ID KCNN3_HUMAN Reviewed; 736 AA.
AC Q9UGI6; B1ANX0; O43517; Q8WXG7;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 01-MAY-2013, entry version 108.
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 [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 [6]
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 [7]
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=2;
CC Name=1;
CC IsoId=Q9UGI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGI6-2; Sequence=VSP_039461, VSP_039462;
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; 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; EAW53182.1; -; Genomic_DNA.
DR EMBL; BC042147; AAH42147.1; -; mRNA.
DR IPI; IPI00032465; -.
DR IPI; IPI00395734; -.
DR RefSeq; NP_001191016.1; NM_001204087.1.
DR RefSeq; NP_002240.3; NM_002249.5.
DR RefSeq; NP_740752.1; NM_170782.2.
DR UniGene; Hs.490765; -.
DR ProteinModelPortal; Q9UGI6; -.
DR STRING; 9606.ENSP00000271915; -.
DR PhosphoSite; Q9UGI6; -.
DR DMDM; 17367120; -.
DR PaxDb; Q9UGI6; -.
DR PRIDE; Q9UGI6; -.
DR DNASU; 3782; -.
DR Ensembl; ENST00000271915; ENSP00000271915; ENSG00000143603.
DR Ensembl; ENST00000361147; ENSP00000354764; ENSG00000143603.
DR GeneID; 3782; -.
DR KEGG; hsa:3782; -.
DR UCSC; uc001ffo.3; human.
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; EOG49CQ7G; -.
DR Reactome; REACT_13685; Neuronal System.
DR BindingDB; Q9UGI6; -.
DR ChEMBL; CHEMBL3381; -.
DR GenomeRNAi; 3782; -.
DR NextBio; 14843; -.
DR ArrayExpress; Q9UGI6; -.
DR Bgee; Q9UGI6; -.
DR CleanEx; HS_KCNN3; -.
DR Genevestigator; Q9UGI6; -.
DR GermOnline; ENSG00000143603; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; IEA:Compara.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IEA:InterPro.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR InterPro; IPR004178; CaM-bd_dom.
DR InterPro; IPR013099; Ion_trans_2.
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; CaM_bd; 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 41 Poly-Gln.
FT COMPBIAS 42 48 Poly-Pro.
FT COMPBIAS 65 85 Poly-Gln.
FT COMPBIAS 688 692 Poly-Gln.
FT COMPBIAS 732 735 Poly-Ser.
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
//
