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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)DescriptionActionsGraphical viewLength
Metal bindingi440MagnesiumBy similarity1
Metal bindingi463MagnesiumBy similarity1
Metal bindingi465MagnesiumBy similarity1
Metal bindingi986Calcium; via carbonyl oxygenBy similarity1
Metal bindingi989Calcium; via carbonyl oxygenBy similarity1
Metal bindingi992CalciumBy similarity1
Metal bindingi994CalciumBy similarity1

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: GO_Central

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)DescriptionActionsGraphical viewLength
Topological domaini1 – 87ExtracellularSequence analysisAdd BLAST87
Transmembranei88 – 108Helical; Name=Segment S0Sequence analysisAdd BLAST21
Topological domaini109 – 179CytoplasmicSequence analysisAdd BLAST71
Transmembranei180 – 200Helical; Name=Segment S1Sequence analysisAdd BLAST21
Topological domaini201 – 215ExtracellularSequence analysisAdd BLAST15
Transmembranei216 – 236Helical; Name=Segment S2Sequence analysisAdd BLAST21
Topological domaini237 – 240CytoplasmicSequence analysis4
Transmembranei241 – 261Helical; Name=Segment S3Sequence analysisAdd BLAST21
Topological domaini262 – 265ExtracellularSequence analysis4
Transmembranei266 – 286Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd BLAST21
Topological domaini287 – 301CytoplasmicSequence analysisAdd BLAST15
Transmembranei302 – 322Helical; Name=Segment S5Sequence analysisAdd BLAST21
Topological domaini323 – 336ExtracellularSequence analysisAdd BLAST14
Intramembranei337 – 359Pore-forming; Name=P regionSequence analysisAdd BLAST23
Topological domaini360 – 368ExtracellularSequence analysis9
Transmembranei369 – 389Helical; Name=Segment S6Sequence analysisAdd BLAST21
Topological domaini390 – 1209CytoplasmicSequence analysisAdd BLAST820

GO - Cellular componenti

  • apical plasma membrane Source: GO_Central
  • 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: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi685 – 686CH → SR: Loss of heme-induced channel inhibition as well as carbon monoxide-induced channel activation. 1 Publication2

Chemistry databases

ChEMBLiCHEMBL5505.
GuidetoPHARMACOLOGYi380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000541371 – 1209Calcium-activated potassium channel subunit alpha-1Add BLAST1209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi119S-palmitoyl cysteineBy similarity1
Lipidationi120S-palmitoyl cysteineBy similarity1
Lipidationi122S-palmitoyl cysteineBy similarity1
Modified residuei710PhosphothreonineBy similarity1
Modified residuei712PhosphoserineCombined sources1
Modified residuei725PhosphoserineBy similarity1
Modified residuei729PhosphoserineBy similarity1
Modified residuei917PhosphothreonineBy similarity1
Modified residuei925PhosphoserineCombined sources1
Modified residuei929PhosphoserineCombined sources1

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

Proteomic databases

PRIDEiQ62976.

PTM databases

iPTMnetiQ62976.
PhosphoSitePlusiQ62976.
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 interactor.
DIPiDIP-40510N.
IntActiQ62976. 40 interactors.
MINTiMINT-1203282.

Chemistry databases

BindingDBiQ62976.

Structurei

3D structure databases

ProteinModelPortaliQ62976.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini416 – 559RCK N-terminalAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni557 – 577Segment S7Add BLAST21
Regioni614 – 634Segment S8Add BLAST21
Regioni682 – 686Heme-binding motif5
Regioni784 – 804Segment S9Add BLAST21
Regioni1006 – 1026Segment S10Add BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi353 – 356Selectivity for potassium4
Motifi977 – 999Calcium bowlAdd BLAST23

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 11Poly-Gly8
Compositional biasi17 – 25Poly-Gly9
Compositional biasi45 – 61Poly-SerAdd BLAST17

