Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P70604 (KCNN2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 117. 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:
Small conductance calcium-activated potassium channel protein 2

Short name=SK2
Short name=SKCa 2
Short name=SKCa2
Alternative name(s):
KCa2.2
Gene names
Name:Kcnn2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. KCa2.2/KCNN2 subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Calm3P621612EBI-1031103,EBI-397530

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Transmembrane140 – 16021Helical; Name=Segment S1; Potential
Transmembrane169 – 18921Helical; Name=Segment S2; Potential
Transmembrane215 – 23521Helical; Name=Segment S3; Potential
Transmembrane257 – 27721Helical; Name=Segment S4; Potential
Transmembrane306 – 32621Helical; Name=Segment S5; Potential
Intramembrane346 – 36621Pore-forming; Name=Segment H5; Potential
Transmembrane375 – 39521Helical; Name=Segment 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

Amino acid modifications

Modified residue1611Phosphotyrosine Ref.3

Secondary structure

......... 580
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P70604 [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

References

« Hide 'large scale' 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CALMODULIN.
[3]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 395-490 WITH CALMODULIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U69882 mRNA. Translation: AAB09563.1.
RefSeqNP_062187.1. NM_019314.1.
UniGeneRn.44421.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G4YX-ray1.60B396-487[»]
1KKDNMR-A396-487[»]
1QX7X-ray3.09D411-487[»]
2PNVX-ray2.10A/B488-526[»]
3SJQX-ray1.90C/D412-487[»]
4G27X-ray1.65B396-487[»]
4G28X-ray1.63B396-487[»]
4J9YX-ray1.51B396-487[»]
4J9ZX-ray1.66B396-487[»]
ProteinModelPortalP70604.
SMRP70604. Positions 396-526.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35337N.
IntActP70604. 1 interaction.
MINTMINT-197486.
STRING10116.ENSRNOP00000022530.

Chemistry

BindingDBP70604.
ChEMBLCHEMBL2547.
GuidetoPHARMACOLOGY382.

PTM databases

PhosphoSiteP70604.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022530; ENSRNOP00000022530; ENSRNOG00000016675.
GeneID54262.
KEGGrno:54262.
UCSCRGD:2963. rat.

Organism-specific databases

CTD3781.
RGD2963. Kcnn2.

Phylogenomic databases

eggNOGNOG320393.
GeneTreeENSGT00500000044784.
HOGENOMHOG000276908.
HOVERGENHBG052241.
InParanoidP70604.
KOK04943.
PhylomeDBP70604.
TreeFamTF315015.

Gene expression databases

GenevestigatorP70604.

Family and domain databases

InterProIPR013099. 2pore_dom_K_chnl_dom.
IPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
[Graphical view]
PANTHERPTHR10153. PTHR10153. 1 hit.
PfamPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSPR01451. SKCHANNEL.
SMARTSM01053. CaMBD. 1 hit.
[Graphical view]
SUPFAMSSF81327. SSF81327. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP70604.
NextBio610790.
PROP70604.

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: June 11, 2014
This is version 117 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