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O54982

- KCNU1_MOUSE

UniProt

O54982 - KCNU1_MOUSE

Protein

Potassium channel subfamily U member 1

Gene

Kcnu1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K+. Represents the primary spermatozoan K+ current. In contrast to KCNMA1/SLO1, it is not activated by Ca2+ or Mg2+. Critical for fertility. May play an important role in sperm osmoregulation required for the acquisition of normal morphology and motility when faced with osmotic challenges, such as those experienced after mixing with seminal fluid and entry into the vagina.8 Publications

    GO - Molecular functioni

    1. large conductance calcium-activated potassium channel activity Source: RefGenome
    2. voltage-gated potassium channel activity Source: RefGenome

    GO - Biological processi

    1. potassium ion transmembrane transport Source: RefGenome

    Keywords - Molecular functioni

    Ion channel, Potassium channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Potassium transport, Transport

    Keywords - Ligandi

    Potassium

    Protein family/group databases

    TCDBi1.A.1.3.5. the voltage-gated ion channel (vic) superfamily.

    Names & Taxonomyi

    Protein namesi
    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
    Pore-forming subunit of the sperm-specific alkalization activated K(+) current
    Short name:
    KSper
    Slowpoke homolog 3
    Short name:
    mSlo3
    pH-sensitive maxi potassium channel
    Gene namesi
    Name:Kcnu1
    Synonyms:Kcnma3, Ksper, Slo3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1202300. Kcnu1.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. voltage-gated potassium channel complex Source: RefGenome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mutant males are infertile, but their sperm retains some fertility within in vitro fertilization assays. Spermatozoa exhibit a higher incidence of morphological abnormalities as compared to wild-type, accentuated by hypotonic challenge and deficits in motility, in the absence of bicarbonate.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi279 – 2791F → Y: Does not induce any change in single channel conductance or variance in open current levels. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11211121Potassium channel subfamily U member 1PRO_0000349188Add
    BLAST

    Proteomic databases

    PRIDEiO54982.

    Expressioni

    Tissue specificityi

    Testis-specific. Mainly expressed in spermatocytes.2 Publications

    Developmental stagei

    Very low expression levels in testis before postnatal day 25 (P25). Levels strongly increase between P25 and P30, and then remain high from P30 through P150.1 Publication

    Gene expression databases

    GenevestigatoriO54982.

    Interactioni

    Subunit structurei

    Homotetramer; which constitutes the calcium-activated potassium channel. May interact with LRRC52; this interaction may change some channel gating properties, such as shifting gating to more negative potentials at a given pH.

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000096457.

    Structurei

    3D structure databases

    ProteinModelPortaliO54982.
    SMRiO54982. Positions 148-316, 331-600, 686-1048.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2424ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini46 – 10156CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini123 – 13715ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini159 – 1657CytoplasmicSequence Analysis
    Topological domaini187 – 1882ExtracellularSequence Analysis
    Topological domaini210 – 22617CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini248 – 25912ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini283 – 2908ExtracellularSequence Analysis
    Topological domaini312 – 1121810CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei260 – 28223Pore-forming; Name=P regionSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei25 – 4521Helical; Name=Segment S0Sequence AnalysisAdd
    BLAST
    Transmembranei102 – 12221Helical; Name=Segment S1Sequence AnalysisAdd
    BLAST
    Transmembranei138 – 15821Helical; Name=Segment S2Sequence AnalysisAdd
    BLAST
    Transmembranei166 – 18621Helical; Name=Segment S3Sequence AnalysisAdd
    BLAST
    Transmembranei189 – 20921Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
    BLAST
    Transmembranei227 – 24721Helical; Name=Segment S5Sequence AnalysisAdd
    BLAST
    Transmembranei291 – 31121Helical; Name=Segment S6Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini339 – 482144RCK N-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni480 – 50021Segment S7Add
    BLAST
    Regioni537 – 55721Segment S8Add
    BLAST
    Regioni716 – 73621Segment S9Add
    BLAST
    Regioni900 – 92021Segment S1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi276 – 2794Selectivity for potassium

    Domaini

    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.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 similaritiesi

    Contains 1 RCK N-terminal domain.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG253173.
    HOGENOMiHOG000019856.
    HOVERGENiHBG052222.
    InParanoidiO54982.
    KOiK05274.
    PhylomeDBiO54982.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR005821. Ion_trans_dom.
    IPR003929. K_chnl_Ca-activ_BK_asu.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF03493. BK_channel_a. 1 hit.
    PF00520. Ion_trans. 1 hit.
    [Graphical view]
    PRINTSiPR01449. BKCHANNELA.

    Sequencei

    Sequence statusi: Complete.

