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Protein

Small conductance calcium-activated potassium channel protein 2

Gene

Kcnn2

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

Functioni

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.

GO - Molecular functioni

  1. calmodulin binding Source: RGD
  2. small conductance calcium-activated potassium channel activity Source: UniProtKB

GO - Biological processi

  1. potassium ion transmembrane transport Source: GOC
  2. potassium ion transport Source: UniProtKB
  3. regulation of neuronal synaptic plasticity Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_199213. Ca2+ activated K+ channels.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Kcnn2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 18

Organism-specific databases

RGDi2963. Kcnn2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei140 – 16021Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Transmembranei169 – 18921Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Transmembranei215 – 23521Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Transmembranei257 – 27721Helical; Name=Segment S4Sequence AnalysisAdd
BLAST
Transmembranei306 – 32621Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Intramembranei346 – 36621Pore-forming; Name=Segment H5Sequence AnalysisAdd
BLAST
Transmembranei375 – 39521Helical; Name=Segment S6Sequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. dendritic spine Source: RGD
  2. integral component of membrane Source: UniProtKB
  3. neuronal cell body Source: RGD
  4. plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580Small conductance calcium-activated potassium channel protein 2PRO_0000155012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

PTM databases

PhosphoSiteiP70604.

Expressioni

Tissue specificityi

Brain.

Gene expression databases

ExpressionAtlasiP70604. baseline and differential.
GenevestigatoriP70604.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Calm3P621612EBI-1031103,EBI-397530

Protein-protein interaction databases

DIPiDIP-35337N.
IntActiP70604. 1 interaction.
MINTiMINT-197486.
STRINGi10116.ENSRNOP00000022530.

Structurei

Secondary structure

1
580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi398 – 4014Combined sources
Helixi414 – 43926Combined sources
Helixi446 – 48540Combined sources
Helixi489 – 52335Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4QNHX-ray2.02B396-487[»]
ProteinModelPortaliP70604.
SMRiP70604. Positions 396-526.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70604.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni413 – 48977Calmodulin-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi42 – 465Poly-Gly
Compositional biasi52 – 565Poly-Ala
Compositional biasi80 – 856Poly-Gly
Compositional biasi88 – 10316Poly-GlyAdd
BLAST
Compositional biasi564 – 5674Poly-Arg

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG320393.
GeneTreeiENSGT00500000044784.
HOGENOMiHOG000276908.
HOVERGENiHBG052241.
InParanoidiP70604.
KOiK04943.
PhylomeDBiP70604.
TreeFamiTF315015.

Family and domain databases

InterProiIPR013099. 2pore_dom_K_chnl_dom.
IPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
[Graphical view]
PANTHERiPTHR10153. PTHR10153. 1 hit.
PfamiPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSiPR01451. SKCHANNEL.
SMARTiSM01053. CaMBD. 1 hit.
[Graphical view]
SUPFAMiSSF81327. SSF81327. 1 hit.

Sequencei

Sequence statusi: Complete.

P70604-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSCRYNGGV MRPLSNLSSS RRNLHEMDSE AQPLQPPASV VGGGGGASSP
60 70 80 90 100
SAAAAASSSA PEIVVSKPEH NNSNNLALYG TGGGGSTGGG GGGGGGGGGS
110 120 130 140 150
GHGSSSGTKS SKKKNQNIGY KLGHRRALFE KRKRLSDYAL IFGMFGIVVM
160 170 180 190 200
VIETELSWGA YDKASLYSLA LKCLISLSTI ILLGLIIVYH AREIQLFMVD
210 220 230 240 250
NGADDWRIAM TYERIFFICL EILVCAIHPI PGNYTFTWTA RLAFSYAPST
260 270 280 290 300
TTADVDIILS IPMFLRLYLI ARVMLLHSKL FTDASSRSIG ALNKINFNTR
310 320 330 340 350
FVMKTLMTIC PGTVLLVFSI SLWIIAAWTV RACERYHDQQ DVTSNFLGAM
360 370 380 390 400
WLISITFLSI GYGDMVPNTY CGKGVCLLTG IMGAGCTALV VAVVARKLEL
410 420 430 440 450
TKAEKHVHNF MMDTQLTKRV KNAAANVLRE TWLIYKNTKL VKKIDHAKVR
460 470 480 490 500
KHQRKFLQAI HQLRSVKMEQ RKLNDQANTL VDLAKTQNIM YDMISDLNER
510 520 530 540 550
SEDFEKRIVT LETKLETLIG SIHALPGLIS QTIRQQQRDF IETQMENYDK
560 570 580
HVTYNAERSR SSSRRRRSSS TAPPTSSESS
Length:580
Mass (Da):63,848
Last modified:February 1, 1997 - v1
Checksum:iF71E0DAF7EEFA8D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U69882 mRNA. Translation: AAB09563.1.
RefSeqiNP_062187.1. NM_019314.1.
UniGeneiRn.44421.

Genome annotation databases

EnsembliENSRNOT00000022530; ENSRNOP00000022530; ENSRNOG00000016675.
GeneIDi54262.
KEGGirno:54262.
UCSCiRGD:2963. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U69882 mRNA. Translation: AAB09563.1.
RefSeqiNP_062187.1. NM_019314.1.
UniGeneiRn.44421.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4QNHX-ray2.02B396-487[»]
ProteinModelPortaliP70604.
SMRiP70604. Positions 396-526.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35337N.
IntActiP70604. 1 interaction.
MINTiMINT-197486.
STRINGi10116.ENSRNOP00000022530.

Chemistry

BindingDBiP70604.
ChEMBLiCHEMBL2096673.
GuidetoPHARMACOLOGYi382.

PTM databases

PhosphoSiteiP70604.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022530; ENSRNOP00000022530; ENSRNOG00000016675.
GeneIDi54262.
KEGGirno:54262.
UCSCiRGD:2963. rat.

Organism-specific databases

CTDi3781.
RGDi2963. Kcnn2.

Phylogenomic databases

eggNOGiNOG320393.
GeneTreeiENSGT00500000044784.
HOGENOMiHOG000276908.
HOVERGENiHBG052241.
InParanoidiP70604.
KOiK04943.
PhylomeDBiP70604.
TreeFamiTF315015.

Enzyme and pathway databases

ReactomeiREACT_199213. Ca2+ activated K+ channels.

Miscellaneous databases

EvolutionaryTraceiP70604.
NextBioi610790.
PROiP70604.

Gene expression databases

ExpressionAtlasiP70604. baseline and differential.
GenevestigatoriP70604.

Family and domain databases

InterProiIPR013099. 2pore_dom_K_chnl_dom.
IPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
[Graphical view]
PANTHERiPTHR10153. PTHR10153. 1 hit.
PfamiPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSiPR01451. SKCHANNEL.
SMARTiSM01053. CaMBD. 1 hit.
[Graphical view]
SUPFAMiSSF81327. SSF81327. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiKCNN2_RAT
AccessioniPrimary (citable) accession number: P70604
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: February 1, 1997
Last modified: February 4, 2015
This is version 123 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.