Swiss-Prot entry

ID   KCNN1_RAT      STANDARD;      PRT;   536 AA.
AC   P70606;
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 1 (SK1).
GN   Name=Kcnn1; Synonyms=Sk1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; 
OC   Muridae; Murinae; Rattus. 
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=98021485; PubMed=9380751 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.94.20.11013;
RA   Joiner W.J., Wang L.-Y., Tang M.D., Kaczmarek L.K.;
RT   "hSK4, a member of a novel subfamily of calcium-activated potassium
RT   channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:11013-11018(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 79-536.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   MEDLINE=96376602; PubMed=8781233 [NCBI, ExPASy, EBI, Israel, Japan];
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).
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 (By
CC       similarity).
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 including brain.
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; AF000973; AAB82740.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; U69885; AAB09564.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P70604; 1KKD. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; P70606; 363-457.
DR   RGD; 2962; Kcnn1.
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; P70606.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P70606.
DR   ProtoNet; P70606.
DR   ProtoMap; P70606.
DR   PRESAGE; P70606.
DR   DIP; P70606.
DR   ModBase; P70606.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Calmodulin-binding; Ion transport; Ionic channel; Transmembrane;
KW   Transport.
FT   TRANSMEM    107    127       Segment S1 (Potential).
FT   TRANSMEM    136    156       Segment S2 (Potential).
FT   TRANSMEM    224    244       Segment S3 (Potential).
FT   TRANSMEM    273    293       Segment S4 (Potential).
FT   TRANSMEM    313    333       Segment S5 (Potential).
FT   TRANSMEM    487    507       Segment S6 (Potential).
FT   REGION      342    362       Segment H5 (pore-forming) (Potential).
FT   REGION      380    459       Calmodulin-binding (By similarity).
FT   COMPBIAS     66     74       Poly-Glu.
SQ   SEQUENCE   536 AA;  59215 MW;  97FF82071B0BE36A CRC64;
     MSSRSHNGSV GRPLGSGPGF LGWEPVDPEA GRPRQPTQGP GLQMMAKGQP AGLSPSGPRG
     HSQAQEEEEE EEDEDRPGSG KPPTVSHRLG HRRALFEKRK RLSDYALIFG MFGIVVMVTE
     TELSWGVYTK ESLCSFALKC LISLSTVILL GLVILYHARE IQLFLVDNGA DDWRIAMTWE
     RVSLISLELA VCAIHPVPGH YRFTWTARLA FSLVPSAAEA DVDVLLSIPM FLRLYLLARV
     MLLHSRIFTD ASSRSIGALN RVTFNTRFVT KTLMTICPGT VLLVFSISSW IVAAWTVRVC
     ERYHDKQEVT SNFLGAMWLI SITFLSIGYG DMVPHTYCGK GVCLLTGIMG AGCTALVVAV
     VARKLELTKA EKHVHNFMMD TQLTKRVKNA AANVLRETWL IYKHTRLVKK PDQSRVRKHQ
     RKFLQAIHQA QKLRTVKIEQ GKVNDQANTL ADLAKAQSIA YEVVSELQAQ QEELEARLAA
     LESRLDVLGA SLQALPSLIA QAICPLPPPW PGPSHLTTAA QSPQSHWLPT TASDCG
//