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Protein

Calcium-activated potassium channel subunit alpha-1

Gene

KCNMA1

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

Functioni

Potassium channel activated by both membrane depolarization or increase in cytosolic Ca2+ that mediates export of K+. It is also activated by the concentration of cytosolic Mg2+. Its activation dampens the excitatory events that elevate the cytosolic Ca2+ concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca2+, caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX).

Enzyme regulationi

Ethanol and carbon monoxide-bound heme increase channel activation. Heme inhibits channel activation.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi439MagnesiumBy similarity1
Metal bindingi462MagnesiumBy similarity1
Metal bindingi464MagnesiumBy similarity1
Metal bindingi1012Calcium; via carbonyl oxygen1
Metal bindingi1015Calcium; via carbonyl oxygen1
Metal bindingi1018Calcium1
Metal bindingi1020Calcium1

GO - Molecular functioni

  • actin binding Source: BHF-UCL
  • calcium-activated potassium channel activity Source: UniProtKB
  • large conductance calcium-activated potassium channel activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • voltage-gated potassium channel activity Source: UniProtKB

GO - Biological processi

  • cellular potassium ion homeostasis Source: UniProtKB
  • micturition Source: UniProtKB
  • negative regulation of cell volume Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • potassium ion transport Source: UniProtKB
  • regulation of membrane potential Source: UniProtKB
  • response to calcium ion Source: UniProtKB
  • response to carbon monoxide Source: UniProtKB
  • response to hypoxia Source: UniProtKB
  • response to osmotic stress Source: UniProtKB
  • smooth muscle contraction involved in micturition Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Potassium

Enzyme and pathway databases

ReactomeiR-HSA-1296052. Ca2+ activated K+ channels.
R-HSA-418457. cGMP effects.
SIGNORiQ12791.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-activated potassium channel subunit alpha-1
Alternative name(s):
BK channel
BKCA alpha
Calcium-activated potassium channel, subfamily M subunit alpha-1
K(VCA)alpha
KCa1.1
Maxi K channel
Short name:
MaxiK
Slo-alpha
Slo1
Slowpoke homolog
Short name:
Slo homolog
Short name:
hSlo
Gene namesi
Name:KCNMA1
Synonyms:KCNMA, SLO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:6284. KCNMA1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 86ExtracellularSequence analysisAdd BLAST86
Transmembranei87 – 107Helical; Name=Segment S0Sequence analysisAdd BLAST21
Topological domaini108 – 178CytoplasmicSequence analysisAdd BLAST71
Transmembranei179 – 199Helical; Name=Segment S1Sequence analysisAdd BLAST21
Topological domaini200 – 214ExtracellularSequence analysisAdd BLAST15
Transmembranei215 – 235Helical; Name=Segment S2Sequence analysisAdd BLAST21
Topological domaini236 – 239CytoplasmicSequence analysis4
Transmembranei240 – 260Helical; Name=Segment S3Sequence analysisAdd BLAST21
Topological domaini261 – 264ExtracellularSequence analysis4
Transmembranei265 – 285Helical; Name=Segment S4Sequence analysisAdd BLAST21
Topological domaini286 – 300CytoplasmicSequence analysisAdd BLAST15
Transmembranei301 – 321Helical; Name=Segment S5Sequence analysisAdd BLAST21
Topological domaini322 – 335ExtracellularSequence analysisAdd BLAST14
Intramembranei336 – 358Pore-forming; Name=P regionSequence analysisAdd BLAST23
Topological domaini359 – 367ExtracellularSequence analysis9
Transmembranei368 – 388Helical; Name=Segment S6Sequence analysisAdd BLAST21
Topological domaini389 – 1236CytoplasmicSequence analysisAdd BLAST848

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • caveola Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • plasma membrane Source: Reactome
  • voltage-gated potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Generalized epilepsy and paroxysmal dyskinesia (GEPD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionEpilepsy is one of the most common and debilitating neurological disorders. Paroxysmal dyskinesias are neurological disorders characterized by sudden, unpredictable, disabling attacks of involuntary movement often requiring life-long treatment. The coexistence of epilepsy and paroxysmal dyskinesia in the same individual or family is an increasingly recognized phenomenon. Patients manifest absence seizures, generalized tonic-clonic seizures, paroxysmal nonkinesigenic dyskinesia, involuntary dystonic or choreiform movements. Onset is usually in childhood and patients may have seizures only, dyskinesia only, or both.
See also OMIM:609446
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023821434D → G in GEPD; may have a synergistic effect with ethanol in the triggering of symptoms. 1 PublicationCorresponds to variant rs137853333dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi118C → A: Decreased localization to the plasma membrane. Abolishes localization to the plasma membrane; when associated with A-119 and A-121. 2 Publications1
Mutagenesisi119C → A: Decreased localization to the plasma membrane. Abolishes localization to the plasma membrane; when associated with A-118 and A-121. 2 Publications1
Mutagenesisi121C → A: Decreased localization to the plasma membrane. Abolishes localization to the plasma membrane; when associated with A-119 and A-121. 2 Publications1
Mutagenesisi269L → R or H: No effect in the coupling between calcium and channel opening. 1 Publication1
Mutagenesisi272R → E: Induces reduction in the coupling between calcium and channel opening. 1 Publication1
Mutagenesisi275R → N: Induces reduction in the coupling between calcium and channel opening. 1 Publication1
Mutagenesisi278R → Q: Induces reduction in the coupling between calcium and channel opening. 1 Publication1
Mutagenesisi281Q → R: No effect in the coupling between calcium and channel opening. 1 Publication1
Mutagenesisi284E → K: No effect in the coupling between calcium and channel opening. 1 Publication1
Mutagenesisi352T → S: Activated at more negative voltages. Slower rate of inactivation. Impaired inhibition by HMIMP. No effect on channel inhibition by Iberiotoxin. 1 Publication1
Mutagenesisi354 – 356GYG → AAA: Loss of function. 1 Publication3
Mutagenesisi380F → A: Loss of function. 1 Publication1
Mutagenesisi381A → S: Activated at more negative voltages. No effect on inhibition by HMIMP. 1 Publication1
Mutagenesisi384V → I: No effect on activation voltage. No effect on inhibition by HMIMP. 1 Publication1
Mutagenesisi680C → S: Loss of heme-induced channel inhibition. 1 Publication1
Mutagenesisi681H → R: Loss of heme-induced channel inhibition. 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

DisGeNETi3778.
MalaCardsiKCNMA1.
MIMi609446. phenotype.
OpenTargetsiENSG00000156113.
Orphaneti79137. Generalized epilepsy - paroxysmal dyskinesia.
PharmGKBiPA220.

Chemistry databases

ChEMBLiCHEMBL4304.
DrugBankiDB00436. Bendroflumethiazide.
DB00356. Chlorzoxazone.
DB01003. Cromoglicic acid.
DB01119. Diazoxide.
DB01159. Halothane.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB01110. Miconazole.
DB00721. Procaine.
GuidetoPHARMACOLOGYi380.

Polymorphism and mutation databases

BioMutaiKCNMA1.
DMDMi46396283.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000541321 – 1236Calcium-activated potassium channel subunit alpha-1Add BLAST1236

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi118S-palmitoyl cysteine2 Publications1
Lipidationi119S-palmitoyl cysteine2 Publications1
Lipidationi121S-palmitoyl cysteine2 Publications1
Modified residuei763PhosphothreonineBy similarity1
Modified residuei765PhosphoserineBy similarity1
Modified residuei778PhosphoserineBy similarity1
Modified residuei782PhosphoserineBy similarity1
Modified residuei970PhosphothreonineBy similarity1
Modified residuei978PhosphoserineBy similarity1
Modified residuei982PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated (Probable). Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity.Curated
Palmitoylation by ZDHHC22 and ZDHHC23 within the intracellular linker between the S0 and S1 transmembrane domains regulates localization to the plasma membrane. Depalmitoylated by LYPLA1 and LYPLAL1, leading to retard exit from the trans-Golgi network.2 Publications

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ12791.
PeptideAtlasiQ12791.
PRIDEiQ12791.

PTM databases

iPTMnetiQ12791.
PhosphoSitePlusiQ12791.
SwissPalmiQ12791.

Expressioni

Tissue specificityi

Widely expressed. Except in myocytes, it is almost ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000156113.
ExpressionAtlasiQ12791. baseline and differential.
GenevisibleiQ12791. HS.

Organism-specific databases

HPAiHPA054648.
HPA057838.

Interactioni

Subunit structurei

Homotetramer; which constitutes the calcium-activated potassium channel. Interacts with RAB11B (By similarity). Interacts with beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4. Interacts with gamma subunits LRRC26, LRRC38, LRRC52 and LRRC55. Beta and gamma subunits are accessory, and modulate its activity.By similarity6 Publications

GO - Molecular functioni

  • actin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109979. 10 interactors.
DIPiDIP-29729N.
IntActiQ12791. 2 interactors.
MINTiMINT-4825316.

Chemistry databases

BindingDBiQ12791.

Structurei

Secondary structure

11236
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi261 – 270Combined sources10
Helixi277 – 280Combined sources4
Beta strandi409 – 415Combined sources7
Helixi418 – 431Combined sources14
Turni433 – 437Combined sources5
Beta strandi439 – 443Combined sources5
Helixi450 – 453Combined sources4
Helixi456 – 459Combined sources4
Beta strandi461 – 466Combined sources6
Beta strandi470 – 472Combined sources3
Helixi473 – 478Combined sources6
Helixi481 – 483Combined sources3
Beta strandi485 – 490Combined sources6
Helixi498 – 515Combined sources18
Beta strandi521 – 526Combined sources6
Helixi528 – 531Combined sources4
Helixi532 – 536Combined sources5
Turni542 – 545Combined sources4
Beta strandi547 – 550Combined sources4
Helixi551 – 564Combined sources14
Helixi568 – 573Combined sources6
Turni574 – 576Combined sources3
Beta strandi586 – 588Combined sources3
Helixi589 – 597Combined sources9
Beta strandi600 – 605Combined sources6
Helixi608 – 610Combined sources3
Helixi615 – 624Combined sources10
Beta strandi629 – 634Combined sources6
Beta strandi638 – 640Combined sources3
Beta strandi645 – 647Combined sources3
Beta strandi659 – 665Combined sources7
Helixi667 – 671Combined sources5
Turni672 – 674Combined sources3
Helixi803 – 805Combined sources3
Helixi823 – 825Combined sources3
Helixi830 – 835Combined sources6
Beta strandi842 – 847Combined sources6
Beta strandi850 – 852Combined sources3
Helixi858 – 861Combined sources4
Helixi863 – 865Combined sources3
Beta strandi867 – 869Combined sources3
Helixi871 – 873Combined sources3
Beta strandi877 – 881Combined sources5
Helixi883 – 893Combined sources11
Beta strandi896 – 904Combined sources9
Helixi909 – 914Combined sources6
Helixi917 – 919Combined sources3
Beta strandi921 – 927Combined sources7
Beta strandi936 – 938Combined sources3
Helixi941 – 951Combined sources11
Helixi996 – 998Combined sources3
Beta strandi1001 – 1006Combined sources6
Helixi1008 – 1011Combined sources4
Beta strandi1016 – 1018Combined sources3
Helixi1026 – 1028Combined sources3
Helixi1030 – 1033Combined sources4
Beta strandi1037 – 1039Combined sources3
Helixi1040 – 1044Combined sources5
Helixi1046 – 1052Combined sources7
Helixi1054 – 1064Combined sources11
Helixi1073 – 1079Combined sources7
Helixi1089 – 1093Combined sources5
Beta strandi1099 – 1104Combined sources6
Turni1105 – 1107Combined sources3
Turni1109 – 1111Combined sources3
Helixi1112 – 1114Combined sources3
Helixi1119 – 1129Combined sources11
Beta strandi1133 – 1141Combined sources9
Beta strandi1144 – 1146Combined sources3
Beta strandi1154 – 1159Combined sources6
Beta strandi1171 – 1176Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K44NMR-A257-284[»]
3MT5X-ray3.00A406-1179[»]
3NAFX-ray3.10A395-681[»]
A782-1182[»]
ProteinModelPortaliQ12791.
SMRiQ12791.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12791.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini415 – 558RCK N-terminalAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni556 – 576Segment S7Add BLAST21
Regioni613 – 633Segment S8Add BLAST21
Regioni677 – 681Heme-binding motif5
Regioni837 – 857Segment S9Add BLAST21
Regioni1032 – 1052Segment S10Add BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi352 – 355Selectivity for potassium4
Motifi1003 – 1025Calcium bowlAdd BLAST23

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 10Poly-Gly7
Compositional biasi13 – 20Poly-Gly8
Compositional biasi39 – 60Poly-SerAdd BLAST22

Domaini

The S0 segment is essential for the modulation by the accessory beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4.
The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor.
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.
The RCK N-terminal domain mediates the homotetramerization, thereby promoting the assembly of monomers into functional potassium channel. It includes binding sites for Ca2+ and Mg2+ (By similarity).By similarity
The calcium bowl constitutes one of the Ca2+ sensors and probably acts as a Ca2+-binding site. There are however other Ca2+ sensors regions required for activation of the channel.
The heme-binding motif mediates inhibition of channel activation by heme. Carbon monoxide-bound heme leads to increased channel activation.

Sequence similaritiesi

Contains 1 RCK N-terminal domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000063026.
HOVERGENiHBG052222.
InParanoidiQ12791.
KOiK04936.
PhylomeDBiQ12791.
TreeFamiTF314283.

Family and domain databases

Gene3Di3.40.50.720. 3 hits.
InterProiIPR005821. Ion_trans_dom.
IPR003929. K_chnl_Ca-activ_BK_asu.
IPR016040. NAD(P)-bd_dom.
IPR028325. VG_K_chnl.
[Graphical view]
PfamiPF03493. BK_channel_a. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01449. BKCHANNELA.
PR00169. KCHANNEL.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Note: May be partially controlled by hormonal stress. Additional isoforms seem to exist.
Isoform 1 (identifier: Q12791-1) [UniParc]FASTAAdd to basket
Also known as: SAKCA

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS
60 70 80 90 100
SSSSSSSSSS VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG
110 120 130 140 150
GLFIILLWRT LKYLWTVCCH CGGKTKEAQK INNGSSQADG TLKPVDEKEE
160 170 180 190 200
AVAAEVGWMT SVKDWAGVMI SAQTLTGRVL VVLVFALSIG ALVIYFIDSS
210 220 230 240 250
NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL WFWLEVNSVV
260 270 280 290 300
DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL
310 320 330 340 350
VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM
360 370 380 390 400
STVGYGDVYA KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS
410 420 430 440 450
YSAVSGRKHI VVCGHITLES VSNFLKDFLH KDRDDVNVEI VFLHNISPNL
460 470 480 490 500
ELEALFKRHF TQVEFYQGSV LNPHDLARVK IESADACLIL ANKYCADPDA
510 520 530 540 550
EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW NWKEGDDAIC
560 570 580 590 600
LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE
610 620 630 640 650
MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRILINPGN
660 670 680 690 700
HLKIQEGTLG FFIASDAKEV KRAFFYCKAC HDDITDPKRI KKCGCKRPKM
710 720 730 740 750
SIYKRMRRAC CFDCGRSERD CSCMSGRVRG NVDTLERAFP LSSVSVNDCS
760 770 780 790 800
TSFRAFEDEQ PSTLSPKKKQ RNGGMRNSPN TSPKLMRHDP LLIPGNDQID
810 820 830 840 850
NMDSNVKKYD STGMFHWCAP KEIEKVILTR SEAAMTVLSG HVVVCIFGDV
860 870 880 890 900
SSALIGLRNL VMPLRASNFH YHELKHIVFV GSIEYLKREW ETLHNFPKVS
910 920 930 940 950
ILPGTPLSRA DLRAVNINLC DMCVILSANQ NNIDDTSLQD KECILASLNI
960 970 980 990 1000
KSMQFDDSIG VLQANSQGFT PPGMDRSSPD NSPVHGMLRQ PSITTGVNIP
1010 1020 1030 1040 1050
IITELVNDTN VQFLDQDDDD DPDTELYLTQ PFACGTAFAV SVLDSLMSAT
1060 1070 1080 1090 1100
YFNDNILTLI RTLVTGGATP ELEALIAEEN ALRGGYSTPQ TLANRDRCRV
1110 1120 1130 1140 1150
AQLALLDGPF ADLGDGGCYG DLFCKALKTY NMLCFGIYRL RDAHLSTPSQ
1160 1170 1180 1190 1200
CTKRYVITNP PYEFELVPTD LIFCLMQFDH NAGQSRASLS HSSHSSQSSS
1210 1220 1230
KKSSSVHSIP STANRQNRPK SRESRDKQKY VQEERL
Length:1,236
Mass (Da):137,560
Last modified:April 13, 2004 - v2
Checksum:iDF9BFEAF374BE553
GO
Isoform 2 (identifier: Q12791-2) [UniParc]FASTAAdd to basket
Also known as: BKTM

The sequence of this isoform differs from the canonical sequence as follows:
     698-756: PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERAFPLSSVSVNDCSTSFRAF → L
     828-828: L → LVTGWMPYLGPRVLMTCLDIGVVCMPTDIQSTSPASIKKFKE

Show »
Length:1,219
Mass (Da):135,495
Checksum:i932986BE30E0D409
GO
Isoform 3 (identifier: Q12791-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     643-643: R → RSRKR

Show »
Length:1,240
Mass (Da):138,087
Checksum:i83DA8EC8C379A3D9
GO
Isoform 4 (identifier: Q12791-4) [UniParc]FASTAAdd to basket
Also known as: hbr5

The sequence of this isoform differs from the canonical sequence as follows:
     698-756: PKMSIYKRMR...NDCSTSFRAF → LKVAARSRYSKDPFEFKKETPNSRLVTEPV

Show »
Length:1,207
Mass (Da):134,362
Checksum:i7B9C03A8BFA5055B
GO
Isoform 5 (identifier: Q12791-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     698-756: PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERAFPLSSVSVNDCSTSFRAF → L

Show »
Length:1,178
Mass (Da):130,999
Checksum:iAD3C9634F8A21EEC
GO
Isoform 6 (identifier: Q12791-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-168: EAQKINNGSS...MTSVKDWAGV → ATHFGSPEMP...ALEVARCRRL
     169-1236: Missing.

Note: No experimental confirmation available.
Show »
Length:168
Mass (Da):17,191
Checksum:i101980B6E7017A03
GO
Isoform 7 (identifier: Q12791-7) [UniParc]FASTAAdd to basket
Also known as: gBK

The sequence of this isoform differs from the canonical sequence as follows:
     698-756: PKMSIYKRMR...NDCSTSFRAF → RWEEHCSLWR...PNSRLVTEPV

Show »
Length:1,239
Mass (Da):138,297
Checksum:iCE8B6449D8C7B9CC
GO

Sequence cautioni

The sequence AAA50216 differs from that shown. Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence AAB65837 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAC50353 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAK91504 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD06365 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25M → N in AAA50216 (PubMed:7987297).Curated1
Sequence conflicti35S → G in AAA50216 (PubMed:7987297).Curated1
Sequence conflicti38A → V in AAA85104 (PubMed:7877450).Curated1
Sequence conflicti449N → D in AAD31173 (Ref. 12) Curated1
Sequence conflicti805N → H in AAC50353 (PubMed:7993625).Curated1
Sequence conflicti1152T → A in AAD31173 (Ref. 12) Curated1
Sequence conflicti1230 – 1236YVQEERL → KEMVYR in CAI39730 (PubMed:15164054).Curated7
Sequence conflicti1230 – 1236YVQEERL → KEMVYR in CAI40870 (PubMed:15164054).Curated7
Sequence conflicti1230 – 1236YVQEERL → KEMVYR in CAI14074 (PubMed:15164054).Curated7
Sequence conflicti1230 – 1236YVQEERL → KEMVYR in CAI16162 (PubMed:15164054).Curated7
Isoform 7 (identifier: Q12791-7)
Sequence conflicti726 – 727FS → SF no nucleotide entry (PubMed:11880513).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023821434D → G in GEPD; may have a synergistic effect with ethanol in the triggering of symptoms. 1 PublicationCorresponds to variant rs137853333dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_009952127 – 168EAQKI…DWAGV → ATHFGSPEMPPAARSWSGSP PEAAVLRGASSLALEVARCR RL in isoform 6. 1 PublicationAdd BLAST42
Alternative sequenceiVSP_009953169 – 1236Missing in isoform 6. 1 PublicationAdd BLAST1068
Alternative sequenceiVSP_009954643R → RSRKR in isoform 3. 1 Publication1
Alternative sequenceiVSP_009955698 – 756PKMSI…SFRAF → L in isoform 2 and isoform 5. 9 PublicationsAdd BLAST59
Alternative sequenceiVSP_009956698 – 756PKMSI…SFRAF → LKVAARSRYSKDPFEFKKET PNSRLVTEPV in isoform 4. 2 PublicationsAdd BLAST59
Alternative sequenceiVSP_009957698 – 756PKMSI…SFRAF → RWEEHCSLWRLESKGNVRRL NYCRGQQTFSVKVKVAARSR YSKDPFEFKKETPNSRLVTE PV in isoform 7. CuratedAdd BLAST59
Alternative sequenceiVSP_009958828L → LVTGWMPYLGPRVLMTCLDI GVVCMPTDIQSTSPASIKKF KE in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13913 mRNA. Translation: AAA85104.1.
U23767 mRNA. Translation: AAA92290.1.
AL157833
, AL731560, AL731556, AL627447, AC021032, AC011439 Genomic DNA. Translation: CAI39730.1.
AL157833
, AC011439, AC021032, AL627447, AL731556, AL731560 Genomic DNA. Translation: CAI39736.1.
AL627447
, AL731560, AL731556, AC021032, AC011439, AL157833 Genomic DNA. Translation: CAI16162.1.
AL627447
, AC011439, AC021032, AL157833, AL731556, AL731560 Genomic DNA. Translation: CAI16171.1.
AL731556
, AC011439, AL157833, AC021032, AL731560, AL627447 Genomic DNA. Translation: CAI14074.1.
AL731556
, AC011439, AC021032, AL157833, AL627447, AL731560 Genomic DNA. Translation: CAI14082.1.
AL731560
, AL157833, AL731556, AC021032, AC011439, AL627447 Genomic DNA. Translation: CAI40870.1.
AL731560
, AC011439, AC021032, AL157833, AL627447, AL731556 Genomic DNA. Translation: CAI40877.1.
AC067745 Genomic DNA. No translation available.
AL607069 Genomic DNA. No translation available.
AL731575 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54599.1.
BC062659 mRNA. Translation: AAH62659.1.
BC137115 mRNA. Translation: AAI37116.1.
BC137137 mRNA. Translation: AAI37138.1.
U11717 mRNA. Translation: AAC50353.1. Different initiation.
AY040849 mRNA. Translation: AAK91504.1. Different initiation.
AB113575 mRNA. Translation: BAD06397.1.
AB113382 mRNA. Translation: BAD06365.1. Different initiation.
U02632 mRNA. Translation: AAA50173.1.
U09384 mRNA. Translation: AAA50216.1. Sequence problems.
AF025999 mRNA. Translation: AAB88802.1.
U11058 mRNA. Translation: AAB65837.1. Different initiation.
AF118141 mRNA. Translation: AAD31173.1.
CCDSiCCDS53545.1. [Q12791-2]
CCDS60569.1. [Q12791-1]
CCDS60571.1. [Q12791-6]
CCDS7352.1. [Q12791-5]
PIRiI38596.
S62904.
RefSeqiNP_001014797.1. NM_001014797.2.
NP_001154824.1. NM_001161352.1. [Q12791-1]
NP_001154825.1. NM_001161353.1. [Q12791-2]
NP_001258447.1. NM_001271518.1.
NP_001258451.1. NM_001271522.1. [Q12791-6]
NP_002238.2. NM_002247.3. [Q12791-5]
UniGeneiHs.144795.
Hs.658064.

