ID   KCNN2_RAT               Reviewed;         580 AA.
AC   P70604;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=Small conductance calcium-activated potassium channel protein 2;
DE   AltName: Full=SK2;
GN   Name=Kcnn2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   MEDLINE=96376602; PubMed=8781233; DOI=10.1126/science.273.5282.1709;
RA   Koehler M., Hirschberg B., Bond C.T., Kinzie J.M., Marrion N.V.,
RA   Maylie J., Adelman J.P.;
RT   "Small-conductance, calcium-activated potassium channels from
RT   mammalian brain.";
RL   Science 273:1709-1714(1996).
RN   [2]
RP   INTERACTION WITH CALMODULIN.
RX   MEDLINE=98445090; PubMed=9774106; DOI=10.1038/26758;
RA   Xia X.M., Fakler B., Rivard A.F., Wayman G., Johnson-Pais T.,
RA   Keen J.E., Ishii T., Hirschberg B., Bond C.T., Lutsenko S., Maylie J.,
RA   Adelman J.P.;
RT   "Mechanism of calcium gating in small-conductance calcium-activated
RT   potassium channels.";
RL   Nature 395:503-507(1998).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 395-490 WITH CALMODULIN.
RX   MEDLINE=21223356; PubMed=11323678; DOI=10.1038/35074145;
RA   Schumacher M.A., Rivard A.F., Bachinger H.P., Adelman J.P.;
RT   "Structure of the gating domain of a Ca2+-activated K+ channel
RT   complexed with Ca2+/calmodulin.";
RL   Nature 410:1120-1124(2001).
CC   -!- FUNCTION: Forms a voltage-independent potassium channel activated
CC       by intracellular calcium. Activation is followed by membrane
CC       hyperpolarization. Thought to regulate neuronal excitability by
CC       contributing to the slow component of synaptic
CC       afterhyperpolarization. The channel is blocked by apamin.
CC   -!- SUBUNIT: Heterooligomer. The complex is composed of 4 channel
CC       subunits each of which binds to a calmodulin subunit which
CC       regulates the channel activity through calcium-binding.
CC   -!- INTERACTION:
CC       P62161:Calm1; NbExp=1; IntAct=EBI-1031103, EBI-397530;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- SIMILARITY: Belongs to the potassium channel KCNN family.
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DR   EMBL; U69882; AAB09563.1; -; mRNA.
DR   IPI; IPI00190493; -.
DR   RefSeq; NP_062187.1; -.
DR   UniGene; Rn.44421; -.
DR   PDB; 1G4Y; X-ray; 1.60 A; B=396-487.
DR   PDB; 1KKD; NMR; -; A=396-487.
DR   PDB; 1QX7; X-ray; 3.09 A; D=411-487.
DR   PDB; 2PNV; X-ray; 2.10 A; A/B=488-526.
DR   PDBsum; 1G4Y; -.
DR   PDBsum; 1KKD; -.
DR   PDBsum; 1QX7; -.
DR   PDBsum; 2PNV; -.
DR   IntAct; P70604; 1.
DR   PhosphoSite; P70604; -.
DR   Ensembl; ENSRNOG00000016675; Rattus norvegicus.
DR   GeneID; 54262; -.
DR   KEGG; rno:54262; -.
DR   RGD; 2963; Kcnn2.
DR   HOVERGEN; P70604; -.
DR   NextBio; 610790; -.
DR   ArrayExpress; P70604; -.
DR   GermOnline; ENSRNOG00000016675; Rattus norvegicus.
DR   GO; GO:0016021; C:integral to membrane; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0016286; F:small conductance calcium-activated potassi...; IDA:UniProtKB.
DR   GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
DR   InterPro; IPR004178; CaM_bd.
DR   InterPro; IPR013099; Ion_trans_2.
DR   InterPro; IPR015449; K_chnl_Ca-activ_SK.
DR   InterPro; IPR011996; K_chnl_Ca-activ_SK_con.
DR   InterPro; IPR003931; K_chnl_Ca-activ_SK_con_sub.
DR   PANTHER; PTHR10153; CaKChannelSK; 1.
DR   Pfam; PF02888; CaMBD; 1.
DR   Pfam; PF07885; Ion_trans_2; 1.
DR   Pfam; PF03530; SK_channel; 1.
DR   PRINTS; PR01451; SKCHANNEL.
PE   1: Evidence at protein level;
KW   3D-structure; Calmodulin-binding; Ion transport; Ionic channel;
KW   Membrane; Transmembrane; Transport.
FT   CHAIN         1    580       Small conductance calcium-activated
FT                                potassium channel protein 2.
FT                                /FTId=PRO_0000155012.
FT   TRANSMEM    140    160       Segment S1 (Potential).
FT   TRANSMEM    169    189       Segment S2 (Potential).
FT   TRANSMEM    215    235       Segment S3 (Potential).
FT   TRANSMEM    257    277       Segment S4 (Potential).
FT   TRANSMEM    306    326       Segment S5 (Potential).
FT   TRANSMEM    346    366       Segment H5 (Potential).
FT   TRANSMEM    375    395       Segment S6 (Potential).
FT   REGION      413    489       Calmodulin-binding.
FT   COMPBIAS     42     46       Poly-Gly.
FT   COMPBIAS     52     56       Poly-Ala.
FT   COMPBIAS     80     85       Poly-Gly.
FT   COMPBIAS     88    103       Poly-Gly.
FT   COMPBIAS    564    567       Poly-Arg.
FT   STRAND      398    401
FT   HELIX       414    439
FT   HELIX       446    485
FT   HELIX       489    523
SQ   SEQUENCE   580 AA;  63848 MW;  F71E0DAF7EEFA8D4 CRC64;
     MSSCRYNGGV MRPLSNLSSS RRNLHEMDSE AQPLQPPASV VGGGGGASSP SAAAAASSSA
     PEIVVSKPEH NNSNNLALYG TGGGGSTGGG GGGGGGGGGS GHGSSSGTKS SKKKNQNIGY
     KLGHRRALFE KRKRLSDYAL IFGMFGIVVM VIETELSWGA YDKASLYSLA LKCLISLSTI
     ILLGLIIVYH AREIQLFMVD NGADDWRIAM TYERIFFICL EILVCAIHPI PGNYTFTWTA
     RLAFSYAPST TTADVDIILS IPMFLRLYLI ARVMLLHSKL FTDASSRSIG ALNKINFNTR
     FVMKTLMTIC PGTVLLVFSI SLWIIAAWTV RACERYHDQQ DVTSNFLGAM WLISITFLSI
     GYGDMVPNTY CGKGVCLLTG IMGAGCTALV VAVVARKLEL TKAEKHVHNF MMDTQLTKRV
     KNAAANVLRE TWLIYKNTKL VKKIDHAKVR KHQRKFLQAI HQLRSVKMEQ RKLNDQANTL
     VDLAKTQNIM YDMISDLNER SEDFEKRIVT LETKLETLIG SIHALPGLIS QTIRQQQRDF
     IETQMENYDK HVTYNAERSR SSSRRRRSSS TAPPTSSESS
//