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   24-JAN-2024, entry version 153.
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   GlyGen; P58391; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P58391; -.
DR   PhosphoSitePlus; P58391; -.
DR   PaxDb; 10090-ENSMUSP00000000811; -.
DR   PeptideAtlas; P58391; -.
DR   ProteomicsDB; 268963; -.
DR   Antibodypedia; 20402; 219 antibodies from 28 providers.
DR   DNASU; 140493; -.
DR   Ensembl; ENSMUST00000000811.8; ENSMUSP00000000811.8; ENSMUSG00000000794.10.
DR   GeneID; 140493; -.
DR   KEGG; mmu:140493; -.
DR   UCSC; uc012cso.1; mouse.
DR   AGR; MGI:2153183; -.
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; GGGCKHR; -.
DR   OrthoDB; 4200919at2759; -.
DR   PhylomeDB; P58391; -.
DR   TreeFam; TF315015; -.
DR   Reactome; R-MMU-1296052; Ca2+ activated K+ channels.
DR   BioGRID-ORCS; 140493; 3 hits in 77 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 49 other cell types or tissues.
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:0031594; C:neuromuscular junction; 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: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:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR   Gene3D; 1.10.287.70; -; 2.
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; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL; 1.
DR   PANTHER; PTHR10153:SF40; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL PROTEIN 3; 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; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   SUPFAM; SSF81327; Small-conductance potassium channel; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   Genevisible; P58391; MM.
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
//