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Reviewed, UniProtKB/Swiss-Prot P70604 (KCNN2_RAT)

Last modified November 25, 2008. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Small conductance calcium-activated potassium channel protein 2
Alternative name(s):
    SK2
Gene names
Name: Kcnn2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.

Subunit structure

Heterooligomer. The complex is composed of 4 channel subunits each of which binds to a calmodulin subunit which regulates the channel activity through calcium-binding.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Brain.

Sequence similarities

Belongs to the potassium channel KCNN family.

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Ontologies

Keywords

   Biological processIon transport
Transport
   Cellular componentMembrane
   DomainTransmembrane
   LigandCalmodulin-binding
   Molecular functionIonic channel
   Technical term3D-structure

Gene Ontology (GO)

   Biological processpotassium ion transport Ref.3

Inferred from direct assay. Source: UniProtKB

   Cellular componentintegral to membrane Ref.3

Inferred from direct assay. Source: UniProtKB

   Molecular functioncalmodulin binding

Inferred from electronic annotation. Source: InterPro

small conductance calcium-activated potassium channel activity Ref.3

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Calm1P621611EBI-1031103,EBI-397530

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 580580Small conductance calcium-activated potassium channel protein 2
PRO_0000155012

Regions

Transmembrane140 – 16021Segment S1 Potential
Transmembrane169 – 18921Segment S2 Potential
Transmembrane215 – 23521Segment S3 Potential
Transmembrane257 – 27721Segment S4 Potential
Transmembrane306 – 32621Segment S5 Potential
Transmembrane346 – 36621Segment H5 Potential
Transmembrane375 – 39521Segment S6 Potential
Region413 – 48977Calmodulin-binding
Compositional bias42 – 465Poly-Gly
Compositional bias52 – 565Poly-Ala
Compositional bias80 – 856Poly-Gly
Compositional bias88 – 10316Poly-Gly
Compositional bias564 – 5674Poly-Arg

Secondary structure

1 ......... 580
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P70604-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: F71E0DAF7EEFA8D4

FASTA58063,848
        10         20         30         40         50         60 
MSSCRYNGGV MRPLSNLSSS RRNLHEMDSE AQPLQPPASV VGGGGGASSP SAAAAASSSA 

        70         80         90        100        110        120 
PEIVVSKPEH NNSNNLALYG TGGGGSTGGG GGGGGGGGGS GHGSSSGTKS SKKKNQNIGY 

       130        140        150        160        170        180 
KLGHRRALFE KRKRLSDYAL IFGMFGIVVM VIETELSWGA YDKASLYSLA LKCLISLSTI 

       190        200        210        220        230        240 
ILLGLIIVYH AREIQLFMVD NGADDWRIAM TYERIFFICL EILVCAIHPI PGNYTFTWTA 

       250        260        270        280        290        300 
RLAFSYAPST TTADVDIILS IPMFLRLYLI ARVMLLHSKL FTDASSRSIG ALNKINFNTR 

       310        320        330        340        350        360 
FVMKTLMTIC PGTVLLVFSI SLWIIAAWTV RACERYHDQQ DVTSNFLGAM WLISITFLSI 

       370        380        390        400        410        420 
GYGDMVPNTY CGKGVCLLTG IMGAGCTALV VAVVARKLEL TKAEKHVHNF MMDTQLTKRV 

       430        440        450        460        470        480 
KNAAANVLRE TWLIYKNTKL VKKIDHAKVR KHQRKFLQAI HQLRSVKMEQ RKLNDQANTL 

       490        500        510        520        530        540 
VDLAKTQNIM YDMISDLNER SEDFEKRIVT LETKLETLIG SIHALPGLIS QTIRQQQRDF 

       550        560        570        580 
IETQMENYDK HVTYNAERSR SSSRRRRSSS TAPPTSSESS

« Hide

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References

[1]"Small-conductance, calcium-activated potassium channels from mammalian brain."
Koehler M., Hirschberg B., Bond C.T., Kinzie J.M., Marrion N.V., Maylie J., Adelman J.P.
Science 273:1709-1714(1996) [PubMed: 8781233] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"Mechanism of calcium gating in small-conductance calcium-activated potassium channels."
Xia X.M., Fakler B., Rivard A.F., Wayman G., Johnson-Pais T., Keen J.E., Ishii T., Hirschberg B., Bond C.T., Lutsenko S., Maylie J., Adelman J.P.
Nature 395:503-507(1998) [PubMed: 9774106] [Abstract]
Cited for: INTERACTION WITH CALMODULIN.
[3]"Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin."
Schumacher M.A., Rivard A.F., Bachinger H.P., Adelman J.P.
Nature 410:1120-1124(2001) [PubMed: 11323678] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 395-490 WITH CALMODULIN.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U69882 mRNA. Translation: AAB09563.1.
RefSeqNP_062187.1.
UniGeneRn.44421

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1G4YX-ray1.60B396-487[»]
1KKDNMR-A396-487[»]
1QX7X-ray3.09D411-487[»]
2PNVX-ray2.10A/B488-526[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP70604.

PTM databases

PhosphoSiteP70604.

Genome annotation databases

EnsemblENSRNOG00000016675. Rattus norvegicus. [Contig view]
GeneID54262.
KEGGrno:54262.

Organism-specific databases

RGD2963. Kcnn2.

Phylogenomic databases

HOVERGENP70604.

Gene expression databases

ArrayExpressP70604.
GermOnlineENSRNOG00000016675. Rattus norvegicus.

Family and domain databases

InterProIPR004178. CaM_bd.
IPR013099. Ion_trans_2.
IPR015449. K_chnl_Ca-activ_SK.
IPR011996. K_chnl_Ca-activ_SK_con.
IPR003931. K_chnl_Ca-activ_SK_con_sub.
[Graphical view]
PANTHERPTHR10153. CaKChannelSK. 1 hit.
PfamPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSPR01451. SKCHANNEL.
ProtoNetSearch...

Other Resources

LinkHubP70604.
NextBio610790.

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Entry information

Entry nameKCNN2_RAT
AccessionPrimary (citable) accession number: P70604
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: February 1, 1997
Last modified: November 25, 2008
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents