Swiss-Prot entry
ID KCNN2_MOUSE STANDARD; PRT; 574 AA.
AC P58390;
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; Synonyms=Sk2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muridae; Murinae; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/c; TISSUE=Colon;
RX MEDLINE=21440983; PubMed=11557517 [NCBI, ExPASy, EBI, Israel, Japan];
RA Ro S., Hatton W.J., Koh S.D., Horowitz B.;
RT "Molecular properties of small-conductance Ca2+-activated K+ channels
RT expressed in murine colonic smooth muscle.";
RL Am. J. Physiol. 281:G964-G973(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 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 -!- 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.
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DR EMBL; AF357240; AAK48901.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P70604; 1KKD. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P58390; 390-481.
DR Ensembl; ENSMUSG00000054477; Mus_musculus
DR MGI; MGI:2153182; Kcnn2.
DR GO; GO:0016021; C:integral to membrane; TAS.
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; P58390.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P58390.
DR ProtoNet; P58390.
DR ProtoMap; P58390.
DR PRESAGE; P58390.
DR DIP; P58390.
DR ModBase; P58390.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Calmodulin-binding; Ion transport; Ionic channel; Transmembrane;
KW Transport.
FT TRANSMEM 133 153 Segment S1 (Potential).
FT TRANSMEM 163 183 Segment S2 (Potential).
FT TRANSMEM 209 229 Segment S3 (Potential).
FT TRANSMEM 251 271 Segment S4 (Potential).
FT TRANSMEM 300 320 Segment S5 (Potential).
FT TRANSMEM 340 360 Segment H5 (pore-forming) (Potential).
FT TRANSMEM 369 389 Segment S6 (Potential).
FT REGION 407 483 Calmodulin-binding (By similarity).
FT COMPBIAS 42 46 Poly-Gly.
FT COMPBIAS 52 56 Poly-Ala.
FT COMPBIAS 80 85 Poly-Gly.
FT COMPBIAS 88 97 Poly-Gly.
FT COMPBIAS 558 561 Poly-Arg.
SQ SEQUENCE 574 AA; 63482 MW; 259CB8CDE4D1CDE6 CRC64;
MSSCRYNGGV MRPLSNLSSS RRNLQEMDSE AQPLQPPASV VGGGGGASSP SAAAAASSSA
PEIVVSKPEH NNSNNLALYG TGGGGSTGGG GGGSGHGSSS GTKSSKKKNQ NIGYKLGHRR
ALFEKRKRLS DYALIFGMFG IVVMVIETEL SWGAYDKASL YSLALKCLIS LSTIILLGLI
IVYHAREIQL FMVDNGADDW RIAMTYERIF FICLEILVCA IHPIPGNYTF TWTARLAFSY
APSTTTADVD IILSIPMFLR LYLIARVMLL HSKLFTDASS RSIGALNKIN FNTRFVMKTL
MTICPGTVLL VFSISLWIIA AWTVRACERY HDQQDVTSNF LGAMWLISIT FLSIGYGDMV
PNTYCGKGVC LLTGIMGAGC TALVVAVVAR KLELTKAEKH VHNFMMDTQL TKRVKNAAAN
VLRETWLIYK NTKLVKKIDH AKVRKHQRKF LQAIHQLRSV KMEQRKLNDQ ANTLVDLAKT
QNIMYDMISD LNERSEDFEK RIVTLETKLE TLIGSIHALP GLISQTIRQQ QRDFIETQME
NYDKHVSYNA ERSRSSSRRR RSSSTAPPTS SESS
//