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Protein

Potassium channel subfamily U member 1

Gene

KCNU1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K+. May represent 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.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

BioCyciZFISH:G66-33782-MONOMER.
ReactomeiR-HSA-1300642. Sperm Motility And Taxes.

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
KCa5
Slowpoke homolog 3
Gene namesi
Name:KCNU1
Synonyms:KCNMA3, KCNMC1, SLO3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:18867. KCNU1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 24ExtracellularSequence analysisAdd BLAST24
Transmembranei25 – 45Helical; Name=Segment S0Sequence analysisAdd BLAST21
Topological domaini46 – 101CytoplasmicSequence analysisAdd BLAST56
Transmembranei102 – 122Helical; Name=Segment S1Sequence analysisAdd BLAST21
Topological domaini123 – 138ExtracellularSequence analysisAdd BLAST16
Transmembranei139 – 159Helical; Name=Segment S2Sequence analysisAdd BLAST21
Topological domaini160 – 163CytoplasmicSequence analysis4
Transmembranei164 – 184Helical; Name=Segment S3Sequence analysisAdd BLAST21
Topological domaini185 – 188ExtracellularSequence analysis4
Transmembranei189 – 209Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd BLAST21
Topological domaini210 – 226CytoplasmicSequence analysisAdd BLAST17
Transmembranei227 – 247Helical; Name=Segment S5Sequence analysisAdd BLAST21
Topological domaini248 – 259ExtracellularSequence analysisAdd BLAST12
Intramembranei260 – 282Pore-forming; Name=P regionSequence analysisAdd BLAST23
Topological domaini283 – 291ExtracellularSequence analysis9
Transmembranei292 – 312Helical; Name=Segment S6Sequence analysisAdd BLAST21
Topological domaini313 – 1149CytoplasmicSequence analysisAdd BLAST837

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi157855.
OpenTargetsiENSG00000215262.
PharmGKBiPA38727.

Chemistry databases

GuidetoPHARMACOLOGYi387.

Polymorphism and mutation databases

BioMutaiKCNU1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003491861 – 1149Potassium channel subfamily U member 1Add BLAST1149

Proteomic databases

PaxDbiA8MYU2.
PRIDEiA8MYU2.

PTM databases

iPTMnetiA8MYU2.
PhosphoSitePlusiA8MYU2.

Expressioni

Tissue specificityi

Testis-specific.1 Publication

Gene expression databases

BgeeiENSG00000215262.
CleanExiHS_KCNU1.
ExpressionAtlasiA8MYU2. baseline and differential.
GenevisibleiA8MYU2. HS.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-60091N.
STRINGi9606.ENSP00000382770.

Structurei

Secondary structure

11149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi333 – 338Combined sources6
Helixi342 – 349Combined sources8
Beta strandi363 – 365Combined sources3
Turni382 – 385Combined sources4
Beta strandi386 – 388Combined sources3
Helixi397 – 403Combined sources7
Helixi405 – 407Combined sources3
Beta strandi408 – 413Combined sources6
Helixi422 – 439Combined sources18
Beta strandi445 – 448Combined sources4
Helixi452 – 456Combined sources5
Helixi457 – 460Combined sources4
Turni466 – 469Combined sources4
Beta strandi471 – 473Combined sources3
Helixi475 – 488Combined sources14
Helixi492 – 498Combined sources7
Helixi512 – 521Combined sources10
Beta strandi527 – 529Combined sources3
Helixi532 – 534Combined sources3
Helixi539 – 549Combined sources11
Beta strandi553 – 558Combined sources6
Beta strandi571 – 573Combined sources3
Beta strandi585 – 591Combined sources7
Helixi593 – 597Combined sources5
Helixi598 – 600Combined sources3
Beta strandi685 – 690Combined sources6
Helixi697 – 700Combined sources4
Beta strandi716 – 720Combined sources5
Helixi732 – 735Combined sources4
Helixi736 – 739Combined sources4
Helixi745 – 747Combined sources3
Beta strandi751 – 755Combined sources5
Helixi757 – 763Combined sources7
Helixi764 – 767Combined sources4
Beta strandi771 – 778Combined sources8
Helixi783 – 788Combined sources6
Helixi791 – 793Combined sources3
Beta strandi795 – 800Combined sources6
Helixi815 – 825Combined sources11
Beta strandi861 – 864Combined sources4
Helixi868 – 870Combined sources3
Helixi871 – 878Combined sources8
Turni882 – 884Combined sources3
Helixi889 – 891Combined sources3
Helixi893 – 897Combined sources5
Beta strandi899 – 901Combined sources3
Helixi903 – 908Combined sources6
Helixi909 – 915Combined sources7
Helixi917 – 928Combined sources12
Beta strandi962 – 966Combined sources5
Beta strandi968 – 971Combined sources4
Helixi972 – 975Combined sources4
Helixi982 – 993Combined sources12
Beta strandi996 – 1003Combined sources8
Beta strandi1015 – 1020Combined sources6
Beta strandi1032 – 1037Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HPFX-ray3.40A/B330-1062[»]
ProteinModelPortaliA8MYU2.
SMRiA8MYU2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini339 – 482RCK N-terminalAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni480 – 500Segment S7Add BLAST21
Regioni537 – 557Segment S8Add BLAST21
Regioni711 – 731Segment S9Add BLAST21
Regioni895 – 915Segment S10Add BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi276 – 279Selectivity for potassium4

