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Database: UniProt
Entry: KCNN3_HUMAN
LinkDB: KCNN3_HUMAN
Original site: KCNN3_HUMAN 
ID   KCNN3_HUMAN             Reviewed;         736 AA.
AC   Q9UGI6; B1ANX0; O43517; Q86VF9; Q8WXG7;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   09-JUL-2014, entry version 120.
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=K3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND POLYMORPHISM OF POLY-GLN
RP   REGION.
RX   PubMed=9491810; DOI=10.1038/sj.mp.4000353;
RA   Chandy K.G., Fantino E., Wittekindt O., Kalman K., Tong L.-L.,
RA   Ho T.-H., Gutman G.A., Crocq M.-A., Ganguli R., Nimgaonkar V.,
RA   Morris-Rosendahl D.J., Gargus J.J.;
RT   "Isolation of a novel potassium channel gene hSKCa3 containing a
RT   polymorphic CAG repeat: a candidate for schizophrenia and bipolar
RT   disorder?";
RL   Mol. Psychiatry 3:32-37(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Terstappen G.C., Pula G., Chen M.X., Roncarati R.;
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Tomita H., Shakkottai V., Wulff H., Sun G., Potkin S.G., Bunney W.E.,
RA   Chandy G.K., Gargus J.J.;
RT   "Splice variants of small conductance calcium-activated potassium
RT   channel gene, KCNN3/ SKCa3 cause dominant-negative suppression of SKCa
RT   currents.";
RL   Am. J. Hum. Genet. 69S:569-569(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   PubMed=11501944; DOI=10.1007/s100380170046;
RA   Sun G., Tomita H., Shakkottai V.G., Gargus J.J.;
RT   "Genomic organization and promoter analysis of human KCNN3 gene.";
RL   J. Hum. Genet. 46:463-470(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX   PubMed=12808432; DOI=10.1038/sj.mp.4001271;
RA   Tomita H., Shakkottai V.G., Gutman G.A., Sun G., Bunney W.E.,
RA   Cahalan M.D., Chandy K.G., Gargus J.J.;
RT   "Novel truncated isoform of SK3 potassium channel is a potent
RT   dominant-negative regulator of SK currents: implications in
RT   schizophrenia.";
RL   Mol. Psychiatry 8:524-535(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lymph;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Forms a voltage-independent potassium channel activated
CC       by intracellular calcium. Activation is followed by membrane
CC       hyperpolarization. Thought to regulate neuronal excitability by
CC       contributing to the slow component of synaptic
CC       afterhyperpolarization. The channel is blocked by apamin.
CC   -!- SUBUNIT: Heterooligomer. 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: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9UGI6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UGI6-2; Sequence=VSP_039461, VSP_039462;
CC       Name=3; Synonyms=SK3-1B;
CC         IsoId=Q9UGI6-3; Sequence=VSP_047641;
CC         Note=Do not produce functional channels, but selectively
CC         suppresses endogenous SK3 currents, in a dominant-negative
CC         fashion. This dominant inhibitory effect extends to other
CC         members of the SK subfamily. Widely distributed in human tissues
CC         and is present at 20-60% of SK3 in the brain;
CC   -!- POLYMORPHISM: The second poly-Gln region of KCNN3 is highly
CC       polymorphic and the number of Gln varies from 12 to 28 in the
CC       population.
CC   -!- SIMILARITY: Belongs to the potassium channel KCNN family.
CC       KCa2.3/KCNN3 subfamily.
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DR   EMBL; AF031815; AAC26099.1; -; mRNA.
DR   EMBL; AJ251016; CAB61331.1; -; mRNA.
DR   EMBL; AF438203; AAL40801.1; -; mRNA.
DR   EMBL; AF336797; AAK15345.1; -; Genomic_DNA.
DR   EMBL; AY138900; AAN46636.1; -; mRNA.
DR   EMBL; AL390204; CAH71150.1; -; Genomic_DNA.
DR   EMBL; AL606500; CAH71150.1; JOINED; Genomic_DNA.
DR   EMBL; AL954342; CAH71150.1; JOINED; Genomic_DNA.
DR   EMBL; AL390204; CAH71151.1; -; Genomic_DNA.
DR   EMBL; AL606500; CAH71151.1; JOINED; Genomic_DNA.
DR   EMBL; AL954342; CAH71151.1; JOINED; Genomic_DNA.
DR   EMBL; AL606500; CAH71910.1; -; Genomic_DNA.
DR   EMBL; AL390204; CAH71910.1; JOINED; Genomic_DNA.
DR   EMBL; AL954342; CAH71910.1; JOINED; Genomic_DNA.
DR   EMBL; AL606500; CAH71911.1; -; Genomic_DNA.
DR   EMBL; AL390204; CAH71911.1; JOINED; Genomic_DNA.
DR   EMBL; AL954342; CAH71911.1; JOINED; Genomic_DNA.
DR   EMBL; AL954342; CAH72738.1; -; Genomic_DNA.
DR   EMBL; AL390204; CAH72738.1; JOINED; Genomic_DNA.
DR   EMBL; AL606500; CAH72738.1; JOINED; Genomic_DNA.
DR   EMBL; AL954342; CAH72739.1; -; Genomic_DNA.
DR   EMBL; AL390204; CAH72739.1; JOINED; Genomic_DNA.
DR   EMBL; AL606500; CAH72739.1; JOINED; Genomic_DNA.
DR   EMBL; CH471121; EAW53180.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53182.1; -; Genomic_DNA.
DR   EMBL; BC042147; AAH42147.1; -; mRNA.
DR   CCDS; CCDS1072.1; -. [Q9UGI6-2]
DR   RefSeq; NP_001191016.1; NM_001204087.1.
DR   RefSeq; NP_002240.3; NM_002249.5.
DR   RefSeq; NP_740752.1; NM_170782.2. [Q9UGI6-2]
DR   UniGene; Hs.490765; -.
DR   ProteinModelPortal; Q9UGI6; -.
DR   SMR; Q9UGI6; 480-679.
DR   BioGrid; 109983; 6.
DR   STRING; 9606.ENSP00000271915; -.
DR   BindingDB; Q9UGI6; -.
DR   ChEMBL; CHEMBL3381; -.
DR   GuidetoPHARMACOLOGY; 383; -.
DR   PhosphoSite; Q9UGI6; -.
DR   DMDM; 17367120; -.
DR   MaxQB; Q9UGI6; -.
DR   PaxDb; Q9UGI6; -.
DR   PRIDE; Q9UGI6; -.
DR   DNASU; 3782; -.
DR   Ensembl; ENST00000358505; ENSP00000351295; ENSG00000143603. [Q9UGI6-3]
DR   Ensembl; ENST00000361147; ENSP00000354764; ENSG00000143603. [Q9UGI6-2]
DR   GeneID; 3782; -.
DR   KEGG; hsa:3782; -.
DR   UCSC; uc001ffo.3; human. [Q9UGI6-2]
DR   UCSC; uc031ppq.1; human. [Q9UGI6-1]
DR   CTD; 3782; -.
DR   GeneCards; GC01M154680; -.
DR   H-InvDB; HIX0023527; -.
DR   HGNC; HGNC:6292; KCNN3.
DR   HPA; HPA017990; -.
DR   MIM; 602983; gene.
DR   neXtProt; NX_Q9UGI6; -.
DR   PharmGKB; PA30072; -.
DR   eggNOG; NOG320393; -.
DR   HOGENOM; HOG000276908; -.
DR   HOVERGEN; HBG052241; -.
DR   InParanoid; Q9UGI6; -.
DR   KO; K04944; -.
DR   OrthoDB; EOG73FQMC; -.
DR   PhylomeDB; Q9UGI6; -.
DR   TreeFam; TF315015; -.
DR   Reactome; REACT_13685; Neuronal System.
DR   GeneWiki; SK3; -.
DR   GenomeRNAi; 3782; -.
DR   NextBio; 14843; -.
DR   PRO; PR:Q9UGI6; -.
DR   ArrayExpress; Q9UGI6; -.
DR   Bgee; Q9UGI6; -.
DR   CleanEx; HS_KCNN3; -.
DR   Genevestigator; Q9UGI6; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IBA:RefGenome.
DR   GO; GO:0005886; C:plasma membrane; IBA:RefGenome.
DR   GO; GO:0005516; F:calmodulin binding; IBA:RefGenome.
DR   GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IBA:RefGenome.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:RefGenome.
DR   GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR   InterPro; IPR013099; 2pore_dom_K_chnl_dom.
DR   InterPro; IPR004178; CaM-bd_dom.
DR   InterPro; IPR015449; K_chnl_Ca-activ_SK.
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   2: Evidence at transcript level;
KW   Alternative splicing; Calmodulin-binding; Complete proteome;
KW   Ion channel; Ion transport; Membrane; Polymorphism;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    736       Small conductance calcium-activated
FT                                potassium channel protein 3.
FT                                /FTId=PRO_0000155013.
FT   TRANSMEM    293    313       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    320    340       Helical; Name=Segment S2; (Potential).
FT   TRANSMEM    371    391       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    410    430       Helical; Name=Segment S4; (Potential).
FT   TRANSMEM    459    479       Helical; Name=Segment S5; (Potential).
FT   INTRAMEM    499    519       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TRANSMEM    528    548       Helical; Name=Segment S6; (Potential).
FT   REGION      566    642       Calmodulin-binding (By similarity).
FT   COMPBIAS     30     99       Gln-rich.
FT   COMPBIAS     42     64       Pro-rich.
FT   COMPBIAS    688    692       Poly-Gln.
FT   COMPBIAS    732    735       Poly-Ser.
FT   VAR_SEQ       1    318       Missing (in isoform 3).
FT                                /FTId=VSP_047641.
FT   VAR_SEQ       1    310       Missing (in isoform 2).
FT                                /FTId=VSP_039461.
FT   VAR_SEQ     311    315       WGLYS -> MERPI (in isoform 2).
FT                                /FTId=VSP_039462.
FT   VARIANT      81     85       Missing.
FT                                /FTId=VAR_012204.
FT   CONFLICT    254    254       T -> A (in Ref. 1; AAC26099).
FT   CONFLICT    281    281       L -> P (in Ref. 1; AAC26099).
FT   CONFLICT    347    347       V -> A (in Ref. 1; AAC26099).
FT   CONFLICT    485    485       V -> A (in Ref. 1; AAC26099).
SQ   SEQUENCE   736 AA;  82026 MW;  CCD0CC1621FFAE9C CRC64;
     MDTSGHFHDS GVGDLDEDPK CPCPSSGDEQ QQQQQQQQQQ QPPPPAPPAA PQQPLGPSLQ
     PQPPQLQQQQ QQQQQQQQQQ QQQQQPPHPL SQLAQLQSQP VHPGLLHSSP TAFRAPPSSN
     STAILHPSSR QGSQLNLNDH LLGHSPSSTA TSGPGGGSRH RQASPLVHRR DSNPFTEIAM
     SSCKYSGGVM KPLSRLSASR RNLIEAETEG QPLQLFSPSN PPEIVISSRE DNHAHQTLLH
     HPNATHNHQH AGTTASSTTF PKANKRKNQN IGYKLGHRRA LFEKRKRLSD YALIFGMFGI
     VVMVIETELS WGLYSKDSMF SLALKCLISL STIILLGLII AYHTREVQLF VIDNGADDWR
     IAMTYERILY ISLEMLVCAI HPIPGEYKFF WTARLAFSYT PSRAEADVDI ILSIPMFLRL
     YLIARVMLLH SKLFTDASSR SIGALNKINF NTRFVMKTLM TICPGTVLLV FSISLWIIAA
     WTVRVCERYH DQQDVTSNFL GAMWLISITF LSIGYGDMVP HTYCGKGVCL LTGIMGAGCT
     ALVVAVVARK LELTKAEKHV HNFMMDTQLT KRIKNAAANV LRETWLIYKH TKLLKKIDHA
     KVRKHQRKFL QAIHQLRSVK MEQRKLSDQA NTLVDLSKMQ NVMYDLITEL NDRSEDLEKQ
     IGSLESKLEH LTASFNSLPL LIADTLRQQQ QQLLSAIIEA RGVSVAVGTT HTPISDSPIG
     VSSTSFPTPY TSSSSC
//
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