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. 2 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: 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 differs from that shown. Reason: Frameshift at position 1203.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti33Missing in AAB51398 (PubMed:9403560).Curated1
Sequence conflicti33Missing in AAA99161 (Ref. 4) Curated1
Sequence conflicti132I → V in AAP82452 (Ref. 7) Curated1
Sequence conflicti158G → V in AAC32866 (PubMed:10384881).Curated1
Sequence conflicti164K → E in AAB51398 (PubMed:9403560).Curated1
Sequence conflicti176L → P in AAP82451 (Ref. 7) Curated1
Sequence conflicti205E → Q in AAC32866 (PubMed:10384881).Curated1
Sequence conflicti238N → K in AAP82451 (Ref. 7) Curated1
Sequence conflicti266N → D in AAP82451 (Ref. 7) Curated1
Sequence conflicti279R → I in AAP82451 (Ref. 7) Curated1
Sequence conflicti281I → V in AAP82452 (Ref. 7) Curated1
Sequence conflicti286I → S in AAP82452 (Ref. 7) Curated1
Sequence conflicti296S → N in AAP82450 (Ref. 7) Curated1
Sequence conflicti338L → P in AAA99161 (Ref. 4) Curated1
Sequence conflicti353T → A in AAP82452 (Ref. 7) Curated1
Sequence conflicti364T → S in AAA99161 (Ref. 4) Curated1
Sequence conflicti364T → TLGT in AAP82452 (Ref. 7) Curated1
Sequence conflicti446N → S in AAP82451 (Ref. 7) Curated1
Sequence conflicti450N → D in AAP82451 (Ref. 7) Curated1
Sequence conflicti468Q → K in AAB51398 (PubMed:9403560).Curated1
Sequence conflicti470S → P in AAP82452 (Ref. 7) Curated1
Sequence conflicti479R → T in AAA99161 (Ref. 4) Curated1
Sequence conflicti549A → S in AAC32866 (PubMed:10384881).Curated1
Sequence conflicti552L → H in AAP82452 (Ref. 7) Curated1
Sequence conflicti553A → V in AAP82454 (PubMed:16166559).Curated1
Sequence conflicti600N → T in AAB51398 (PubMed:9403560).Curated1
Sequence conflicti605E → G in AAA99161 (Ref. 4) Curated1
Sequence conflicti637K → R in AAP82452 (Ref. 7) Curated1
Sequence conflicti659I → T in AAB96356 (Ref. 3) Curated1
Sequence conflicti660Q → R in AAB51398 (PubMed:9403560).Curated1
Sequence conflicti677R → K in AAB51398 (PubMed:9403560).Curated1
Sequence conflicti685 – 687CHD → YHE in AAP82452 (Ref. 7) Curated3
Sequence conflicti734R → K in AAD34786 (PubMed:10651830).Curated1
Sequence conflicti739L → S in AAP82454 (PubMed:16166559).Curated1
Sequence conflicti762F → L in AAA99161 (Ref. 4) Curated1
Sequence conflicti780A → V in AAP82454 (PubMed:16166559).Curated1
Sequence conflicti806N → NRN in AAP82451 (Ref. 7) Curated1
Sequence conflicti864I → L in AAC32866 (PubMed:10384881).Curated1
Sequence conflicti885L → V in AAC32866 (PubMed:10384881).Curated1
Sequence conflicti940I → T in AAP82453 (PubMed:16166559).Curated1
Sequence conflicti989D → G in AAP82451 (Ref. 7) Curated1
Sequence conflicti1005P → L in AAA99161 (Ref. 4) Curated1
Sequence conflicti1012F → S in AAC32866 (PubMed:10384881).Curated1
Sequence conflicti1093Y → C in AAP82452 (Ref. 7) Curated1
Sequence conflicti1107L → F in AAP82451 (Ref. 7) Curated1
Sequence conflicti1173S → P in AAP82453 (PubMed:16166559).Curated1
Sequence conflicti1188N → S in AAP82454 (PubMed:16166559).Curated1
Sequence conflicti1203K → NR in AAB51398 (PubMed:9403560).Curated1
Sequence conflicti1203K → NR in AAD34786 (PubMed:10651830).Curated1
Sequence conflicti1203K → NR in AAP82454 (PubMed:16166559).Curated1
Sequence conflicti1203K → NR in AAP82451 (Ref. 7) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0099701 – 30Missing in isoform 2, isoform 3 and isoform 6. 5 PublicationsAdd BLAST30
Alternative sequenceiVSP_009971181L → AFERSSLLARISIQKDGCQC VLFSSHFMPRLLM in isoform 7. Curated1
Alternative sequenceiVSP_009973644 – 647Missing in isoform 2, isoform 3 and isoform 5. 4 Publications4
Alternative sequenceiVSP_009974703L → LIYSKMSIYKRMSRACCFDC GRSERDCSCMSGRVRGNVDT LERNFPLSSVSVNDCSTSFR AF in isoform 4. 1 Publication1
Alternative sequenceiVSP_009976949 – 975Missing in isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6. 6 PublicationsAdd BLAST27
Alternative sequenceiVSP_0099781128 – 1165RYVIT…ASLSH → SNRRCWWFSKRQDIHQQKRN GLQMRRIMPIPETFKSSP in isoform 5. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_0099791166 – 1209Missing in isoform 5. 1 PublicationAdd BLAST44
Alternative sequenceiVSP_0099821203 – 1209KKEMVYR → NNRRCWWFSKRQDIHQQKRN GLQMRRIMPIPETFKSSP in isoform 3. 1 Publication7

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 interactor.
DIPiDIP-40510N.
IntActiQ62976. 40 interactors.
MINTiMINT-1203282.

Chemistry databases

BindingDBiQ62976.
ChEMBLiCHEMBL5505.
GuidetoPHARMACOLOGYi380.

Protein family/group databases

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

PTM databases

iPTMnetiQ62976.
PhosphoSitePlusiQ62976.
SwissPalmiQ62976.

Proteomic databases

PRIDEiQ62976.

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. 2 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_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: November 30, 2016
This is version 142 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.