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.By similarity

Sequence similaritiesi

Contains 1 RCK N-terminal domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1420. Eukaryota.
ENOG410YUX1. LUCA.
GeneTreeiENSGT00530000063026.
HOGENOMiHOG000019856.
HOVERGENiHBG052222.
InParanoidiA8MYU2.
KOiK05274.
OMAiDSSGMFH.
OrthoDBiEOG091G148D.
PhylomeDBiA8MYU2.
TreeFamiTF314283.

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.

A8MYU2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQTKLRNET WEDLPKMSCT TEIQAAFILS SFVTFFSGLI ILLIFRLIWR
60 70 80 90 100
SVKKWQIIKG TGIILELFTS GTIARSHVRS LHFQGQFRDH IEMLLSAQTF
110 120 130 140 150
VGQVLVILVF VLSIGSLIIY FINSADPVGS CSSYEDKTIP IDLVFNAFFS
160 170 180 190 200
FYFGLRFMAA DDKIKFWLEM NSIVDIFTIP PTFISYYLKS NWLGLRFLRA
210 220 230 240 250
LRLLELPQIL QILRAIKTSN SVKFSKLLSI ILSTWFTAAG FIHLVENSGD
260 270 280 290 300
PWLKGRNSQN ISYFESIYLV MATTSTVGFG DVVAKTSLGR TFIMFFTLGS
310 320 330 340 350
LILFANYIPE MVELFANKRK YTSSYEALKG KKFIVVCGNI TVDSVTAFLR
360 370 380 390 400
NFLRDKSGEI NTEIVFLGET PPSLELETIF KCYLAYTTFI SGSAMKWEDL
410 420 430 440 450
RRVAVESAEA CLIIANPLCS DSHAEDISNI MRVLSIKNYD STTRIIIQIL
460 470 480 490 500
QSHNKVYLPK IPSWNWDTGD NIICFAELKL GFIAQGCLVP GLCTFLTSLF
510 520 530 540 550
VEQNKKVMPK QTWKKHFLNS MKNKILTQRL SDDFAGMSFP EVARLCFLKM
560 570 580 590 600
HLLLIAIEYK SLFTDGFCGL ILNPPPQVRI RKNTLGFFIA ETPKDVRRAL
610 620 630 640 650
FYCSVCHDDV FIPELITNCG CKSRSRQHIT VPSVKRMKKC LKGISSRISG
660 670 680 690 700
QDSPPRVSAS TSSISNFTTR TLQHDVEQDS DQLDSSGMFH WCKPTSLDKV
710 720 730 740 750
TLKRTGKSKY KFRNHIVACV FGDAHSAPMG LRNFVMPLRA SNYTRKELKD
760 770 780 790 800
IVFIGSLDYL QREWRFLWNF PQIYILPGCA LYSGDLHAAN IEQCSMCAVL
810 820 830 840 850
SPPPQPSSNQ TLVDTEAIMA TLTIGSLQID SSSDPSPSVS EETPGYTNGH
860 870 880 890 900
NEKSNCRKVP ILTELKNPSN IHFIEQLGGL EGSLQETNLH LSTAFSTGTV
910 920 930 940 950
FSGSFLDSLL ATAFYNYHVL ELLQMLVTGG VSSQLEQHLD KDKVYGVADS
960 970 980 990 1000
CTSLLSGRNR CKLGLLSLHE TILSDVNPRN TFGQLFCGSL DLFGILCVGL
1010 1020 1030 1040 1050
YRIIDEEELN PENKRFVITR PANEFKLLPS DLVFCAIPFS TACYKRNEEF
1060 1070 1080 1090 1100
SLQKSYEIVN KASQTTETHS DTNCPPTIDS VTETLYSPVY SYQPRTNSLS
1110 1120 1130 1140
FPKQIAWNQS RTNSIISSQI PLGDNAKENE RKTSDEVYDE DPFAYSEPL
Length:1,149
Mass (Da):129,543
Last modified:September 2, 2008 - v2
Checksum:iBA527F41498B6AA7
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_060148175D → N.Corresponds to variant rs1111125dbSNPEnsembl.1
Natural variantiVAR_053868768W → R.Corresponds to variant rs28608091dbSNPEnsembl.1
Natural variantiVAR_053869916N → S.Corresponds to variant rs16885577dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC124076 Genomic DNA. No translation available.
CCDSiCCDS55220.1.
RefSeqiNP_001027006.2. NM_001031836.2.
UniGeneiHs.13861.

