KCNE3_RAT
ID KCNE3_RAT Reviewed; 107 AA.
AC Q9JJV7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Potassium voltage-gated channel subfamily E member 3;
DE AltName: Full=MinK-related peptide 2;
DE AltName: Full=Minimum potassium ion channel-related peptide 2;
DE AltName: Full=Potassium channel subunit beta MiRP2;
GN Name=Kcne3;
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=Wistar; TISSUE=Colon;
RX PubMed=11220365; DOI=10.1007/s002320010045;
RA Kunzelmann K., Huebner M., Schreiber R., Levy-Holzman R., Garty H.,
RA Bleich M., Warth R., Slavik M., von Hahn T., Greger R.;
RT "Cloning and function of the rat colonic epithelial K+ channel KVLQT1.";
RL J. Membr. Biol. 179:155-164(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INTERACTION WITH KCNB1, AND SUBCELLULAR LOCATION.
RX PubMed=12954870; DOI=10.1523/jneurosci.23-22-08077.2003;
RA McCrossan Z.A., Lewis A., Panaghie G., Jordan P.N., Christini D.J.,
RA Lerner D.J., Abbott G.W.;
RT "MinK-related peptide 2 modulates Kv2.1 and Kv3.1 potassium channels in
RT mammalian brain.";
RL J. Neurosci. 23:8077-8091(2003).
RN [4]
RP SUBUNIT, INTERACTION WITH KCNC2, AND SUBCELLULAR LOCATION.
RX PubMed=14679187; DOI=10.1074/jbc.m310501200;
RA Lewis A., McCrossan Z.A., Abbott G.W.;
RT "MinK, MiRP1, and MiRP2 diversify Kv3.1 and Kv3.2 potassium channel
RT gating.";
RL J. Biol. Chem. 279:7884-7892(2004).
RN [5]
RP INTERACTION WITH KCNQ1, AND FUNCTION.
RX PubMed=21911611; DOI=10.1113/jphysiol.2011.215772;
RA Alzamora R., O'Mahony F., Bustos V., Rapetti-Mauss R., Urbach V., Cid L.P.,
RA Sepulveda F.V., Harvey B.J.;
RT "Sexual dimorphism and oestrogen regulation of KCNE3 expression modulates
RT the functional properties of KCNQ1 K[+] channels.";
RL J. Physiol. (Lond.) 589:5091-5107(2011).
CC -!- FUNCTION: Ancillary protein that assembles as a beta subunit with a
CC voltage-gated potassium channel complex of pore-forming alpha subunits.
CC Modulates the gating kinetics and enhances stability of the channel
CC complex. Assembled with KCNB1 modulates the gating characteristics of
CC the delayed rectifier voltage-dependent potassium channel KCNB1
CC (PubMed:12954870). Associated with KCNC4/Kv3.4 is proposed to form the
CC subthreshold voltage-gated potassium channel in skeletal muscle and to
CC establish the resting membrane potential (RMP) in muscle cells (By
CC similarity). Associated with KCNQ1/KCLQT1 may form the intestinal cAMP-
CC stimulated potassium channel involved in chloride secretion that
CC produces a current with nearly instantaneous activation with a linear
CC current-voltage relationship (PubMed:21911611).
CC {ECO:0000250|UniProtKB:Q9Y6H6, ECO:0000269|PubMed:12954870,
CC ECO:0000269|PubMed:21911611}.
CC -!- SUBUNIT: Interacts with KCNB1 (PubMed:12954870). Interacts with KCNC2
CC (PubMed:14679187). Associates with KCNC4/Kv3.4 (By similarity).
CC Interacts with KCNQ1; produces a current with nearly instantaneous
CC activation with a linear current-voltage relationship and alters
CC membrane raft localization (PubMed:21911611).
CC {ECO:0000250|UniProtKB:Q9Y6H6, ECO:0000269|PubMed:12954870,
CC ECO:0000269|PubMed:14679187, ECO:0000269|PubMed:21911611}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12954870,
CC ECO:0000269|PubMed:14679187}; Single-pass type I membrane protein
CC {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:12954870}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9Y6H6}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9Y6H6}. Membrane raft
CC {ECO:0000250|UniProtKB:Q9Y6H6}. Note=Colocalizes with KCNB1 at high-
CC density somatodendritic clusters on the surface of hippocampal neurons.
CC {ECO:0000250|UniProtKB:Q9Y6H6}.
CC -!- SIMILARITY: Belongs to the potassium channel KCNE family.
CC {ECO:0000305}.
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DR EMBL; AJ271742; CAB72139.1; -; mRNA.
DR EMBL; BC086406; AAH86406.1; -; mRNA.
DR RefSeq; NP_071571.1; NM_022235.2.
DR RefSeq; XP_006229848.1; XM_006229786.3.
DR AlphaFoldDB; Q9JJV7; -.
DR SMR; Q9JJV7; -.
DR STRING; 10116.ENSRNOP00000044706; -.
DR GlyGen; Q9JJV7; 3 sites.
DR PaxDb; Q9JJV7; -.
DR GeneID; 63883; -.
DR KEGG; rno:63883; -.
DR UCSC; RGD:621384; rat.
DR CTD; 10008; -.
DR RGD; 621384; Kcne3.
DR eggNOG; ENOG502S4UF; Eukaryota.
DR HOGENOM; CLU_180169_0_0_1; -.
DR InParanoid; Q9JJV7; -.
DR OMA; AYMYILF; -.
DR OrthoDB; 1608208at2759; -.
DR PhylomeDB; Q9JJV7; -.
DR TreeFam; TF335981; -.
DR Reactome; R-RNO-5576890; Phase 3 - rapid repolarisation.
DR Reactome; R-RNO-5576893; Phase 2 - plateau phase.
DR PRO; PR:Q9JJV7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017054; Expressed in colon and 16 other tissues.
DR Genevisible; Q9JJV7; RN.
DR GO; GO:1990794; C:basolateral part of cell; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; ISO:RGD.
DR GO; GO:0086011; P:membrane repolarization during action potential; IBA:GO_Central.
DR GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; IEA:GOC.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:1905025; P:negative regulation of membrane repolarization during ventricular cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:1903765; P:negative regulation of potassium ion export across plasma membrane; ISO:RGD.
DR GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; IDA:RGD.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:0043266; P:regulation of potassium ion transport; IMP:RGD.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; ISO:RGD.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IBA:GO_Central.
DR InterPro; IPR000369; K_chnl_KCNE.
DR InterPro; IPR005426; K_chnl_volt-dep_bsu_KCNE3.
DR PANTHER; PTHR15282; PTHR15282; 1.
DR PANTHER; PTHR15282:SF6; PTHR15282:SF6; 1.
DR Pfam; PF02060; ISK_Channel; 1.
DR PRINTS; PR01606; KCNE3CHANNEL.
DR PRINTS; PR00168; KCNECHANNEL.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasm; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..107
FT /note="Potassium voltage-gated channel subfamily E member
FT 3"
FT /id="PRO_0000144291"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 31..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 107 AA; 12001 MW; D0F62FE342E66E8F CRC64;
METSNGTETW YKSLHAVLKA LNTTLHSHLL CRPGPGPGSG TGPDNQTEDH RASLPGRNDN
SYMYILFVMF LFAVTVGSLI LGYTRSRKVD KRSDPYHVYI KNRVSMI
