Q12791 (KCMA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	KCNMA1
Synonyms:	KCNMA, SLO

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1236 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 regulation	Ethanol and carbon monoxide-bound heme increase channel activation. Heme inhibits channel activation. Ref.22
Subunit structure	Homotetramer; which constitutes the calcium-activated potassium channel. 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. Ref.18 Ref.19 Ref.20 Ref.21 Ref.24 Ref.26 Ref.27
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Widely expressed. Except in myocytes, it is almost ubiquitously expressed. Ref.13
Domain	The S0 segment is essential for the modulation by the accessory beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4. Ref.15 Ref.17 The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor. Ref.15 Ref.17 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. Ref.15 Ref.17 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. Ref.15 Ref.17 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. Ref.15 Ref.17 The heme-binding motif mediates inhibition of channel activation by heme. Carbon monoxide-bound heme leads to increased channel activation. Ref.15 Ref.17
Post-translational modification	Phosphorylated Probable. Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity.
Involvement in disease	Generalized epilepsy and paroxysmal dyskinesia (GEPD) [MIM:609446]: Epilepsy 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.28
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+.
Sequence similarities	Belongs to the potassium channel family. Calcium-activated (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily. [View classification] Contains 1 RCK N-terminal domain.
Sequence caution	The sequence AAA50216.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part. The sequence AAB65837.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAC50353.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAK91504.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAD06365.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Epilepsy
Domain	Transmembrane Transmembrane helix
Ligand	Calcium Magnesium Metal-binding Potassium
Molecular function	Ion channel Potassium channel Voltage-gated channel
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult walking behavior Inferred from electronic annotation. Source: Compara auditory receptor cell differentiation Inferred from electronic annotation. Source: Compara blood coagulation Traceable author statement. Source: Reactome cell maturation Inferred from electronic annotation. Source: Compara cellular potassium ion homeostasis Inferred from direct assay PubMed 11245614. Source: UniProtKB eye blink reflex Inferred from electronic annotation. Source: Compara locomotor rhythm Inferred from electronic annotation. Source: Compara negative regulation of cell volume Inferred from direct assay PubMed 12388065. Source: UniProtKB neuromuscular process controlling balance Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from mutant phenotype PubMed 11245614. Source: UniProtKB protein homooligomerization Inferred from electronic annotation. Source: Compara regulation of action potential in neuron Inferred from electronic annotation. Source: Compara regulation of aldosterone metabolic process Inferred from electronic annotation. Source: Compara regulation of membrane potential Inferred from direct assay Ref.1Ref.6. Source: UniProtKB relaxation of vascular smooth muscle Inferred from electronic annotation. Source: Compara response to calcium ion Inferred from direct assay PubMed 12388065PubMed 18458941. Source: UniProtKB response to carbon monoxide Inferred from direct assay PubMed 15528406. Source: UniProtKB response to hypoxia Inferred from direct assay PubMed 15528406. Source: UniProtKB response to osmotic stress Inferred from direct assay PubMed 10840032PubMed 12388065. Source: UniProtKB saliva secretion Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from electronic annotation. Source: Compara smooth muscle contraction involved in micturition Inferred from direct assay PubMed 11641143. Source: UniProtKB synaptic transmission Traceable author statement. Source: Reactome
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 10840032. Source: UniProtKB caveola Inferred from direct assay PubMed 15703204. Source: BHF-UCL endoplasmic reticulum Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to membrane Inferred from direct assay Ref.13. Source: UniProtKB postsynaptic membrane Inferred from electronic annotation. Source: Compara terminal bouton Inferred from electronic annotation. Source: Compara voltage-gated potassium channel complex Inferred from direct assay Ref.2Ref.1Ref.6. Source: UniProtKB
Molecular_function	actin binding Inferred from direct assay PubMed 15703204. Source: BHF-UCL calcium-activated potassium channel activity Inferred from direct assay Ref.13. Source: UniProtKB large conductance calcium-activated potassium channel activity Inferred from direct assay Ref.6. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro voltage-gated potassium channel activity Inferred from direct assay PubMed 12388065Ref.1Ref.6Ref.13. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Note: May be partially controlled by hormonal stress. Additional isoforms seem to exist.

Isoform 1 (identifier: Q12791-1)

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.

Isoform 2 (identifier: Q12791-2)

Also known as: BKTM;

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

Isoform 3 (identifier: Q12791-3)

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

Isoform 4 (identifier: Q12791-4)

Also known as: hbr5;

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

Isoform 5 (identifier: Q12791-5)

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

Isoform 6 (identifier: Q12791-6)

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.

Isoform 7 (identifier: Q12791-7)

Also known as: gBK;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1236

1236

Calcium-activated potassium channel subunit alpha-1

PRO_0000054132

Regions

Topological domain

1 – 86

86

Extracellular Potential

Transmembrane

87 – 107

21

Helical; Name=Segment S0; Potential

Topological domain

108 – 178

71

Cytoplasmic Potential

Transmembrane

179 – 199

21

Helical; Name=Segment S1; Potential

Topological domain

200 – 214

15

Extracellular Potential

Transmembrane

215 – 235

21

Helical; Name=Segment S2; Potential

Topological domain

236 – 239

4

Cytoplasmic Potential

Transmembrane

240 – 260

21

Helical; Name=Segment S3; Potential

Topological domain

261 – 264

4

Extracellular Potential

Transmembrane

265 – 285

21

Helical; Name=Segment S4; Potential

Topological domain

286 – 300

15

Cytoplasmic Potential

Transmembrane

301 – 321

21

Helical; Name=Segment S5; Potential

Topological domain

322 – 335

14

Extracellular Potential

Intramembrane

336 – 358

23

Pore-forming; Name=P region; Potential

Topological domain

359 – 367

9

Extracellular Potential

Transmembrane

368 – 388

21

Helical; Name=Segment S6; Potential

Topological domain

389 – 1236

848

Cytoplasmic Potential

Domain

415 – 558

144

RCK N-terminal

Region

556 – 576

21

Segment S7

Region

613 – 633

21

Segment S8

Region

677 – 681

5

Heme-binding motif

Region

837 – 857

21

Segment S9

Region

1032 – 1052

21

Segment S10

Motif

352 – 355

4

Selectivity for potassium

Motif

1003 – 1025

23

Calcium bowl

Compositional bias

4 – 10

7

Poly-Gly

Compositional bias

13 – 20

8

Poly-Gly

Compositional bias

39 – 60

22

Poly-Ser

Sites

Metal binding

439

1

Magnesium By similarity

Metal binding

462

1

Magnesium By similarity

Metal binding

464

1

Magnesium By similarity

Metal binding

1012

1

Calcium; via carbonyl oxygen

Metal binding

1015

1

Calcium; via carbonyl oxygen

Metal binding

1018

1

Calcium

Metal binding

1020

1

Calcium

Amino acid modifications

Modified residue

765

1

Phosphoserine By similarity

Modified residue

1088

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

127 – 168

42

EAQKI…DWAGV → ATHFGSPEMPPAARSWSGSP PEAAVLRGASSLALEVARCR RL in isoform 6.

VSP_009952

Alternative sequence

169 – 1236

1068

Missing in isoform 6.

VSP_009953

Alternative sequence

643

1

R → RSRKR in isoform 3.

VSP_009954

Alternative sequence

698 – 756

59

PKMSI…SFRAF → L in isoform 2 and isoform 5.

VSP_009955

Alternative sequence

698 – 756

59

PKMSI…SFRAF → LKVAARSRYSKDPFEFKKET PNSRLVTEPV in isoform 4.

VSP_009956

Alternative sequence

698 – 756

59

PKMSI…SFRAF → RWEEHCSLWRLESKGNVRRL NYCRGQQTSFVKVKVAARSR YSKDPFEFKKETPNSRLVTE PV in isoform 7.

VSP_009957

Alternative sequence

828

1

L → LVTGWMPYLGPRVLMTCLDI GVVCMPTDIQSTSPASIKKF KE in isoform 2.

VSP_009958

Natural variant

434

1

D → G in GEPD; may have a synergistic effect with ethanol in the triggering of symptoms. Ref.28

VAR_023821

Experimental info

Mutagenesis

269

1

L → R or H: No effect in the coupling between calcium and channel opening. Ref.17

Mutagenesis

272

1

R → E: Induces reduction in the coupling between calcium and channel opening. Ref.17

Mutagenesis

275

1

R → N: Induces reduction in the coupling between calcium and channel opening. Ref.17

Mutagenesis

278

1

R → Q: Induces reduction in the coupling between calcium and channel opening. Ref.17

Mutagenesis

281

1

Q → R: No effect in the coupling between calcium and channel opening. Ref.17

Mutagenesis

284

1

E → K: No effect in the coupling between calcium and channel opening. Ref.17

Mutagenesis

352

1

T → S: Activated at more negative voltages. Slower rate of inactivation. Impaired inhibition by HMIMP. No effect on channel inhibition by Iberiotoxin. Ref.25

Mutagenesis

354 – 356

3

GYG → AAA: Loss of function. Ref.20

Mutagenesis

380

1

F → A: Loss of function. Ref.25

Mutagenesis

381

1

A → S: Activated at more negative voltages. No effect on inhibition by HMIMP. Ref.25

Mutagenesis

384

1

V → I: No effect on activation voltage. No effect on inhibition by HMIMP. Ref.25

Mutagenesis

680

1

C → S: Loss of heme-induced channel inhibition. Ref.22

Mutagenesis

681

1

H → R: Loss of heme-induced channel inhibition. Ref.22

Sequence conflict

25

1

M → N in AAA50216. Ref.9

Sequence conflict

35

1

S → G in AAA50216. Ref.9

Sequence conflict

38

1

A → V in AAA85104. Ref.1

Sequence conflict

449

1

N → D in AAD31173. Ref.12

Sequence conflict

805

1

N → H in AAC50353. Ref.6

Sequence conflict

1152

1

T → A in AAD31173. Ref.12

Sequence conflict

1230 – 1236

7

YVQEERL → KEMVYR in CAI39730. Ref.3

Sequence conflict

1230 – 1236

7

YVQEERL → KEMVYR in CAI40870. Ref.3

Sequence conflict

1230 – 1236

7

YVQEERL → KEMVYR in CAI14074. Ref.3

Sequence conflict

1230 – 1236

7

YVQEERL → KEMVYR in CAI16162. Ref.3

Secondary structure

1

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1236

Helix Strand Turn

Details...