Genome annotation databases

EnsembliENST00000286627; ENSP00000286627; ENSG00000156113. [Q12791-5]
ENST00000286628; ENSP00000286628; ENSG00000156113. [Q12791-1]
ENST00000480683; ENSP00000474686; ENSG00000156113. [Q12791-6]
ENST00000626620; ENSP00000485867; ENSG00000156113. [Q12791-2]
GeneIDi3778.
KEGGihsa:3778.
UCSCiuc001jxm.4. human. [Q12791-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13913 mRNA. Translation: AAA85104.1.
U23767 mRNA. Translation: AAA92290.1.
AL157833
, AL731560, AL731556, AL627447, AC021032, AC011439 Genomic DNA. Translation: CAI39730.1.
AL157833
, AC011439, AC021032, AL627447, AL731556, AL731560 Genomic DNA. Translation: CAI39736.1.
AL627447
, AL731560, AL731556, AC021032, AC011439, AL157833 Genomic DNA. Translation: CAI16162.1.
AL627447
, AC011439, AC021032, AL157833, AL731556, AL731560 Genomic DNA. Translation: CAI16171.1.
AL731556
, AC011439, AL157833, AC021032, AL731560, AL627447 Genomic DNA. Translation: CAI14074.1.
AL731556
, AC011439, AC021032, AL157833, AL627447, AL731560 Genomic DNA. Translation: CAI14082.1.
AL731560
, AL157833, AL731556, AC021032, AC011439, AL627447 Genomic DNA. Translation: CAI40870.1.
AL731560
, AC011439, AC021032, AL157833, AL627447, AL731556 Genomic DNA. Translation: CAI40877.1.
AC067745 Genomic DNA. No translation available.
AL607069 Genomic DNA. No translation available.
AL731575 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54599.1.
BC062659 mRNA. Translation: AAH62659.1.
BC137115 mRNA. Translation: AAI37116.1.
BC137137 mRNA. Translation: AAI37138.1.
U11717 mRNA. Translation: AAC50353.1. Different initiation.
AY040849 mRNA. Translation: AAK91504.1. Different initiation.
AB113575 mRNA. Translation: BAD06397.1.
AB113382 mRNA. Translation: BAD06365.1. Different initiation.
U02632 mRNA. Translation: AAA50173.1.
U09384 mRNA. Translation: AAA50216.1. Sequence problems.
AF025999 mRNA. Translation: AAB88802.1.
U11058 mRNA. Translation: AAB65837.1. Different initiation.
AF118141 mRNA. Translation: AAD31173.1.
CCDSiCCDS53545.1. [Q12791-2]
CCDS60569.1. [Q12791-1]
CCDS60571.1. [Q12791-6]
CCDS7352.1. [Q12791-5]
PIRiI38596.
S62904.
RefSeqiNP_001014797.1. NM_001014797.2.
NP_001154824.1. NM_001161352.1. [Q12791-1]
NP_001154825.1. NM_001161353.1. [Q12791-2]
NP_001258447.1. NM_001271518.1.
NP_001258451.1. NM_001271522.1. [Q12791-6]
NP_002238.2. NM_002247.3. [Q12791-5]
UniGeneiHs.144795.
Hs.658064.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K44NMR-A257-284[»]
3MT5X-ray3.00A406-1179[»]
3NAFX-ray3.10A395-681[»]
A782-1182[»]
ProteinModelPortaliQ12791.
SMRiQ12791.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109979. 10 interactors.
DIPiDIP-29729N.
IntActiQ12791. 2 interactors.
MINTiMINT-4825316.

