Swiss-Prot entry
ID KCNN3_HUMAN STANDARD; PRT; 736 AA.
AC Q9UGI6; O43517;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE Small conductance calcium-activated potassium channel protein 3 (SK3)
DE (SKCa3).
GN Name=KCNN3; Synonyms=K3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND POLYMORPHISM OF POLY-GLN REGION.
RX MEDLINE=98150774; PubMed=9491810 [NCBI, ExPASy, EBI, Israel, Japan]; 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.
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.
RX MEDLINE=21392854; PubMed=11501944 [NCBI, ExPASy, EBI, Israel, Japan]; 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).
CC -!- FUNCTION: Forms a voltage-independent potassium channel activated
CC by intracellular calcium. Activation is followed by membrane
CC hyperpolarization. Thought to regulate neuronal excitabilty by
CC contributing to the slow component of synaptic
CC afterhyperpolarization. The channel is blocked by apamin.
CC -!- SUBUNIT: Hetero-oligomer. 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: Integral membrane protein.
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 --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; AF031815; AAC26099.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AJ251016; CAB61331.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF336797; AAK15345.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P70604; 1KKD. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q9UGI6; 549-640.
DR Ensembl; ENSG00000143603; Homo_sapiens
DR HGNC; HGNC:6292; KCNN3.
DR CleanEx; HGNC:6292; KCNN3.
DR MIM; 602983; -. [NCBI / EBI]
DR GeneCards; KCNN3.
DR GeneLynx; KCNN3.
DR GenAtlas; KCNN3.
DR SOURCE; KCNN3.
DR InterPro; IPR004178; CaM_bd.
DR InterPro; IPR001622; K+channel_pore.
DR InterPro; IPR011996; SK.
DR InterPro; IPR003931; SK_channel.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF02888; CaMBD; 1.
DR Pfam; PF03530; SK_channel; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR01451; SKCHANNEL.
DR CMR; Q9UGI6.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q9UGI6.
DR ProtoNet; Q9UGI6.
DR ProtoMap; Q9UGI6.
DR PRESAGE; Q9UGI6.
DR DIP; Q9UGI6.
DR ModBase; Q9UGI6.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Calmodulin-binding; Ion transport; Ionic channel; Polymorphism;
KW Transmembrane; Transport.
FT TRANSMEM 293 313 Segment S1 (Potential).
FT TRANSMEM 320 340 Segment S2 (Potential).
FT TRANSMEM 371 391 Segment S3 (Potential).
FT TRANSMEM 410 430 Segment S4 (Potential).
FT TRANSMEM 459 479 Segment S5 (Potential).
FT TRANSMEM 499 519 Segment H5 (pore-forming) (Potential).
FT TRANSMEM 528 548 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 VARIANT 81 85 Missing.
FT /FTId=VAR_012204.
FT CONFLICT 254 254 T -> A (in Ref. 1).
FT CONFLICT 281 281 L -> P (in Ref. 1).
FT CONFLICT 347 347 V -> A (in Ref. 1).
FT CONFLICT 485 485 V -> A (in Ref. 1).
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
//