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Q9D808 (KCNE2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel subfamily E member 2
Alternative name(s):
MinK-related peptide 1
Minimum potassium ion channel-related peptide 1
Potassium channel subunit beta MiRP1
Gene names
Name:Kcne2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length123 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Associated with KCNH2/HERG is proposed to form the rapidly activating component of the delayed rectifying potassium current in heart (IKr). May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type current. May associate with KCNQ1/KCLQT1 and elicit a voltage-independent current By similarity.

Subunit structure

Associates with KCNH2/ERG1 By similarity. May associate with KCNQ1/KVLQT1, KCNQ2 and KCNQ3. Associates with HCN1 and probably HCN2 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the potassium channel KCNE family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 123123Potassium voltage-gated channel subfamily E member 2
PRO_0000144286

Regions

Transmembrane49 – 6921Helical; Potential
Topological domain70 – 12354Cytoplasmic Potential

Amino acid modifications

Glycosylation61N-linked (GlcNAc...) Potential
Glycosylation291N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict821H → D in BAB25781. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D808 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: 0A52784967FD741C

FASTA12314,370
        10         20         30         40         50         60 
MATLANLTQT LEDAFKKIFI TYMDSWRRNT TAEEQALQAR VDAENFYYVI LYLMVMIGMF 

        70         80         90        100        110        120 
SFIVVAILVS TVKSKRREHS QHPYHQYIVE DWQEKYKSQI LHLEDSKATI HENMGATGFT 


VSP

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Stomach.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK008619 mRNA. Translation: BAB25781.1.
BC022699 mRNA. Translation: AAH22699.1.
IPIIPI00318395.
RefSeqNP_598871.1. NM_134110.3.
UniGeneMm.156736.

3D structure databases

ProteinModelPortalQ9D808.
SMRQ9D808. Positions 51-100.
ModBaseSearch...

Protein family/group databases

TCDB8.A.10.2.1. slow voltage-gated K+ channel accessory protein (MinK) family.

PTM databases

PhosphoSiteQ9D808.

Proteomic databases

PRIDEQ9D808.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047383; ENSMUSP00000048849; ENSMUSG00000039672.
ENSMUST00000113971; ENSMUSP00000109604; ENSMUSG00000039672.
GeneID246133.
KEGGmmu:246133.
UCSCuc007zyw.2. mouse.

Organism-specific databases

CTD9992.
MGIMGI:1891123. Kcne2.

Phylogenomic databases

eggNOGNOG43841.
GeneTreeENSGT00510000048894.
HOGENOMHOG000113208.
HOVERGENHBG052227.
InParanoidQ9D808.
KOK04896.
OrthoDBEOG4Z62Q0.

Gene expression databases

BgeeQ9D808.
GenevestigatorQ9D808.
GermOnlineENSMUSG00000039672. Mus musculus.

Family and domain databases

InterProIPR000369. K_chnl_volt-dep_bsu_KCNE.
IPR005425. K_chnl_volt-dep_bsu_KCNE2.
[Graphical view]
PANTHERPTHR15259. PTHR15259. 1 hit.
PfamPF02060. ISK_Channel. 1 hit.
[Graphical view]
PRINTSPR01605. KCNE2CHANNEL.
ProtoNetSearch...

Other

NextBio387099.
SOURCESearch...

Entry information

Entry nameKCNE2_MOUSE
AccessionPrimary (citable) accession number: Q9D808
Secondary accession number(s): Q8R1Z7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: November 28, 2002
Last modified: May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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