    O54982-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQTLLDSLN QKELTETSCT IEIQAAFILS SLATFFGGLI ILFLFRIALK     50
    SSRSWKYVKG PRGLLELFSS RRIEANPLRK LYFHGVFRQR IEMLLSAQTV 100
    VGQVLVILVF VLSIGSLVIY FINSMDPVRR CSSYEDKIVH GDLSFNAFFS 150
    FYFGLRFWAA EDKIKFWLEM NSIVDIFTIP PTFISYYLKS NWLGLRFLRA 200
    LRLLELPKIL QILQVIKTSN SVKLSKLLSI VISTWFTAAG FLHLVENSGD 250
    PWLNGRNSQT MSYFESIYLV TATMSTVGFG DVVAKTSLGR IFIVFFTLGS 300
    LILFANYIPE MVELFSTRKK YTKPYEAVKG KKFIVVCGNI TVDSVTAFLR 350
    NFLHWKSGEI NIEIVFLGET LPCLELETLL KCHTSCTNFV CGTALKFEDL 400
    KRVAVENSEA CLILANHFCS DLHDEDNSNI MRVLSIKNYY PQTRVIIQIL 450
    QSQNKVFLSK IPNWDWSAGD NILCFAELKL GFIAQGCLVP GLCTFLTTLF 500
    IEQNQKVFPK HPWQKHFLNG LKNKILTQRL SNDFVGMTFP QVSRLCFVKL 550
    NLMLIAIQHK PFFHSCCTLI LNPSSQVRLN KDTLGFFIAD SSKAVKRAFF 600
    YCSNCHSDVC NPELIGKCNC KIKSRQQLIA PTIMVMKSSL TDFTTSSHIH 650
    ASMSTEIHTC FSREQPSLIT ITTNRPTTND TVDDTDMLDS SGMFHWCRAM 700
    PLDKVVLKRS EKAKHEFQNH IVVCVFGDAQ CTLVGLRNFV MPLRASNYTR 750
    QELKDIVFIG SLEYFQREWR FLRNFPKIHI MPGSALYMGD LIAVNVEQCS 800
    MCVILATPYK ALSSQILVDT EAIMATLNIQ SLRITSPTPG SSKSEVKPSS 850
    AFDSKERKQR YKQIPILTEL KNPSNIHFIE QMGGLDGMLK GTSLHLSTSF 900
    STGAVFSDTF LDSLLATSFY NYHVVELLQM LVTGGISSEM EHYLVKEKPY 950
    KTTDDYEAIK SGRTRCKLGL LSLDQTVLSG INPRKTFGQL FCGSLDNFGI 1000
    LCVGLYRMID EEEPSQEHKR FVITRPSNEC HLLPSDLVFC AIPFNTTCGK 1050
    SDSSPSIQAQ NNSTNATTPL AQGSNFFDSH HADESHDLYP VDDTGERWSQ 1100
    HHHSRVYPLD TLDASDIVQE K 1121
    Length:1,121
    Mass (Da):126,870
    Last modified:March 7, 2006 - v2
    Checksum:i4D7E0425B97B47A1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039213 mRNA. Translation: AAB99742.2.
    CCDSiCCDS52530.1.
    PIRiT42383.
    RefSeqiNP_032458.3. NM_008432.3.
    UniGeneiMm.289679.

    Genome annotation databases

    GeneIDi16532.
    KEGGimmu:16532.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039213 mRNA. Translation: AAB99742.2 .
    CCDSi CCDS52530.1.
    PIRi T42383.
    RefSeqi NP_032458.3. NM_008432.3.
    UniGenei Mm.289679.

    3D structure databases

    ProteinModelPortali O54982.
    SMRi O54982. Positions 148-316, 331-600, 686-1048.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000096457.

    Chemistry

    GuidetoPHARMACOLOGYi 387.

    Protein family/group databases

    TCDBi 1.A.1.3.5. the voltage-gated ion channel (vic) superfamily.

    Proteomic databases

    PRIDEi O54982.

    Protocols and materials databases

    DNASUi 16532.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 16532.
    KEGGi mmu:16532.

    Organism-specific databases

    CTDi 157855.
    MGIi MGI:1202300. Kcnu1.

    Phylogenomic databases

    eggNOGi NOG253173.
    HOGENOMi HOG000019856.
    HOVERGENi HBG052222.
    InParanoidi O54982.
    KOi K05274.
    PhylomeDBi O54982.

    Miscellaneous databases

    NextBioi 289949.
    PROi O54982.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori O54982.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR005821. Ion_trans_dom.
    IPR003929. K_chnl_Ca-activ_BK_asu.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF03493. BK_channel_a. 1 hit.
    PF00520. Ion_trans. 1 hit.
    [Graphical view ]
    PRINTSi PR01449. BKCHANNELA.
    ProtoNeti Search...

    Publicationsi

    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.
    7. "Deletion of the Slo3 gene abolishes alkalization-activated K+ current in mouse spermatozoa."
      Zeng X.H., Yang C., Kim S.T., Lingle C.J., Xia X.M.
      Proc. Natl. Acad. Sci. U.S.A. 108:5879-5884(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION AS KSPER, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    8. "LRRC52 (leucine-rich-repeat-containing protein 52), a testis-specific auxiliary subunit of the alkalization-activated Slo3 channel."
      Yang C., Zeng X.H., Zhou Y., Xia X.M., Lingle C.J.
      Proc. Natl. Acad. Sci. U.S.A. 108:19419-19424(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRRC52, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    9. "Functional and structural analysis of the human SLO3 pH- and voltage-gated K+ channel."
      Leonetti M.D., Yuan P., Hsiung Y., Mackinnon R.
      Proc. Natl. Acad. Sci. U.S.A. 109:19274-19279(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PH DEPENDENCE.

    Entry informationi

    Entry nameiKCNU1_MOUSE
    AccessioniPrimary (citable) accession number: O54982
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3