Helix

261 – 270

10

Helix

277 – 280

4

Beta strand

406 – 414

9

Helix

418 – 428

11

Beta strand

438 – 446

9

Helix

450 – 458

9

Turn

459 – 462

4

Beta strand

463 – 467

5

Beta strand

470 – 472

3

Helix

473 – 478

6

Helix

481 – 483

3

Beta strand

485 – 489

5

Helix

498 – 515

18

Beta strand

521 – 526

6

Helix

530 – 532

3

Helix

534 – 536

3

Turn

542 – 545

4

Beta strand

547 – 550

4

Helix

551 – 564

14

Helix

568 – 576

9

Helix

589 – 597

9

Beta strand

602 – 605

4

Helix

608 – 610

3

Helix

615 – 625

11

Beta strand

630 – 636

7

Beta strand

638 – 640

3

Beta strand

642 – 647

6

Beta strand

659 – 662

4

Helix

668 – 671

4

Helix

672 – 674

3

Helix

823 – 825

3

Helix

830 – 835

6

Beta strand

842 – 847

6

Beta strand

850 – 852

3

Helix

858 – 865

8

Beta strand

867 – 869

3

Beta strand

877 – 881

5

Helix

883 – 890

8

Turn

891 – 895

5

Beta strand

896 – 901

6

Helix

909 – 914

6

Beta strand

921 – 929

9

Beta strand

936 – 938

3

Helix

941 – 952

12

Beta strand

1001 – 1007

7

Helix

1010 – 1014

5

Helix

1026 – 1028

3

Helix

1030 – 1034

5

Beta strand

1036 – 1039

4

Helix

1042 – 1052

11

Helix

1055 – 1064

10

Helix

1069 – 1079

11

Helix

1091 – 1093

3

Beta strand

1099 – 1105

7

Turn

1110 – 1116

7

Helix

1119 – 1123

5

Helix

1125 – 1128

4

Beta strand

1136 – 1141

6

Beta strand

1144 – 1146

3

Beta strand

1154 – 1159

6

Beta strand

1171 – 1176

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SAKCA) [UniParc]. Last modified April 13, 2004. Version 2. Checksum: DF9BFEAF374BE553	FASTA	1,236	137,560
	10 20 30 40 50 60 MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS SSSSSSSSSS 70 80 90 100 110 120 VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH 130 140 150 160 170 180 CGGKTKEAQK INNGSSQADG TLKPVDEKEE AVAAEVGWMT SVKDWAGVMI SAQTLTGRVL 190 200 210 220 230 240 VVLVFALSIG ALVIYFIDSS NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL 250 260 270 280 290 300 WFWLEVNSVV DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL 310 320 330 340 350 360 VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM STVGYGDVYA 370 380 390 400 410 420 KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS YSAVSGRKHI VVCGHITLES 430 440 450 460 470 480 VSNFLKDFLH KDRDDVNVEI VFLHNISPNL ELEALFKRHF TQVEFYQGSV LNPHDLARVK 490 500 510 520 530 540 IESADACLIL ANKYCADPDA EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW 550 560 570 580 590 600 NWKEGDDAIC LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE 610 620 630 640 650 660 MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRILINPGN HLKIQEGTLG 670 680 690 700 710 720 FFIASDAKEV KRAFFYCKAC HDDITDPKRI KKCGCKRPKM SIYKRMRRAC CFDCGRSERD 730 740 750 760 770 780 CSCMSGRVRG NVDTLERAFP LSSVSVNDCS TSFRAFEDEQ PSTLSPKKKQ RNGGMRNSPN 790 800 810 820 830 840 TSPKLMRHDP LLIPGNDQID NMDSNVKKYD STGMFHWCAP KEIEKVILTR SEAAMTVLSG 850 860 870 880 890 900 HVVVCIFGDV SSALIGLRNL VMPLRASNFH YHELKHIVFV GSIEYLKREW ETLHNFPKVS 910 920 930 940 950 960 ILPGTPLSRA DLRAVNINLC DMCVILSANQ NNIDDTSLQD KECILASLNI KSMQFDDSIG 970 980 990 1000 1010 1020 VLQANSQGFT PPGMDRSSPD NSPVHGMLRQ PSITTGVNIP IITELVNDTN VQFLDQDDDD 1030 1040 1050 1060 1070 1080 DPDTELYLTQ PFACGTAFAV SVLDSLMSAT YFNDNILTLI RTLVTGGATP ELEALIAEEN 1090 1100 1110 1120 1130 1140 ALRGGYSTPQ TLANRDRCRV AQLALLDGPF ADLGDGGCYG DLFCKALKTY NMLCFGIYRL 1150 1160 1170 1180 1190 1200 RDAHLSTPSQ CTKRYVITNP PYEFELVPTD LIFCLMQFDH NAGQSRASLS HSSHSSQSSS 1210 1220 1230 KKSSSVHSIP STANRQNRPK SRESRDKQKY VQEERL
	Isoform 2 (BKTM) [UniParc]. Checksum: 932986BE30E0D409	FASTA	1,219	135,495
	10 20 30 40 50 60 MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS SSSSSSSSSS 70 80 90 100 110 120 VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH 130 140 150 160 170 180 CGGKTKEAQK INNGSSQADG TLKPVDEKEE AVAAEVGWMT SVKDWAGVMI SAQTLTGRVL 190 200 210 220 230 240 VVLVFALSIG ALVIYFIDSS NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL 250 260 270 280 290 300 WFWLEVNSVV DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL 310 320 330 340 350 360 VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM STVGYGDVYA 370 380 390 400 410 420 KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS YSAVSGRKHI VVCGHITLES 430 440 450 460 470 480 VSNFLKDFLH KDRDDVNVEI VFLHNISPNL ELEALFKRHF TQVEFYQGSV LNPHDLARVK 490 500 510 520 530 540 IESADACLIL ANKYCADPDA EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW 550 560 570 580 590 600 NWKEGDDAIC LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE 610 620 630 640 650 660 MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRILINPGN HLKIQEGTLG 670 680 690 700 710 720 FFIASDAKEV KRAFFYCKAC HDDITDPKRI KKCGCKRLED EQPSTLSPKK KQRNGGMRNS 730 740 750 760 770 780 PNTSPKLMRH DPLLIPGNDQ IDNMDSNVKK YDSTGMFHWC APKEIEKVIL VTGWMPYLGP 790 800 810 820 830 840 RVLMTCLDIG VVCMPTDIQS TSPASIKKFK ETRSEAAMTV LSGHVVVCIF GDVSSALIGL 850 860 870 880 890 900 RNLVMPLRAS NFHYHELKHI VFVGSIEYLK REWETLHNFP KVSILPGTPL SRADLRAVNI 910 920 930 940 950 960 NLCDMCVILS ANQNNIDDTS LQDKECILAS LNIKSMQFDD SIGVLQANSQ GFTPPGMDRS 970 980 990 1000 1010 1020 SPDNSPVHGM LRQPSITTGV NIPIITELVN DTNVQFLDQD DDDDPDTELY LTQPFACGTA 1030 1040 1050 1060 1070 1080 FAVSVLDSLM SATYFNDNIL TLIRTLVTGG ATPELEALIA EENALRGGYS TPQTLANRDR 1090 1100 1110 1120 1130 1140 CRVAQLALLD GPFADLGDGG CYGDLFCKAL KTYNMLCFGI YRLRDAHLST PSQCTKRYVI 1150 1160 1170 1180 1190 1200 TNPPYEFELV PTDLIFCLMQ FDHNAGQSRA SLSHSSHSSQ SSSKKSSSVH SIPSTANRQN 1210 RPKSRESRDK QKYVQEERL
	Isoform 3 [UniParc]. Checksum: 83DA8EC8C379A3D9	FASTA	1,240	138,087
	10 20 30 40 50 60 MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS SSSSSSSSSS 70 80 90 100 110 120 VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH 130 140 150 160 170 180 CGGKTKEAQK INNGSSQADG TLKPVDEKEE AVAAEVGWMT SVKDWAGVMI SAQTLTGRVL 190 200 210 220 230 240 VVLVFALSIG ALVIYFIDSS NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL 250 260 270 280 290 300 WFWLEVNSVV DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL 310 320 330 340 350 360 VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM STVGYGDVYA 370 380 390 400 410 420 KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS YSAVSGRKHI VVCGHITLES 430 440 450 460 470 480 VSNFLKDFLH KDRDDVNVEI VFLHNISPNL ELEALFKRHF TQVEFYQGSV LNPHDLARVK 490 500 510 520 530 540 IESADACLIL ANKYCADPDA EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW 550 560 570 580 590 600 NWKEGDDAIC LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE 610 620 630 640 650 660 MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRSRKRILI NPGNHLKIQE 670 680 690 700 710 720 GTLGFFIASD AKEVKRAFFY CKACHDDITD PKRIKKCGCK RPKMSIYKRM RRACCFDCGR 730 740 750 760 770 780 SERDCSCMSG RVRGNVDTLE RAFPLSSVSV NDCSTSFRAF EDEQPSTLSP KKKQRNGGMR 790 800 810 820 830 840 NSPNTSPKLM RHDPLLIPGN DQIDNMDSNV KKYDSTGMFH WCAPKEIEKV ILTRSEAAMT 850 860 870 880 890 900 VLSGHVVVCI FGDVSSALIG LRNLVMPLRA SNFHYHELKH IVFVGSIEYL KREWETLHNF 910 920 930 940 950 960 PKVSILPGTP LSRADLRAVN INLCDMCVIL SANQNNIDDT SLQDKECILA SLNIKSMQFD 970 980 990 1000 1010 1020 DSIGVLQANS QGFTPPGMDR SSPDNSPVHG MLRQPSITTG VNIPIITELV NDTNVQFLDQ 1030 1040 1050 1060 1070 1080 DDDDDPDTEL YLTQPFACGT AFAVSVLDSL MSATYFNDNI LTLIRTLVTG GATPELEALI 1090 1100 1110 1120 1130 1140 AEENALRGGY STPQTLANRD RCRVAQLALL DGPFADLGDG GCYGDLFCKA LKTYNMLCFG 1150 1160 1170 1180 1190 1200 IYRLRDAHLS TPSQCTKRYV ITNPPYEFEL VPTDLIFCLM QFDHNAGQSR ASLSHSSHSS 1210 1220 1230 1240 QSSSKKSSSV HSIPSTANRQ NRPKSRESRD KQKYVQEERL
	Isoform 4 (hbr5) [UniParc]. Checksum: 7B9C03A8BFA5055B	FASTA	1,207	134,362
	10 20 30 40 50 60 MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS SSSSSSSSSS 70 80 90 100 110 120 VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH 130 140 150 160 170 180 CGGKTKEAQK INNGSSQADG TLKPVDEKEE AVAAEVGWMT SVKDWAGVMI SAQTLTGRVL 190 200 210 220 230 240 VVLVFALSIG ALVIYFIDSS NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL 250 260 270 280 290 300 WFWLEVNSVV DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL 310 320 330 340 350 360 VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM STVGYGDVYA 370 380 390 400 410 420 KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS YSAVSGRKHI VVCGHITLES 430 440 450 460 470 480 VSNFLKDFLH KDRDDVNVEI VFLHNISPNL ELEALFKRHF TQVEFYQGSV LNPHDLARVK 490 500 510 520 530 540 IESADACLIL ANKYCADPDA EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW 550 560 570 580 590 600 NWKEGDDAIC LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE 610 620 630 640 650 660 MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRILINPGN HLKIQEGTLG 670 680 690 700 710 720 FFIASDAKEV KRAFFYCKAC HDDITDPKRI KKCGCKRLKV AARSRYSKDP FEFKKETPNS 730 740 750 760 770 780 RLVTEPVEDE QPSTLSPKKK QRNGGMRNSP NTSPKLMRHD PLLIPGNDQI DNMDSNVKKY 790 800 810 820 830 840 DSTGMFHWCA PKEIEKVILT RSEAAMTVLS GHVVVCIFGD VSSALIGLRN LVMPLRASNF 850 860 870 880 890 900 HYHELKHIVF VGSIEYLKRE WETLHNFPKV SILPGTPLSR ADLRAVNINL CDMCVILSAN 910 920 930 940 950 960 QNNIDDTSLQ DKECILASLN IKSMQFDDSI GVLQANSQGF TPPGMDRSSP DNSPVHGMLR 970 980 990 1000 1010 1020 QPSITTGVNI PIITELVNDT NVQFLDQDDD DDPDTELYLT QPFACGTAFA VSVLDSLMSA 1030 1040 1050 1060 1070 1080 TYFNDNILTL IRTLVTGGAT PELEALIAEE NALRGGYSTP QTLANRDRCR VAQLALLDGP 1090 1100 1110 1120 1130 1140 FADLGDGGCY GDLFCKALKT YNMLCFGIYR LRDAHLSTPS QCTKRYVITN PPYEFELVPT 1150 1160 1170 1180 1190 1200 DLIFCLMQFD HNAGQSRASL SHSSHSSQSS SKKSSSVHSI PSTANRQNRP KSRESRDKQK YVQEERL
	Isoform 5 [UniParc]. Checksum: AD3C9634F8A21EEC	FASTA	1,178	130,999
	10 20 30 40 50 60 MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS SSSSSSSSSS 70 80 90 100 110 120 VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH 130 140 150 160 170 180 CGGKTKEAQK INNGSSQADG TLKPVDEKEE AVAAEVGWMT SVKDWAGVMI SAQTLTGRVL 190 200 210 220 230 240 VVLVFALSIG ALVIYFIDSS NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL 250 260 270 280 290 300 WFWLEVNSVV DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL 310 320 330 340 350 360 VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM STVGYGDVYA 370 380 390 400 410 420 KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS YSAVSGRKHI VVCGHITLES 430 440 450 460 470 480 VSNFLKDFLH KDRDDVNVEI VFLHNISPNL