KCNN2_MOUSE
ID KCNN2_MOUSE Reviewed; 839 AA.
AC P58390; E9QNY5; Q3UF29; Q540U9; Q8CCH4;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Small conductance calcium-activated potassium channel protein 2;
DE Short=SK2;
DE Short=SKCa 2;
DE Short=SKCa2;
DE AltName: Full=KCa2.2;
GN Name=Kcnn2; Synonyms=Sk2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Sympathetic ganglion, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 241-839, FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=C3H/HeJ; TISSUE=Cochlea;
RX PubMed=14657188; DOI=10.1152/jn.00630.2003;
RA Nie L., Song H., Chen M.F., Chiamvimonvat N., Beisel K.W., Yamoah E.N.,
RA Vazquez A.E.;
RT "Cloning and expression of a small-conductance Ca(2+)-activated K+ channel
RT from the mouse cochlea: coexpression with alpha9/alpha10 acetylcholine
RT receptors.";
RL J. Neurophysiol. 91:1536-1544(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-839.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 266-839, FUNCTION, ACTIVITY REGULATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Colon;
RX PubMed=11557517; DOI=10.1152/ajpgi.2001.281.4.g964;
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).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 266-839, FUNCTION, ACTIVITY REGULATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Heart;
RX PubMed=13679367; DOI=10.1074/jbc.m307508200;
RA Xu Y., Tuteja D., Zhang Z., Xu D., Zhang Y., Rodriguez J., Nie L.,
RA Tuxson H.R., Young J.N., Glatter K.A., Vazquez A.E., Yamoah E.N.,
RA Chiamvimonvat N.;
RT "Molecular identification and functional roles of a Ca(2+)-activated K+
RT channel in human and mouse hearts.";
RL J. Biol. Chem. 278:49085-49094(2003).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=16055520; DOI=10.1152/ajpheart.00534.2005;
RA Tuteja D., Xu D., Timofeyev V., Lu L., Sharma D., Zhang Z., Xu Y., Nie L.,
RA Vazquez A.E., Young J.N., Glatter K.A., Chiamvimonvat N.;
RT "Differential expression of small-conductance Ca2+-activated K+ channels
RT SK1, SK2, and SK3 in mouse atrial and ventricular myocytes.";
RL Am. J. Physiol. 289:H2714-H2723(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH MPP2.
RX PubMed=26880549; DOI=10.7554/elife.12637;
RA Kim G., Lujan R., Schwenk J., Kelley M.H., Aguado C., Watanabe M.,
RA Fakler B., Maylie J., Adelman J.P.;
RT "Membrane palmitoylated protein 2 is a synaptic scaffold protein required
RT for synaptic SK2-containing channel function.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Forms a voltage-independent potassium channel activated by
CC intracellular calcium (PubMed:11557517, PubMed:13679367,
CC PubMed:14657188). Activation is followed by membrane hyperpolarization.
CC Thought to regulate neuronal excitability by contributing to the slow
CC component of synaptic afterhyperpolarization.
CC {ECO:0000269|PubMed:11557517, ECO:0000269|PubMed:13679367,
CC ECO:0000269|PubMed:14657188}.
CC -!- ACTIVITY REGULATION: Inhibited by bee venom neurotoxin apamin
CC (PubMed:11557517, PubMed:13679367, PubMed:14657188). Inhibited by UCL
CC 1684 and tetraethylammonium (TEA) (By similarity).
CC {ECO:0000250|UniProtKB:P70604, ECO:0000269|PubMed:11557517,
CC ECO:0000269|PubMed:13679367, ECO:0000269|PubMed:14657188}.
CC -!- SUBUNIT: Heterooligomer. The complex is composed of 4 channel subunits
CC each of which binds to a calmodulin subunit which regulates the channel
CC activity through calcium-binding (By similarity). Interacts (via N-
CC terminal domain) with MPP2 (PubMed:26880549).
CC {ECO:0000250|UniProtKB:P70604, ECO:0000269|PubMed:26880549}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in atrial and ventricular myocytes with
CC higher levels in atrial myocytes (at protein level). Highly expressed
CC in brain, liver and colon with low levels in kidney and testis. In
CC colon, detected in smooth muscle cells. {ECO:0000269|PubMed:11557517,
CC ECO:0000269|PubMed:13679367, ECO:0000269|PubMed:16055520}.
CC -!- SIMILARITY: Belongs to the potassium channel KCNN family. KCa2.2/KCNN2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI25476.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI37657.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM88568.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC28176.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE28732.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EDL09992.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK033158; BAC28176.1; ALT_FRAME; mRNA.
