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Protein

Calcium-activated potassium channel subunit alpha-1

Gene

Kcnma1

Organism
Rattus norvegicus (Rat)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi440 – 4401MagnesiumBy similarity
Metal bindingi463 – 4631MagnesiumBy similarity
Metal bindingi465 – 4651MagnesiumBy similarity
Metal bindingi986 – 9861Calcium; via carbonyl oxygenBy similarity
Metal bindingi989 – 9891Calcium; via carbonyl oxygenBy similarity
Metal bindingi992 – 9921CalciumBy similarity
Metal bindingi994 – 9941CalciumBy similarity

GO - Molecular functioni

  • calcium-activated potassium channel activity Source: RGD
  • large conductance calcium-activated potassium channel activity Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • protein complex binding Source: RGD
  • protein homodimerization activity Source: RGD
  • voltage-gated potassium channel activity Source: InterPro

GO - Biological processi

  • aging Source: RGD
  • negative regulation of small intestine smooth muscle contraction Source: RGD
  • positive regulation of neuron apoptotic process Source: RGD
  • positive regulation of vasodilation Source: RGD
  • protein homotetramerization Source: RGD
  • regulation of vasodilation Source: RGD
  • response to calcium ion Source: RGD
  • response to corticosteroid Source: RGD
  • response to estrogen Source: RGD
  • response to hypoxia Source: RGD
  • response to pH Source: RGD
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-RNO-1296052. Ca2+ activated K+ channels.

Protein family/group databases

TCDBi1.A.1.3.2. the voltage-gated ion channel (vic) superfamily.

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
Gene namesi
Name:Kcnma1
Synonyms:Kcnma
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi620715. Kcnma1.

Subcellular locationi

Isoform 7 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8787ExtracellularSequence analysisAdd
BLAST
Transmembranei88 – 10821Helical; Name=Segment S0Sequence analysisAdd
BLAST
Topological domaini109 – 17971CytoplasmicSequence analysisAdd
BLAST
Transmembranei180 – 20021Helical; Name=Segment S1Sequence analysisAdd
BLAST
Topological domaini201 – 21515ExtracellularSequence analysisAdd
BLAST
Transmembranei216 – 23621Helical; Name=Segment S2Sequence analysisAdd
BLAST
Topological domaini237 – 2404CytoplasmicSequence analysis
Transmembranei241 – 26121Helical; Name=Segment S3Sequence analysisAdd
BLAST
Topological domaini262 – 2654ExtracellularSequence analysis
Transmembranei266 – 28621Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd
BLAST
Topological domaini287 – 30115CytoplasmicSequence analysisAdd
BLAST
Transmembranei302 – 32221Helical; Name=Segment S5Sequence analysisAdd
BLAST
Topological domaini323 – 33614ExtracellularSequence analysisAdd
BLAST
Intramembranei337 – 35923Pore-forming; Name=P regionSequence analysisAdd
BLAST
Topological domaini360 – 3689ExtracellularSequence analysis
Transmembranei369 – 38921Helical; Name=Segment S6Sequence analysisAdd
BLAST
Topological domaini390 – 1209820CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • dendrite Source: RGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • external side of plasma membrane Source: RGD
  • neuronal cell body Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: RGD
  • presynaptic active zone membrane Source: RGD
  • protein complex Source: RGD
  • voltage-gated potassium channel complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi685 – 6862CH → SR: Loss of heme-induced channel inhibition as well as carbon monoxide-induced channel activation. 1 Publication

Chemistry

ChEMBLiCHEMBL5505.
GuidetoPHARMACOLOGYi380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12091209Calcium-activated potassium channel subunit alpha-1PRO_0000054137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi119 – 1191S-palmitoyl cysteineBy similarity
Lipidationi120 – 1201S-palmitoyl cysteineBy similarity
Lipidationi122 – 1221S-palmitoyl cysteineBy similarity
Modified residuei710 – 7101PhosphothreonineBy similarity
Modified residuei712 – 7121PhosphoserineCombined sources
Modified residuei725 – 7251PhosphoserineBy similarity
Modified residuei729 – 7291PhosphoserineBy similarity
Modified residuei917 – 9171PhosphothreonineBy similarity
Modified residuei925 – 9251PhosphoserineCombined sources
Modified residuei929 – 9291PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated (Probable). Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity (By similarity).By similarityCurated
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 (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

PTM databases

iPTMnetiQ62976.
PhosphoSiteiQ62976.
SwissPalmiQ62976.

Expressioni

Gene expression databases

ExpressionAtlasiQ62976. baseline and differential.

Interactioni

Subunit structurei

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. Interacts with RAB11B (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MbpP026884EBI-1638146,EBI-1638296

GO - Molecular functioni

  • protein complex binding Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi249823. 1 interaction.
DIPiDIP-40510N.
IntActiQ62976. 40 interactions.
MINTiMINT-1203282.

Chemistry

BindingDBiQ62976.

Structurei

3D structure databases

ProteinModelPortaliQ62976.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini416 – 559144RCK N-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni557 – 57721Segment S7Add
BLAST
Regioni614 – 63421Segment S8Add
BLAST
Regioni682 – 6865Heme-binding motif
Regioni784 – 80421Segment S9Add
BLAST
Regioni1006 – 102621Segment S10Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi353 – 3564Selectivity for potassium
Motifi977 – 99923Calcium bowlAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 118Poly-Gly
Compositional biasi17 – 259Poly-Gly
Compositional biasi45 – 6117Poly-SerAdd
BLAST

Domaini

The S0 segment is essential for the modulation by the accessory beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4.By similarity
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. 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 (By similarity).By similarity
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.
InParanoidiQ62976.
KOiK04936.
PhylomeDBiQ62976.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
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: Q62976-1) [UniParc]FASTAAdd to basket

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 GSSGSSGGGG GGGGGETALR MSSNIHANHL SLDASSSSSS
60 70 80 90 100
SSSSSSSSSS SVHEPKMDAL IIPVTMEVPC DSRGQRMWWA FLASSMVTFF
110 120 130 140 150
GGLFIILLWR TLKYLWTVCC HCGGKTKEAQ KINNGSSQAD GTLKPVDEKE
160 170 180 190 200
EVVAAEVGWM TSVKDWAGVM ISAQTLTGRV LVVLVFALSI GALVIYFIDS
210 220 230 240 250
SNPIESCQNF YKDFTLQIDM AFNVFFLLYF GLRFIAANDK LWFWLEVNSV
260 270 280 290 300
VDFFTVPPVF VSVYLNRSWL GLRFLRALRL IQFSEILQFL NILKTSNSIK
310 320 330 340 350
LVNLLSIFIS TWLTAAGFIH LVENSGDPWE NFQNNQALTY WECVYLLMVT
360 370 380 390 400
MSTVGYGDVY AKTTLGRLFM VFFILGGLAM FASYVPEIIE LIGNRKKYGG
410 420 430 440 450
SYSAVSGRKH IVVCGHITLE SVSNFLKDFL HKDRDDVNVE IVFLHNISPN
460 470 480 490 500
LELEALFKRH FTQVEFYQGS VLNPHDLARV KIESADACLI LANKYCADPD
510 520 530 540 550
AEDASNIMRV ISIKNYHPKI RIITQMLQYH NKAHLLNIPS WNWKEGDDAI
560 570 580 590 600
CLAELKLGFI AQSCLAQGLS TMLANLFSMR SFIKIEEDTW QKYYLEGVSN
610 620 630 640 650
EMYTEYLSSA FVGLSFPTVC ELCFVKLKLL MIAIEYKSAN RESRSRKRIL
660 670 680 690 700
INPGNHLKIQ EGTLGFFIAS DAKEVKRAFF YCKACHDDVT DPKRIKKCGC
710 720 730 740 750
RRLEDEQPPT LSPKKKQRNG GMRNSPNTSP KLMRHDPLLI PGNDQIDNMD
760 770 780 790 800
SNVKKYDSTG MFHWCAPKEI EKVILTRSEA AMTVLSGHVV VCIFGDVSSA
810 820 830 840 850
LIGLRNLVMP LRASNFHYHE LKHIVFVGSI EYLKREWETL HNFPKVSILP
860 870 880 890 900
GTPLSRADLR AVNINLCDMC VILSANQNNI DDTSLQDKEC ILASLNIKSM
910 920 930 940 950
QFDDSIGVLQ ANSQGFTPPG MDRSSPDNSP VHGMLRQPSI TTGVNIPIIT
960 970 980 990 1000
ELAKPGKLPL VSVNQEKNSG THILMITELV NDTNVQFLDQ DDDDDPDTEL
1010 1020 1030 1040 1050
YLTQPFACGT AFAVSVLDSL MSATYFNDNI LTLIRTLVTG GATPELEALI
1060 1070 1080 1090 1100
AEENALRGGY STPQTLANRD RCRVAQLALL DGPFADLGDG GCYGDLFCKA
1110 1120 1130 1140 1150
LKTYNMLCFG IYRLRDAHLS TPSQCTKRYV ITNPPYEFEL VPTDLIFCLM
1160 1170 1180 1190 1200
QFDHNAGQSR ASLSHSSHSS QSSSKKSSSV HSIPSTANRP NRPKSRESRD