ELEALFKRHF TQVEFYQGSV LNPHDLARVK 490 500 510 520 530 540 IESADACLIL ANKYCADPDA EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW 550 560 570 580 590 600 NWKEGDDAIC LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE 610 620 630 640 650 660 MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRILINPGN HLKIQEGTLG 670 680 690 700 710 720 FFIASDAKEV KRAFFYCKAC HDDITDPKRI KKCGCKRLED EQPSTLSPKK KQRNGGMRNS 730 740 750 760 770 780 PNTSPKLMRH DPLLIPGNDQ IDNMDSNVKK YDSTGMFHWC APKEIEKVIL TRSEAAMTVL 790 800 810 820 830 840 SGHVVVCIFG DVSSALIGLR NLVMPLRASN FHYHELKHIV FVGSIEYLKR EWETLHNFPK 850 860 870 880 890 900 VSILPGTPLS RADLRAVNIN LCDMCVILSA NQNNIDDTSL QDKECILASL NIKSMQFDDS 910 920 930 940 950 960 IGVLQANSQG FTPPGMDRSS PDNSPVHGML RQPSITTGVN IPIITELVND TNVQFLDQDD 970 980 990 1000 1010 1020 DDDPDTELYL TQPFACGTAF AVSVLDSLMS ATYFNDNILT LIRTLVTGGA TPELEALIAE 1030 1040 1050 1060 1070 1080 ENALRGGYST PQTLANRDRC RVAQLALLDG PFADLGDGGC YGDLFCKALK TYNMLCFGIY 1090 1100 1110 1120 1130 1140 RLRDAHLSTP SQCTKRYVIT NPPYEFELVP TDLIFCLMQF DHNAGQSRAS LSHSSHSSQS 1150 1160 1170 SSKKSSSVHS IPSTANRQNR PKSRESRDKQ KYVQEERL
	Isoform 6 [UniParc]. Checksum: 101980B6E7017A03	FASTA	168	17,191
	10 20 30 40 50 60 MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS SSSSSSSSSS 70 80 90 100 110 120 VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH 130 140 150 160 CGGKTKATHF GSPEMPPAAR SWSGSPPEAA VLRGASSLAL EVARCRRL
	Isoform 7 (gBK) [UniParc]. Checksum: CB186CA7A8C7B9CC	FASTA	1,239	138,297
	10 20 30 40 50 60 MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS SSSSSSSSSS 70 80 90 100 110 120 VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH 130 140 150 160 170 180 CGGKTKEAQK INNGSSQADG TLKPVDEKEE AVAAEVGWMT SVKDWAGVMI SAQTLTGRVL 190 200 210 220 230 240 VVLVFALSIG ALVIYFIDSS NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL 250 260 270 280 290 300 WFWLEVNSVV DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL 310 320 330 340 350 360 VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM STVGYGDVYA 370 380 390 400 410 420 KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS YSAVSGRKHI VVCGHITLES 430 440 450 460 470 480 VSNFLKDFLH KDRDDVNVEI VFLHNISPNL ELEALFKRHF TQVEFYQGSV LNPHDLARVK 490 500 510 520 530 540 IESADACLIL ANKYCADPDA EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW 550 560 570 580 590 600 NWKEGDDAIC LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE 610 620 630 640 650 660 MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRILINPGN HLKIQEGTLG 670 680 690 700 710 720 FFIASDAKEV KRAFFYCKAC HDDITDPKRI KKCGCKRRWE EHCSLWRLES KGNVRRLNYC 730 740 750 760 770 780 RGQQTSFVKV KVAARSRYSK DPFEFKKETP NSRLVTEPVE DEQPSTLSPK KKQRNGGMRN 790 800 810 820 830 840 SPNTSPKLMR HDPLLIPGND QIDNMDSNVK KYDSTGMFHW CAPKEIEKVI LTRSEAAMTV 850 860 870 880 890 900 LSGHVVVCIF GDVSSALIGL RNLVMPLRAS NFHYHELKHI VFVGSIEYLK REWETLHNFP 910 920 930 940 950 960 KVSILPGTPL SRADLRAVNI NLCDMCVILS ANQNNIDDTS LQDKECILAS LNIKSMQFDD 970 980 990 1000 1010 1020 SIGVLQANSQ GFTPPGMDRS SPDNSPVHGM LRQPSITTGV NIPIITELVN DTNVQFLDQD 1030 1040 1050 1060 1070 1080 DDDDPDTELY LTQPFACGTA FAVSVLDSLM SATYFNDNIL TLIRTLVTGG ATPELEALIA 1090 1100 1110 1120 1130 1140 EENALRGGYS TPQTLANRDR CRVAQLALLD GPFADLGDGG CYGDLFCKAL KTYNMLCFGI 1150 1160 1170 1180 1190 1200 YRLRDAHLST PSQCTKRYVI TNPPYEFELV PTDLIFCLMQ FDHNAGQSRA SLSHSSHSSQ 1210 1220 1230 SSSKKSSSVH SIPSTANRQN RPKSRESRDK QKYVQEERL

