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Entry version 163 (02 Jun 2021)
Sequence version 2 (13 Apr 2004)
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Protein

Calcium-activated potassium channel subunit alpha-1

Gene

KCNMA1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Potassium channel activated by both membrane depolarization or increase in cytosolic Ca2+ that mediates export of K+. It is also activated by 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) (By similarity).

By similarity

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+.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Ethanol and carbon monoxide-bound heme increase channel activation. Heme inhibits channel activation (By similarity). Phosphorylation of Thr-139 leads to inhibition of channel activity by ethanol.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi427MagnesiumBy similarity1
Metal bindingi450MagnesiumBy similarity1
Metal bindingi452MagnesiumBy similarity1
Metal bindingi942Calcium; via carbonyl oxygenBy similarity1
Metal bindingi945Calcium; via carbonyl oxygenBy similarity1
Metal bindingi948CalciumBy similarity1
Metal bindingi950CalciumBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIon channel, Potassium channel, Voltage-gated channel
Biological processIon transport, Potassium transport, Transport
LigandCalcium, Magnesium, Metal-binding, Potassium

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
bSlo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:KCNMA1
Synonyms:KCNMA
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 28

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:30479, KCNMA1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 74ExtracellularSequence analysisAdd BLAST74
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei75 – 95Helical; Name=Segment S0Sequence analysisAdd BLAST21
Topological domaini96 – 166CytoplasmicSequence analysisAdd BLAST71
Transmembranei167 – 187Helical; Name=Segment S1Sequence analysisAdd BLAST21
Topological domaini188 – 202ExtracellularSequence analysisAdd BLAST15
Transmembranei203 – 223Helical; Name=Segment S2Sequence analysisAdd BLAST21
Topological domaini224 – 227CytoplasmicSequence analysis4
Transmembranei228 – 248Helical; Name=Segment S3Sequence analysisAdd BLAST21
Topological domaini249 – 252ExtracellularSequence analysis4
Transmembranei253 – 273Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd BLAST21
Topological domaini274 – 288CytoplasmicSequence analysisAdd BLAST15
Transmembranei289 – 309Helical; Name=Segment S5Sequence analysisAdd BLAST21
Topological domaini310 – 323ExtracellularSequence analysisAdd BLAST14
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei324 – 346Pore-forming; Name=P regionSequence analysisAdd BLAST23
Topological domaini347 – 355ExtracellularSequence analysis9
Transmembranei356 – 376Helical; Name=Segment S6Sequence analysisAdd BLAST21
Topological domaini377 – 1166CytoplasmicSequence analysisAdd BLAST790

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi139T → V: Loss of phosphorylation by CaMK2 and, therefore, inhibition of channel activity in response to ethanol. 1 Publication1
Mutagenesisi1151S → A: Induces a stimulation by PKA instead of PKG; when associated with A-1154. 1 Publication1
Mutagenesisi1154S → A: Induces a stimulation by PKA instead of PKG; when associated with A-1151. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2111364

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000541301 – 1166Calcium-activated potassium channel subunit alpha-1Add BLAST1166

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi106S-palmitoyl cysteineBy similarity1
Lipidationi107S-palmitoyl cysteineBy similarity1
Lipidationi109S-palmitoyl cysteineBy similarity1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei139Phosphothreonine; by CamK21 Publication1
Modified residuei693PhosphothreonineBy similarity1
Modified residuei695PhosphoserineBy similarity1
Modified residuei708PhosphoserineBy similarity1
Modified residuei712PhosphoserineBy similarity1
Modified residuei900PhosphothreonineBy similarity1
Modified residuei908PhosphoserineBy similarity1
Modified residuei912PhosphoserineBy similarity1
Modified residuei1151Phosphoserine; by PKG1 Publication1
Modified residuei1154Phosphoserine; by PKG1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. Isoform 1 and isoform 2 are stimulated by PKG, but not by PKA. In contrast, isoform 3 is exclusively stimulated by PKA. In smooth muscles, phosphorylation affects its activity.1 Publication
Incremental phosphorylation of Thr-139 of the KCNMA1 tetramer changes the response to ethanol from increased activation to inhibition of channel activity.2 Publications
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

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q28204

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q28204

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000013300, Expressed in myometrium and 91 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q28204, baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
159786, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000047743

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
Q28204

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q28204

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini403 – 546RCK N-terminalAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 20DisorderedSequence analysisAdd BLAST20
Regioni30 – 51DisorderedSequence analysisAdd BLAST22
Regioni544 – 564Segment S7Add BLAST21
Regioni601 – 621Segment S8Add BLAST21
Regioni665 – 669Heme-binding motif5
Regioni689 – 717DisorderedSequence analysisAdd BLAST29
Regioni767 – 787Segment S9Add BLAST21
Regioni962 – 982Segment S10Add BLAST21
Regioni1116 – 1166DisorderedSequence analysisAdd BLAST51

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi340 – 343Selectivity for potassium4
Motifi933 – 955Calcium bowlAdd BLAST23

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi696 – 714Polar residuesSequence analysisAdd BLAST19
Compositional biasi1116 – 1147Polar residuesSequence analysisAdd BLAST32
Compositional biasi1148 – 1166Basic and acidic residuesSequence analysisAdd BLAST19

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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 (By similarity).By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1420, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154935

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q28204

Identification of Orthologs from Complete Genome Data

More...
OMAi
KYSTNPD

Database of Orthologous Groups

More...
OrthoDBi
124461at2759

TreeFam database of animal gene trees

More...
TreeFami
TF314283

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.120.350, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR024939, Ca-act_K_channel_Slo-1
IPR005821, Ion_trans_dom
IPR003929, K_chnl_BK_asu
IPR036291, NAD(P)-bd_dom_sf
IPR027359, Volt_channel_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR10027:SF28, PTHR10027:SF28, 2 hits

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03493, BK_channel_a, 1 hit
PF00520, Ion_trans, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735, SSF51735, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: May be partially controlled by hormonal stress. Additional isoforms seem to exist.

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q28204-1) [UniParc]FASTAAdd to basket
Also known as: A, BKA

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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 GGGGSSLRMS SNIHANHLSL DASSSSSSSS SSSSSSSSVH
60 70 80 90 100
EPKMDALIIP VTMEVPCDSR GQRMWWAFLA SSMVTFFGGL FIILLWRTLK
110 120 130 140 150
YLWTVCCHCG GKTKEAQKIN NGSSQADGTL KPVDEKEETV AAEVGWMTSV
160 170 180 190 200
KDWAGVMISA QTLTGRVLVV LVFALSIGAL VIYFIDSSNP IESCQNFYKD
210 220 230 240 250
FTLQIDMAFN VFFLLYFGLR FIAANDKLWF WLEVNSVVDF FTVPPVFVSV
260 270 280 290 300
YLNRSWLGLR FLRALRLIQF SEILQFLNIL KTSNSIKLVN LLSIFISTWL
310 320 330 340 350
TAAGFIHLVE NSGDPWENFQ NNQALTYWEC VYLLMVTMST VGYGDVYAKT
360 370 380 390 400
TLGRLFMVFF ILGGLAMFAS YVPEIIELIG NRKKYGGSYS AVSGRKHIVV
410 420 430 440 450
CGHITLESVS NFLKDFLHKD RDDVNVEIVF LHNISPNLEL EALFKRHFTQ
460 470 480 490 500
VEFYQGSVLN PHDLARVKIE SADACLILAN KYCADPDAED ASNIMRVISI
510 520 530 540 550
KNYHPKIRII TQMLQYHNKA HLLNIPSWNW KEGDDAICLA ELKLGFIAQS
560 570 580 590 600
CLAQGLSTML ANLFSMRSFI KIEEDTWQKY YLEGVSNEMY TEYLSSAFVG
610 620 630 640 650
LSFPTVCELC FVKLKLLMIA IEYKSANRES RILINPGNHL KIQEGTLGFF
660 670 680 690 700
IASDAKEVKR AFFYCKACHD DITDPKRIKK CGCKRLEDEQ PSTLSPKKKQ
710 720 730 740 750
RNGGMRNSPS SSPKLMRHDP LLIPGNDQID NMDSNVKKYD STGMFHWCAP
760 770 780 790 800
KEIEKVILTR SEAAMTVLSG HVVVCIFGDV SSALIGLRNL VMPLRASNFH
810 820 830 840 850
YHELKHIVFV GSIEYLKREW ETLHNFPKVS ILPGTPLSRA DLRAVNINLC
860 870 880 890 900
DMCVILSANQ NNIDDTSLQD KECILASLNI KSMQFDDSIG VLQANSQGFT
910 920 930 940 950
PPGMDRSSPD NSPVHGMLRQ PSITTGVNIP IITELVNDTN VQFLDQDDDD
960 970 980 990 1000
DPDTELYLTQ PFACGTAFAV SVLDSLMSAT YFNDNILTLI RTLVTGGATP
1010 1020 1030 1040 1050
ELEALIAEEN ALRGGYSTPQ TLANRDRCRV AQLALLDGPF ADLGDGGCYG
1060 1070 1080 1090 1100
DLFCKALKTY NMLCFGIYRL RDAHLSTPSQ CTKRYVITNP PYEFELVPTD
1110 1120 1130 1140 1150
LIFCLMQFDH NAGQSRASLS HSSHSSQSSS KKSSSVHSIP STANRQNRPK
1160
SRESRDKQKY VQEERL
Length:1,166
Mass (Da):130,063
Last modified:April 13, 2004 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5E7DE4845D94743F
GO
Isoform 2 (identifier: Q28204-2) [UniParc]FASTAAdd to basket
Also known as: B, BKB

