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Entry version 140 (11 Dec 2019)
Sequence version 2 (13 Apr 2004)
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Protein

Calcium-activated potassium channel subunit alpha-1

Gene

KCNMA1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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 transcript 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 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) (By similarity).By similarity1 Publication

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+.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi377MagnesiumBy similarity1
Metal bindingi400MagnesiumBy similarity1
Metal bindingi402MagnesiumBy similarity1
Metal bindingi892Calcium; via carbonyl oxygenBy similarity1
Metal bindingi895Calcium; via carbonyl oxygenBy similarity1
Metal bindingi898CalciumBy similarity1
Metal bindingi900CalciumBy 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_and_taxonomy_section">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9615 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002254 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Unplaced

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 domaini‹1 – 24ExtracellularSequence analysisAdd BLAST›24
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei25 – 45Helical; Name=Segment S0Sequence analysisAdd BLAST21
Topological domaini46 – 116CytoplasmicSequence analysisAdd BLAST71
Transmembranei117 – 137Helical; Name=Segment S1Sequence analysisAdd BLAST21
Topological domaini138 – 152ExtracellularSequence analysisAdd BLAST15
Transmembranei153 – 173Helical; Name=Segment S2Sequence analysisAdd BLAST21
Topological domaini174 – 177CytoplasmicSequence analysis4
Transmembranei178 – 198Helical; Name=Segment S3Sequence analysisAdd BLAST21
Topological domaini199 – 202ExtracellularSequence analysis4
Transmembranei203 – 223Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd BLAST21
Topological domaini224 – 238CytoplasmicSequence analysisAdd BLAST15
Transmembranei239 – 259Helical; Name=Segment S5Sequence analysisAdd BLAST21
Topological domaini260 – 273ExtracellularSequence analysisAdd BLAST14
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Intramembranei274 – 296Pore-forming; Name=P regionSequence analysisAdd BLAST23
Topological domaini297 – 305ExtracellularSequence analysis9
Transmembranei306 – 326Helical; Name=Segment S6Sequence analysisAdd BLAST21
Topological domaini327 – 1159CytoplasmicSequence analysisAdd BLAST833

Keywords - Cellular componenti

Cell membrane, Membrane

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000054131‹1 – 1159Calcium-activated potassium channel subunit alpha-1Add BLAST›1159

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Lipidationi56S-palmitoyl cysteineBy similarity1
Lipidationi57S-palmitoyl cysteineBy similarity1
Lipidationi59S-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 residuei643PhosphothreonineBy similarity1
Modified residuei645PhosphoserineBy similarity1
Modified residuei658PhosphoserineBy similarity1
Modified residuei662PhosphoserineBy similarity1
Modified residuei850PhosphothreonineBy similarity1
Modified residuei858PhosphoserineBy similarity1
Modified residuei862PhosphoserineBy similarity1
Modified residuei1101PhosphoserineBy similarity1
Modified residuei1104PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 (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

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

More...
PaxDbi
Q28265

PRoteomics IDEntifications database

More...
PRIDEi
Q28265

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q28265

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in all vascular and smooth muscles.1 Publication

<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_section">'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_section">'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

STRING: functional protein association networks

More...
STRINGi
9612.ENSCAFP00000022784

<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

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

More...
SMRi
Q28265

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_and_domains_section">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>Domaini353 – 496RCK 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>Regioni494 – 514Segment S7Add BLAST21
Regioni551 – 571Segment S8Add BLAST21
Regioni615 – 619Heme-binding motif5
Regioni717 – 737Segment S9Add BLAST21
Regioni912 – 932Segment S10Add BLAST21

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>Motifi290 – 293Selectivity for potassium4
Motifi883 – 905Calcium bowlAdd BLAST23

<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
ENOG410YUX1 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000019856

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q28265

KEGG Orthology (KO)

More...
KOi
K04936

Database of Orthologous Groups

More...
OrthoDBi
124461at2759

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, 1 hit

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_length">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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: Fragment.

