159. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily A member 2
Alternative name(s):
RAK
RBK2
RCK5
Voltage-gated potassium channel subunit Kv1.2
Gene namesi
Name:Kcna2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi2950. Kcna2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei164 – 18219Helical; Name=Segment S1Add
BLAST
Transmembranei222 – 24322Helical; Name=Segment S2Add
BLAST
Transmembranei255 – 27521Helical; Name=Segment S3Add
BLAST
Transmembranei293 – 31119Helical; Voltage-sensor; Name=Segment S4Add
BLAST
Transmembranei328 – 34720Helical; Name=Segment S5Add
BLAST
Transmembranei389 – 41123Helical; Name=Segment S6Add
BLAST

GO - Cellular componenti

  1. juxtaparanode region of axon Source: BHF-UCL
  2. voltage-gated potassium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341R → L: No effect on channel opening. 1 Publication
Mutagenesisi38 – 381N → A: Interferes with voltage-sensitive channel opening. 1 Publication
Mutagenesisi40 – 401S → A: No effect on channel opening. 1 Publication
Mutagenesisi41 – 411G → A: Loss of channel activity. 1 Publication
Mutagenesisi42 – 421L → A: No effect on channel opening. 1 Publication
Mutagenesisi43 – 431R → A: No effect on channel opening. 1 Publication
Mutagenesisi44 – 441F → A: Interferes with voltage-sensitive channel opening. 1 Publication
Mutagenesisi45 – 451E → A: Interferes with voltage-sensitive channel opening. 1 Publication
Mutagenesisi46 – 461T → D: Loss of tetramerization and channel activity. 1 Publication
Mutagenesisi46 – 461T → V or A: Interferes with voltage-sensitive channel opening. 1 Publication
Mutagenesisi47 – 471Q → A: No effect on channel opening. 1 Publication
Mutagenesisi50 – 501T → A: Interferes with voltage-sensitive channel opening. 1 Publication
Mutagenesisi70 – 701D → A: No effect on channel opening. 1 Publication
Mutagenesisi73 – 731R → A: No effect on channel opening. 1 Publication
Mutagenesisi75 – 751E → A: No effect on channel opening. 1 Publication
Mutagenesisi77 – 771F → W: Interferes with voltage-sensitive channel opening. 1 Publication
Mutagenesisi79 – 791D → N: Interferes with voltage-sensitive channel opening. 1 Publication
Mutagenesisi81 – 811N → A: No effect on channel opening. 1 Publication
Mutagenesisi82 – 821R → A: Loss of channel activity. 1 Publication
Mutagenesisi86 – 861D → A: Interferes with voltage-sensitive channel opening. 1 Publication
Mutagenesisi89 – 891L → A: No effect on channel opening. 1 Publication
Mutagenesisi90 – 901Y → A: No effect on channel opening. 1 Publication
Mutagenesisi93 – 931Q → A: Loss of channel activity. 1 Publication
Mutagenesisi97 – 971R → A: No effect on channel opening. 1 Publication
Mutagenesisi99 – 991R → A: No effect on channel opening. 1 Publication
Mutagenesisi102 – 1021V → T: Interferes with voltage-sensitive channel opening. 1 Publication
Mutagenesisi103 – 1031N → A: No effect on channel opening. 1 Publication
Mutagenesisi105 – 1051P → A: No effect on channel opening. 1 Publication
Mutagenesisi107 – 1071D → A: Strongly interferes with voltage-sensitive channel opening. 1 Publication
Mutagenesisi108 – 1081I → A: No effect on channel opening. 1 Publication
Mutagenesisi111 – 1111E → A: Interferes with voltage-sensitive channel opening. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Potassium voltage-gated channel subfamily A member 2PRO_0000053975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
Lipidationi244 – 2441S-palmitoyl cysteineSequence Analysis
Modified residuei429 – 4291PhosphotyrosineBy similarity
Modified residuei449 – 4491Phosphoserine; by PKASequence Analysis

Post-translational modificationi

Phosphorylated on tyrosine residues by activated PTK2B/PYK2; this regulates ion channel activity.1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP63142.
PRIDEiP63142.

PTM databases

PhosphoSiteiP63142.

Expressioni

Gene expression databases

GenevestigatoriP63142.

Interactioni

Subunit structurei

Heterotetramer of potassium channel proteins. Binds PDZ domains of DLG1, DLG2 and DLG4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DLG4P783522EBI-631446,EBI-80389From a different organism.

