Potassium channel subfamily U member 1

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O54982 (KCNU1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Potassium channel subfamily U member 1

Alternative name(s):
Calcium-activated potassium channel subunit alpha-3
Calcium-activated potassium channel, subfamily M subunit alpha-3
Slowpoke homolog 3
Short name=mSlo3
pH-sensitive maxi potassium channel

Gene names

Name:	Kcnu1
Synonyms:	Kcnma3, Slo3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1121 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K⁺. May be involved in sperm capacitation and/or the acrosome reaction, essential steps in fertilization where changes in both intracellular pH and membrane potential are known to occur. In contrast to KCNMA1/SLO1, it is not activated by Ca²⁺ or Mg²⁺. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6
Subunit structure	Homotetramer; which constitutes the calcium-activated potassium channel.
Subcellular location	Membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Testis-specific. Mainly expressed in spermatocytes. Ref.1
Domain	The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor By similarity. The pore-forming domain (also referred as P region) is imbedded into the membrane, and forms the selectivity filter of the pore. It contains the signature sequence of potassium channels that displays selectivity to potassium By similarity. The RCK N-terminal domain mediates the homotetramerization, thereby promoting the assembly of monomers into functional potassium channel By similarity. The C-terminal cytosolic region confers the pH-dependence.
Sequence similarities	Belongs to the potassium channel family. Calcium-activated (TC 1.A.1.3) subfamily. KCa5.1/KCNU1 sub-subfamily. [View classification] Contains 1 RCK N-terminal domain.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Potassium
Molecular function	Ion channel Potassium channel Voltage-gated channel
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	voltage-gated potassium channel complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	large conductance calcium-activated potassium channel activity Inferred from Biological aspect of Ancestor. Source: RefGenome voltage-gated potassium channel activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1121

1121

Potassium channel subfamily U member 1

PRO_0000349188

Regions

Topological domain

1 – 24

Extracellular Potential

Transmembrane

25 – 45

Helical; Name=Segment S0; Potential

Topological domain

46 – 101

Cytoplasmic Potential

Transmembrane

102 – 122

Helical; Name=Segment S1; Potential

Topological domain

123 – 137

Extracellular Potential

Transmembrane

138 – 158

Helical; Name=Segment S2; Potential

Topological domain

159 – 165

Cytoplasmic Potential

Transmembrane

166 – 186

Helical; Name=Segment S3; Potential

Topological domain

187 – 188

Extracellular Potential

Transmembrane

189 – 209

Helical; Voltage-sensor; Name=Segment S4; Potential

Topological domain

210 – 226

Cytoplasmic Potential

Transmembrane

227 – 247

Helical; Name=Segment S5; Potential

Topological domain

248 – 259

Extracellular Potential

Intramembrane

260 – 282

Pore-forming; Name=P region; Potential

Topological domain

283 – 290

Extracellular Potential

Transmembrane

291 – 311

Helical; Name=Segment S6; Potential

Topological domain

312 – 1121

810

Cytoplasmic Potential

Domain

339 – 482

144

RCK N-terminal

Region

480 – 500

Segment S7

Region

537 – 557

Segment S8

Region

716 – 736

Segment S9

Region

900 – 920

Segment S1

Motif

276 – 279

Selectivity for potassium

Experimental info

Mutagenesis

279

F → Y: Does not induce any change in single channel conductance or variance in open current levels. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

O54982 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 4D7E0425B97B47A1
Show »

FASTA

1,121

126,870

        10         20         30         40         50         60 
MSQTLLDSLN QKELTETSCT IEIQAAFILS SLATFFGGLI ILFLFRIALK SSRSWKYVKG 

        70         80         90        100        110        120 
PRGLLELFSS RRIEANPLRK LYFHGVFRQR IEMLLSAQTV VGQVLVILVF VLSIGSLVIY 

       130        140        150        160        170        180 
FINSMDPVRR CSSYEDKIVH GDLSFNAFFS FYFGLRFWAA EDKIKFWLEM NSIVDIFTIP 

       190        200        210        220        230        240 
PTFISYYLKS NWLGLRFLRA LRLLELPKIL QILQVIKTSN SVKLSKLLSI VISTWFTAAG 

       250        260        270        280        290        300 
FLHLVENSGD PWLNGRNSQT MSYFESIYLV TATMSTVGFG DVVAKTSLGR IFIVFFTLGS 

       310        320        330        340        350        360 
LILFANYIPE MVELFSTRKK YTKPYEAVKG KKFIVVCGNI TVDSVTAFLR NFLHWKSGEI 

       370        380        390        400        410        420 
NIEIVFLGET LPCLELETLL KCHTSCTNFV CGTALKFEDL KRVAVENSEA CLILANHFCS 

       430        440        450        460        470        480 
DLHDEDNSNI MRVLSIKNYY PQTRVIIQIL QSQNKVFLSK IPNWDWSAGD NILCFAELKL 

       490        500        510        520        530        540 
GFIAQGCLVP GLCTFLTTLF IEQNQKVFPK HPWQKHFLNG LKNKILTQRL SNDFVGMTFP 

       550        560        570        580        590        600 
QVSRLCFVKL NLMLIAIQHK PFFHSCCTLI LNPSSQVRLN KDTLGFFIAD SSKAVKRAFF 

       610        620        630        640        650        660 
YCSNCHSDVC NPELIGKCNC KIKSRQQLIA PTIMVMKSSL TDFTTSSHIH ASMSTEIHTC 

       670        680        690        700        710        720 
FSREQPSLIT ITTNRPTTND TVDDTDMLDS SGMFHWCRAM PLDKVVLKRS EKAKHEFQNH 

       730        740        750        760        770        780 
IVVCVFGDAQ CTLVGLRNFV MPLRASNYTR QELKDIVFIG SLEYFQREWR FLRNFPKIHI 

       790        800        810        820        830        840 
MPGSALYMGD LIAVNVEQCS MCVILATPYK ALSSQILVDT EAIMATLNIQ SLRITSPTPG 

       850        860        870        880        890        900 
SSKSEVKPSS AFDSKERKQR YKQIPILTEL KNPSNIHFIE QMGGLDGMLK GTSLHLSTSF 

       910        920        930        940        950        960 
STGAVFSDTF LDSLLATSFY NYHVVELLQM LVTGGISSEM EHYLVKEKPY KTTDDYEAIK 

       970        980        990       1000       1010       1020 
SGRTRCKLGL LSLDQTVLSG INPRKTFGQL FCGSLDNFGI LCVGLYRMID EEEPSQEHKR 

      1030       1040       1050       1060       1070       1080 
FVITRPSNEC HLLPSDLVFC AIPFNTTCGK SDSSPSIQAQ NNSTNATTPL AQGSNFFDSH 

      1090       1100       1110       1120 
HADESHDLYP VDDTGERWSQ HHHSRVYPLD TLDASDIVQE K

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References

[1]	"Slo3, a novel pH-sensitive K+ channel from mammalian spermatocytes." Schreiber M., Wei A., Yuan A., Gaut J., Saito M., Salkoff L. J. Biol. Chem. 273:3509-3516(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]	"Intracellular Mg(2+) enhances the function of BK-type Ca(2+)-activated K(+) channels." Shi J., Cui J. J. Gen. Physiol. 118:589-606(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[3]	"Gating and conductance properties of BK channels are modulated by the S9-S10 tail domain of the alpha subunit. A study of mSlo1 and mSlo3 wild-type and chimeric channels." Moss B.L., Magleby K.L. J. Gen. Physiol. 118:711-734(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Ligand-dependent activation of Slo family channels is defined by interchangeable cytosolic domains." Xia X.-M., Zhang X., Lingle C.J. J. Neurosci. 24:5585-5591(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Slo3 K+ channels: voltage and pH dependence of macroscopic currents." Zhang X., Zeng X., Lingle C.J. J. Gen. Physiol. 128:317-336(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"pH-regulated Slo3 K+ channels: properties of unitary currents." Zhang X., Zeng X., Xia X.-M., Lingle C.J. J. Gen. Physiol. 128:301-315(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PHE-279.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF039213 mRNA. Translation: AAB99742.2.
IPI	IPI00120028.
PIR	T42383.
RefSeq	NP_032458.3. NM_008432.3.
UniGene	Mm.289679.
3D structure databases
ProteinModelPortal	O54982.
SMR	O54982. Positions 148-316, 331-1048.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000096457.
Protein family/group databases
TCDB	1.A.1.3.5. voltage-gated ion channel (VIC) superfamily.
Proteomic databases
PRIDE	O54982.
Protocols and materials databases
DNASU	16532.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	16532.
KEGG	mmu:16532.
Organism-specific databases
CTD	157855.
MGI	MGI:1202300. Kcnu1.
Phylogenomic databases
eggNOG	NOG253173.
HOGENOM	HOG000019856.
HOVERGEN	HBG052222.
InParanoid	O54982.
KO	K05274.
OrthoDB	EOG4CG07D.
Gene expression databases
Genevestigator	O54982.
Family and domain databases
Gene3D	3.40.50.720. 2 hits.
InterPro	IPR005821. Ion_trans_dom. IPR003929. K_chnl_Ca-activ_BK_asu. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF03493. BK_channel_a. 1 hit. PF00520. Ion_trans. 1 hit. [Graphical view]
PRINTS	PR01449. BKCHANNELA.
PROSITE	PS51201. RCK_N. False negative. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL3804.
NextBio	289949.
SOURCE	Search...

Entry information

Entry name

KCNU1_MOUSE

Accession

Primary (citable) accession number: O54982

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	March 7, 2006
Last modified:	May 29, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents