Small conductance calcium-activated potassium channel protein 2

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P70604 (KCNN2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

Kcnn2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Calmodulin-binding
Molecular function	Ion channel
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of neuronal synaptic plasticity Inferred from mutant phenotype PubMed 21521760. Source: RGD
Cellular_component	dendritic spine Inferred from direct assay PubMed 21521760. Source: RGD integral to membrane Inferred from direct assay Ref.3. Source: UniProtKB neuronal cell body Inferred from direct assay PubMed 15680700. Source: RGD
Molecular_function	calmodulin binding Inferred from mutant phenotype PubMed 18701069. Source: RGD protein heterodimerization activity Inferred from mutant phenotype PubMed 14559917. Source: RGD small conductance calcium-activated potassium channel activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Calm3	P62161	2	EBI-1031103,EBI-397530

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 580

580

Small conductance calcium-activated potassium channel protein 2

PRO_0000155012

Regions

Transmembrane

140 – 160

Helical; Name=Segment S1; Potential

Transmembrane

169 – 189

Helical; Name=Segment S2; Potential

Transmembrane

215 – 235

Helical; Name=Segment S3; Potential

Transmembrane

257 – 277

Helical; Name=Segment S4; Potential

Transmembrane

306 – 326

Helical; Name=Segment S5; Potential

Intramembrane

346 – 366

Pore-forming; Name=Segment H5; Potential

Transmembrane

375 – 395

Helical; Name=Segment S6; Potential

Region

413 – 489

Calmodulin-binding

Compositional bias

42 – 46

Poly-Gly

Compositional bias

52 – 56

Poly-Ala

Compositional bias

80 – 85

Poly-Gly

Compositional bias

88 – 103

Poly-Gly

Compositional bias

564 – 567

Poly-Arg

Secondary structure

580

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P70604 [UniParc].

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

FASTA

580

63,848

        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

[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]	"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.

IPI

IPI00190493.

RefSeq

NP_062187.1. NM_019314.1.

UniGene

Rn.44421.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G4Y	X-ray	1.60	B	396-487	[»]
1KKD	NMR	-	A	396-487	[»]
1QX7	X-ray	3.09	D	411-487	[»]
2PNV	X-ray	2.10	A/B	488-526	[»]
3SJQ	X-ray	1.90	C/D	412-487	[»]
4G27	X-ray	1.65	B	396-487	[»]
4G28	X-ray	1.63	B	396-487	[»]

ProteinModelPortal

P70604.

SMR

P70604. Positions 396-526.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35337N.

IntAct

P70604. 1 interaction.

MINT

MINT-197486.

STRING

10116.ENSRNOP00000022530.

PTM databases

PhosphoSite

P70604.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000022530; ENSRNOP00000022530; ENSRNOG00000016675.

GeneID

54262.

KEGG

rno:54262.

UCSC

RGD:2963. rat.

Organism-specific databases

CTD

3781.

RGD

2963. Kcnn2.

Phylogenomic databases

eggNOG

NOG320393.

GeneTree

ENSGT00500000044784.

HOGENOM

HOG000276908.

HOVERGEN

HBG052241.

InParanoid

P70604.

K04943.

OrthoDB

EOG49CQ7G.

Gene expression databases

ArrayExpress

P70604.

Genevestigator

P70604.

GermOnline

ENSRNOG00000016675. Rattus norvegicus.

Family and domain databases

InterPro

IPR004178. CaM-bd_dom.
IPR013099. Ion_trans_2.
IPR015449. K_chnl_Ca-activ_SK.
[Graphical view]

PANTHER

PTHR10153. PTHR10153. 1 hit.

Pfam

PF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]

PRINTS

PR01451. SKCHANNEL.

SMART

SM01053. CaMBD. 1 hit.
[Graphical view]

SUPFAM

SSF81327. CaM_bd. 1 hit.

ProtoNet

Search...

Other

BindingDB

P70604.

ChEMBL

CHEMBL2547.

EvolutionaryTrace

P70604.

NextBio

610790.

Entry information

Entry name

KCNN2_RAT

Accession

Primary (citable) accession number: P70604

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	February 1, 1997
Last modified:	April 3, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents