KCNN3_PIG
ID KCNN3_PIG Reviewed; 724 AA.
AC P58392;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 25-MAY-2022, entry version 99.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Coronary artery;
RX PubMed=11877319; DOI=10.1038/sj.bjp.0704551;
RA Burnham M.P., Bychkov R., Feletou M., Richards G.R., Vanhoutte P.M.,
RA Weston A.H., Edwards G.;
RT "Characterization of an apamin-sensitive small-conductance Ca(2+)-activated
RT K(+) channel in porcine coronary artery endothelium: relevance to EDHF.";
RL Br. J. Pharmacol. 135:1133-1143(2002).
CC -!- FUNCTION: Forms a voltage-independent potassium channel activated by
CC intracellular calcium (PubMed:11877319). Activation is followed by
CC membrane hyperpolarization (PubMed:11877319). Thought to regulate
CC neuronal excitability by contributing to the slow component of synaptic
CC afterhyperpolarization (PubMed:11877319).
CC {ECO:0000269|PubMed:11877319}.
CC -!- ACTIVITY REGULATION: Inhibited by bee venom neurotoxin apamin.
CC {ECO:0000269|PubMed:11877319}.
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; AY038049; AAK71498.1; -; mRNA.
DR RefSeq; NP_999150.1; NM_213985.1.
DR AlphaFoldDB; P58392; -.
DR SMR; P58392; -.
DR STRING; 9823.ENSSSCP00000006973; -.
DR PRIDE; P58392; -.
DR Ensembl; ENSSSCT00015072349; ENSSSCP00015029018; ENSSSCG00015054109.
DR GeneID; 397045; -.
DR KEGG; ssc:397045; -.
DR CTD; 3782; -.
DR InParanoid; P58392; -.
DR OrthoDB; 907751at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
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..724
FT /note="Small conductance calcium-activated potassium
FT channel protein 3"
FT /id="PRO_0000155015"
FT TRANSMEM 281..301
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 487..507
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..630
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 702..724
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 31..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58391"
SQ SEQUENCE 724 AA; 80372 MW; AFB689A935B4196F CRC64;
MDTSGHFHDS GVGDLDEDPK CPCPSSGDEQ QQQQPPPPPP PPAPPAAPQQ PPGPPLQPQP
LQLQQQQQQQ QQQPPHPLSQ LAQLQSQPVH PGLLHSSPTA FRAPPSSNST AILHPSSRQG
SQLNLNDHLL GHSPSSTATS GPGGGGRHRQ ASPLVHRRDS NPFTEIAMSS CKYSGGVMKP
LSRLSASRRN LIEAEPEGQP LQLFSPSNPP EIIISSREDN HAHQTLLHHP NATHNHQHAG
TTASSTTFPK ANKRKNQNIG YKLGHRRALF EKRKRLSDYA LIFGMFGIVV MVIETELSWG
LYSKDSMFSL ALKCLISLST IILLGLIIAY HTREVQLFVI DNGADDWRIA MTYERILYIS
LEMLVCAIHP IPGEYKFFWT ARLAFSYTPS RAEADVDIIL SIPMFLRLYL IARVMLLHSK
LFTDASSRSI GALNKINFNT RFVMKTLMTI CPGTVLLVFS ISLWIIAAWT VRVCERYHDQ
QDVTSNFLGA MWLISITFLS IGYGDMVPHT YCGKGVCLLT GIMGAGCTAL VVAVVARKLE
LTKAEKHVHN FMMDTQLTKR IKNAAANVLR ETWLIYKHTK LLKKIDHAKV RKHQRKFLQA
IHQLRSVKME QRKLSDQANT LVDLSKMQNV MYDLITELND RSEDLEKQIG SLESKLEHLT
ASFNSLPLLI ADTLRQQQQQ LLSALMEARG VSVAVGTTHT PLSDSPIGVS STSFPTPYTS
SSSC