Protein-protein interaction databases

BioGridi247501. 5 interactions.
IntActiP63142. 1 interaction.
STRINGi10116.ENSRNOP00000042653.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 396Combined sources
Beta strandi42 – 476Combined sources
Helixi48 – 525Combined sources
Turni58 – 603Combined sources
Helixi62 – 665Combined sources
Turni71 – 744Combined sources
Beta strandi75 – 784Combined sources
Turni82 – 843Combined sources
Helixi85 – 939Combined sources
Helixi106 – 11611Combined sources
Helixi120 – 13011Combined sources
Turni143 – 1453Combined sources
Helixi146 – 1494Combined sources
Turni150 – 1545Combined sources
Beta strandi156 – 1583Combined sources
Helixi160 – 18223Combined sources
Helixi186 – 1894Combined sources
Beta strandi190 – 1923Combined sources
Turni193 – 1964Combined sources
Helixi202 – 2109Combined sources
Helixi236 – 2427Combined sources
Beta strandi243 – 2453Combined sources
Turni249 – 2524Combined sources
Helixi254 – 2607Combined sources
Turni261 – 2633Combined sources
Helixi264 – 2674Combined sources
Helixi268 – 2703Combined sources
Beta strandi273 – 2786Combined sources
Beta strandi280 – 2834Combined sources
Turni284 – 2863Combined sources
Turni291 – 2944Combined sources
Helixi295 – 2984Combined sources
Helixi301 – 3099Combined sources
Helixi312 – 32312Combined sources
Helixi325 – 35127Combined sources
Helixi361 – 37212Combined sources
Beta strandi378 – 3803Combined sources
Helixi385 – 40319Combined sources
Helixi406 – 41813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DSXX-ray1.60A/B/C/D/E/F/G/H33-119[»]
1QDVX-ray1.60A/B/C/D33-131[»]
1QDWX-ray2.10A/B/C/D/E/F/G/H33-119[»]
2A79X-ray2.90B1-499[»]
2R9RX-ray2.40B/H1-499[»]
3LNMX-ray2.90B/D1-266[»]
B/D303-499[»]
3LUTX-ray2.90B1-499[»]
4JTAX-ray2.50B/Q1-266[»]
B/Q304-499[»]
4JTCX-ray2.56B/H1-266[»]
B/H304-499[»]
4JTDX-ray2.54B/H1-266[»]
B/H304-499[»]
ProteinModelPortaliP63142.
SMRiP63142. Positions 3-421.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63142.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi374 – 3796Selectivity filter
Motifi497 – 4993PDZ-binding

Domaini

The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP63142.
KOiK04875.
OMAiMTFHTYS.
OrthoDBiEOG7M0NRD.
PhylomeDBiP63142.
TreeFamiTF313103.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003972. K_chnl_volt-dep_Kv1.
IPR004049. K_chnl_volt-dep_Kv1.2.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01509. KV12CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

P63142-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVATGDPVD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT
60 70 80 90 100
LAQFPETLLG DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR
110 120 130 140 150
PVNVPLDIFS EEIRFYELGE EAMEMFREDE GYIKEEERPL PENEFQRQVW
160 170 180 190 200
LLFEYPESSG PARIIAIVSV MVILISIVSF CLETLPIFRD ENEDMHGGGV
210 220 230 240 250
TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR FFACPSKAGF
260 270 280 290 300
FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR
310 320 330 340 350
VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE
360 370 380 390 400
ADERDSQFPS IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL
410 420 430 440 450
TIALPVPVIV SNFNYFYHRE TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA
460 470 480 490
STISKSDYME IQEGVNNSNE DFREENLKTA NCTLANTNYV NITKMLTDV
Length:499
Mass (Da):56,701
Last modified:September 13, 2004 - v1
Checksum:iA8FEA6F3F59AF42A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti411 – 4111S → F in AAA19867. (PubMed:1715584)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04731 mRNA. Translation: AAA40819.1.
X16003 mRNA. Translation: CAA34134.1.
M74449 mRNA. Translation: AAA19867.1.
PIRiA33814.
RefSeqiNP_037102.1. NM_012970.3.
XP_006233194.1. XM_006233132.2.
XP_006233195.1. XM_006233133.2.
XP_006233196.1. XM_006233134.2.
XP_006233197.1. XM_006233135.2.
XP_008759593.1. XM_008761371.1.
UniGeneiRn.10298.
Rn.40779.

