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Potassium channel subfamily U member 1 (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) (KSper) (Slowpoke homolog 3) (mSlo3) (pH-sensitive maxi potassium channel)

 KCNU1_MOUSE             Reviewed;        1121 AA.
O54982;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 2.
25-APR-2018, entry version 131.
RecName: Full=Potassium channel subfamily U member 1;
AltName: Full=Calcium-activated potassium channel subunit alpha-3;
AltName: Full=Calcium-activated potassium channel, subfamily M subunit alpha-3;
AltName: Full=Pore-forming subunit of the sperm-specific alkalization activated K(+) current;
Short=KSper;
AltName: Full=Slowpoke homolog 3;
Short=mSlo3;
AltName: Full=pH-sensitive maxi potassium channel;
Name=Kcnu1; Synonyms=Kcnma3, Ksper, Slo3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=9452476; DOI=10.1074/jbc.273.6.3509;
Schreiber M., Wei A., Yuan A., Gaut J., Saito M., Salkoff L.;
"Slo3, a novel pH-sensitive K+ channel from mammalian spermatocytes.";
J. Biol. Chem. 273:3509-3516(1998).
[2]
FUNCTION.
PubMed=11696614; DOI=10.1085/jgp.118.5.589;
Shi J., Cui J.;
"Intracellular Mg(2+) enhances the function of BK-type Ca(2+)-
activated K(+) channels.";
J. Gen. Physiol. 118:589-606(2001).
[3]
FUNCTION.
PubMed=11723163; DOI=10.1085/jgp.118.6.711;
Moss B.L., Magleby K.L.;
"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.";
J. Gen. Physiol. 118:711-734(2001).
[4]
FUNCTION.
PubMed=15201331; DOI=10.1523/JNEUROSCI.1296-04.2004;
Xia X.-M., Zhang X., Lingle C.J.;
"Ligand-dependent activation of Slo family channels is defined by
interchangeable cytosolic domains.";
J. Neurosci. 24:5585-5591(2004).
[5]
FUNCTION.
PubMed=16940555; DOI=10.1085/jgp.200609552;
Zhang X., Zeng X., Lingle C.J.;
"Slo3 K+ channels: voltage and pH dependence of macroscopic
currents.";
J. Gen. Physiol. 128:317-336(2006).
[6]
FUNCTION, AND MUTAGENESIS OF PHE-279.
PubMed=16940554; DOI=10.1085/jgp.200609551;
Zhang X., Zeng X., Xia X.-M., Lingle C.J.;
"pH-regulated Slo3 K+ channels: properties of unitary currents.";
J. Gen. Physiol. 128:301-315(2006).
[7]
FUNCTION, IDENTIFICATION AS KSPER, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
PubMed=21427226; DOI=10.1073/pnas.1100240108;
Zeng X.H., Yang C., Kim S.T., Lingle C.J., Xia X.M.;
"Deletion of the Slo3 gene abolishes alkalization-activated K+ current
in mouse spermatozoa.";
Proc. Natl. Acad. Sci. U.S.A. 108:5879-5884(2011).
[8]
INTERACTION WITH LRRC52, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
PubMed=22084117; DOI=10.1073/pnas.1111104108;
Yang C., Zeng X.H., Zhou Y., Xia X.M., Lingle C.J.;
"LRRC52 (leucine-rich-repeat-containing protein 52), a testis-specific
auxiliary subunit of the alkalization-activated Slo3 channel.";
Proc. Natl. Acad. Sci. U.S.A. 108:19419-19424(2011).
[9]
FUNCTION, AND PH DEPENDENCE.
PubMed=23129643; DOI=10.1073/pnas.1215078109;
Leonetti M.D., Yuan P., Hsiung Y., Mackinnon R.;
"Functional and structural analysis of the human SLO3 pH- and voltage-
gated K+ channel.";
Proc. Natl. Acad. Sci. U.S.A. 109:19274-19279(2012).
-!- FUNCTION: 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 Ca(2+) or Mg(2+).
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. {ECO:0000269|PubMed:11696614, ECO:0000269|PubMed:11723163,
ECO:0000269|PubMed:15201331, ECO:0000269|PubMed:16940554,
ECO:0000269|PubMed:16940555, ECO:0000269|PubMed:21427226,
ECO:0000269|PubMed:23129643, ECO:0000269|PubMed:9452476}.
-!- SUBUNIT: 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.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22084117};
Multi-pass membrane protein {ECO:0000269|PubMed:22084117}.
-!- TISSUE SPECIFICITY: Testis-specific. Mainly expressed in
spermatocytes. {ECO:0000269|PubMed:21427226,
ECO:0000269|PubMed:9452476}.
-!- DEVELOPMENTAL STAGE: 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.
{ECO:0000269|PubMed:22084117}.
-!- 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. {ECO:0000250}.
-!- DOMAIN: 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).
{ECO:0000250}.
-!- DOMAIN: The RCK N-terminal domain mediates the
homotetramerization, thereby promoting the assembly of monomers
into functional potassium channel. {ECO:0000250}.
-!- DOMAIN: The C-terminal cytosolic region confers the pH-dependence.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:21427226}.
-!- SIMILARITY: Belongs to the potassium channel family. Calcium-
activated (TC 1.A.1.3) subfamily. KCa5.1/KCNU1 sub-subfamily.
{ECO:0000305}.
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EMBL; AF039213; AAB99742.2; -; mRNA.
CCDS; CCDS52530.1; -.
PIR; T42383; T42383.
RefSeq; NP_032458.3; NM_008432.3.
UniGene; Mm.289679; -.
ProteinModelPortal; O54982; -.
