Swiss-Prot entry
ID KCNN4_MOUSE STANDARD; PRT; 425 AA.
AC O89109; Q9CY39;
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 Intermediate conductance calcium-activated potassium channel protein 4
DE (SK4) (KCa4) (IK1).
GN Name=Kcnn4;
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, AND FUNCTION.
RC STRAIN=CD-1;
RX MEDLINE=98370984; PubMed=9705284 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.273.34.21542;
RA Vandorpe D.H., Shmukler B.E., Jiang L., Lim B., Maylie J.,
RA Adelman J.P., de Franceschi L., Cappellini M.D., Brugnara C.,
RA Alper S.L.;
RT "cDNA cloning and functional characterization of the mouse Ca2+-gated
RT K+ channel, mIK1. Roles in regulatory volume decrease and erythroid
RT differentiation.";
RL J. Biol. Chem. 273:21542-21553(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Logsdon N.J., Aiyar J.;
RT "Murine intermediate conductance calcium-activated potassium channel
RT (mKCa4, KCNN4) complete cds.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver;
RX MEDLINE=22354683; PubMed=12466851 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/nature01266;
RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S.,
RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H.,
RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T.,
RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J.,
RA Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W.,
RA Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S.,
RA Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S.,
RA Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J.,
RA Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D.,
RA Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L.,
RA Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A.,
RA Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H.,
RA Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G.,
RA Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S.,
RA Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M.,
RA Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K.,
RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M.,
RA Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C.,
RA Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L.,
RA Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N.,
RA Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K.,
RA Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S.,
RA Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I.,
RA Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A.,
RA Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J.,
RA Birney E., Hayashizaki Y.;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Forms a voltage-independent potassium channel that is
CC activated by intracellular calcium. Activation is followed by
CC membrane hyperpolarization which promotes calcium influx. The
CC channel is blocked by clotrimazole and charybdotoxin but is
CC insensitive to apamin.
CC -!- SUBUNIT: Heterotetramer of potassium channel proteins (Probable).
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.
CC --------------------------------------------------------------------------
DR EMBL; AF042487; AAC32051.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF072884; AAC32829.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AK010943; BAB27283.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC010274; AAH10274.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P70604; 1KKD. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR Ensembl; ENSMUSG00000054342; Mus_musculus
DR MGI; MGI:1277957; Kcnn4.
DR GO; GO:0005887; C:integral to plasma membrane; IC.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IDA.
DR GO; GO:0050714; P:positive regulation of protein secretion; IDA.
DR InterPro; IPR004178; CaM_bd.
DR InterPro; IPR001622; K+channel_pore.
DR InterPro; IPR003091; K_channel.
DR InterPro; IPR011996; SK.
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 CMR; O89109.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; O89109.
DR ProtoNet; O89109.
DR ProtoMap; O89109.
DR PRESAGE; O89109.
DR DIP; O89109.
DR ModBase; O89109.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Calmodulin-binding; Ion transport; Ionic channel; Transmembrane;
KW Transport.
FT TRANSMEM 30 50 Segment S1 (Potential).
FT TRANSMEM 59 79 Segment S2 (Potential).
FT TRANSMEM 105 121 Segment S3 (Potential).
FT TRANSMEM 141 161 Segment S4 (Potential).
FT TRANSMEM 205 225 Segment S5 (Potential).
FT TRANSMEM 239 259 Segment H5 (pore-forming) (Potential).
FT TRANSMEM 263 283 Segment S6 (Potential).
FT REGION 284 345 Calmodulin-binding (By similarity).
FT COMPBIAS 413 416 Poly-Gln.
FT CONFLICT 181 181 G -> E (in Ref. 3).
SQ SEQUENCE 425 AA; 47784 MW; DCD2FC86BDD69A73 CRC64;
MGGELVTGLG ALRRRKRLLE QEKRVAGWAL VLAGTGIGLM VLHAEMLWFL GCKWVLYLLL
VKCLITLSTA FLLCLIVVFH AKEVQLFMTD NGLRDWRVAL TRRQVAQILL ELLVCGVHPV
PLRSPHCALA GEATDAQPWP GFLGEGEALL SLAMLLRLYL VPRAVLLRSG VLLNASYRSI
GALNQVRFRH WFVAKLYMNT HPGRLLLGLT LGLWLTTAWV LSVAERQAVN ATGHLTDTLW
LIPITFLTIG YGDVVPGTMW GKIVCLCTGV MGVCCTALLV AVVARKLEFN KAEKHVHNFM
MDIHYAKEMK ESAARLLQEA WMYYKHTRRK DSRAARRHQR KMLAAIHTFR QVRLKHRKLR
EQVNSMVDIS KMHMILCDLQ LGLSSSHRAL EKRIDGLAGK LDALTELLGT ALQQQQLPEP
SQEAT
//