KCNN3_RAT
ID KCNN3_RAT Reviewed; 732 AA.
AC P70605; Q9EQ81; Q9ERQ4;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 3.
DT 25-MAY-2022, entry version 147.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8781233; DOI=10.1126/science.273.5282.1709;
RA Koehler M., Hirschberg B., Bond C.T., Kinzie J.M., Marrion N.V., Maylie J.,
RA Adelman J.P.;
RT "Small-conductance, calcium-activated potassium channels from mammalian
RT brain.";
RL Science 273:1709-1714(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=11533126; DOI=10.1111/j.1469-7793.2001.00323.x;
RA Hosseini R., Benton D.C., Dunn P.M., Jenkinson D.H., Moss G.W.;
RT "SK3 is an important component of K(+) channels mediating the
RT afterhyperpolarization in cultured rat SCG neurones.";
RL J. Physiol. (Lond.) 535:323-334(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, AND VARIANT
RP 78-GLN-GLN-79 DEL.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=11245600; DOI=10.1152/ajpcell.2001.280.4.c836;
RA Barfod E.T., Moore A.L., Lidofsky S.D.;
RT "Cloning and functional expression of a liver isoform of the small
RT conductance Ca2+-activated K+ channel SK3.";
RL Am. J. Physiol. 280:C836-C842(2001).
CC -!- FUNCTION: Forms a voltage-independent potassium channel activated by
CC intracellular calcium (PubMed:11533126, PubMed:11245600). Activation is
CC followed by membrane hyperpolarization (PubMed:11533126). Thought to
CC regulate neuronal excitability by contributing to the slow component of
CC synaptic afterhyperpolarization (PubMed:11533126).
CC {ECO:0000269|PubMed:11245600, ECO:0000269|PubMed:11533126}.
CC -!- ACTIVITY REGULATION: Inhibited by bee venom neurotoxin apamin.
CC {ECO:0000269|PubMed:11245600, ECO:0000269|PubMed:11533126}.
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 -!- SIMILARITY: Belongs to the potassium channel KCNN family. KCa2.3/KCNN3
CC subfamily. {ECO:0000305}.
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DR EMBL; U69884; AAB81653.1; -; mRNA.
DR EMBL; AF292389; AAG13967.1; -; mRNA.
DR EMBL; AF284345; AAG38878.1; -; mRNA.
DR RefSeq; NP_062188.2; NM_019315.2.
DR AlphaFoldDB; P70605; -.
DR SMR; P70605; -.
DR IntAct; P70605; 1.
DR STRING; 10116.ENSRNOP00000028117; -.
DR BindingDB; P70605; -.
DR ChEMBL; CHEMBL3780; -.
DR DrugCentral; P70605; -.
DR GuidetoPHARMACOLOGY; 383; -.
DR PhosphoSitePlus; P70605; -.
DR PaxDb; P70605; -.
DR PRIDE; P70605; -.
DR GeneID; 54263; -.
DR KEGG; rno:54263; -.
DR UCSC; RGD:2964; rat.
DR CTD; 3782; -.
DR RGD; 2964; Kcnn3.
DR eggNOG; KOG3684; Eukaryota.
DR InParanoid; P70605; -.
DR OrthoDB; 907751at2759; -.
DR PhylomeDB; P70605; -.
DR Reactome; R-RNO-1296052; Ca2+ activated K+ channels.
DR PRO; PR:P70605; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IMP:RGD.
DR GO; GO:0006811; P:ion transport; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006813; P:potassium ion transport; IMP:RGD.
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; 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 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_0000155016"
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 103..162
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 35..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..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:0000250|UniProtKB:P58391"
FT VARIANT 78..79
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:11245600"
FT CONFLICT 9
FT /note="D -> E (in Ref. 1; AAB81653)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="L -> V (in Ref. 1; AAB81653)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="L -> V (in Ref. 1; AAB81653)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="L -> V (in Ref. 1; AAB81653)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="S -> N (in Ref. 1; AAB81653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 81448 MW; C44579B78EFB6ADA CRC64;
MDTSGHFHDS GVGDLDEDPK CPCPSSGDEQ QQQQQPPPPS APPAVPQQPP GPLLQPQPPQ
LQQQQQQQQQ QQQQQQQQQQ APLHPLPQLA QLQSQLVHPG LLHSSPTAFR APNSANSTAI
LHPSSRQGSQ LNLNDHLLGH SPSSTATSGP GGGSRHRQAS PLVHRRDSNP FTEIAMSSCK
YSGGVMKPLS RLSASRRNLI EAEPEGQPLQ LFSPSNPPEI IISSREDNHA HQTLLHHPNA
THNHQHAGTT AGSTTFPKAN KRKNQNIGYK LGHRRALFEK RKRLSDYALI FGMFGIVVMV
IETELSWGLY SKDSMFSLAL KCLISLSTII 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