Chemistry databases

BindingDBiQ12791.
ChEMBLiCHEMBL4304.
DrugBankiDB00436. Bendroflumethiazide.
DB00356. Chlorzoxazone.
DB01003. Cromoglicic acid.
DB01119. Diazoxide.
DB01159. Halothane.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB01110. Miconazole.
DB00721. Procaine.
GuidetoPHARMACOLOGYi380.

PTM databases

iPTMnetiQ12791.
PhosphoSitePlusiQ12791.
SwissPalmiQ12791.

Polymorphism and mutation databases

BioMutaiKCNMA1.
DMDMi46396283.

Proteomic databases

MaxQBiQ12791.
PeptideAtlasiQ12791.
PRIDEiQ12791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000286627; ENSP00000286627; ENSG00000156113. [Q12791-5]
ENST00000286628; ENSP00000286628; ENSG00000156113. [Q12791-1]
ENST00000480683; ENSP00000474686; ENSG00000156113. [Q12791-6]
ENST00000626620; ENSP00000485867; ENSG00000156113. [Q12791-2]
GeneIDi3778.
KEGGihsa:3778.
UCSCiuc001jxm.4. human. [Q12791-1]

Organism-specific databases

CTDi3778.
DisGeNETi3778.
GeneCardsiKCNMA1.
HGNCiHGNC:6284. KCNMA1.
HPAiHPA054648.
HPA057838.
MalaCardsiKCNMA1.
MIMi600150. gene.
609446. phenotype.
neXtProtiNX_Q12791.
OpenTargetsiENSG00000156113.
Orphaneti79137. Generalized epilepsy - paroxysmal dyskinesia.
PharmGKBiPA220.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000063026.
HOVERGENiHBG052222.
InParanoidiQ12791.
KOiK04936.
PhylomeDBiQ12791.
TreeFamiTF314283.

Enzyme and pathway databases

ReactomeiR-HSA-1296052. Ca2+ activated K+ channels.
R-HSA-418457. cGMP effects.
SIGNORiQ12791.

Miscellaneous databases

ChiTaRSiKCNMA1. human.
EvolutionaryTraceiQ12791.
GenomeRNAii3778.
PROiQ12791.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000156113.
ExpressionAtlasiQ12791. baseline and differential.
GenevisibleiQ12791. HS.

Family and domain databases

Gene3Di3.40.50.720. 3 hits.
InterProiIPR005821. Ion_trans_dom.
IPR003929. K_chnl_Ca-activ_BK_asu.
IPR016040. NAD(P)-bd_dom.
IPR028325. VG_K_chnl.
[Graphical view]
PfamiPF03493. BK_channel_a. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01449. BKCHANNELA.
PR00169. KCHANNEL.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKCMA1_HUMAN
AccessioniPrimary (citable) accession number: Q12791
Secondary accession number(s): F8WA96
, Q12886, Q12917, Q12921, Q12960, Q13150, Q5JQ23, Q5SQR9, Q96LG8, Q9UBB0, Q9UCX0, Q9UQK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: November 30, 2016
This is version 169 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

Miscellaneous

The protein was initially thought to contain two functionally distinct parts: The core channel (from the N-terminus to the S9 segment) that mediates the channel activity, and the cytoplasmic tail (from the S9 segment to the C-terminus) that mediates the calcium sensing. The situation is however more complex, since the core channel also contains binding sites for Ca2+ and Mg2+.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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.