References

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[1]	"Cloning and expression of a human large-conductance calcium-activated potassium channel." Dworetzky S.I., Trojnacki J.T., Gribkoff V.K. Brain Res. Mol. Brain Res. 27:189-193(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). Tissue: Substantia nigra.
[2]	"A human calcium-activated potassium channel gene expressed in vascular smooth muscle." McCobb D.P., Fowler N.L., Featherstone T., Lingle C.J., Saito M., Krause J.E., Salkoff L. Am. J. Physiol. 269:H767-H777(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). Tissue: Aortic smooth muscle and Umbilical smooth muscle.
[3]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6). Tissue: Cerebellum, Neuroectoderm and Testis.
[6]	"Cloning, expression, and distribution of functionally distinct Ca(2+)-activated K+ channel isoforms from human brain." Tseng-Crank J., Foster C.D., Krause J.D., Mertz R., Godinot N., DiChiara T.J., Reinhart P.H. Neuron 13:1315-1330(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-1236 (ISOFORM 5).
[7]	"Calcium-activated potassium channel expression in human myometrium: effect of pregnancy." Mazzone J.N., Kaiser R.A., Buxton I.L.O. Proc. West. Pharmacol. Soc. 45:184-186(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-1236 (ISOFORM 5). Tissue: Myometrium.
[8]	"BK variant from human heart." Naruse K. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-1236 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 25-1236 (ISOFORM 2). Tissue: Heart.
[9]	"Cloning and characterization of human and mouse homologs of the Drosophila calcium-activated potassium channel gene, slowpoke." Pallanck L., Ganetzky B. Hum. Mol. Genet. 3:1239-1243(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-670 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 323-1236 (ISOFORM 4). Tissue: Muscle.
[10]	"Identification of potassium channels in human lens epithelium." Rae J.L., Shepard A.R. (In) Civan M.M. (eds.); Current topics in membranes. The eye's aqueous humor - from secretion to glaucoma, pp.45:69-104, Academic Press, San Diego (1998) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-1236 (ISOFORM 5). Tissue: Lens epithelium.
[11]	"Characterization of and modulation by a beta-subunit of a human maxi KCa channel cloned from myometrium." Wallner M., Meera P., Ottolia M., Kaczorowski G.J., Latorre R., Garcia M.L., Stefani E., Toro L. Recept. Channels 3:185-199(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-1236 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 693-764 (ISOFORM 4). Tissue: Myometrium.
[12]	"Cloning and characterization of BKCA alpha subunit from human pulmonary artery." Cairns V.R., Aebly M.R., Rusch N.J. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-1236 (ISOFORM 5). Tissue: Pulmonary artery.
[13]	"Cloning and characterization of glioma BK, a novel BK channel isoform highly expressed in human glioma cells." Liu X., Chang Y., Reinhart P.H., Sontheimer H., Chang Y. J. Neurosci. 22:1840-1849(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 7), TISSUE SPECIFICITY. Tissue: Glioblastoma.
[14]	Erratum Liu X., Chang Y., Reinhart P.H., Sontheimer H., Chang Y. J. Neurosci. 22:1B-1B(2002)
[15]	"Determinant for beta-subunit regulation in high-conductance voltage-activated and Ca(2+)-sensitive K+ channels: an additional transmembrane region at the N-terminus." Wallner M., Meera P., Toro L. Proc. Natl. Acad. Sci. U.S.A. 93:14922-14927(1996) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN S0.
[16]	"Large conductance voltage- and calcium-dependent K+ channel, a distinct member of voltage-dependent ion channels with seven N-terminal transmembrane segments (S0-S6), an extracellular N-terminus, and an intracellular (S9-S10) C-terminus." Meera P., Wallner M., Song M., Toro L. Proc. Natl. Acad. Sci. U.S.A. 94:14066-14071(1997) [PubMed] [Europe PMC] [Abstract] Cited for: MEMBRANE TOPOLOGY.
[17]	"Role of the S4 segment in a voltage-dependent calcium-sensitive potassium (hSlo) channel." Diaz L., Meera P., Amigo J., Stefani E., Alvarez O., Toro L., Latorre R. J. Biol. Chem. 273:32430-32436(1998) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN S4, MUTAGENESIS OF LEU-269; ARG-272; ARG-275; ARG-278; GLN-281 AND GLU-284.
[18]	"Molecular basis of fast inactivation in voltage and Ca2+-activated K+ channels: a transmembrane beta-subunit homolog." Wallner M., Meera P., Toro L. Proc. Natl. Acad. Sci. U.S.A. 96:4137-4142(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNMB2.
[19]	"Cloning and functional characterization of novel large conductance calcium-activated potassium channel beta subunits, hKCNMB3 and hKCNMB4." Brenner R., Jegla T.J., Wickenden A., Liu Y., Aldrich R.W. J. Biol. Chem. 275:6453-6461(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNMB3 AND KCNMB4.
[20]	"Identification of a novel tetramerization domain in large conductance K(ca) channels." Quirk J.C., Reinhart P.H. Neuron 32:13-23(2001) [PubMed] [Europe PMC] [Abstract] Cited for: HOMOTETRAMERIZATION, MUTAGENESIS OF 354-GLY--GLY-356.
[21]	"Consequences of the stoichiometry of Slo1 alpha and auxiliary beta subunits on functional properties of large-conductance Ca2+-activated K+ channels." Wang Y.-W., Ding J.-P., Xia X.-M., Lingle C.J. J. Neurosci. 22:1550-1561(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNMB1; KCNMB2; KCNMB3 AND KCNMB4.
[22]	"Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels." Tang X.D., Xu R., Reynolds M.F., Garcia M.L., Heinemann S.H., Hoshi T. Nature 425:531-535(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, MUTAGENESIS OF CYS-680 AND HIS-681.
[23]	"Gating mechanism of BK (Slo1) channels: so near, yet so far." Magleby K.L. J. Gen. Physiol. 121:81-96(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[24]	"LRRC26 auxiliary protein allows BK channel activation at resting voltage without calcium." Yan J., Aldrich R.W. Nature 466:513-516(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LRRC26.
[25]	"Characterizing the role of Thr352 in the inhibition of the large conductance Ca2+-activated K+ channels by 1-[1-Hexyl-6-(methyloxy)-1H-indazol-3-yl]-2-methyl-1-propanone." Gordon E., Semus S.F., Lozinskaya I.M., Lin Z., Xu X. J. Pharmacol. Exp. Ther. 334:402-409(2010) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF THR-352; PHE-380; ALA-381 AND VAL-384.
[26]	"BK potassium channel modulation by leucine-rich repeat-containing proteins." Yan J., Aldrich R.W. Proc. Natl. Acad. Sci. U.S.A. 109:7917-7922(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GAMMA SUBUNITS LRRC26; LRRC38; LRRC52 AND LRRC55.
[27]	"Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution." Yuan P., Leonetti M.D., Pico A.R., Hsiung Y., MacKinnon R. Science 329:182-186(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 406-1179, CALCIUM-BINDING SITES, SUBUNIT.
[28]	"Calcium-sensitive potassium channelopathy in human epilepsy and paroxysmal movement disorder." Du W., Bautista J.F., Yang H., Diez-Sampedro A., You S.-A., Wang L., Kotagal P., Lueders H.O., Shi J., Cui J., Richerson G.B., Wang Q.K. Nat. Genet. 37:733-738(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GEPD GLY-434.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
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.

