Swiss-Prot entry

ID   KCNN1_MOUSE    STANDARD;      PRT;   580 AA.
AC   Q9EQR3; Q99JA9;
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   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, ALTERNATIVE SPLICING, AND POLYMORPHISM OF
RP   POLY-GLU REGION.
RC   STRAIN=CD-1;
RX   MEDLINE=21167369; PubMed=11267657 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S0167-4781(01)00166-X;
RA   Shmukler B.E., Bond C.T., Wilhelm S., Bruening-Wright A., Maylie J.,
RA   Adelman J.P., Alper S.L.;
RT   "Structure and complex transcription pattern of the mouse SK1 KCa
RT   channel gene, KCNN1.";
RL   Biochim. Biophys. Acta 1518:36-46(2001).
RN   [2]
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=At least 16 isoforms are produced. The gene is composed
CC         of at least 12 exons. Exons A, 3.2 or C, B, 3.2, 6, 8, 8, 10, 8,
CC         10, 8A and 10 are alternatively spliced;
CC       Name=1;
CC         IsoId=Q9EQR3-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Widely expressed including brain.
CC   -!- POLYMORPHISM: The poly-Glu region of KCNN1 is polymorphic and the
CC       number of Glu varies between strains (from 10 to 12). The repeat
CC       with 10 Glu residues (shown here) is found in BALB/c, DBA/2J,
CC       129/SvJ, A/J, C3H/HeJ, BALB/cJ, BXD-31, SM/J, ST/BJ, FVB/NJ,
CC       NZB/B1NJ, CBA/J and CAST/Ei.
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; AF116525; AAG43216.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF297870; AAK30363.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF297869; AAK30363.1; JOINED; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF303461; AAK29550.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF303462; AAK29551.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF303463; AAK29552.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF357239; AAK48900.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P70604; 1KKD. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; Q9EQR3; 407-501.
DR   Ensembl; ENSMUSG00000002908; Mus_musculus
DR   MGI; MGI:1933993; Kcnn1.
DR   GO; GO:0016021; C:integral to membrane; TAS.
DR   GO; GO:0005516; F:calmodulin binding; IDA.
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; Q9EQR3.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; Q9EQR3.
DR   ProtoNet; Q9EQR3.
DR   ProtoMap; Q9EQR3.
DR   PRESAGE; Q9EQR3.
DR   DIP; Q9EQR3.
DR   ModBase; Q9EQR3.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Alternative splicing; Calmodulin-binding; Ion transport;
KW   Ionic channel; Polymorphism; Transmembrane; Transport.
FT   TRANSMEM    151    171       Segment S1 (Potential).
FT   TRANSMEM    180    200       Segment S2 (Potential).
FT   TRANSMEM    219    239       Segment S3 (Potential).
FT   TRANSMEM    268    288       Segment S4 (Potential).
FT   TRANSMEM    317    337       Segment S5 (Potential).
FT   REGION      357    377       Segment H5 (pore-forming) (Potential).
FT   REGION      386    406       Segment S6 (Potential).
FT   REGION      424    503       Calmodulin-binding (By similarity).
FT   COMPBIAS    107    118       Poly-Glu.
FT   VARSPLIC      1     43       Missing (in isoforms without exon A/3.2
FT                                OR C/B/3.2).
FT                                /FTId=VSP_002809.
FT   VARSPLIC    394    430       Missing (in isoforms without exon 6/8).
FT                                /FTId=VSP_002810.
FT   VARSPLIC    466    580       KFLQAIHQAQKLRSVKIEQGKVNDQANTLAELAKAQSIAYE
FT                                VVSELQAQQEELEARLAALESRLDVLGASLQALPGLIAQAI
FT                                CPLPPPWPGPGHLATATHSPQSHWLPTMGSDCG -> LRSS
FT                                EV (in isoforms with exon 8/10).
FT                                /FTId=VSP_002811.
FT   VARSPLIC    466    580       KFLQAIHQAQKLRSVKIEQGKVNDQANTLAELAKAQSIAYE
FT                                VVSELQAQQEELEARLAALESRLDVLGASLQALPGLIAQAI
FT                                CPLPPPWPGPGHLATATHSPQSHWLPTMGSDCG -> SEV
FT                                (in isoforms with exon 8/10).
FT                                /FTId=VSP_002812.
FT   VARSPLIC    474    476       Missing (in isoforms without exon 8A/10).
FT                                /FTId=VSP_002813.
FT   VARIANT     109    109       E -> EE (in strain C57BL/6J, strain A/HeJ
FT                                and strain SPRET/Ei).
FT   VARIANT     109    109       E -> EEE (in strain SWR/J, strain AKR/J,
FT                                strain RBF/DNJ and strain P/J).
FT   VARIANT     565    565       H -> Q (in strain C57BL/6J).
SQ   SEQUENCE   580 AA;  64066 MW;  7B30C8A28B349C80 CRC64;
     MFWNGQGDVQ PLLSPQVHSE ALLRNHAGPQ RACCTPSPRR QVAMSSHSHN GSVGQPLGSG
     PGFLGWEPVD PEAGRPLQPT QGPGLQMVAK GQPVRLSPGG SRGHPQEQEE EEEEEEEEDK
     TGSGKPPTVS HRLGHRRALF EKRKRLSDYA LIFGMFGIVV MVTETELSWG VYTKESLCSF
     ALKCLISLST VILLGLVILY HAREIQLFLV DNGADDWRIA MTWERVSLIS LELVVCAIHP
     VPGHYRFTWT ARLAFSLVPS AAEADLDVLL SIPMFLRLYL LARVMLLHSR IFTDASSRSI
     GALNRVTFNT RFVTKTLMTI CPGTVLLVFS VSSWIVAAWT VRVCERYHDK QEVTSNFLGA
     MWLISITFLS IGYGDMVPHT YCGKGVCLLT GIMGAGCTAL VVAVVARKLE LTKAEKHVHN
     FMMDTQLTKR VKNAAANVLR ETWLIYKHTR LVKKPDQGRV RKHQRKFLQA IHQAQKLRSV
     KIEQGKVNDQ ANTLAELAKA QSIAYEVVSE LQAQQEELEA RLAALESRLD VLGASLQALP
     GLIAQAICPL PPPWPGPGHL ATATHSPQSH WLPTMGSDCG
//