STRING; 10090.ENSMUSP00000096457; -.
GuidetoPHARMACOLOGY; 387; -.
TCDB; 1.A.1.3.5; the voltage-gated ion channel (vic) superfamily.
PhosphoSitePlus; O54982; -.
PaxDb; O54982; -.
PRIDE; O54982; -.
DNASU; 16532; -.
GeneID; 16532; -.
KEGG; mmu:16532; -.
CTD; 157855; -.
MGI; MGI:1202300; Kcnu1.
eggNOG; KOG1420; Eukaryota.
eggNOG; ENOG410YUX1; LUCA.
HOGENOM; HOG000019856; -.
HOVERGEN; HBG052222; -.
InParanoid; O54982; -.
KO; K05274; -.
PhylomeDB; O54982; -.
PRO; PR:O54982; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IBA:GO_Central.
GO; GO:0005267; F:potassium channel activity; IMP:MGI.
GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
GO; GO:0006813; P:potassium ion transport; IMP:MGI.
GO; GO:0050821; P:protein stabilization; IMP:MGI.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0022414; P:reproductive process; IMP:MGI.
Gene3D; 1.20.120.350; -; 1.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003929; K_chnl_BK_asu.
InterPro; IPR027359; Volt_channel_dom_sf.
Pfam; PF03493; BK_channel_a; 1.
Pfam; PF00520; Ion_trans; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Ion channel; Ion transport;
Membrane; Potassium; Potassium channel; Potassium transport;
Reference proteome; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
CHAIN 1 1121 Potassium channel subfamily U member 1.
/FTId=PRO_0000349188.
TOPO_DOM 1 24 Extracellular. {ECO:0000255}.
TRANSMEM 25 45 Helical; Name=Segment S0. {ECO:0000255}.
TOPO_DOM 46 101 Cytoplasmic. {ECO:0000255}.
TRANSMEM 102 122 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 123 137 Extracellular. {ECO:0000255}.
TRANSMEM 138 158 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 159 165 Cytoplasmic. {ECO:0000255}.
TRANSMEM 166 186 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 187 188 Extracellular. {ECO:0000255}.
TRANSMEM 189 209 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 210 226 Cytoplasmic. {ECO:0000255}.
TRANSMEM 227 247 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 248 259 Extracellular. {ECO:0000255}.
INTRAMEM 260 282 Pore-forming; Name=P region.
{ECO:0000255}.
TOPO_DOM 283 290 Extracellular. {ECO:0000255}.
TRANSMEM 291 311 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 312 1121 Cytoplasmic. {ECO:0000255}.
DOMAIN 339 482 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.
MUTAGEN 279 279 F->Y: Does not induce any change in
single channel conductance or variance in
open current levels.
{ECO:0000269|PubMed:16940554}.
SEQUENCE 1121 AA; 126870 MW; 4D7E0425B97B47A1 CRC64;
MSQTLLDSLN QKELTETSCT IEIQAAFILS SLATFFGGLI ILFLFRIALK SSRSWKYVKG
PRGLLELFSS RRIEANPLRK LYFHGVFRQR IEMLLSAQTV VGQVLVILVF VLSIGSLVIY
FINSMDPVRR CSSYEDKIVH GDLSFNAFFS FYFGLRFWAA EDKIKFWLEM NSIVDIFTIP
PTFISYYLKS NWLGLRFLRA LRLLELPKIL QILQVIKTSN SVKLSKLLSI VISTWFTAAG
FLHLVENSGD PWLNGRNSQT MSYFESIYLV TATMSTVGFG DVVAKTSLGR IFIVFFTLGS
LILFANYIPE MVELFSTRKK YTKPYEAVKG KKFIVVCGNI TVDSVTAFLR NFLHWKSGEI
NIEIVFLGET LPCLELETLL KCHTSCTNFV CGTALKFEDL KRVAVENSEA CLILANHFCS
DLHDEDNSNI MRVLSIKNYY PQTRVIIQIL QSQNKVFLSK IPNWDWSAGD NILCFAELKL
GFIAQGCLVP GLCTFLTTLF IEQNQKVFPK HPWQKHFLNG LKNKILTQRL SNDFVGMTFP
QVSRLCFVKL NLMLIAIQHK PFFHSCCTLI LNPSSQVRLN KDTLGFFIAD SSKAVKRAFF
YCSNCHSDVC NPELIGKCNC KIKSRQQLIA PTIMVMKSSL TDFTTSSHIH ASMSTEIHTC
FSREQPSLIT ITTNRPTTND TVDDTDMLDS SGMFHWCRAM PLDKVVLKRS EKAKHEFQNH
IVVCVFGDAQ CTLVGLRNFV MPLRASNYTR QELKDIVFIG SLEYFQREWR FLRNFPKIHI
MPGSALYMGD LIAVNVEQCS MCVILATPYK ALSSQILVDT EAIMATLNIQ SLRITSPTPG
SSKSEVKPSS AFDSKERKQR YKQIPILTEL KNPSNIHFIE QMGGLDGMLK GTSLHLSTSF
STGAVFSDTF LDSLLATSFY NYHVVELLQM LVTGGISSEM EHYLVKEKPY KTTDDYEAIK
SGRTRCKLGL LSLDQTVLSG INPRKTFGQL FCGSLDNFGI LCVGLYRMID EEEPSQEHKR
FVITRPSNEC HLLPSDLVFC AIPFNTTCGK SDSSPSIQAQ NNSTNATTPL AQGSNFFDSH
HADESHDLYP VDDTGERWSQ HHHSRVYPLD TLDASDIVQE K


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