This entry describes 1 <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> isoform i produced by alternative splicing. AlignAdd to basket
Note: May be partially controlled by hormonal stress. A number of isoforms are produced.
Isoform 1 (identifier: Q28265-1) [UniParc]FASTAAdd to basket

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
EPNMDALIIP VTMEVPCDSR GQRMWWAFLA SSMVTFFGGL FIILLWRTLK
60 70 80 90 100
YLWTVCCHCG DKTKEAQKIN NGSSQADGTL KPVDEKEEAV AAEVGWMTSV
110 120 130 140 150
KDWAGVMISA QTLTGRVLVV LVFALSIGAL VIYFIDSSNP IESCQNFYKD
160 170 180 190 200
FTLQIDMAFN VFFLLYFGLR FIAANDNLWF WLEVNSVVDF FTVPPVFVSV
210 220 230 240 250
YLNRSWLGLR FLRALRLIQF SEILQFLNIL KTSNSIKLVN LLSIFISTWL
260 270 280 290 300
TAAGFIHLVE NSGDPWENFQ NSQALTYWEC VYLLMVTMST VGYGDVYAKT
310 320 330 340 350
TPGGLFIVFF ILGGLAMFAS YVPEIIEIIG NRKKYGGSYS AVSGRKHIVV
360 370 380 390 400
CGHITLESVS HFLKDFLHKD RDDVNVEIVF LHNISPNLEL EALFKRHFTQ
410 420 430 440 450
VEFYQGSVLN PHDLARVKIE SADACLILAN KYCDDPDAED ASNIMRVISI
460 470 480 490 500
KNYHPKIRII TQMLQYHNKA HLLNIPSWNW KEGDDAICLA ELRLGFIAQS
510 520 530 540 550
CLAQGLSTML ANLFSIGSFI KIEEDTWHKY YLEGVSNEMY TEYLSSAFVG
560 570 580 590 600
LSFPTVCELC FVKLKLLMIA IEYKSANRES RILINPGNHL KIQEGTSGFF
610 620 630 640 650
IASDAKEVKR AFFYCKACHN DITDPKRIKK CGCKRLEDEQ PSTLSPKKKQ
660 670 680 690 700
RNGGMRNSPS SSPKLMRHDP LLIPGNDQID NMDSNVKKYD STGMFHWCAP
710 720 730 740 750
KEIEKVISTR SEAAMTVLSG HVVVCIFGHV SSALIGLRNL VMPLRASNFH
760 770 780 790 800
YHELKHIVFV GSIEYLKREW ETLHNFPKVS ILPGTPLTRA DLRAVNINLC
810 820 830 840 850
DMCVILSANQ NNIDDTSLQD KECILASLNI KSMQFDDSIG VLQANSQGFT
860 870 880 890 900
PPGMDKSSPD NSPVHGMLRQ PSITTGVNIP IITELVNDTN VQFLDQDDDD
910 920 930 940 950
DPDTELYLTQ PFACGTAFAV SVLDSLMSAT YFNDNILTLI RTLVTGGATP
960 970 980 990 1000
ELEALIAEEN ALRGGYSTPQ TLANRDRCRV AQLALLDGPF ADLGDGGCYG
1010 1020 1030 1040 1050
DLFCKALKTY NMLCFGIYRL RDAHLSTPSQ CTKRYVITNP PYRFELVPTD
1060 1070 1080 1090 1100
LIFCLMQFDH NAGQSRASLS HSSHSSQSSS KKSSSVHSIP STANRQNRPK
1110 1120 1130 1140 1150
SRESRDKQTE KKWFTDEPDN AYPRNIQIEP MSTHMANQIN QYKSTSSLIP

PIREVEDEC
Length:1,159
Mass (Da):130,296
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:iD8CF38C32971BB64
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei11

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U41001 mRNA Translation: AAA84000.1

NCBI Reference Sequences

More...
RefSeqi
NP_001003300.2, NM_001003300.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
403984

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cfa:403984

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
U41001 mRNA Translation: AAA84000.1
RefSeqiNP_001003300.2, NM_001003300.2

3D structure databases

SMRiQ28265
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9612.ENSCAFP00000022784

PTM databases

iPTMnetiQ28265

Proteomic databases

PaxDbiQ28265
PRIDEiQ28265

Genome annotation databases

GeneIDi403984
KEGGicfa:403984

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3778

Phylogenomic databases

eggNOGiKOG1420 Eukaryota
ENOG410YUX1 LUCA
HOGENOMiHOG000019856
InParanoidiQ28265
KOiK04936
OrthoDBi124461at2759

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, 1 hit
PfamiView protein in Pfam
PF03493 BK_channel_a, 1 hit
PF00520 Ion_trans, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_CANLF
<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: Q28265
<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_and_isoforms">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: December 11, 2019
This is version 140 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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