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 05-OCT-2010, entry version 84. 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 MEDLINE=98150774; 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 supression of SKCa RT currents."; RL Am. J. Hum. Genet. 69S:569-569(2001). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RX MEDLINE=21392854; 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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_002240.3; -. DR RefSeq; NP_740752.1; -. DR UniGene; Hs.490765; -. DR ProteinModelPortal; Q9UGI6; -. DR SMR; Q9UGI6; 466-550, 495-626, 549-640, 641-679. DR STRING; Q9UGI6; -. DR PhosphoSite; Q9UGI6; -. DR Ensembl; ENST00000271915; ENSP00000271915; ENSG00000143603. DR Ensembl; ENST00000361147; ENSP00000354764; ENSG00000143603. DR GeneID; 3782; -. DR KEGG; hsa:3782; -. DR CTD; 3782; -. DR GeneCards; GC01M154680; -. DR H-InvDB; HIX0023527; -. DR HGNC; HGNC:6292; KCNN3. DR MIM; 602983; gene. DR PharmGKB; PA30072; -. DR eggNOG; prNOG14887; -. DR HOVERGEN; HBG052241; -. DR InParanoid; Q9UGI6; -. DR NextBio; 14843; -. DR ArrayExpress; Q9UGI6; -. DR Bgee; Q9UGI6; -. DR CleanEx; HS_KCNN3; -. DR Genevestigator; Q9UGI6; -. DR GermOnline; ENSG00000143603; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR InterPro; IPR004178; CaM-bd_dom. DR InterPro; IPR013099; Ion_trans_2. DR InterPro; IPR015449; K_chnl_Ca-activ_SK. DR InterPro; IPR011996; K_chnl_Ca-activ_SK_con. DR InterPro; IPR003931; K_chnl_Ca-activ_SK_sub. DR PANTHER; PTHR10153; CaKChannelSK; 1. DR Pfam; PF02888; CaMBD; 1. DR Pfam; PF07885; Ion_trans_2; 1. DR Pfam; PF03530; SK_channel; 1. DR PRINTS; PR01451; SKCHANNEL. DR SUPFAM; SSF81327; CaM_bd; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Calmodulin-binding; Complete proteome; KW Ion transport; Ionic channel; Membrane; Polymorphism; Transmembrane; KW 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 //