KQKKEMVYR
Length:1,209
Mass (Da):134,374
Last modified:February 5, 2008 - v3
Checksum:i14F19072DA7F22FE
GO
Isoform 2 (identifier: Q62976-2) [UniParc]FASTAAdd to basket

Also known as: B, C, cvb1, cvb2

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     644-647: Missing.
     949-975: Missing.

Show »
Length:1,148
Mass (Da):128,684
Checksum:i7518E011D0AED714
GO
Isoform 3 (identifier: Q62976-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     644-647: Missing.
     949-975: Missing.
     1203-1209: KKEMVYR → NNRRCWWFSKRQDIHQQKRNGLQMRRIMPIPETFKSSP

Show »
Length:1,179
Mass (Da):132,502
Checksum:iB88D1A037BE26970
GO
Isoform 4 (identifier: Q62976-8) [UniParc]FASTAAdd to basket

Also known as: STTEX

The sequence of this isoform differs from the canonical sequence as follows:
     703-703: L → LIYSKMSIYKRMSRACCFDCGRSERDCSCMSGRVRGNVDTLERNFPLSSVSVNDCSTSFRAF
     949-975: Missing.

Show »
Length:1,243
Mass (Da):138,388
Checksum:i37BDFB5E50D15FAF
GO
Isoform 5 (identifier: Q62976-9) [UniParc]FASTAAdd to basket

Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     644-647: Missing.
     949-975: Missing.
     1128-1165: RYVITNPPYE...AGQSRASLSH → SNRRCWWFSK...PIPETFKSSP
     1166-1209: Missing.

Show »
Length:1,134
Mass (Da):126,309
Checksum:i959090FF5F757293
GO
Isoform 6 (identifier: Q62976-10) [UniParc]FASTAAdd to basket

Also known as: SLON-1

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     949-975: Missing.

