KCNU1_MACFA
ID KCNU1_MACFA Reviewed; 1149 AA.
AC A5LFX5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Potassium channel subfamily U member 1;
DE AltName: Full=Calcium-activated potassium channel subunit alpha-3;
DE AltName: Full=Calcium-activated potassium channel, subfamily M subunit alpha-3;
DE AltName: Full=Slowpoke homolog 3;
GN Name=KCNU1; Synonyms=KCNMA3, SLO3; ORFNames=QtsA-16614;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Testis-specific potassium channel activated by both
CC intracellular pH and membrane voltage that mediates export of K(+). May
CC represent the primary spermatozoan K(+) current. In contrast to
CC KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for
CC fertility. May play an important role in sperm osmoregulation required
CC for the acquisition of normal morphology and motility when faced with
CC osmotic challenges, such as those experienced after mixing with seminal
CC fluid and entry into the vagina (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer; which constitutes the calcium-activated
CC potassium channel. May interact with LRRC52; this interaction may
CC change some channel gating properties, such as shifting gating to more
CC negative potentials at a given pH. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis-specific.
CC -!- DOMAIN: The S4 segment, which is characterized by a series of
CC positively charged amino acids at every third position, is part of the
CC voltage-sensor. {ECO:0000250}.
CC -!- DOMAIN: The pore-forming domain (also referred as P region) is imbedded
CC into the membrane, and forms the selectivity filter of the pore. It
CC contains the signature sequence of potassium channels that displays
CC selectivity to potassium (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The RCK N-terminal domain mediates the homotetramerization,
CC thereby promoting the assembly of monomers into functional potassium
CC channel. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal cytosolic region confers the pH-dependence.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC (TC 1.A.1.3) subfamily. KCa5.1/KCNU1 sub-subfamily. {ECO:0000305}.
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DR EMBL; AB169017; BAF63660.1; -; mRNA.
DR RefSeq; NP_001270492.1; NM_001283563.1.
DR AlphaFoldDB; A5LFX5; -.
DR SMR; A5LFX5; -.
DR STRING; 9541.XP_005563107.1; -.
DR GeneID; 101925188; -.
DR CTD; 157855; -.
DR eggNOG; KOG1420; Eukaryota.
DR OrthoDB; 858812at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF00520; Ion_trans; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1149
FT /note="Potassium channel subfamily U member 1"
FT /id="PRO_0000349187"
FT TOPO_DOM 1..24
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Name=Segment S0"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 260..282
FT /note="Pore-forming; Name=P region"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..1149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 339..482
FT /note="RCK N-terminal"
FT REGION 480..500
FT /note="Segment S7"
FT REGION 537..557
FT /note="Segment S8"
FT REGION 711..731
FT /note="Segment S9"
FT REGION 829..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..915
FT /note="Segment S10"
FT REGION 1106..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 276..279
FT /note="Selectivity for potassium"
FT COMPBIAS 1106..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 129492 MW; 5E0DA12045FDD530 CRC64;
MFQTKLRNES WEDLQKMSCT TEIQVAFILS SFMTFISGLI ILLIFRLIWR TVKKWQIIKG
TGIILELFTS GSIRRNHVRS LHFHGRFRDR IEMLLSAQTF VGQVLVILVF VLSIGSLIIY
FINSADPVGS CSSYEDKTIP VDLVFNAFFS FYFGLRFMAA DDKIKFWLEM NSIVDIFTIP
PTFISYYLKS NWLGLRFLRA LRLLELPRIL QILRAIKTSN SVKFSKLLSI VLSTWFTAAG
FIHLVENSGD PWLKGRNSQN ISYFDSVYLV MATTSTVGFG DVVAKTSLGR TFIIFFTLGS
LILFANYIPE MVELFANKRK YTSSYEALKG KKFIVVCGNI TVDSVTAFLR NFLRRKSGEI
NTEIVFLGES PPSLELETIF KCYLAYTTFI SGSAMKWEDL RRVAVESAEA CLIIANPLCS
DSHAEDISNI MRVLSIKNYD STTRIIIQIL QSHNKVYLPK IPSWDWDAGD NIICFAELKL
GFIAQGCLVP GLCTFLTSLF VEQNRKVTPK QTWQKHFLNS MKNNILTQRL SDDFAGMSFP
EVARLCFLKM HLLLIAIEYK SLFTDGFCGL ILNPPAQIRI HKNTLGFFIA ETPKEVKRAL
FYCSVCHDDV FIPELITNCG CKSRSRQHVT VPAVKIVKKC MKGLSSHMAG QDSPPRVHAS
PSRISDFTTR TFPHDVEQDS DQLDSSGMFH WCKPISLDKV TLKRSRKLKH KFRNHIVACV
FGDAQSALIG LRNFVMPLRA SNYTRKELKD IVFIGSLDYL QREWRFLRNF PQIYILPGCA
LYSGDLHAAN IEQCSMCVVL SPPSKPSSSQ TLVDAEAILA TLTIGSLQID SSSDSSPSVS
EETASCTNGH NEKSNCRKVP ILIELKNPSN IHFIEQLGGL EGSLQETNLH LSTAFSTGTV
FSGSFLDSLL ATSFYNYHVL ELLQMLVTGG VSSQLEQHLD KDKVYGVADS CTTLLSGRNR
CKMGLLSLHQ TILSDVNPRN TFGQLFCGSL DLFGILCVGL YRIIDEEELN PENKRFVITR
PANEFKLLPS DLVFCAIPFS TACYKRNEEF SSQKSYEIIK EASQTTETHS DTNFPPTIYS
VDETSYSPVY SYPSRTNSVY SANQTARNQI RTNSSITSQK PLGDNAKKNG KKISDEISDE
DPFAYSEPL
