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P63141 (KCNA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 99. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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):
MK2
Voltage-gated potassium channel subunit Kv1.2
Gene names
Name:Kcna2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Regulates neuronal excitability and is involved in non-rapid eye movement (NREM) sleep.

Subunit structure

Heterotetramer of potassium channel proteins. Binds PDZ domains of DLG1, DLG2 and DLG4 By similarity.

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 By similarity.

Disruption phenotype

Death by P28 due to generalized seizures. Pups display less non-rapid eye movement (NREM) sleep and significantly more waking periods. Mice appear healthy and develop normally during the first 2 weeks, but die suddenly between around P12 and P28 due to an episode of generalized seizure, followed by full tonic extension, which in mice often results in fatal apne. At P17 seizures are either absent or very rare and abnormal electroencephalograph activity is only present during the seizure. P17 pups have significantly less non-rapid NREM sleep (-23%) and significantly more waking (+21%) than wild-type siblings with no change in rapid eye movement (REM) sleep time. The decrease in NREM sleep is due to an increase in the number of waking episodes, with no change in number or duration of sleep episodes. Ref.4

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Potassium voltage-gated channel subfamily A member 2
PRO_0000053973

Regions

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

Amino acid modifications

Modified residue4211Phosphothreonine Ref.6
Modified residue4291Phosphotyrosine Ref.5
Modified residue4331Phosphothreonine Ref.6
Modified residue4491Phosphoserine; by PKA Potential
Lipidation2441S-palmitoyl cysteine Potential
Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict331E → G in BAC31877. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P63141 [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

« Hide 'large scale' references
[1]"A family of three mouse potassium channel genes with intronless coding regions."
Chandy K.G., Williams C.B., Spencer R.H., Aguilar B.A., Ghanshani S., Tempel B.L., Gutman G.A.
Science 247:973-975(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Retina.
[3]"Expression of voltage-gated K+ channels in insulin-producing cells. Analysis by polymerase chain reaction."
Betsholtz C., Baumann A., Kenna S., Ashcroft F.M., Ashcroft S.J.H., Berggren P.-O., Grupe A., Pongs O., Rorsman P., Sandblom J., Welsh M.
FEBS Lett. 263:121-126(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-394.
[4]"Sleep in Kcna2 knockout mice."
Douglas C.L., Vyazovskiy V., Southard T., Chiu S.-Y., Messing A., Tononi G., Cirelli C.
BMC Biol. 5:42-42(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[5]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-429, MASS SPECTROMETRY.
Tissue: Brain.
[6]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-421 AND THR-433, MASS SPECTROMETRY.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M30440 Genomic DNA. Translation: AAA39713.1.
AK044342 mRNA. Translation: BAC31877.1.
IPIIPI00129774.
PIRI84204. B40090.
RefSeqNP_032443.3. NM_008417.5.
UniGeneMm.39285.

3D structure databases

ProteinModelPortalP63141.
SMRP63141. Positions 3-421.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-32239N.
IntActP63141. 3 interactions.
MINTMINT-1659109.

Proteomic databases

PaxDbP63141.
PRIDEP63141.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038695; ENSMUSP00000041702; ENSMUSG00000040724.
GeneID16490.
KEGGmmu:16490.
UCSCuc008qws.2. mouse.

Organism-specific databases

CTD3737.
MGIMGI:96659. Kcna2.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00560000076957.
HOGENOMHOG000231015.
HOVERGENHBG052230.
InParanoidP63141.
KOK04875.
OMAAQYLQVN.
OrthoDBEOG4DR9CB.

Gene expression databases

ArrayExpressP63141.
BgeeP63141.
GenevestigatorP63141.
GermOnlineENSMUSG00000040724. Mus musculus.

Family and domain databases

Gene3D1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR005821. Ion_trans_dom.
IPR027359. K_channel_four-helix_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.
[Graphical view]
PANTHERPTHR11537. PTHR11537. 1 hit.
PfamPF00520. Ion_trans. 1 hit.
PF02214. K_tetra. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
PR01509. KV12CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. BTB/POZ_fold. 1 hit.
ProtoNetSearch...

Other

ChEMBLCHEMBL4475.
NextBio289787.
SOURCESearch...

Entry information

Entry nameKCNA2_MOUSE
AccessionPrimary (citable) accession number: P63141
Secondary accession number(s): P15386, Q02010, Q8C8W4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: May 29, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents