KCNN1_RAT
ID KCNN1_RAT Reviewed; 536 AA.
AC P70606;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Small conductance calcium-activated potassium channel protein 1;
DE Short=SK1;
DE Short=SKCa 1;
DE Short=SKCa1;
DE AltName: Full=KCa2.1;
GN Name=Kcnn1; Synonyms=Sk1;
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 TISSUE=Brain;
RX PubMed=9380751; DOI=10.1073/pnas.94.20.11013;
RA Joiner W.J., Wang L.-Y., Tang M.D., Kaczmarek L.K.;
RT "hSK4, a member of a novel subfamily of calcium-activated potassium
RT channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11013-11018(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 79-536, FUNCTION, AND ACTIVITY REGULATION.
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Forms a voltage-independent potassium channel activated by
CC intracellular calcium (PubMed:8781233). Activation is followed by
CC membrane hyperpolarization (By similarity). Thought to regulate
CC neuronal excitability by contributing to the slow component of synaptic
CC afterhyperpolarization (By similarity). {ECO:0000250|UniProtKB:Q9EQR3,
CC ECO:0000269|PubMed:8781233}.
CC -!- ACTIVITY REGULATION: Inhibited by bee venom neurotoxin apamin
CC (PubMed:8781233). Inhibited by d-tubocurarine and tetraethylammonium
CC (TEA) (By similarity). {ECO:0000250|UniProtKB:Q92952,
CC ECO:0000269|PubMed:8781233}.
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed including brain.
CC -!- SIMILARITY: Belongs to the potassium channel KCNN family. KCa2.1/KCNN1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF000973; AAB82740.1; -; mRNA.
DR EMBL; U69885; AAB09564.1; -; mRNA.
DR RefSeq; NP_062186.1; NM_019313.1.
DR RefSeq; XP_017455721.1; XM_017600232.1.
DR AlphaFoldDB; P70606; -.
DR SMR; P70606; -.
DR IntAct; P70606; 1.
DR MINT; P70606; -.
DR STRING; 10116.ENSRNOP00000042517; -.
DR BindingDB; P70606; -.
DR ChEMBL; CHEMBL3743; -.
DR iPTMnet; P70606; -.
DR PhosphoSitePlus; P70606; -.
DR PaxDb; P70606; -.
DR PRIDE; P70606; -.
DR GeneID; 54261; -.
DR KEGG; rno:54261; -.
DR CTD; 3780; -.
DR RGD; 2962; Kcnn1.
DR VEuPathDB; HostDB:ENSRNOG00000029264; -.
DR eggNOG; KOG3684; Eukaryota.
DR InParanoid; P70606; -.
DR OMA; PPCQWPP; -.
DR OrthoDB; 907751at2759; -.
DR PhylomeDB; P70606; -.
DR Reactome; R-RNO-1296052; Ca2+ activated K+ channels.
DR PRO; PR:P70606; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000029264; Expressed in frontal cortex and 16 other tissues.
DR ExpressionAtlas; P70606; baseline and differential.
DR Genevisible; P70606; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO: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 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 1: Evidence at protein level;
KW Calmodulin-binding; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..536
FT /note="Small conductance calcium-activated potassium
FT channel protein 1"
FT /id="PRO_0000155009"
FT TRANSMEM 107..127
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 342..362
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..459
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 514..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 59215 MW; 97FF82071B0BE36A CRC64;
MSSRSHNGSV GRPLGSGPGF LGWEPVDPEA GRPRQPTQGP GLQMMAKGQP AGLSPSGPRG
HSQAQEEEEE EEDEDRPGSG KPPTVSHRLG HRRALFEKRK RLSDYALIFG MFGIVVMVTE
TELSWGVYTK ESLCSFALKC LISLSTVILL GLVILYHARE IQLFLVDNGA DDWRIAMTWE
RVSLISLELA VCAIHPVPGH YRFTWTARLA FSLVPSAAEA DVDVLLSIPM FLRLYLLARV
MLLHSRIFTD ASSRSIGALN RVTFNTRFVT KTLMTICPGT VLLVFSISSW IVAAWTVRVC
ERYHDKQEVT SNFLGAMWLI SITFLSIGYG DMVPHTYCGK GVCLLTGIMG AGCTALVVAV
VARKLELTKA EKHVHNFMMD TQLTKRVKNA AANVLRETWL IYKHTRLVKK PDQSRVRKHQ
RKFLQAIHQA QKLRTVKIEQ GKVNDQANTL ADLAKAQSIA YEVVSELQAQ QEELEARLAA
LESRLDVLGA SLQALPSLIA QAICPLPPPW PGPSHLTTAA QSPQSHWLPT TASDCG