Show »
Length:1,152
Mass (Da):129,211
Checksum:i9BB5D98E6BD5D293
GO
Isoform 7 (identifier: Q62976-11) [UniParc]FASTAAdd to basket

Also known as: SV1

The sequence of this isoform differs from the canonical sequence as follows:
     181-181: L → AFERSSLLARISIQKDGCQCVLFSSHFMPRLLM

Show »
Length:1,241
Mass (Da):138,029
Checksum:i4777BC0BFBE348FF
GO

Sequence cautioni

The sequence AAB51398.1 differs from that shown. Reason: Frameshift at position 1203. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331Missing in AAB51398 (PubMed:9403560).Curated
Sequence conflicti33 – 331Missing in AAA99161 (Ref. 4) Curated
Sequence conflicti132 – 1321I → V in AAP82452 (Ref. 7) Curated
Sequence conflicti158 – 1581G → V in AAC32866 (PubMed:10384881).Curated
Sequence conflicti164 – 1641K → E in AAB51398 (PubMed:9403560).Curated
Sequence conflicti176 – 1761L → P in AAP82451 (Ref. 7) Curated
Sequence conflicti205 – 2051E → Q in AAC32866 (PubMed:10384881).Curated
Sequence conflicti238 – 2381N → K in AAP82451 (Ref. 7) Curated
Sequence conflicti266 – 2661N → D in AAP82451 (Ref. 7) Curated
Sequence conflicti279 – 2791R → I in AAP82451 (Ref. 7) Curated
Sequence conflicti281 – 2811I → V in AAP82452 (Ref. 7) Curated
Sequence conflicti286 – 2861I → S in AAP82452 (Ref. 7) Curated
Sequence conflicti296 – 2961S → N in AAP82450 (Ref. 7) Curated
Sequence conflicti338 – 3381L → P in AAA99161 (Ref. 4) Curated
Sequence conflicti353 – 3531T → A in AAP82452 (Ref. 7) Curated
Sequence conflicti364 – 3641T → S in AAA99161 (Ref. 4) Curated
Sequence conflicti364 – 3641T → TLGT in AAP82452 (Ref. 7) Curated
Sequence conflicti446 – 4461N → S in AAP82451 (Ref. 7) Curated
Sequence conflicti450 – 4501N → D in AAP82451 (Ref. 7) Curated
Sequence conflicti468 – 4681Q → K in AAB51398 (PubMed:9403560).Curated
Sequence conflicti470 – 4701S → P in AAP82452 (Ref. 7) Curated
Sequence conflicti479 – 4791R → T in AAA99161 (Ref. 4) Curated
Sequence conflicti549 – 5491A → S in AAC32866 (PubMed:10384881).Curated
Sequence conflicti552 – 5521L → H in AAP82452 (Ref. 7) Curated
Sequence conflicti553 – 5531A → V in AAP82454 (PubMed:16166559).Curated
Sequence conflicti600 – 6001N → T in AAB51398 (PubMed:9403560).Curated
Sequence conflicti605 – 6051E → G in AAA99161 (Ref. 4) Curated
Sequence conflicti637 – 6371K → R in AAP82452 (Ref. 7) Curated
Sequence conflicti659 – 6591I → T in AAB96356 (Ref. 3) Curated
Sequence conflicti660 – 6601Q → R in AAB51398 (PubMed:9403560).Curated
Sequence conflicti677 – 6771R → K in AAB51398 (PubMed:9403560).Curated
Sequence conflicti685 – 6873CHD → YHE in AAP82452 (Ref. 7) Curated
Sequence conflicti734 – 7341R → K in AAD34786 (PubMed:10651830).Curated
Sequence conflicti739 – 7391L → S in AAP82454 (PubMed:16166559).Curated
Sequence conflicti762 – 7621F → L in AAA99161 (Ref. 4) Curated
Sequence conflicti780 – 7801A → V in AAP82454 (PubMed:16166559).Curated
Sequence conflicti806 – 8061N → NRN in AAP82451 (Ref. 7) Curated
Sequence conflicti864 – 8641I → L in AAC32866 (PubMed:10384881).Curated
Sequence conflicti885 – 8851L → V in AAC32866 (PubMed:10384881).Curated
Sequence conflicti940 – 9401I → T in AAP82453 (PubMed:16166559).Curated
Sequence conflicti989 – 9891D → G in AAP82451 (Ref. 7) Curated
Sequence conflicti1005 – 10051P → L in AAA99161 (Ref. 4) Curated
Sequence conflicti1012 – 10121F → S in AAC32866 (PubMed:10384881).Curated
Sequence conflicti1093 – 10931Y → C in AAP82452 (Ref. 7) Curated
Sequence conflicti1107 – 11071L → F in AAP82451 (Ref. 7) Curated
Sequence conflicti1173 – 11731S → P in AAP82453 (PubMed:16166559).Curated
Sequence conflicti1188 – 11881N → S in AAP82454 (PubMed:16166559).Curated
Sequence conflicti1203 – 12031K → NR in AAB51398 (PubMed:9403560).Curated
Sequence conflicti1203 – 12031K → NR in AAD34786 (PubMed:10651830).Curated
Sequence conflicti1203 – 12031K → NR in AAP82454 (PubMed:16166559).Curated
Sequence conflicti1203 – 12031K → NR in AAP82451 (Ref. 7) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3030Missing in isoform 2, isoform 3 and isoform 6. 5 PublicationsVSP_009970Add
BLAST
Alternative sequencei181 – 1811L → AFERSSLLARISIQKDGCQC VLFSSHFMPRLLM in isoform 7. CuratedVSP_009971
Alternative sequencei644 – 6474Missing in isoform 2, isoform 3 and isoform 5. 4 PublicationsVSP_009973
Alternative sequencei703 – 7031L → LIYSKMSIYKRMSRACCFDC GRSERDCSCMSGRVRGNVDT LERNFPLSSVSVNDCSTSFR AF in isoform 4. 1 PublicationVSP_009974
Alternative sequencei949 – 97527Missing in isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6. 6 PublicationsVSP_009976Add
BLAST
Alternative sequencei1128 – 116538RYVIT…ASLSH → SNRRCWWFSKRQDIHQQKRN GLQMRRIMPIPETFKSSP in isoform 5. 1 PublicationVSP_009978Add
BLAST
Alternative sequencei1166 – 120944Missing in isoform 5. 1 PublicationVSP_009979Add
BLAST
Alternative sequencei1203 – 12097KKEMVYR → NNRRCWWFSKRQDIHQQKRN GLQMRRIMPIPETFKSSP in isoform 3. 1 PublicationVSP_009982

