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P63142 (KCNA2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel subfamily A member 2
Alternative name(s):
RAK
RBK2
RCK5
Voltage-gated potassium channel subunit Kv1.2
Gene names
Name:Kcna2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

Heterotetramer of potassium channel proteins. Binds PDZ domains of DLG1, DLG2 and DLG4. Ref.7 Ref.8

Subcellular location

Membrane; Multi-pass membrane protein.

Domain

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.

Post-translational modification

Phosphorylated on tyrosine residues by activated PTK2B/PYK2; this regulates ion channel activity. Ref.6

Sequence similarities

Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.2/KCNA2 sub-subfamily. [View classification]

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DLG4P783522EBI-631446,EBI-80389From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Potassium voltage-gated channel subfamily A member 2
PRO_0000053975

Regions

Transmembrane164 – 18219Helical; Name=Segment S1
Transmembrane222 – 24322Helical; Name=Segment S2
Transmembrane255 – 27521Helical; Name=Segment S3
Transmembrane293 – 31119Helical; Voltage-sensor; Name=Segment S4
Transmembrane328 – 34720Helical; Name=Segment S5
Transmembrane389 – 41123Helical; Name=Segment S6
Motif374 – 3796Selectivity filter
Motif497 – 4993PDZ-binding

Amino acid modifications

Modified residue4291Phosphotyrosine By similarity
Modified residue4491Phosphoserine; by PKA Potential
Lipidation2441S-palmitoyl cysteine Potential
Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis341R → L: No effect on channel opening. Ref.7
Mutagenesis381N → A: Interferes with voltage-sensitive channel opening. Ref.7
Mutagenesis401S → A: No effect on channel opening. Ref.7
Mutagenesis411G → A: Loss of channel activity. Ref.7
Mutagenesis421L → A: No effect on channel opening. Ref.7
Mutagenesis431R → A: No effect on channel opening. Ref.7
Mutagenesis441F → A: Interferes with voltage-sensitive channel opening. Ref.7
Mutagenesis451E → A: Interferes with voltage-sensitive channel opening. Ref.7
Mutagenesis461T → D: Loss of tetramerization and channel activity. Ref.7
Mutagenesis461T → V or A: Interferes with voltage-sensitive channel opening. Ref.7
Mutagenesis471Q → A: No effect on channel opening. Ref.7
Mutagenesis501T → A: Interferes with voltage-sensitive channel opening. Ref.7
Mutagenesis701D → A: No effect on channel opening. Ref.7
Mutagenesis731R → A: No effect on channel opening. Ref.7
Mutagenesis751E → A: No effect on channel opening. Ref.7
Mutagenesis771F → W: Interferes with voltage-sensitive channel opening. Ref.7
Mutagenesis791D → N: Interferes with voltage-sensitive channel opening. Ref.7
Mutagenesis811N → A: No effect on channel opening. Ref.7
Mutagenesis821R → A: Loss of channel activity. Ref.7
Mutagenesis861D → A: Interferes with voltage-sensitive channel opening. Ref.7
Mutagenesis891L → A: No effect on channel opening. Ref.7
Mutagenesis901Y → A: No effect on channel opening. Ref.7
Mutagenesis931Q → A: Loss of channel activity. Ref.7
Mutagenesis971R → A: No effect on channel opening. Ref.7
Mutagenesis991R → A: No effect on channel opening. Ref.7
Mutagenesis1021V → T: Interferes with voltage-sensitive channel opening. Ref.7
Mutagenesis1031N → A: No effect on channel opening. Ref.7
Mutagenesis1051P → A: No effect on channel opening. Ref.7
Mutagenesis1071D → A: Strongly interferes with voltage-sensitive channel opening. Ref.7
Mutagenesis1081I → A: No effect on channel opening. Ref.7
Mutagenesis1111E → A: Interferes with voltage-sensitive channel opening. Ref.7
Sequence conflict4111S → F in AAA19867. Ref.4

Secondary structure

............................................................ 499
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63142 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: A8FEA6F3F59AF42A

FASTA49956,701
        10         20         30         40         50         60 
MTVATGDPVD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT LAQFPETLLG 

        70         80         90        100        110        120 
DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR PVNVPLDIFS EEIRFYELGE 

       130        140        150        160        170        180 
EAMEMFREDE GYIKEEERPL PENEFQRQVW LLFEYPESSG PARIIAIVSV MVILISIVSF 

       190        200        210        220        230        240 
CLETLPIFRD ENEDMHGGGV TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR 

       250        260        270        280        290        300 
FFACPSKAGF FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR 

       310        320        330        340        350        360 
VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE ADERDSQFPS 

       370        380        390        400        410        420 
IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL TIALPVPVIV SNFNYFYHRE 

       430        440        450        460        470        480 
TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA STISKSDYME IQEGVNNSNE DFREENLKTA 

       490 
NCTLANTNYV NITKMLTDV 

« Hide

References

[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]"Cloning and expression of a rat cardiac delayed rectifier potassium channel."
Paulmichl M., Nasmith P., Herllmiss R., Reed K., Boyle W.A., Nerbonne J.M., Peralta E.G., Clapham D.E.
Proc. Natl. Acad. Sci. U.S.A. 88:7892-7895(1991) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04731 mRNA. Translation: AAA40819.1.
X16003 mRNA. Translation: CAA34134.1.
M74449 mRNA. Translation: AAA19867.1.
PIRA33814.
RefSeqNP_037102.1. NM_012970.3.
XP_006233194.1. XM_006233132.1.
XP_006233195.1. XM_006233133.1.
XP_006233196.1. XM_006233134.1.
XP_006233197.1. XM_006233135.1.
UniGeneRn.10298.
Rn.40779.

3D structure databases

PDBe
RCSB-PDB
PDBj
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/Q1-499[»]
4JTCX-ray2.56B/H1-266[»]
B/H304-499[»]
4JTDX-ray2.54B/H1-266[»]
B/H304-499[»]
ProteinModelPortalP63142.
SMRP63142. Positions 3-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247501. 5 interactions.
IntActP63142. 1 interaction.
STRING10116.ENSRNOP00000042653.

Chemistry

GuidetoPHARMACOLOGY539.

PTM databases

PhosphoSiteP63142.

Proteomic databases

PaxDbP63142.
PRIDEP63142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000050149; ENSRNOP00000042653; ENSRNOG00000018285.
GeneID25468.
KEGGrno:25468.

Organism-specific databases

CTD3737.
RGD2950. Kcna2.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00740000115256.
HOGENOMHOG000231015.
HOVERGENHBG052230.
InParanoidP63142.
KOK04875.
OMAMTFHTYS.
OrthoDBEOG7M0NRD.
PhylomeDBP63142.
TreeFamTF313103.

Gene expression databases

GenevestigatorP63142.

Family and domain databases

Gene3D1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProIPR000210. 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]
PANTHERPTHR11537. PTHR11537. 1 hit.
PfamPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
PR01509. KV12CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP63142.
NextBio289787.
PROP63142.

Entry information

Entry nameKCNA2_RAT
AccessionPrimary (citable) accession number: P63142
Secondary accession number(s): P15386, Q02010
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references