KCNN3_MOUSE
ID KCNN3_MOUSE Reviewed; 732 AA.
AC P58391; Q3UUY9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Small conductance calcium-activated potassium channel protein 3;
DE Short=SK3;
DE Short=SKCa 3;
DE Short=SKCa3;
DE AltName: Full=KCa2.3;
GN Name=Kcnn3; Synonyms=Sk3;
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 [MRNA], FUNCTION, AND ACTIVITY REGULATION.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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).
CC -!- FUNCTION: Forms a voltage-independent potassium channel activated by
CC intracellular calcium (PubMed:11557517). Activation is followed by
CC membrane hyperpolarization (By similarity). Thought to regulate
CC neuronal excitability by contributing to the slow component of synaptic
CC afterhyperpolarization (By similarity). {ECO:0000250|UniProtKB:P70605,
CC ECO:0000269|PubMed:11557517}.
CC -!- ACTIVITY REGULATION: Inhibited by bee venom neurotoxin apamin.
CC {ECO:0000269|PubMed:11557517}.
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 with CALM1
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UGI6}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in atrial and ventricular
CC myocytes (at protein level). {ECO:0000269|PubMed:16055520}.
CC -!- SIMILARITY: Belongs to the potassium channel KCNN family. KCa2.3/KCNN3
CC subfamily. {ECO:0000305}.
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DR EMBL; AF357241; AAK48902.1; -; mRNA.
DR EMBL; AK137738; BAE23484.1; -; mRNA.
DR EMBL; AC166364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC171273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106769; AAI06770.1; -; mRNA.
DR EMBL; BC106770; AAI06771.1; -; mRNA.
DR CCDS; CCDS38495.1; -.
DR RefSeq; NP_536714.2; NM_080466.2.
DR AlphaFoldDB; P58391; -.
DR SMR; P58391; -.
DR STRING; 10090.ENSMUSP00000000811; -.
DR GuidetoPHARMACOLOGY; 383; -.
DR iPTMnet; P58391; -.
DR PhosphoSitePlus; P58391; -.
DR PaxDb; P58391; -.
DR PeptideAtlas; P58391; -.
DR PRIDE; P58391; -.
DR ProteomicsDB; 268963; -.
DR Antibodypedia; 20402; 177 antibodies from 28 providers.
DR DNASU; 140493; -.
DR Ensembl; ENSMUST00000000811; ENSMUSP00000000811; ENSMUSG00000000794.
DR GeneID; 140493; -.
DR KEGG; mmu:140493; -.
DR UCSC; uc012cso.1; mouse.
DR CTD; 3782; -.
DR MGI; MGI:2153183; Kcnn3.
DR VEuPathDB; HostDB:ENSMUSG00000000794; -.
DR eggNOG; KOG3684; Eukaryota.
DR GeneTree; ENSGT00950000182904; -.
DR HOGENOM; CLU_014617_1_2_1; -.
DR InParanoid; P58391; -.
DR OMA; EDPPYGH; -.
DR OrthoDB; 907751at2759; -.
DR PhylomeDB; P58391; -.
DR TreeFam; TF315015; -.
DR Reactome; R-MMU-1296052; Ca2+ activated K+ channels.
DR BioGRID-ORCS; 140493; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Kcnn3; mouse.
DR PRO; PR:P58391; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P58391; protein.
DR Bgee; ENSMUSG00000000794; Expressed in embryonic brain and 48 other tissues.
DR Genevisible; P58391; MM.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; ISO:MGI.
DR GO; GO:0006811; P:ion transport; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006813; P:potassium ion 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..732
FT /note="Small conductance calcium-activated potassium
FT channel protein 3"
FT /id="PRO_0000155014"
FT TRANSMEM 289..309
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 495..515
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..638
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 704..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 80
FT /note="Missing (in Ref. 1; AAK48902)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="L -> F (in Ref. 1; AAK48902)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="A -> T (in Ref. 1; AAK48902)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="I -> V (in Ref. 1; AAK48902)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 81333 MW; 62347E83FFE9DC9B CRC64;
MDTSGHFHDS GVGDLDEDPK CPCPSSGDEQ QQQQQPPPPP APPAVPQQPP GPLLQPQPPQ
PQQQQSQQQQ QQQSQQQQQQ APLHPLPQLA QLQSQLVHPG LLHSSPTAFR APTSANSTAI
LHPSSRQGSQ LNLNDHLLGH SPSSTATSGP GGGSRHRQAS PLVHRRDSNP FTEIAMSSCK
YSGGVMKPLS RLSASRRNLI EAEPEGQPLQ LFSPSNPPEI IISSREDNHA HQTLLHHPNA
THNHQHAGTT AGSTTFPKAN KRKNQNIGYK LGHRRALFEK RKRLSDYALI FGMFGIVVMV
IETELSWGLY SKDSMFSLAL KCLISLSTVI LLGLIIAYHT REVQLFVIDN GADDWRIAMT
YERILYISLE MLVCAIHPIP GEYKFFWTAR LAFSYTPSRA EADVDIILSI PMFLRLYLIA
RVMLLHSKLF TDASSRSIGA LNKINFNTRF VMKTLMTICP GTVLLVFSIS LWIIAAWTVR
VCERYHDQQD VTSNFLGAMW LISITFLSIG YGDMVPHTYC GKGVCLLTGI MGAGCTALVV
AVVARKLELT KAEKHVHNFM MDTQLTKRIK NAAANVLRET WLIYKHTKLL KKIDHAKVRK
HQRKFLQAIH QLRGVKMEQR KLSDQANTLV DLSKMQNVMY DLITELNDRS EDLEKQIGSL
ESKLEHLTAS FNSLPLLIAD TLRQQQQQLL TAFVEARGIS VAVGTSHAPP SDSPIGISST
SFPTPYTSSS SC