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93052 mRNA. Translation: AAB51398.1. Frameshift.
AF135265 mRNA. Translation: AAD34786.1.
U40603 mRNA. Translation: AAB96356.1.
U55995 mRNA. Translation: AAA99161.1.
AF083341 mRNA. Translation: AAC32866.1.
AY330290 mRNA. Translation: AAP82450.1.
AY330291 mRNA. Translation: AAP82451.1.
AY330292 mRNA. Translation: AAP82452.1.
AY330293 mRNA. Translation: AAP82453.2.
AY330294 mRNA. Translation: AAP82454.1.
RefSeqiNP_114016.1. NM_031828.1.
UniGeneiRn.30616.

Genome annotation databases

EnsembliENSRNOT00000066928; ENSRNOP00000061684; ENSRNOG00000005985. [Q62976-3]
GeneIDi83731.
KEGGirno:83731.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93052 mRNA. Translation: AAB51398.1. Frameshift.
AF135265 mRNA. Translation: AAD34786.1.
U40603 mRNA. Translation: AAB96356.1.
U55995 mRNA. Translation: AAA99161.1.
AF083341 mRNA. Translation: AAC32866.1.
AY330290 mRNA. Translation: AAP82450.1.
AY330291 mRNA. Translation: AAP82451.1.
AY330292 mRNA. Translation: AAP82452.1.
AY330293 mRNA. Translation: AAP82453.2.
AY330294 mRNA. Translation: AAP82454.1.
RefSeqiNP_114016.1. NM_031828.1.
UniGeneiRn.30616.

