KCNE2_MOUSE
ID KCNE2_MOUSE Reviewed; 123 AA.
AC Q9D808; Q8R1Z7;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Potassium voltage-gated channel subfamily E member 2;
DE AltName: Full=MinK-related peptide 1;
DE AltName: Full=Minimum potassium ion channel-related peptide 1;
DE AltName: Full=Potassium channel subunit beta MiRP1;
GN Name=Kcne2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
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 Associated with KCNH2/HERG is proposed to form the rapidly activating
CC component of the delayed rectifying potassium current in heart (IKr).
CC May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type
CC current. May associate with HCN1 and HCN2 and increase potassium
CC current (By similarity). Interacts with KCNQ1; forms a heterooligomer
CC complex leading to currents with an apparently instantaneous
CC activation, a rapid deactivation process and a linear current-voltage
CC relationship and decreases the amplitude of the outward current (By
CC similarity). {ECO:0000250|UniProtKB:P63161,
CC ECO:0000250|UniProtKB:Q9Y6J6}.
CC -!- SUBUNIT: Interacts with KCNB1. Associates with KCNH2/ERG1. May
CC associate with KCNQ2 and KCNQ3. Associates with HCN1 and probably HCN2.
CC Heteromultimer with KCNC2. Interacts with KCNC2 (By similarity).
CC Interacts with KCNQ1; forms a heterooligomer complex that targets to
CC the membrane raft and leading to currents with an apparently
CC instantaneous activation, a rapid deactivation process and a linear
CC current-voltage relationship and decreases the amplitude of the outward
CC current (By similarity). {ECO:0000250|UniProtKB:P63161,
CC ECO:0000250|UniProtKB:Q9Y6J6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63161,
CC ECO:0000250|UniProtKB:Q9Y6J6}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P63161}. Note=Colocalizes with KCNB1 at the
CC plasma membrane. {ECO:0000250|UniProtKB:P63161}.
CC -!- SIMILARITY: Belongs to the potassium channel KCNE family.
CC {ECO:0000305}.
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DR EMBL; AK008619; BAB25781.1; -; mRNA.
DR EMBL; BC022699; AAH22699.1; -; mRNA.
DR CCDS; CCDS28333.1; -.
DR RefSeq; NP_598871.1; NM_134110.3.
DR RefSeq; XP_006523096.1; XM_006523033.3.
DR AlphaFoldDB; Q9D808; -.
DR SMR; Q9D808; -.
DR ComplexPortal; CPX-3197; Voltage-gated potassium channel complex variant 2.
DR STRING; 10090.ENSMUSP00000048849; -.
DR TCDB; 8.A.10.2.1; the slow voltage-gated k+) channel accessory protein (mink) family.
DR GlyGen; Q9D808; 2 sites.
DR iPTMnet; Q9D808; -.
DR PhosphoSitePlus; Q9D808; -.
DR PaxDb; Q9D808; -.
DR PRIDE; Q9D808; -.
DR ProteomicsDB; 269452; -.
DR DNASU; 246133; -.
DR GeneID; 246133; -.
DR KEGG; mmu:246133; -.
DR UCSC; uc007zyw.2; mouse.
DR CTD; 9992; -.
DR MGI; MGI:1891123; Kcne2.
DR eggNOG; ENOG502S1GJ; Eukaryota.
DR InParanoid; Q9D808; -.
DR OrthoDB; 1493495at2759; -.
DR PhylomeDB; Q9D808; -.
DR TreeFam; TF336058; -.
DR Reactome; R-MMU-5576890; Phase 3 - rapid repolarisation.
DR Reactome; R-MMU-5576893; Phase 2 - plateau phase.
DR BioGRID-ORCS; 246133; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9D808; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D808; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:MGI.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISO:MGI.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0015705; P:iodide transport; IMP:MGI.
DR GO; GO:0086009; P:membrane repolarization; ISO:MGI.
DR GO; GO:0086011; P:membrane repolarization during action potential; ISO:MGI.
DR GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0033555; P:multicellular organismal response to stress; IMP:MGI.
DR GO; GO:0015798; P:myo-inositol transport; IMP:MGI.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISO:MGI.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:1902159; P:regulation of cyclic nucleotide-gated ion channel activity; ISO:MGI.
DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:1901979; P:regulation of inward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0060306; P:regulation of membrane repolarization; ISO:MGI.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:MGI.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:MGI.
DR InterPro; IPR000369; K_chnl_KCNE.
DR InterPro; IPR005425; K_chnl_volt-dep_bsu_KCNE2.
DR PANTHER; PTHR15282; PTHR15282; 1.
DR Pfam; PF02060; ISK_Channel; 1.
DR PRINTS; PR01605; KCNE2CHANNEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..123
FT /note="Potassium voltage-gated channel subfamily E member
FT 2"
FT /id="PRO_0000144286"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 82
FT /note="H -> D (in Ref. 1; BAB25781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 123 AA; 14370 MW; 0A52784967FD741C CRC64;
MATLANLTQT LEDAFKKIFI TYMDSWRRNT TAEEQALQAR VDAENFYYVI LYLMVMIGMF
SFIVVAILVS TVKSKRREHS QHPYHQYIVE DWQEKYKSQI LHLEDSKATI HENMGATGFT
VSP