Genome annotation databases

EnsembliENST00000399881; ENSP00000382770; ENSG00000215262.
GeneIDi157855.
KEGGihsa:157855.
UCSCiuc010lvw.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC124076 Genomic DNA. No translation available.
CCDSiCCDS55220.1.
RefSeqiNP_001027006.2. NM_001031836.2.
UniGeneiHs.13861.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HPFX-ray3.40A/B330-1062[»]
ProteinModelPortaliA8MYU2.
SMRiA8MYU2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60091N.
STRINGi9606.ENSP00000382770.

Chemistry databases

GuidetoPHARMACOLOGYi387.

PTM databases

iPTMnetiA8MYU2.
PhosphoSitePlusiA8MYU2.

Polymorphism and mutation databases

BioMutaiKCNU1.

Proteomic databases

PaxDbiA8MYU2.
PRIDEiA8MYU2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000399881; ENSP00000382770; ENSG00000215262.
GeneIDi157855.
KEGGihsa:157855.
UCSCiuc010lvw.5. human.

Organism-specific databases

CTDi157855.
DisGeNETi157855.
GeneCardsiKCNU1.
H-InvDBHIX0020845.
HGNCiHGNC:18867. KCNU1.
MIMi615215. gene.
neXtProtiNX_A8MYU2.
OpenTargetsiENSG00000215262.
PharmGKBiPA38727.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1420. Eukaryota.
ENOG410YUX1. LUCA.
GeneTreeiENSGT00530000063026.
HOGENOMiHOG000019856.
HOVERGENiHBG052222.
InParanoidiA8MYU2.
KOiK05274.
OMAiDSSGMFH.
OrthoDBiEOG091G148D.
PhylomeDBiA8MYU2.
TreeFamiTF314283.

Enzyme and pathway databases

BioCyciZFISH:G66-33782-MONOMER.
ReactomeiR-HSA-1300642. Sperm Motility And Taxes.

Miscellaneous databases

GeneWikiiKCNU1.
GenomeRNAii157855.
PROiA8MYU2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000215262.
CleanExiHS_KCNU1.
ExpressionAtlasiA8MYU2. baseline and differential.
GenevisibleiA8MYU2. HS.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiKCNU1_HUMAN
AccessioniPrimary (citable) accession number: A8MYU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: November 30, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.