3D structure databases

ProteinModelPortaliQ62976.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249823. 1 interaction.
DIPiDIP-40510N.
IntActiQ62976. 40 interactions.
MINTiMINT-1203282.

Chemistry

BindingDBiQ62976.
ChEMBLiCHEMBL5505.
GuidetoPHARMACOLOGYi380.

Protein family/group databases

TCDBi1.A.1.3.2. the voltage-gated ion channel (vic) superfamily.

PTM databases

iPTMnetiQ62976.
PhosphoSiteiQ62976.
SwissPalmiQ62976.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000066928; ENSRNOP00000061684; ENSRNOG00000005985. [Q62976-3]
GeneIDi83731.
KEGGirno:83731.

Organism-specific databases

CTDi3778.
RGDi620715. Kcnma1.

Phylogenomic databases

GeneTreeiENSGT00530000063026.
HOVERGENiHBG052222.
InParanoidiQ62976.
KOiK04936.
PhylomeDBiQ62976.

Enzyme and pathway databases

ReactomeiR-RNO-1296052. Ca2+ activated K+ channels.

Miscellaneous databases

PROiQ62976.

Gene expression databases

ExpressionAtlasiQ62976. baseline and differential.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Increased expression of Ca2+-sensitive K+ channels in aorta of hypertensive rats."
    Liu Y., Pleyte K., Knaus H.-G., Rusch N.J.
    Hypertension 30:1403-1409(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: Sprague-Dawley.
    Tissue: Aortic smooth muscle.
  2. "Functional characteristics of two BKCa channel variants differentially expressed in rat brain tissues."
    Ha T.S., Jeong S.Y., Cho S.-W., Jeon H.-K., Roh G.S., Choi W.S., Park C.-S.
    Eur. J. Biochem. 267:910-918(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. Reimann F.
    Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Strain: Sprague-Dawley.
    Tissue: Brain cortex.
  4. "Cloning and expression of smooth muscle specific isoforms of a rat calcium-activated potassium channel."
    Lawrence K.M., Fenech C.J., Zhang H., Bolton T.B.
    Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Strain: Wistar HsdOla.
    Tissue: Myometrium.
  5. "Identification and localization of Ca(2+)-activated K+ channels in rat sciatic nerve."
    Mi H., Harris-Warrick R.M., Deerinck T.J., Inman I., Ellisman M.H., Schwarz T.L.
    Glia 26:166-175(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1028 (ISOFORM 6).
    Strain: Sprague-Dawley.
  6. "Heme is a carbon monoxide receptor for large-conductance Ca2+-activated K+ channels."
    Jaggar J.H., Li A., Parfenova H., Liu J., Umstot E.S., Dopico A.M., Leffler C.W.
    Circ. Res. 97:805-812(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-1209 (ISOFORM 2), ENZYME REGULATION, MUTAGENESIS OF 685-CYS-HIS-686.
    Strain: Sprague-Dawley.
    Tissue: Cerebral artery.
  7. "Slo subunits cloned from freshly isolated rat cerebral artery myocytes."
    Liu J., Asuncion-Chin M.T., Liu P., Dopico A.M.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-1209 (ISOFORMS 2 AND 5).
    Strain: Sprague-Dawley.
    Tissue: Aorta and Cerebral artery.
  8. "A novel MaxiK splice variant exhibits dominant-negative properties for surface expression."
    Zarei M.M., Zhu N., Alioua A., Eghbali M., Stefani E., Toro L.
    J. Biol. Chem. 276:16232-16239(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 7).
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712; SER-925 AND SER-929, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKCMA1_RAT
AccessioniPrimary (citable) accession number: Q62976
Secondary accession number(s): O08626
, O55180, O88659, Q7TMZ7, Q7TMZ8, Q7TQ55, Q7TQ56, Q7TQ57, Q9WUI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: February 5, 2008
Last modified: June 8, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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 contains binding sites for Ca2+ and Mg2+.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.