DR EMBL; AK149082; BAE28732.1; ALT_INIT; mRNA.
DR EMBL; AC099590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC101593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466528; EDL09992.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY123778; AAM88568.1; ALT_INIT; mRNA.
DR EMBL; BC125475; AAI25476.1; ALT_INIT; mRNA.
DR EMBL; BC137656; AAI37657.1; ALT_INIT; mRNA.
DR EMBL; AF357240; AAK48901.1; -; mRNA.
DR EMBL; AF533008; AAQ10283.1; -; mRNA.
DR RefSeq; NP_001299834.1; NM_001312905.1.
DR RefSeq; NP_536713.1; NM_080465.2.
DR AlphaFoldDB; P58390; -.
DR BMRB; P58390; -.
DR SMR; P58390; -.
DR BioGRID; 228265; 1.
DR STRING; 10090.ENSMUSP00000067884; -.
DR GuidetoPHARMACOLOGY; 382; -.
DR iPTMnet; P58390; -.
DR PhosphoSitePlus; P58390; -.
DR MaxQB; P58390; -.
DR PaxDb; P58390; -.
DR PRIDE; P58390; -.
DR ProteomicsDB; 269205; -.
DR ABCD; P58390; 1 sequenced antibody.
DR Antibodypedia; 13591; 127 antibodies from 30 providers.
DR DNASU; 140492; -.
DR Ensembl; ENSMUST00000066890; ENSMUSP00000067884; ENSMUSG00000054477.
DR GeneID; 140492; -.
DR KEGG; mmu:140492; -.
DR UCSC; uc008evd.1; mouse.
DR CTD; 3781; -.
DR MGI; MGI:2153182; Kcnn2.
DR VEuPathDB; HostDB:ENSMUSG00000054477; -.
DR eggNOG; KOG3684; Eukaryota.
DR GeneTree; ENSGT00950000182904; -.
DR InParanoid; P58390; -.
DR PhylomeDB; P58390; -.
DR TreeFam; TF315015; -.
DR Reactome; R-MMU-1296052; Ca2+ activated K+ channels.
DR BioGRID-ORCS; 140492; 1 hit in 33 CRISPR screens.
DR ChiTaRS; Kcnn2; mouse.
DR PRO; PR:P58390; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P58390; protein.
DR Bgee; ENSMUSG00000054477; Expressed in adrenal gland and 184 other tissues.
DR ExpressionAtlas; P58390; baseline and differential.
DR Genevisible; P58390; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:MGI.
DR GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IMP:UniProtKB.
DR GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:MGI.
DR InterPro; IPR004178; CaM-bd_dom.
DR InterPro; IPR036122; CaM-bd_dom_sf.
DR InterPro; IPR015449; K_chnl_Ca-activ_SK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR10153; PTHR10153; 1.
DR Pfam; PF02888; CaMBD; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR Pfam; PF03530; SK_channel; 1.
DR PRINTS; PR01451; SKCHANNEL.
DR SMART; SM01053; CaMBD; 1.
DR SUPFAM; SSF81327; SSF81327; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..839
FT /note="Small conductance calcium-activated potassium
FT channel protein 2"
FT /id="PRO_0000155011"
FT TRANSMEM 398..418
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 605..625
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..748
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 810..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 420
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P70604"
FT CONFLICT 87
FT /note="Q -> K (in Ref. 1; BAC28176)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="S -> R (in Ref. 1; BAC28176)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="D -> N (in Ref. 1; BAC28176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 839 AA; 91604 MW; 5FF152099CDC2885 CRC64;
MPIVLVRPTN RTRRLDSTGA GMGPSSHQQQ ESPLPTITHC AGCTTAWSPC SFNSSDMETP
LQFQRGFFPE QPPPPPRSSH LHCQQQQQSQ DKPCAPFAPL PHPHHHPHLA HQQPGSGGSS
PCLRCNSCAS SGAPAAGAGA GDNLSLLLRT SSPGGAFRTR TSSPLSGSSC CCCCSSRRGS
QLNVSELTPS SHASALRQQY AQQPASASQY HQCHSLQPAT SPTGSLGSLG SGPPLSHHHH
HPHPAHHQHH QPQARRESNP FTEIAMSSCR YNGGVMRPLS NLSSSRRNLQ EMDSEAQPLQ
PPASVVGGGG GASSPSAAAA ASSSAPEIVV SKPEHNNSNN LALYGTGGGG STGGGGGGSG
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 ETQMENYDKH VSYNAERSRS SSRRRRSSST APPTSSESS
