Swiss-Prot entry

ID   KCNN2_HUMAN    STANDARD;      PRT;   579 AA.
AC   Q9H2S1;
DT   28-FEB-2003 (Rel. 41, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   Small conductance calcium-activated potassium channel protein 2 (SK2).
GN   Name=KCNN2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; 
OC   Homo. 
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=20568244; PubMed=10991935 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.M001562200;
RA   Desai R., Peretz A., Idelson H., Lazarovici P., Attali B.;
RT   "Ca2+-activated K+ channels in human leukemic Jurkat T cells.
RT   Molecular cloning, biochemical and functional characterization.";
RL   J. Biol. Chem. 275:39954-39963(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Myometrium;
RA   Mazzone J.N., Kaiser R.A., Buxton I.L.O.;
RT   "Characterization of calcium-activated potassium channels in human
RT   myometrium.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms a voltage-independent potassium channel activated
CC       by intracellular calcium. Activation is followed by membrane
CC       hyperpolarization. Thought to regulate neuronal excitabilty by
CC       contributing to the slow component of synaptic
CC       afterhyperpolarization. The channel is blocked by apamin.
CC   -!- SUBUNIT: Hetero-oligomer. 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 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the potassium channel KCNN family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AF239613; AAG16728.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF397175; AAK84039.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P70604; 1KKD. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; Q9H2S1; 395-486.
DR   Ensembl; ENSG00000080709; Homo_sapiens
DR   HGNC; HGNC:6291; KCNN2.
DR   CleanEx; HGNC:6291; KCNN2.
DR   MIM; 605879; -. [NCBI / EBI]
DR   GeneCards; KCNN2.
DR   GeneLynx; KCNN2.
DR   GenAtlas; KCNN2.
DR   SOURCE; KCNN2.
DR   GO; GO:0016021; C:integral to membrane; NAS.
DR   GO; GO:0016286; F:small conductance calcium-activated potassi...; TAS.
DR   GO; GO:0006813; P:potassium ion transport; NAS.
DR   InterPro; IPR004178; CaM_bd.
DR   InterPro; IPR001622; K+channel_pore.
DR   InterPro; IPR011996; SK.
DR   InterPro; IPR003931; SK_channel.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF02888; CaMBD; 1.
DR   Pfam; PF03530; SK_channel; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR01451; SKCHANNEL.
DR   CMR; Q9H2S1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; Q9H2S1.
DR   ProtoNet; Q9H2S1.
DR   ProtoMap; Q9H2S1.
DR   PRESAGE; Q9H2S1.
DR   DIP; Q9H2S1.
DR   ModBase; Q9H2S1.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Calmodulin-binding; Ion transport; Ionic channel; Transmembrane;
KW   Transport.
FT   TRANSMEM    138    158       Segment S1 (Potential).
FT   TRANSMEM    168    188       Segment S2 (Potential).
FT   TRANSMEM    214    234       Segment S3 (Potential).
FT   TRANSMEM    256    276       Segment S4 (Potential).
FT   TRANSMEM    305    325       Segment S5 (Potential).
FT   TRANSMEM    345    365       Segment H5 (pore-forming) (Potential).
FT   TRANSMEM    374    394       Segment S6 (Potential).
FT   REGION      412    488       Calmodulin-binding (By similarity).
FT   COMPBIAS     41     45       Poly-Gly.
FT   COMPBIAS     51     58       Poly-Ala.
FT   COMPBIAS     83     88       Poly-Gly.
FT   COMPBIAS     91    102       Poly-Gly.
FT   COMPBIAS    563    566       Poly-Arg.
FT   CONFLICT     52     52       D -> AA (in Ref. 2).
FT   CONFLICT    323    323       I -> T (in Ref. 2).
FT   CONFLICT    530    530       Q -> R (in Ref. 2).
SQ   SEQUENCE   579 AA;  63804 MW;  B1DAE3513C106182 CRC64;
     MSSCRYNGGV MRPLSNLSAS RRNLHEMDSE AQPLQPPASV GGGGGASSPS ADAAAAAAVS
     SSAPEIVVSK PEHNNSNNLA LYGTGGGGST GGGGGGGGSG HGSSSGTKSS KKKNQNIGYK
     LGHRRALFEK RKRLSDYALI FGMFGIVVMV IETELSWGAY DKASLYSLAL KCLISLSTII
     LLGLIIVYHA REIQLFMVDN GADDWRIAMT YERIFFICLE ILVCAIHPIP GNYTFTWTAR
     LAFSYAPSTT TADVDIILSI PMFLRLYLIA RVMLLHSKLF TDASSRSIGA LNKINFNTRF
     VMKTLMTICP GTVLLVFSIS LWIIAAWTVR ACERYHDQQD VTSNFLGAMW LISITFLSIG
     YGDMVPNTYC GKGVCLLTGI MGAGCTALVV AVVARKLELT KAEKHVHNFM MDTQLTKRVK
     NAAANVLRET WLIYKNTKLV KKIDHAKVRK HQRKFLQAIH QLRSVKMEQR KLNDQANTLV
     DLAKTQNIMY DMISDLNERS EDFEKRIVTL ETKLETLIGS IHALPGLISQ TIRQQQRDFI
     EAQMESYDKH VTYNAERSRS SSRRRRSSST APPTSSESS
//