The sequence of this isoform differs from the canonical sequence as follows:
     1160-1166: YVQEERL → KEMVYL

Show »
Length:1,165
Mass (Da):129,909
Checksum:i7ED4DD9DCDBC5F2B
GO
Isoform 3 (identifier: Q28204-3) [UniParc]FASTAAdd to basket
Also known as: C, BKC

The sequence of this isoform differs from the canonical sequence as follows:
     1141-1166: STANRQNRPKSRESRDKQKYVQEERL → PQT

Show »
Length:1,143
Mass (Da):127,203
Checksum:i8120AF5B18EA6834
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1MSP6F1MSP6_BOVIN
BK channel
KCNMA1
1,129Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A3Q1MJG6A0A3Q1MJG6_BOVIN
BK channel
KCNMA1
1,108Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F1MST8F1MST8_BOVIN
BK channel
KCNMA1
1,165Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti33 – 35SSS → GST in AAB03663 (PubMed:8973172).Curated3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0099501141 – 1166STANR…QEERL → PQT in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_0099511160 – 1166YVQEERL → KEMVYL in isoform 2. 1 Publication7

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY033472 mRNA Translation: AAK54352.1
AY033473 mRNA Translation: AAK54353.1
AY033474 mRNA Translation: AAK54354.1
U60105 mRNA Translation: AAB03663.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B53145

NCBI Reference Sequences

More...
RefSeqi
NP_777105.1, NM_174680.2 [Q28204-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000054334; ENSBTAP00000047743; ENSBTAG00000013300 [Q28204-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
282573

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
bta:282573

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033472 mRNA Translation: AAK54352.1
AY033473 mRNA Translation: AAK54353.1
AY033474 mRNA Translation: AAK54354.1
U60105 mRNA Translation: AAB03663.1
PIRiB53145
RefSeqiNP_777105.1, NM_174680.2 [Q28204-1]

3D structure databases

BMRBiQ28204
SMRiQ28204
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi159786, 1 interactor
STRINGi9913.ENSBTAP00000047743

Chemistry databases

ChEMBLiCHEMBL2111364

PTM databases

iPTMnetiQ28204

Proteomic databases

PaxDbiQ28204

Genome annotation databases

EnsembliENSBTAT00000054334; ENSBTAP00000047743; ENSBTAG00000013300 [Q28204-1]
GeneIDi282573
KEGGibta:282573

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3778
VGNCiVGNC:30479, KCNMA1

Phylogenomic databases

eggNOGiKOG1420, Eukaryota
GeneTreeiENSGT00940000154935
InParanoidiQ28204
OMAiKYSTNPD
OrthoDBi124461at2759
TreeFamiTF314283

Gene expression databases

BgeeiENSBTAG00000013300, Expressed in myometrium and 91 other tissues
ExpressionAtlasiQ28204, baseline and differential

Family and domain databases

Gene3Di1.20.120.350, 1 hit
InterProiView protein in InterPro
IPR024939, Ca-act_K_channel_Slo-1
IPR005821, Ion_trans_dom
IPR003929, K_chnl_BK_asu
IPR036291, NAD(P)-bd_dom_sf
IPR027359, Volt_channel_dom_sf
PANTHERiPTHR10027:SF28, PTHR10027:SF28, 2 hits
PfamiView protein in Pfam
PF03493, BK_channel_a, 1 hit
PF00520, Ion_trans, 1 hit
SUPFAMiSSF51735, SSF51735, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKCMA1_BOVIN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q28204
Secondary accession number(s): Q95J89, Q95J90, Q95J91
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: June 2, 2021
This is version 163 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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