IPI

IPI00164387.
IPI00410168.
IPI00410169.
IPI00410170.
IPI00410172.
IPI00410173.
IPI00478411.

PIR

I38596.
S62904.

RefSeq

NP_001014797.1. NM_001014797.2.
NP_001154824.1. NM_001161352.1.
NP_001154825.1. NM_001161353.1.
NP_001258447.1. NM_001271518.1.
NP_001258451.1. NM_001271522.1.
NP_002238.2. NM_002247.3.

UniGene

Hs.144795.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K44	NMR	-	A	257-284	[»]
3MT5	X-ray	3.00	A	406-1179	[»]
3NAF	X-ray	3.10	A	395-1178	[»]

ProteinModelPortal

Q12791.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29729N.

IntAct

Q12791. 1 interaction.

PTM databases

PhosphoSite

Q12791.

Polymorphism databases

DMDM

46396283.

Proteomic databases

PaxDb

Q12791.

PRIDE

Q12791.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000286627; ENSP00000286627; ENSG00000156113.
ENST00000372440; ENSP00000361517; ENSG00000156113.
ENST00000404857; ENSP00000385806; ENSG00000156113.

GeneID

3778.

KEGG

hsa:3778.

UCSC

uc001jxj.2. human.
uc001jxn.3. human.
uc001jxo.3. human.
uc001jxs.4. human.
uc009xrt.1. human.

Organism-specific databases

CTD

3778.

GeneCards

GC10M078629.

HGNC

HGNC:6284. KCNMA1.

MIM

600150. gene.
609446. phenotype.

neXtProt

NX_Q12791.

Orphanet

79137. Generalized epilepsy - paroxysmal dyskinesia.

PharmGKB

PA220.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1226.

HOVERGEN

HBG052222.

InParanoid

Q12791.

KO

K04936.

Enzyme and pathway databases

Reactome

REACT_13685. Neuronal System.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q12791.

Bgee

Q12791.

Genevestigator

Q12791.

GermOnline

ENSG00000156113. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR024939. Ca-act_K_channel_Slo.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003929. K_chnl_Ca-activ_BK_asu.
IPR016040. NAD(P)-bd_dom.
IPR003148. RCK_N.
[Graphical view]

PANTHER

PTHR10027:SF3. PTHR10027:SF3. 1 hit.

Pfam

PF03493. BK_channel_a. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]

PRINTS

PR01449. BKCHANNELA.
PR00169. KCHANNEL.

PROSITE

PS51201. RCK_N. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q12791.

ChEMBL

CHEMBL4304.

ChiTaRS

KCNMA1. human.

DrugBank

DB00436. Bendroflumethiazide.
DB00562. Benzthiazide.
DB00880. Chlorothiazide.
DB00356. Chlorzoxazone.
DB01003. Cromoglicate.
DB00606. Cyclothiazide.
DB01119. Diazoxide.
DB00228. Enflurane.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00232. Methyclothiazide.
DB01325. Quinethazone.
DB01021. Trichlormethiazide.

EvolutionaryTrace

Q12791.

GenomeRNAi

3778.

NextBio

14823.

SOURCE

Search...

Entry information

Entry name

KCMA1_HUMAN

Accession

Primary (citable) accession number: Q12791
Secondary accession number(s): Q12886 , Q12917, Q12921, Q12960, Q13150, Q5JQ23, Q5SQR9, Q96LG8, Q9UBB0, Q9UCX0, Q9UQK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.