Genome annotation databases

EnsembliENSRNOT00000050149; ENSRNOP00000042653; ENSRNOG00000018285.
GeneIDi25468.
KEGGirno:25468.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04731 mRNA. Translation: AAA40819.1 .
X16003 mRNA. Translation: CAA34134.1 .
M74449 mRNA. Translation: AAA19867.1 .
PIRi A33814.
RefSeqi NP_037102.1. NM_012970.3.
XP_006233194.1. XM_006233132.2.
XP_006233195.1. XM_006233133.2.
XP_006233196.1. XM_006233134.2.
XP_006233197.1. XM_006233135.2.
XP_008759593.1. XM_008761371.1.
UniGenei Rn.10298.
Rn.40779.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DSX X-ray 1.60 A/B/C/D/E/F/G/H 33-119 [» ]
1QDV X-ray 1.60 A/B/C/D 33-131 [» ]
1QDW X-ray 2.10 A/B/C/D/E/F/G/H 33-119 [» ]
2A79 X-ray 2.90 B 1-499 [» ]
2R9R X-ray 2.40 B/H 1-499 [» ]
3LNM X-ray 2.90 B/D 1-266 [» ]
B/D 303-499 [» ]
3LUT X-ray 2.90 B 1-499 [» ]
4JTA X-ray 2.50 B/Q 1-266 [» ]
B/Q 304-499 [» ]
4JTC X-ray 2.56 B/H 1-266 [» ]
B/H 304-499 [» ]
4JTD X-ray 2.54 B/H 1-266 [» ]
B/H 304-499 [» ]
ProteinModelPortali P63142.
SMRi P63142. Positions 3-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247501. 5 interactions.
IntActi P63142. 1 interaction.
STRINGi 10116.ENSRNOP00000042653.

Chemistry

GuidetoPHARMACOLOGYi 539.

PTM databases

PhosphoSitei P63142.

Proteomic databases

PaxDbi P63142.
PRIDEi P63142.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000050149 ; ENSRNOP00000042653 ; ENSRNOG00000018285 .
GeneIDi 25468.
KEGGi rno:25468.

Organism-specific databases

CTDi 3737.
RGDi 2950. Kcna2.

Phylogenomic databases

eggNOGi COG1226.
GeneTreei ENSGT00760000118846.
HOGENOMi HOG000231015.
HOVERGENi HBG052230.
InParanoidi P63142.
KOi K04875.
OMAi MTFHTYS.
OrthoDBi EOG7M0NRD.
PhylomeDBi P63142.
TreeFami TF313103.

Enzyme and pathway databases

Reactomei REACT_199159. Voltage gated Potassium channels.

Miscellaneous databases

EvolutionaryTracei P63142.
NextBioi 289787.
PROi P63142.

Gene expression databases

Genevestigatori P63142.

Family and domain databases

Gene3Di 1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProi IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003972. K_chnl_volt-dep_Kv1.
IPR004049. K_chnl_volt-dep_Kv1.2.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view ]
PANTHERi PTHR11537. PTHR11537. 1 hit.
Pfami PF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view ]
PRINTSi PR00169. KCHANNEL.
PR01509. KV12CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTi SM00225. BTB. 1 hit.
[Graphical view ]
SUPFAMi SSF54695. SSF54695. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Isolation of a cDNA clone coding for a putative second potassium channel indicates the existence of a gene family."
    McKinnon D.
    J. Biol. Chem. 264:8230-8236(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain."
    Stuehmer W., Ruppersberg J.P., Schroerter K.H., Sakmann B., Stocker M., Giese K.P., Perschke A., Baumann A., Pongs O.
    EMBO J. 8:3235-3244(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. Ludwig J.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart atrium.
  5. "Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases."
    Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M.
    Nature 378:85-88(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLG1; DLG2 AND DLG4.
  6. "Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions."
    Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., Plowman G.D., Rudy B., Schlessinger J.
    Nature 376:737-745(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
    Tissue: Brain.
  7. "The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel."
    Minor D.L. Jr., Lin Y.-F., Mobley B.C., Avelar A., Jan Y.N., Jan L.Y., Berger J.M.
    Cell 102:657-670(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 33-119, TETRAMERIZATION, MUTAGENESIS OF ARG-34; ASN-38; SER-40; GLY-41; LEU-42; ARG-43; PHE-44; GLU-45; THR-46; GLN-47; THR-50; ASP-70; ARG-73; GLU-75; PHE-77; ASP-79; ASN-81; ARG-82; ASP-86; LEU-89; TYR-90; GLN-93; ARG-97; ARG-99; VAL-102; ASN-103; PRO-105; ASP-107; ILE-108 AND GLU-111.
  8. "Crystal structure of a mammalian voltage-dependent Shaker family K+ channel."
    Long S.B., Campbell E.B., Mackinnon R.
    Science 309:897-903(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH KCNAB2, SUBUNIT.

Entry informationi

Entry nameiKCNA2_RAT
AccessioniPrimary (citable) accession number: P63142
Secondary accession number(s): P15386, Q02010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: November 26, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3